ID 6PGL_NEIMB Reviewed; 231 AA. AC P63337; Q9JR64; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=6-phosphogluconolactonase; DE Short=6PGL; DE EC=3.1.1.31; GN Name=pgl; OrderedLocusNames=NMB1391; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2/3. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41755.1; -; Genomic_DNA. DR PIR; F81089; F81089. DR RefSeq; NP_274405.1; NC_003112.2. DR RefSeq; WP_002213145.1; NC_003112.2. DR ProteinModelPortal; P63337; -. DR STRING; 122586.NMB1391; -. DR PaxDb; P63337; -. DR EnsemblBacteria; AAF41755; AAF41755; NMB1391. DR GeneID; 903813; -. DR KEGG; nme:NMB1391; -. DR PATRIC; 20358465; VBINeiMen85645_1744. DR eggNOG; ENOG4108Q79; Bacteria. DR eggNOG; COG0363; LUCA. DR HOGENOM; HOG000256284; -. DR KO; K01057; -. DR OMA; PEANIHG; -. DR OrthoDB; EOG63FW46; -. DR BioCyc; NMEN122586:GHGG-1429-MONOMER; -. DR UniPathway; UPA00115; UER00409. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 231 6-phosphogluconolactonase. FT /FTId=PRO_0000090098. SQ SEQUENCE 231 AA; 24980 MW; 5EF54C495553D073 CRC64; MFVWHEYENA AEAAQSLADA VADALQGALD EKGGAVLAVS GGRSPIAFFN ALSQKDLDWK NVGITLADER IVPTVHADSN TGLVREYLLK NKAEAAMWIP MVEDGKTETE LHPDAVVDYA LKHYKQPDVL VLGMGNDGHT ASIFPKAPQF QTAIDGSAGV ALVHTTPVTA PHERVSMTLD AIAHTGHVFL AIRGEEKKAV FDQAAQGENR EYPINLVLNH QGVNCHVFYA E // ID ACPS_NEIMB Reviewed; 125 AA. AC P0A0Q5; Q9RML8; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101}; DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101}; DE EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101}; DE AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101}; GN Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101}; Synonyms=dpj; GN OrderedLocusNames=NMB0452; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme CC A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP- CC Rule:MF_00101}. CC -!- CATALYTIC ACTIVITY: CoA-(4'-phosphopantetheine) + apo-[acyl- CC carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl- CC carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00101}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}. CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS CC family. {ECO:0000255|HAMAP-Rule:MF_00101}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40889.1; -; Genomic_DNA. DR PIR; F81197; F81197. DR RefSeq; NP_273499.1; NC_003112.2. DR RefSeq; WP_002212541.1; NC_003112.2. DR ProteinModelPortal; P0A0Q5; -. DR STRING; 122586.NMB0452; -. DR PaxDb; P0A0Q5; -. DR EnsemblBacteria; AAF40889; AAF40889; NMB0452. DR GeneID; 902568; -. DR KEGG; nme:NMB0452; -. DR PATRIC; 20356118; VBINeiMen85645_0575. DR eggNOG; ENOG4105KJV; Bacteria. DR eggNOG; COG0736; LUCA. DR HOGENOM; HOG000014316; -. DR KO; K00997; -. DR OMA; AQGVFWR; -. DR OrthoDB; EOG6384R9; -. DR BioCyc; NMEN122586:GHGG-476-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.470.20; -; 1. DR HAMAP; MF_00101; AcpS; 1. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_SF. DR InterPro; IPR002582; ACPS. DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom. DR Pfam; PF01648; ACPS; 1. DR ProDom; PD004282; PPantethiene-prot_Trfase; 1. DR SUPFAM; SSF56214; SSF56214; 1. DR TIGRFAMs; TIGR00516; acpS; 1. DR TIGRFAMs; TIGR00556; pantethn_trn; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Reference proteome; Transferase. FT CHAIN 1 125 Holo-[acyl-carrier-protein] synthase. FT /FTId=PRO_0000175677. FT METAL 8 8 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. FT METAL 57 57 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. SQ SEQUENCE 125 AA; 13677 MW; 64AD823F8529EC6A CRC64; MIYGIGTDIV SLKRIIRLNK KFGQAFAGRI LTPEELLEFP QAGKPVNYLA KRFAAKEAFA KAVGTGIRGA VSFRNIGIGH DALGKPEFFY GPALSKWLEE QGISRVSLSM SDEEDTVLAF VVAEK // ID ACP_NEIMB Reviewed; 78 AA. AC P63442; Q9JR72; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217}; DE Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217}; GN Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217}; GN OrderedLocusNames=NMB0220; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of apo-ACP by AcpS. This modification is essential for CC activity because fatty acids are bound in thioester linkage to the CC sulfhydryl of the prosthetic group. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40676.1; -; Genomic_DNA. DR PIR; F81222; F81222. DR RefSeq; NP_273277.1; NC_003112.2. DR RefSeq; WP_002215574.1; NC_003112.2. DR ProteinModelPortal; P63442; -. DR SMR; P63442; 2-76. DR STRING; 122586.NMB0220; -. DR PaxDb; P63442; -. DR EnsemblBacteria; AAF40676; AAF40676; NMB0220. DR GeneID; 902332; -. DR KEGG; nme:NMB0220; -. DR PATRIC; 20355512; VBINeiMen85645_0280. DR eggNOG; ENOG4105VNB; Bacteria. DR eggNOG; COG0236; LUCA. DR HOGENOM; HOG000178184; -. DR KO; K02078; -. DR OMA; IKPESSF; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; NMEN122586:GHGG-235-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000036; F:ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1200.10; -; 1. DR HAMAP; MF_01217; Acyl_carrier; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR TIGRFAMs; TIGR00517; acyl_carrier; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Phosphopantetheine; Phosphoprotein; Reference proteome. FT CHAIN 1 78 Acyl carrier protein. FT /FTId=PRO_0000180157. FT MOD_RES 37 37 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|HAMAP-Rule:MF_01217}. SQ SEQUENCE 78 AA; 8511 MW; 5A36838AC5072BE5 CRC64; MSNIEQQVKK IVAEQLGVNE ADVKNESSFQ DDLGADSLDT VELVMALEEA FGCEIPDEDA EKITTVQLAI DYINAHNG // ID ACCA_NEIMB Reviewed; 319 AA. AC Q9JRV8; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE EC=6.4.1.2 {ECO:0000255|HAMAP-Rule:MF_00823}; GN Name=accA1 {ECO:0000255|HAMAP-Rule:MF_00823}; GN OrderedLocusNames=NMB1139; GN and GN Name=accA2 {ECO:0000255|HAMAP-Rule:MF_00823}; GN OrderedLocusNames=NMB1177; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. First, biotin carboxylase catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the carboxyltransferase to acetyl-CoA to form CC malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) CC and two subunits each of ACCase subunit alpha (AccA) and ACCase CC subunit beta (AccD). {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP- CC Rule:MF_00823}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41562.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41527.1; -; Genomic_DNA. DR PIR; B81119; B81119. DR RefSeq; NP_274168.1; NC_003112.2. DR RefSeq; NP_274204.1; NC_003112.2. DR RefSeq; WP_010980898.1; NC_003112.2. DR ProteinModelPortal; Q9JRV8; -. DR SMR; Q9JRV8; 5-314. DR STRING; 122586.NMB1177; -. DR PaxDb; Q9JRV8; -. DR EnsemblBacteria; AAF41527; AAF41527; NMB1139. DR EnsemblBacteria; AAF41562; AAF41562; NMB1177. DR GeneID; 903560; -. DR GeneID; 903597; -. DR KEGG; nme:NMB1139; -. DR KEGG; nme:NMB1177; -. DR PATRIC; 20357853; VBINeiMen85645_1442. DR eggNOG; ENOG4107QM9; Bacteria. DR eggNOG; COG0825; LUCA. DR HOGENOM; HOG000273832; -. DR KO; K01962; -. DR OMA; HSVYTVA; -. DR OrthoDB; EOG6HQSSF; -. DR BioCyc; NMEN122586:GHGG-1175-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1212-MONOMER; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1. DR InterPro; IPR001095; Acetyl_CoA_COase_a_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011763; COA_CT_C. DR Pfam; PF03255; ACCA; 1. DR PRINTS; PR01069; ACCCTRFRASEA. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00513; accA; 1. DR PROSITE; PS50989; COA_CT_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 319 Acetyl-coenzyme A carboxylase carboxyl FT transferase subunit alpha. FT /FTId=PRO_0000223790. SQ SEQUENCE 319 AA; 35507 MW; CCAE5172FD149D7F CRC64; MKPVFLDFEQ PIAELTNKID ELRFVQDESA VDISDEIHRL QKKSNDLTKS IFSKLTPAQI SQVSRHPQRP YTLDYIEALF TDFEELHGDR HFADDYAIVG GLARFNGQSV MVVGHQKGRD TKEKIRRNFG MPRPEGYRKA LRLMKTAEKF GLPVMTFIDT PGAYPGIGAE ERGQSEAIGK NLYELTRLRV PVLCTVIGEG GSGGALAVAL GDYVNMLQYS TYSVISPEGC ASILWKTAEK AADAAQALGI TADRLQKLDL VDTVIKEPLG GAHRDFGQTM KNVKAVLEKQ LHEAQSIPLA DLLSRRFDRI MAYGKFSEQ // ID ACKA2_NEIMB Reviewed; 399 AA. AC Q9K0X1; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 83. DE RecName: Full=Acetate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase 2 {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA2 {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=NMB0435; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40873.1; -; Genomic_DNA. DR PIR; D81198; D81198. DR RefSeq; NP_273483.1; NC_003112.2. DR RefSeq; WP_002222042.1; NC_003112.2. DR ProteinModelPortal; Q9K0X1; -. DR STRING; 122586.NMB0435; -. DR PaxDb; Q9K0X1; -. DR EnsemblBacteria; AAF40873; AAF40873; NMB0435. DR GeneID; 902551; -. DR KEGG; nme:NMB0435; -. DR PATRIC; 20356072; VBINeiMen85645_0551. DR eggNOG; ENOG4105C6H; Bacteria. DR eggNOG; COG0282; LUCA. DR HOGENOM; HOG000288399; -. DR KO; K00925; -. DR OMA; DYEANKT; -. DR OrthoDB; EOG69975F; -. DR BioCyc; NMEN122586:GHGG-459-MONOMER; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro. DR HAMAP; MF_00020; Acetate_kinase; 1. DR InterPro; IPR004372; Ac/propionate_kinase. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR PANTHER; PTHR21060; PTHR21060; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR00016; ackA; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 399 Acetate kinase 2. FT /FTId=PRO_0000107593. FT NP_BIND 206 210 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 281 283 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 329 333 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 384 384 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 239 239 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. SQ SEQUENCE 399 AA; 42795 MW; B672CDD77F8B7A78 CRC64; MSDQLILVLN CGSSSLKGAV IDRKSGSVVL SCLGERLTTP EAVITFNKDG NKRQVPLSGR NCHAGAVGML LNELEKHGLH DRIKAIGHRI AHGGEKYSES VLIDQAVMDE LNACIPLAPL HNPANISGIL AAQEHFPGLP NVGVMDTSFH QTMPERAYTY AVPRELRKKY AFRRYGFHGT SMRYVAPEAA RILGKPLEDI RMIIAHLGNG ASITAIKNGK SVDTSMGFTP IEGLVMGTRC GDIDPGVYSY LTSHAGMDVA QVDEMLNKKS GLLGISELSN DCRTLEIAAD EGHEGARLAL EVMTYRLAKY IASMAVGCGG VDALVFTGGI GENSRNIRAK TVSYLDFLGL HIDTKANMEK RYGNSGIISP TDSSPAVLVV PTNEELMIAC DTAELAGIL // ID ACKA1_NEIMB Reviewed; 398 AA. AC Q9JYM1; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Acetate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase 1 {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA1 {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=NMB1518; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41874.1; -; Genomic_DNA. DR PIR; E81074; E81074. DR RefSeq; NP_274526.1; NC_003112.2. DR RefSeq; WP_002222237.1; NC_003112.2. DR ProteinModelPortal; Q9JYM1; -. DR STRING; 122586.NMB1518; -. DR PaxDb; Q9JYM1; -. DR PRIDE; Q9JYM1; -. DR EnsemblBacteria; AAF41874; AAF41874; NMB1518. DR GeneID; 903996; -. DR KEGG; nme:NMB1518; -. DR PATRIC; 20358828; VBINeiMen85645_1924. DR eggNOG; ENOG4105C6H; Bacteria. DR eggNOG; COG0282; LUCA. DR HOGENOM; HOG000288399; -. DR KO; K00925; -. DR OMA; IDMANEK; -. DR OrthoDB; EOG69975F; -. DR BioCyc; NMEN122586:GHGG-1558-MONOMER; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro. DR HAMAP; MF_00020; Acetate_kinase; 1. DR InterPro; IPR004372; Ac/propionate_kinase. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR PANTHER; PTHR21060; PTHR21060; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR00016; ackA; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 398 Acetate kinase 1. FT /FTId=PRO_0000107592. FT NP_BIND 206 210 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 281 283 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 329 333 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 384 384 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 239 239 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. SQ SEQUENCE 398 AA; 42410 MW; 600D71F7BC7AE336 CRC64; MSQKLILVLN CGSSSLKGAV LDNGSGEVLL SCLAEKLNLP DAYITFKVNG EKHKVDLSAH PDHTGAVEAL MEELKAHGLD SRIGAIGHRV VSGGELYSES ILVDDEVIAG IEKCIPLAPL HNPAHLLGLR AAQSIFKGLP NVVVFDTSFH QTMPEVAYKY AVPQELYEKY GLRRYGAHGT SYRFVADETA RFLGKDKKDL RMVIAHLGNG ASITAVANGE SRDTSMGLTP LEGLVMGTRS GDIDPSVFGF LAENANMTIA QITEMLNKKS GLLGISGLSN DCRTIEEEAA KGHKGAKLAL DMFIYRLAKY IGSMAVAAGG LDALVFTGGI GENSDIIRER VIGYLGFLGL NIDQEANLKA RFGNAGVITT ADSKAVAVVI PTNEELMIAH DTARLSGL // ID ALR_NEIMB Reviewed; 352 AA. AC Q9JYC4; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201}; GN Name=alr; OrderedLocusNames=NMB1651; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D- CC alanine. May also act on other amino acids. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D- CC alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. CC {ECO:0000255|HAMAP-Rule:MF_01201}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42000.1; -; Genomic_DNA. DR PIR; B81059; B81059. DR RefSeq; NP_274656.1; NC_003112.2. DR RefSeq; WP_002224993.1; NC_003112.2. DR ProteinModelPortal; Q9JYC4; -. DR SMR; Q9JYC4; 1-351. DR STRING; 122586.NMB1651; -. DR PaxDb; Q9JYC4; -. DR EnsemblBacteria; AAF42000; AAF42000; NMB1651. DR GeneID; 903465; -. DR KEGG; nme:NMB1651; -. DR PATRIC; 20359224; VBINeiMen85645_2124. DR eggNOG; ENOG4105CJ4; Bacteria. DR eggNOG; COG0787; LUCA. DR HOGENOM; HOG000031446; -. DR KO; K01775; -. DR OMA; PSDWVRP; -. DR OrthoDB; EOG6PP9NJ; -. DR BioCyc; NMEN122586:GHGG-1700-MONOMER; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_01201; Ala_racemase; 1. DR InterPro; IPR000821; Ala_racemase. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C; 1. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR00492; alr; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 352 Alanine racemase. FT /FTId=PRO_0000114541. FT ACT_SITE 33 33 Proton acceptor; specific for D-alanine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT ACT_SITE 250 250 Proton acceptor; specific for L-alanine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT BINDING 129 129 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01201}. FT BINDING 298 298 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT MOD_RES 33 33 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. SQ SEQUENCE 352 AA; 38820 MW; 0AC586A9E12860E6 CRC64; MRPLNVQIRL GNLRHNYRIL KEMHGGKLLA VVKADAYGHG AVRCAFALAD LADGFAVATI DEGIRLRESG ITHPIVLLEG VFEASEYEAV EQYSLWPAVG NQWQLEALLI RHWKKTVKVW LKMDSGMHRT GFFPHDYASA YAALKQSEYV DSIVKFSHFS CADEPESGMT EIQMEAFDLG TEGLEGEESL ANSAAILNVP EARRDWGRAG LALYGISPFG GGDDRLKPVM RLSTRIFGER VLQPHSPIGY GATFYTSKST RVGLIACGYA DGYPRRAPSN SPVAVDGKLT RVIGRVSMDM MTIELDASQE GLGHEVELWG DTVNINTVAE AAGTIPYELM CNIKRAKFTY IE // ID ANMK_NEIMB Reviewed; 367 AA. AC Q9K118; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 2. DT 13-APR-2016, entry version 77. DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270}; DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270}; DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270}; GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; GN OrderedLocusNames=NMB0377; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N- CC acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of CC the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the CC utilization of anhMurNAc either imported from the medium or CC derived from its own cell wall murein, and thus plays a role in CC cell wall recycling. {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- CATALYTIC ACTIVITY: ATP + 1,6-anhydro-N-acetyl-beta-muramate + CC H(2)O = ADP + N-acetylmuramate 6-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01270}. CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate CC degradation. {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase CC family. {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40817.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40817.1; ALT_INIT; Genomic_DNA. DR PIR; E81207; E81207. DR RefSeq; NP_273426.1; NC_003112.2. DR ProteinModelPortal; Q9K118; -. DR STRING; 122586.NMB0377; -. DR PaxDb; Q9K118; -. DR EnsemblBacteria; AAF40817; AAF40817; NMB0377. DR GeneID; 902492; -. DR KEGG; nme:NMB0377; -. DR PATRIC; 20355913; VBINeiMen85645_0474. DR eggNOG; ENOG4105ED7; Bacteria. DR eggNOG; COG2377; LUCA. DR HOGENOM; HOG000256309; -. DR KO; K09001; -. DR OMA; GCHGQTI; -. DR OrthoDB; EOG64N9WW; -. DR BioCyc; NMEN122586:GHGG-399-MONOMER; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006040; P:amino sugar metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01270; AnhMurNAc_kinase; 1. DR InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase. DR Pfam; PF03702; UPF0075; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 367 Anhydro-N-acetylmuramic acid kinase. FT /FTId=PRO_0000250015. FT NP_BIND 13 20 ATP. {ECO:0000255|HAMAP-Rule:MF_01270}. SQ SEQUENCE 367 AA; 39986 MW; 4C397A27DCCDC53B CRC64; MMETQLYIGI MSGTSMDGAD AVLIRMDGGK WLGAEGHAFT PYPGRLRRQL LDLQDTGADE LHRSRILSQE LSRLYAQTAA ELLCSQNLAP SDITALGCHG QTVRHAPEHG YSIQLADLPL LAERTRIFTV GDFRSRDLAA GGQGAPLVPA FHEALFRDNR ETRAVLNIGG IANISVLPPD APAFGFDTGP GNMLMDAWTQ AHWQLPYDKN GAKAAQGNIL PQLLDRLLAH PYFAQPHPKS TGRELFALNW LETYLDGGEN RYDVLRTLSR FTAQTVCDAV SHAAADARQM YICGGGIRNP VLMADLAECF GTRVSLHSTA DLNLDPQWVE AAAFAWLAAC WINRIPGSPH KATGASKPCI LGAGYYY // ID AMIC_NEIMB Reviewed; 416 AA. AC Q9K0V3; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiC; DE EC=3.5.1.28; DE Flags: Precursor; GN Name=amiC; OrderedLocusNames=NMB0456; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during CC cell division. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl CC residues and L-amino acid residues in certain cell-wall CC glycopeptides. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40893.1; -; Genomic_DNA. DR PIR; B81198; B81198. DR RefSeq; NP_273503.1; NC_003112.2. DR RefSeq; WP_002224939.1; NC_003112.2. DR ProteinModelPortal; Q9K0V3; -. DR STRING; 122586.NMB0456; -. DR PaxDb; Q9K0V3; -. DR DNASU; 902572; -. DR EnsemblBacteria; AAF40893; AAF40893; NMB0456. DR GeneID; 902572; -. DR KEGG; nme:NMB0456; -. DR PATRIC; 20356126; VBINeiMen85645_0579. DR eggNOG; ENOG4105C5C; Bacteria. DR eggNOG; COG0860; LUCA. DR HOGENOM; HOG000263827; -. DR KO; K01448; -. DR OMA; KRYFAAN; -. DR OrthoDB; EOG6CP3X3; -. DR BioCyc; NMEN122586:GHGG-480-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.40.630.40; -; 2. DR InterPro; IPR021731; AMIN_dom. DR InterPro; IPR002508; CW_Hdrlase/autolysin_cat. DR Pfam; PF01520; Amidase_3; 1. DR Pfam; PF11741; AMIN; 1. DR SMART; SM00646; Ami_3; 1. PE 1: Evidence at protein level; KW Cell wall biogenesis/degradation; Complete proteome; Hydrolase; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 416 N-acetylmuramoyl-L-alanine amidase AmiC. FT /FTId=PRO_0000320265. SQ SEQUENCE 416 AA; 45190 MW; 5E89E0A60DE8AD21 CRC64; MIKLTRRQII RRTAGTLFAL SPIASAVAKT VRAPQFTAAR IWPSHTYTRL TLESTAALKY QHFTLDNPGR LVVDIQNANI NTVLHGLSQK VMADDPFIRS IRAGQNTPTT VRLVIDLKQP THAQVFALPP VGGFKNRLVV DLYPHGMDAD DPMMALLNGS LNKTLRGSPE ADLAQNTTPQ PGRGRNGRRP VIMLDPGHGG EDPGAISPGG LQEKHVVLSI ARETKNQLEA LGYNVFMTRN EDVFIPLGVR VAKGRARRAD VFVSIHADAF TSPSARGTGV YMLNTKGATS SAAKFLEQTQ NNADAVGGVP TSGNRNVDTA LLDMTQTATL RDSRKLGKLV LEELGRLNHL HKGRVDEANF AVLRAPDMPS ILVETAFLSN PAEEKLLGSE SFRRQCAQSI ASGVQRYINT SVLKRG // ID ANIA_NEIMB Reviewed; 390 AA. AC Q9JYE1; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Copper-containing nitrite reductase; DE EC=1.7.2.1; DE Flags: Precursor; GN Name=aniA; OrderedLocusNames=NMB1623; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION. RC STRAIN=MC58; RX PubMed=12003939; DOI=10.1128/JB.184.11.2987-2993.2002; RA Anjum M.F., Stevanin T.M., Read R.C., Moir J.W.B.; RT "Nitric oxide metabolism in Neisseria meningitidis."; RL J. Bacteriol. 184:2987-2993(2002). CC -!- FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO). CC It could be essential for growth and survival in oxygen-depleted CC environments. {ECO:0000269|PubMed:12003939}. CC -!- CATALYTIC ACTIVITY: Nitric oxide + H(2)O + ferricytochrome c = CC nitrite + ferrocytochrome c + 2 H(+). CC -!- COFACTOR: CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000250}; CC Note=Binds 1 Cu(+) ion. {ECO:0000250}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; CC Note=Binds 1 Cu(2+) ion. {ECO:0000250}; CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 plastocyanin-like domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41975.1; -; Genomic_DNA. DR PIR; E81062; E81062. DR RefSeq; NP_274629.1; NC_003112.2. DR RefSeq; WP_002225006.1; NC_003112.2. DR ProteinModelPortal; Q9JYE1; -. DR SMR; Q9JYE1; 53-354. DR STRING; 122586.NMB1623; -. DR PaxDb; Q9JYE1; -. DR EnsemblBacteria; AAF41975; AAF41975; NMB1623. DR GeneID; 904036; -. DR KEGG; nme:NMB1623; -. DR PATRIC; 20359146; VBINeiMen85645_2084. DR eggNOG; ENOG4105CEI; Bacteria. DR eggNOG; COG2132; LUCA. DR HOGENOM; HOG000217143; -. DR KO; K00368; -. DR OMA; MPISEGV; -. DR OrthoDB; EOG61ZTJ4; -. DR BioCyc; NMEN122586:GHGG-1672-MONOMER; -. DR BRENDA; 1.7.2.1; 3593. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.420; -; 2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR001287; NO2-reductase_Cu. DR Pfam; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; SSF49503; 2. DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Copper; Lipoprotein; Membrane; KW Metal-binding; Oxidoreductase; Palmitate; Reference proteome; Repeat; KW Signal. FT SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 19 390 Copper-containing nitrite reductase. FT /FTId=PRO_0000002999. FT DOMAIN 101 195 Plastocyanin-like 1. FT DOMAIN 245 346 Plastocyanin-like 2. FT REPEAT 371 375 1. FT REPEAT 376 380 2. FT REPEAT 381 385 3. FT REGION 371 385 3 X 5 AA tandem repeats of A-A-S-A-P. FT METAL 134 134 Copper 1; type 1. {ECO:0000250}. FT METAL 139 139 Copper 2; type 2. {ECO:0000250}. FT METAL 174 174 Copper 2; type 2. {ECO:0000250}. FT METAL 175 175 Copper 1; type 1. {ECO:0000250}. FT METAL 183 183 Copper 1; type 1. {ECO:0000250}. FT METAL 188 188 Copper 1; type 1. {ECO:0000250}. FT METAL 329 329 Copper 2; type 2. {ECO:0000250}. FT BINDING 139 139 Substrate. {ECO:0000250}. FT BINDING 280 280 Substrate. {ECO:0000250}. FT LIPID 19 19 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 19 19 S-diacylglycerol cysteine. {ECO:0000305}. SQ SEQUENCE 390 AA; 40763 MW; C503F9D47DD1169D CRC64; MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP SGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGAI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD TAYAGNGAAP AASAPAASAP AASASEKSVY // ID ARGJ_NEIMB Reviewed; 406 AA. AC P63574; Q9JRJ2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 82. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106}; GN Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106}; GN OrderedLocusNames=NMB2005; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes two activities which are involved in the CC cyclic version of arginine biosynthesis: the synthesis of N- CC acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, CC and of ornithine by transacetylation between N(2)-acetylornithine CC and glutamate. {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)- CC acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e. CC capable of catalyzing only the fifth step of the arginine CC biosynthetic pathway. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42332.1; -; Genomic_DNA. DR PIR; C81017; C81017. DR RefSeq; NP_274997.1; NC_003112.2. DR RefSeq; WP_002235259.1; NC_003112.2. DR ProteinModelPortal; P63574; -. DR STRING; 122586.NMB2005; -. DR MEROPS; T05.001; -. DR PaxDb; P63574; -. DR EnsemblBacteria; AAF42332; AAF42332; NMB2005. DR GeneID; 904115; -. DR KEGG; nme:NMB2005; -. DR PATRIC; 20360109; VBINeiMen85645_2559. DR eggNOG; ENOG4105C5V; Bacteria. DR eggNOG; COG1364; LUCA. DR HOGENOM; HOG000022798; -. DR KO; K00620; -. DR OMA; WTCDLTH; -. DR OrthoDB; EOG6P8TQQ; -. DR BioCyc; NMEN122586:GHGG-2062-MONOMER; -. DR UniPathway; UPA00068; UER00106. DR UniPathway; UPA00068; UER00111. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.70.12; -; 1. DR HAMAP; MF_01106; ArgJ; 1. DR InterPro; IPR002813; Arg_biosynth_ArgJ. DR InterPro; IPR016117; ArgJ-like_dom. DR PANTHER; PTHR23100; PTHR23100; 1. DR Pfam; PF01960; ArgJ; 1. DR SUPFAM; SSF56266; SSF56266; 1. DR TIGRFAMs; TIGR00120; ArgJ; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; KW Autocatalytic cleavage; Complete proteome; Cytoplasm; KW Multifunctional enzyme; Reference proteome; Transferase. FT CHAIN 1 189 Arginine biosynthesis bifunctional FT protein ArgJ alpha chain. FT {ECO:0000255|HAMAP-Rule:MF_01106}. FT /FTId=PRO_0000002201. FT CHAIN 190 406 Arginine biosynthesis bifunctional FT protein ArgJ beta chain. FT {ECO:0000255|HAMAP-Rule:MF_01106}. FT /FTId=PRO_0000002202. FT ACT_SITE 190 190 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 152 152 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 179 179 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 190 190 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 277 277 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 401 401 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 406 406 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 119 119 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 120 120 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 189 190 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_01106}. SQ SEQUENCE 406 AA; 42812 MW; 0915D50CE69CA656 CRC64; MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVLPFSTG VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDKH TVRATGIAKG SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTRDEARQAA YAVARSPLVK TAFFASDPNL GRLLAAIGYA GVADLDTDLV EMYLDDILVA EHGGRAASYT EAQGQAVMSK AEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS // ID ARGC_NEIMB Reviewed; 347 AA. AC Q9JY18; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150}; DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150}; DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150}; DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150}; DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150}; GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150}; GN OrderedLocusNames=NMB1787; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00150}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00150}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}. CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42126.1; -; Genomic_DNA. DR PIR; D81043; D81043. DR RefSeq; NP_274786.1; NC_003112.2. DR RefSeq; WP_002225637.1; NC_003112.2. DR ProteinModelPortal; Q9JY18; -. DR STRING; 122586.NMB1787; -. DR PaxDb; Q9JY18; -. DR EnsemblBacteria; AAF42126; AAF42126; NMB1787. DR GeneID; 903312; -. DR KEGG; nme:NMB1787; -. DR PATRIC; 20359537; VBINeiMen85645_2274. DR eggNOG; ENOG4105C0N; Bacteria. DR eggNOG; COG0002; LUCA. DR HOGENOM; HOG000254904; -. DR KO; K00145; -. DR OMA; TFVPHLT; -. DR OrthoDB; EOG6XSZS3; -. DR BioCyc; NMEN122586:GHGG-1842-MONOMER; -. DR UniPathway; UPA00068; UER00108. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00150; ArgC_type1; 1. DR InterPro; IPR023013; AGPR_AS. DR InterPro; IPR000706; AGPR_type-1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01850; argC; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 347 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112428. FT ACT_SITE 152 152 {ECO:0000255|HAMAP-Rule:MF_00150}. SQ SEQUENCE 347 AA; 37214 MW; A927C570DE19ECD1 CRC64; MSKKIKVGIV GATGYTGVEL LRLLAAHPDV EVAAVTSRSE AGTAVADYFP SLRGVYGLAF QTPDEAGLEQ CDIVFFATPN GIAMKDAPRL IEQGVRVIDL SADFRIRDIP TWEHWYGMTH AAPDLVSQAV YGLSELNREA VAQARLVANP GCYPTCVSLP LVPLLRQCRL KPGMPLIADC KSGVSGAGRK GNVGSLLCEA GDNFKAYGIA GHRHLPEIRQ TIAGLQDGIA EGFVFTPHLA PMIRGMHATV YLHLSDGSDP ETVLRDYYRD SPFVDILPTG SAPETRSVRG ANLCRISIQQ AAQSDVWVVL SVIDNLVKGA AGQAVQNMNI MFGLEETHGL DAIPLLP // ID AROA_NEIMB Reviewed; 433 AA. AC Q9JYU1; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210}; DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210}; GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; GN OrderedLocusNames=NMB1432; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- CC phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and CC inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00210}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41793.1; -; Genomic_DNA. DR PIR; A81085; A81085. DR RefSeq; NP_274444.1; NC_003112.2. DR RefSeq; WP_002225114.1; NC_003112.2. DR ProteinModelPortal; Q9JYU1; -. DR STRING; 122586.NMB1432; -. DR PaxDb; Q9JYU1; -. DR EnsemblBacteria; AAF41793; AAF41793; NMB1432. DR GeneID; 903854; -. DR KEGG; nme:NMB1432; -. DR PATRIC; 20358577; VBINeiMen85645_1800. DR eggNOG; ENOG4105CMY; Bacteria. DR eggNOG; COG0128; LUCA. DR HOGENOM; HOG000247372; -. DR KO; K00800; -. DR OMA; IGRNSVQ; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NMEN122586:GHGG-1470-MONOMER; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00210; EPSP_synth; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 433 3-phosphoshikimate 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000088275. FT REGION 23 24 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT REGION 93 96 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT REGION 170 172 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT ACT_SITE 317 317 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT ACT_SITE 345 345 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 28 28 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 123 123 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 198 198 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 344 344 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 348 348 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 391 391 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 416 416 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. SQ SEQUENCE 433 AA; 47060 MW; 5AB429C874721370 CRC64; MTESVRLPVA RLKPSTVALP GSKSISNRTL LLAALSDNAC EIHSLLKSDD TDRMLEALDK LGVQIEYLAE DRLKVHGTGG RFPNRTADLF LGNAGTAFRP LTAALAVLGG DYHLHGVPRM HERPIGDLVD ALRIAGADVE YLGKEHYPPL HIGERQDNGE RVIPIKGNVS SQFLTALLMA LPLTGQAFEI RMVGELISKP YIDITLKLMA QFGVQVINEG YRVFKIPADA HYHAPEHLHV EGDASSASYF LAAGLIAATP VRVTGIGANS IQGDVAFARE LEKIGADVVW GENFVEVSRP KERAVQSFDL DANHIPDAAM TLAIVALATG QTCTLRNIGS WRVKETDRIA AMANELRKLG AKVVEEAEAI HITPPETLTP DAVIDTYDDH RMAMCFSLVS LLGVPVVIND PKCTHKTFPT YFDVFSSLTE TAE // ID ARGB_NEIMB Reviewed; 298 AA. AC Q9JZF7; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082}; DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082}; DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082}; DE AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082}; DE Short=AGK {ECO:0000255|HAMAP-Rule:MF_00082}; GN Name=argB {ECO:0000255|HAMAP-Rule:MF_00082}; GN OrderedLocusNames=NMB1074; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- CC glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00082}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP- CC Rule:MF_00082}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00082}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41469.1; -; Genomic_DNA. DR PIR; E81124; E81124. DR RefSeq; NP_274107.1; NC_003112.2. DR RefSeq; WP_002217262.1; NC_003112.2. DR ProteinModelPortal; Q9JZF7; -. DR SMR; Q9JZF7; 9-291. DR STRING; 122586.NMB1074; -. DR PaxDb; Q9JZF7; -. DR EnsemblBacteria; AAF41469; AAF41469; NMB1074. DR GeneID; 903493; -. DR KEGG; nme:NMB1074; -. DR PATRIC; 20357697; VBINeiMen85645_1365. DR eggNOG; ENOG4105CAS; Bacteria. DR eggNOG; COG0548; LUCA. DR HOGENOM; HOG000233259; -. DR KO; K00930; -. DR OMA; PKTECCI; -. DR OrthoDB; EOG6T1WVF; -. DR BioCyc; NMEN122586:GHGG-1111-MONOMER; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00082_B; ArgB_B; 1. DR InterPro; IPR004662; AcgluKinase. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00761; argB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 298 Acetylglutamate kinase. FT /FTId=PRO_0000112639. FT REGION 69 70 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00082}. FT BINDING 91 91 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00082}. FT BINDING 191 191 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00082}. FT SITE 34 34 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00082}. FT SITE 251 251 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00082}. SQ SEQUENCE 298 AA; 31283 MW; 7A19DFE8D5BA1A74 CRC64; MESENIISAA DKARILAEAL PYIRRFSGSV AVIKYGGNAM TEPALKEGFA RDVVLLKLVG IHPVIVHGGG PQINAMLEKV GKKGEFVQGM RVTDKEAMDI VEMVLGGHVN KEIVSMINTY GGHAVGVSGR DDHFIKAKKL LIDTPEQNGV DIGQVGTVES IDTGLVKGLI ERGCIPVVAP VGVGEKGEAF NINADLVAGK LAEELNAEKL LMMTNIAGVM DKTGNLLTKL TPKRIDELIA DGTLYGGMLP KIASAVEAAV NGVKATHIID GRLPNALLLE IFTDAGIGSM ILGGGEDA // ID AROC_NEIMB Reviewed; 366 AA. AC Q9JY99; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; GN OrderedLocusNames=NMB1680; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42028.1; -; Genomic_DNA. DR PIR; B81055; B81055. DR RefSeq; NP_274684.1; NC_003112.2. DR RefSeq; WP_002224985.1; NC_003112.2. DR ProteinModelPortal; Q9JY99; -. DR STRING; 122586.NMB1680; -. DR PaxDb; Q9JY99; -. DR EnsemblBacteria; AAF42028; AAF42028; NMB1680. DR GeneID; 903428; -. DR KEGG; nme:NMB1680; -. DR PATRIC; 20359311; VBINeiMen85645_2162. DR eggNOG; ENOG4105D10; Bacteria. DR eggNOG; COG0082; LUCA. DR HOGENOM; HOG000060335; -. DR KO; K01736; -. DR OMA; MLSINAV; -. DR OrthoDB; EOG6WDSHT; -. DR BioCyc; NMEN122586:GHGG-1735-MONOMER; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP; KW Reference proteome. FT CHAIN 1 366 Chorismate synthase. FT /FTId=PRO_0000140618. FT NP_BIND 125 127 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 238 239 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 293 297 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 48 48 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 54 54 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 278 278 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 319 319 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. SQ SEQUENCE 366 AA; 39448 MW; FDB7BE6CEA789D47 CRC64; MAGNTFGQLF TVTTFGESHG AGLGCIIDGC PPGLELSEAD IQFDLDRRKP GTSRHVTQRR EADQVEILSG VFEGKTTGTP IALLIRNTDQ RSKDYGNIAT SFRPGHADYT YWHKYGTRDY RGGGRSSARE TAARVAAGAV AKKWLKEKFG TEITAYVTQV GEKEIRFEGC EHISQNPFFA ANHSQIAELE NYMDSVRKSL DSVGAKLHIE AANVPVGLGE PVFDRLDAEI AYAMMGINAV KGVEIGAGFD SVTQRGSEHG DELTPQGFLS NHSGGILGGI STGQDIRVNI AIKPTSSIAT PRRSIDINGN PIELATHGRH DPCVGLRSAP IAEAMLALVL IDHALRHRAQ NADVQVNTPD ITLSNK // ID AROB_NEIMB Reviewed; 359 AA. AC Q9JY01; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110}; GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; GN OrderedLocusNames=NMB1814; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110}; CC Note=Binds 1 divalent metal cation per subunit. Can use either CC Co(2+) or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}. CC -!- SIMILARITY: Belongs to the dehydroquinate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00110}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42149.1; -; Genomic_DNA. DR PIR; G81038; G81038. DR RefSeq; NP_274811.1; NC_003112.2. DR RefSeq; WP_002221481.1; NC_003112.2. DR ProteinModelPortal; Q9JY01; -. DR STRING; 122586.NMB1814; -. DR PaxDb; Q9JY01; -. DR EnsemblBacteria; AAF42149; AAF42149; NMB1814. DR GeneID; 903286; -. DR KEGG; nme:NMB1814; -. DR PATRIC; 20359605; VBINeiMen85645_2308. DR eggNOG; ENOG4105D49; Bacteria. DR eggNOG; COG0337; LUCA. DR HOGENOM; HOG000007970; -. DR KO; K01735; -. DR OMA; IERSCAA; -. DR OrthoDB; EOG6SJJGD; -. DR BioCyc; NMEN122586:GHGG-1869-MONOMER; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00110; DHQ_synthase; 1. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030963; DHQ_synth_fam. DR InterPro; IPR030960; DHQS/DOIS. DR Pfam; PF01761; DHQ_synthase; 1. DR PIRSF; PIRSF001455; DHQ_synth; 1. DR TIGRFAMs; TIGR01357; aroB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt; KW Complete proteome; Cytoplasm; Lyase; NAD; Reference proteome; Zinc. FT CHAIN 1 359 3-dehydroquinate synthase. FT /FTId=PRO_0000140760. SQ SEQUENCE 359 AA; 38745 MW; E9D2B7B679BDD498 CRC64; MKTLTVHTPS HSYPIFIGNG LLPQAGSLLK PHLGKRAAII ANETVAPLYL GTLQTALDAA GVSHFSIILP DGEAHKNWQT LNLIFDGLMQ NRAERKTTLI ALGGGVIGDM VGFAAATYQR GAPFVQIPTT LLSQVDSSVG GKTAINHPLG KNMIGAFYQP QAVLADLDTL HTLPARELSA GMAEVIKYGA LGDIGFFEWL EQHMPELMTL DREKLAQAVY RCCQMKADIV AQDETEQGIR AWLNLGHTFG HAIETEMGYG TWLHGEAIAA GCVLAARLSE QLGKTSAADT ARLAALLEAA GLPSAPPVFA FEKWLEHMSH DKKVSGGIMR FIGLNRLGEA NITEITDTDI LRRTLQPYL // ID AROE_NEIMB Reviewed; 269 AA. AC P56992; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 09-DEC-2015, entry version 101. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; GN OrderedLocusNames=NMB0358; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which CC leads to the biosynthesis of aromatic amino acids. Catalyzes the CC reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to CC yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00222}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40801.1; -; Genomic_DNA. DR PIR; E81208; E81208. DR RefSeq; NP_273407.1; NC_003112.2. DR RefSeq; WP_002224888.1; NC_003112.2. DR ProteinModelPortal; P56992; -. DR SMR; P56992; 5-267. DR STRING; 122586.NMB0358; -. DR PaxDb; P56992; -. DR EnsemblBacteria; AAF40801; AAF40801; NMB0358. DR GeneID; 902474; -. DR KEGG; nme:NMB0358; -. DR PATRIC; 20355869; VBINeiMen85645_0452. DR eggNOG; ENOG4105E2X; Bacteria. DR eggNOG; COG0169; LUCA. DR HOGENOM; HOG000237876; -. DR KO; K00014; -. DR OMA; FGNPIKH; -. DR OrthoDB; EOG6RRKMV; -. DR BioCyc; NMEN122586:GHGG-380-MONOMER; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR011342; Shikimate_DH. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00507; aroE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 269 Shikimate dehydrogenase (NADP(+)). FT /FTId=PRO_0000136020. FT NP_BIND 130 134 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT NP_BIND 154 159 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT REGION 17 19 Shikimate binding. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT ACT_SITE 68 68 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 64 64 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 80 80 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT BINDING 89 89 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 105 105 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 213 213 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT BINDING 215 215 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 237 237 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. SQ SEQUENCE 269 AA; 28565 MW; 216EA766C30BA66B CRC64; MTALPRYAVF GNPVAHSKSP QIHQQFALQE GVDIEYERIC ADIGGFAQAV STFFETGGCG ANVTVPFKQE AFHLADEHSE RALAAGAVNT LIPLKNGKLR GDNTDGIGLT NDITQVKNIA IEGKTILLLG AGGAVRGVIP VLKEHRPARI VIANRTRAKA EELAQLFGIE AVPMADVNGG FDIIINGTSG GLNGQIPDIP PDIFQNCALA YDMVYGCAAK PFLDFARQSG AKKTADGLGM LVGQAAASYA LWRGFTPDIR PVIEYMKAL // ID AROK_NEIMB Reviewed; 170 AA. AC P63600; Q9JQV1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Putative shikimate kinase; DE Short=SK {ECO:0000255|HAMAP-Rule:MF_00109}; DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00109}; GN Name=aroK {ECO:0000255|HAMAP-Rule:MF_00109}; GN OrderedLocusNames=NMB1813; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00109}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42148.1; -; Genomic_DNA. DR PIR; F81038; F81038. DR RefSeq; NP_274810.1; NC_003112.2. DR RefSeq; WP_002222978.1; NC_003112.2. DR ProteinModelPortal; P63600; -. DR STRING; 122586.NMB1813; -. DR PaxDb; P63600; -. DR PRIDE; P63600; -. DR EnsemblBacteria; AAF42148; AAF42148; NMB1813. DR GeneID; 903287; -. DR KEGG; nme:NMB1813; -. DR PATRIC; 20359603; VBINeiMen85645_2307. DR eggNOG; ENOG4105KHV; Bacteria. DR eggNOG; COG0703; LUCA. DR HOGENOM; HOG000032568; -. DR KO; K00891; -. DR OMA; LYRECAD; -. DR OrthoDB; EOG6SJJGD; -. DR BioCyc; NMEN122586:GHGG-1868-MONOMER; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 170 Putative shikimate kinase. FT /FTId=PRO_0000192396. FT NP_BIND 15 20 ATP. {ECO:0000255|HAMAP-Rule:MF_00109}. FT METAL 19 19 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 37 37 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 61 61 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 83 83 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00109}. FT BINDING 121 121 ATP. {ECO:0000255|HAMAP-Rule:MF_00109}. FT BINDING 140 140 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. SQ SEQUENCE 170 AA; 18980 MW; BAA6F8A2EBF9B9A5 CRC64; MKNFNGKLIL IGLMGAGKTT LGRQMAQRLD YRFYDSDHEI AAAAGVPIPT IFEMEGEQGF RSRETAILKK LVILPHIVLS TGGGAVLKEE NRALIRKSGT VVYLHAPPET LLERTRCDNS RPLLQVADPL AKLRELYAAR DPVYRQTADF TVESANCRET VQTLLKRLSR // ID APT_NEIMB Reviewed; 188 AA. AC Q9JYB4; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=NMB1662; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42011.1; -; Genomic_DNA. DR PIR; H81055; H81055. DR RefSeq; NP_274667.1; NC_003112.2. DR RefSeq; WP_002224990.1; NC_003112.2. DR ProteinModelPortal; Q9JYB4; -. DR STRING; 122586.NMB1662; -. DR PaxDb; Q9JYB4; -. DR EnsemblBacteria; AAF42011; AAF42011; NMB1662. DR GeneID; 903448; -. DR KEGG; nme:NMB1662; -. DR PATRIC; 20359262; VBINeiMen85645_2139. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; NMEN122586:GHGG-1716-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149422. SQ SEQUENCE 188 AA; 20443 MW; EF32F7CB7980AF4D CRC64; MLVHPEAMSV GALADKIRKI ENWPQKGILF HDITPVLQSA EYFRLLVDLL VYRYMDQKID IVAGLDARGF IIGAALAYQL NVGFVPIRKK GKLPFETVSQ SYALEYGEAA VEIHTDAVKL GSRVLLVDDL IATGGTMLAG LELIRKLGGE IVEAAAILEF TDLQGGKNIR ASGAPLFTLL QNEGCMKG // ID ARLY_NEIMB Reviewed; 458 AA. AC Q9K0G8; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006}; DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006}; DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006}; DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006}; GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; GN OrderedLocusNames=NMB0637; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate + CC L-arginine. {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 3/3. CC {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41060.1; -; Genomic_DNA. DR PIR; B81175; B81175. DR RefSeq; NP_273680.1; NC_003112.2. DR RefSeq; WP_002225520.1; NC_003112.2. DR ProteinModelPortal; Q9K0G8; -. DR STRING; 122586.NMB0637; -. DR PaxDb; Q9K0G8; -. DR EnsemblBacteria; AAF41060; AAF41060; NMB0637. DR GeneID; 902748; -. DR KEGG; nme:NMB0637; -. DR PATRIC; 20356573; VBINeiMen85645_0806. DR eggNOG; ENOG4105CH7; Bacteria. DR eggNOG; COG0165; LUCA. DR HOGENOM; HOG000242744; -. DR KO; K01755; -. DR OMA; AHHLMAY; -. DR OrthoDB; EOG6P5ZF8; -. DR BioCyc; NMEN122586:GHGG-663-MONOMER; -. DR UniPathway; UPA00068; UER00114. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro. DR Gene3D; 1.10.275.10; -; 1. DR HAMAP; MF_00006; Arg_succ_lyase; 1. DR InterPro; IPR029419; Arg_succ_lyase_C. DR InterPro; IPR009049; Argininosuccinate_lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1. DR Pfam; PF14698; ASL_C2; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00838; argH; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Lyase; Reference proteome. FT CHAIN 1 458 Argininosuccinate lyase. FT /FTId=PRO_0000137795. SQ SEQUENCE 458 AA; 51244 MW; C8CE8BD2F0A29F4C CRC64; MHDKTWSGRF NEPVSELVKQ YTASIGFDRR LAEWDIQGSL AHAQMLKETG VLDEGDLADI RRGMAEILEE IRSGKIEWSS DLEDVHMNIE RRLTDKIGDA GKRLHTGRSR NDQVATDIRL WLRDQITVIQ SLIQSLQTAL LDLAEQNAET VMPGFTHLQV AQPVSFGHHM LAYVEMLGRD NERMADCRCR VNRMPLGAAA LAGTTYPIQR EITAELLGFE QICQNSLDAV SDRDFAIEFT AAASLVMVHL SRLSEELILW MSPRFGFIDI ADRFCTGSSI MPQKKNPDVP ELVRGKSGRV IGHLIGLITL MKSQPLAYNK DNQEDKEPLF DTADTLIDTL RIYADMMRGV TVKPDNMRAA VMQGFATATD LADYLVKKGM PFRDAHEVVA QAVRHADQAG VDLSELPLEV LQGFSDLIAD DVYGVLTPEG SLNARNHLGG TAPEQVRFQV KRWREMLA // ID AROD_NEIMB Reviewed; 254 AA. AC Q9JYT0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214}; GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; GN OrderedLocusNames=NMB1446; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the third step of the chorismate pathway, CC which leads to the biosynthesis of aromatic amino acids. Catalyzes CC the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the CC first double bond of the aromatic ring to yield 3- CC dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family. CC {ECO:0000255|HAMAP-Rule:MF_00214}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41806.1; -; Genomic_DNA. DR PIR; G81082; G81082. DR RefSeq; NP_274458.1; NC_003112.2. DR RefSeq; WP_002239900.1; NC_003112.2. DR ProteinModelPortal; Q9JYT0; -. DR STRING; 122586.NMB1446; -. DR PaxDb; Q9JYT0; -. DR EnsemblBacteria; AAF41806; AAF41806; NMB1446. DR GeneID; 903866; -. DR KEGG; nme:NMB1446; -. DR PATRIC; 20358621; VBINeiMen85645_1822. DR eggNOG; ENOG4105FF2; Bacteria. DR eggNOG; COG0710; LUCA. DR HOGENOM; HOG000105514; -. DR KO; K03785; -. DR OMA; LFTFRSK; -. DR OrthoDB; EOG6P33BK; -. DR BioCyc; NMEN122586:GHGG-1484-MONOMER; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00214; AroD; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001381; DHquinase_I. DR Pfam; PF01487; DHquinase_I; 1. DR TIGRFAMs; TIGR01093; aroD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Schiff base. FT CHAIN 1 254 3-dehydroquinate dehydratase. FT /FTId=PRO_0000138803. FT REGION 47 49 3-dehydroquinate binding. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT ACT_SITE 144 144 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT ACT_SITE 171 171 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT BINDING 83 83 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 213 213 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 232 232 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 236 236 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. SQ SEQUENCE 254 AA; 27186 MW; A4936FB6FEFB4DC3 CRC64; MCSCLVVKNT VIGSGRTKIA VPLVARDAAE LSAVLEQIKN MPFDIAEFRA DFLECAGSIG EILHHTQTVR DALPDKPLLF TFRRHGEGGS FPCSDDYYFE LLDALIESRL PDIIDIELFS GETAVRCAVA NAQKNGIAAL LCNHEFHRTP PQEEIVCRLK QMEDCGADIC KIAVMPQSAE DVLTLLSATL KAKELAAKPI VTMSMGQTGA VSRLAGQVFG SSITFGSGTQ NSAPGQIGVS ALRATLDCLE NGAD // ID ARGA_NEIMB Reviewed; 436 AA. AC Q9JXU9; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Amino-acid acetyltransferase; DE EC=2.3.1.1; DE AltName: Full=N-acetylglutamate synthase; DE Short=AGS; DE Short=NAGS; GN Name=argA; OrderedLocusNames=NMB1876; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 1/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme CC ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), CC ArgA fulfills an anaplerotic role. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42210.1; -; Genomic_DNA. DR PIR; B81033; B81033. DR RefSeq; NP_274872.1; NC_003112.2. DR RefSeq; WP_002217983.1; NC_003112.2. DR ProteinModelPortal; Q9JXU9; -. DR SMR; Q9JXU9; 5-436. DR STRING; 122586.NMB1876; -. DR PaxDb; Q9JXU9; -. DR EnsemblBacteria; AAF42210; AAF42210; NMB1876. DR GeneID; 904312; -. DR KEGG; nme:NMB1876; -. DR PATRIC; 20359783; VBINeiMen85645_2397. DR eggNOG; ENOG4107R2T; Bacteria. DR eggNOG; COG0548; LUCA. DR eggNOG; COG1246; LUCA. DR HOGENOM; HOG000262225; -. DR KO; K14682; -. DR OMA; KQALYNY; -. DR OrthoDB; EOG6T1WVF; -. DR BioCyc; NMEN122586:GHGG-1932-MONOMER; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1160.10; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR HAMAP; MF_01105; N_acetyl_glu_synth; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR010167; NH2A_AcTrfase_ArgA. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR PIRSF; PIRSF000423; ArgA; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 436 Amino-acid acetyltransferase. FT /FTId=PRO_0000186795. FT DOMAIN 287 436 N-acetyltransferase. SQ SEQUENCE 436 AA; 47299 MW; 1D3854A524544050 CRC64; MSAPDLFVAH FREAVPYIRQ MRGKTLVAGI DDRLLEGDTL NKLAADIGLL SQLGIRLVLI HGARHFLDRH AAAQGRTPHY CRGLRVTDET SLEQAQQFAG TVRSRFEAAL CGSVSGFARA PSVPLVSGNF LTARPIGVID GTDMEYAGVI RKTDTAALRF QLDAGNIVWL PPLGHSYSGK TFYLDMLQTA ASAAVSLQAE KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAGGETRR LISSAVAALE GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI AALIRPLEEQ GILLHRSREY LENHISEFSI LEHDGNLYGC AALKTFAEAD CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA ERGFQTASED ELPETRRKDY RSNGRNSHIL VRRLHR // ID ARGD_NEIMB Reviewed; 398 AA. AC Q9JYY4; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107}; DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; GN OrderedLocusNames=NMB1371; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01107}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP- CC Rule:MF_01107}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41745.1; -; Genomic_DNA. DR PIR; H81090; H81090. DR RefSeq; NP_274389.1; NC_003112.2. DR RefSeq; WP_002222328.1; NC_003112.2. DR ProteinModelPortal; Q9JYY4; -. DR SMR; Q9JYY4; 2-393. DR STRING; 122586.NMB1371; -. DR PaxDb; Q9JYY4; -. DR EnsemblBacteria; AAF41745; AAF41745; NMB1371. DR GeneID; 903793; -. DR KEGG; nme:NMB1371; -. DR PATRIC; 20358413; VBINeiMen85645_1718. DR eggNOG; ENOG4105C8Y; Bacteria. DR eggNOG; COG4992; LUCA. DR HOGENOM; HOG000020206; -. DR KO; K00821; -. DR OMA; LQVSKRP; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NMEN122586:GHGG-1409-MONOMER; -. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03246; arg_catab_astC; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; KW Complete proteome; Cytoplasm; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 398 Acetylornithine aminotransferase. FT /FTId=PRO_0000112760. FT REGION 214 217 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 129 129 Pyridoxal phosphate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 132 132 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 271 271 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 272 272 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01107}. FT MOD_RES 243 243 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. SQ SEQUENCE 398 AA; 42815 MW; 41C4592BFD1DA04D CRC64; MQNYLTPNFA FAPMIPERAS GSRVWDTKGR EYIDFSGGIA VNALGHCHPA LVDALNAQMH KLWHISNIYT TRPAQELAQK LVANSFADKV FFCNSGSEAN EAALKLARKY ARDRFGGGKS EIVACINSFH GRTLFTVSVG GQPKYSKDYA PLPQGITHVP FNDIAALEAA VGEQTCAVII EPIQGESGIL PATAEYLQTA RRLCDRHNAL LILDEVQTGM GHTGRLFAYE HYGIVPDILS SAKALGCGFP IGAMLATEKI AAAFQPGTHG STFGGNPMAC AVGSRAFDII NTPETLNHVR EQGQKLQTAL LDLCRKTGLF SQVRGMGLLL GCVLDEAYRG RASEITAAAL KHGVMILVAG ADVLRFAPSL LLNDEDMAEG LRRLEHALTE FAATSDNP // ID ASSY_NEIMB Reviewed; 447 AA. AC Q9JXC1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=NMB2129; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 2 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42437.1; -; Genomic_DNA. DR PIR; B81003; B81003. DR RefSeq; NP_275114.1; NC_003112.2. DR RefSeq; WP_002223213.1; NC_003112.2. DR ProteinModelPortal; Q9JXC1; -. DR SMR; Q9JXC1; 6-445. DR STRING; 122586.NMB2129; -. DR PaxDb; Q9JXC1; -. DR EnsemblBacteria; AAF42437; AAF42437; NMB2129. DR GeneID; 903396; -. DR KEGG; nme:NMB2129; -. DR PATRIC; 20360434; VBINeiMen85645_2713. DR eggNOG; ENOG4105CDH; Bacteria. DR eggNOG; COG0137; LUCA. DR HOGENOM; HOG000230094; -. DR KO; K01940; -. DR OMA; AFHIRSG; -. DR OrthoDB; EOG6K9QCV; -. DR BioCyc; NMEN122586:GHGG-2194-MONOMER; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.400; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00581; Arg_succ_synth_type2; 1. DR InterPro; IPR023437; Arg_succ_synth_type2_subfam. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR024073; AS_multimer_C_tail. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00764; Arginosuc_synth; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 447 Argininosuccinate synthase. FT /FTId=PRO_0000148702. FT NP_BIND 20 28 ATP. {ECO:0000250}. FT BINDING 46 46 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 102 102 Citrulline. {ECO:0000250}. FT BINDING 132 132 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 134 134 Aspartate. {ECO:0000250}. FT BINDING 134 134 ATP. {ECO:0000250}. FT BINDING 138 138 Aspartate. {ECO:0000250}. FT BINDING 138 138 Citrulline. {ECO:0000250}. FT BINDING 139 139 Aspartate. {ECO:0000250}. FT BINDING 139 139 ATP. {ECO:0000250}. FT BINDING 142 142 Citrulline. {ECO:0000250}. FT BINDING 195 195 Citrulline. {ECO:0000250}. FT BINDING 197 197 ATP. {ECO:0000250}. FT BINDING 204 204 Citrulline. {ECO:0000250}. FT BINDING 206 206 Citrulline. {ECO:0000250}. FT BINDING 283 283 Citrulline. {ECO:0000250}. SQ SEQUENCE 447 AA; 49664 MW; 8A11C502DB4C0506 CRC64; MSQNHTILQS LPVGQKVGIA FSGGLDTSAA LLWMKLKGAL PYAYTANLGQ PDEDDYNAIP KKAMEYGAEN ARLIDCRAQL AHEGIAAIQC GAFHVSTGGI AYFNTTPLGR AVTGTMLVSA MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT NPALKIYKPW LDQQFIDELG GRHEMSEFLI ANGFNYKMSV EKAYSTDSNM LGATHEAKDL EFLNSGIKIV KPIMGVAFWD ENVEVSPEEV SVRFEEGVPV ALNGKEYADP VELFLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM ALFHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET AQRWVAKAVT GEVTLELRRG NDYSILNTES PNLTYQPERL SMEKVEDAAF TPLDRIGQLT MRNLDITDTR VKLGIYSQSG LLSLGEGSVL PQLGNKQ // ID ARSC_NEIMB Reviewed; 117 AA. AC P63622; Q9JQU0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Putative arsenate reductase; DE EC=1.20.4.1; GN Name=arsC; OrderedLocusNames=NMB0005; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Reduction of arsenate [As(V)] to arsenite [As(III)]. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite + CC glutaredoxin disulfide + H(2)O. CC -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40484.1; -; Genomic_DNA. DR PIR; C81247; C81247. DR RefSeq; NP_273071.1; NC_003112.2. DR RefSeq; WP_002225750.1; NC_003112.2. DR ProteinModelPortal; P63622; -. DR STRING; 122586.NMB0005; -. DR PaxDb; P63622; -. DR EnsemblBacteria; AAF40484; AAF40484; NMB0005. DR GeneID; 902107; -. DR KEGG; nme:NMB0005; -. DR PATRIC; 20354937; VBINeiMen85645_0005. DR eggNOG; ENOG4105K89; Bacteria. DR eggNOG; COG1393; LUCA. DR HOGENOM; HOG000059717; -. DR KO; K00537; -. DR OMA; MIKIYHN; -. DR OrthoDB; EOG6PP9QC; -. DR BioCyc; NMEN122586:GHGG-5-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR006659; Arsenate_reductase. DR InterPro; IPR006660; Arsenate_reductase-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF03960; ArsC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00014; arsC; 1. DR PROSITE; PS51353; ARSC; 1. PE 3: Inferred from homology; KW Arsenical resistance; Complete proteome; Oxidoreductase; KW Reference proteome. FT CHAIN 1 117 Putative arsenate reductase. FT /FTId=PRO_0000162542. SQ SEQUENCE 117 AA; 12869 MW; C834075A7941EBE5 CRC64; MPEIKIFHNP RCSKSRAALS LLEERGIAAE VVKYLDTPPD LSELKDIFNK LGLASARGMM RVKDDLYKEL GLDNPNLDND ALLRAIADHP ALLERPIVLA NGKAAVGRPL ENIEAVL // ID ATPA_NEIMB Reviewed; 515 AA. AC Q9JXQ0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; GN OrderedLocusNames=NMB1936; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01346}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42265.1; -; Genomic_DNA. DR PIR; A81025; A81025. DR RefSeq; NP_274930.1; NC_003112.2. DR RefSeq; WP_002225830.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ0; -. DR SMR; Q9JXQ0; 29-511. DR STRING; 122586.NMB1936; -. DR PaxDb; Q9JXQ0; -. DR PRIDE; Q9JXQ0; -. DR EnsemblBacteria; AAF42265; AAF42265; NMB1936. DR GeneID; 904216; -. DR KEGG; nme:NMB1936; -. DR PATRIC; 20359919; VBINeiMen85645_2464. DR eggNOG; ENOG4105CDG; Bacteria. DR eggNOG; COG0056; LUCA. DR HOGENOM; HOG000130111; -. DR KO; K02111; -. DR OMA; PVFCIYV; -. DR OrthoDB; EOG67X1S1; -. DR BioCyc; NMEN122586:GHGG-1993-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR005294; ATPase_F1-cplx_asu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15184:SF3; PTHR15184:SF3; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 515 ATP synthase subunit alpha. FT /FTId=PRO_0000238301. FT NP_BIND 169 176 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 373 373 Required for activity. FT {ECO:0000255|HAMAP-Rule:MF_01346}. SQ SEQUENCE 515 AA; 55291 MW; 259A0C328AACFC34 CRC64; MQLNPAEISD LIKAKIENLS VNAEVRTCGT VISVTDGIVR IHGLSDAMQG EMLEFPGNTF GLAMNLERDS VGAVVLGEYE HIKEGDTVTC TGRILEVPVG RELVGRVVDA LGRPIDGKGP INTTLTAPIE KIAPGVIARK SVDQPMQTGL KAIDSMVPVG RGQRELIIGD RQTGKTAVAL DAIVNQKGTG VICIYVAIGQ KASSIANVVR KLEEHGAMEH TIVVAATASE AAALQYIAPY SGCTMGEFFR DRGEDALIVY DDLSKQAVAY RQISLLLRRP PGREAYPGDV FYLHSRLLER AARVNEHEVE KLTNGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETDLF NAGIRPAINA GISVSRVGGA AQTKVIKKLG GGIRLALAQY RELAAFSQFA SDLDEATRKQ LEHGEVVTEL MKQKQFSTLN TAEMALTLWA INNGSYSDVP VAKALAFESE FLSFVRTQHP EVLEAVNASG AMSDESEKTL EAAMKSFKSS YAYQA // ID ATPD_NEIMB Reviewed; 177 AA. AC Q9JXP9; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; GN OrderedLocusNames=NMB1937; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CC CF(1). It either transmits conformational changes from CF(0) to CC CF(1) or is implicated in proton conduction. {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42266.1; -; Genomic_DNA. DR PIR; B81025; B81025. DR RefSeq; NP_274931.1; NC_003112.2. DR RefSeq; WP_002225831.1; NC_003112.2. DR ProteinModelPortal; Q9JXP9; -. DR STRING; 122586.NMB1937; -. DR PaxDb; Q9JXP9; -. DR EnsemblBacteria; AAF42266; AAF42266; NMB1937. DR GeneID; 904215; -. DR KEGG; nme:NMB1937; -. DR PATRIC; 20359921; VBINeiMen85645_2465. DR eggNOG; ENOG4107S15; Bacteria. DR eggNOG; COG0712; LUCA. DR HOGENOM; HOG000075825; -. DR KO; K02113; -. DR OMA; ITSAFEM; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; NMEN122586:GHGG-1994-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.520.20; -; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR026015; ATPase_OSCP/delta_N. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR PANTHER; PTHR11910; PTHR11910; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 1. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 177 ATP synthase subunit delta. FT /FTId=PRO_0000371035. SQ SEQUENCE 177 AA; 19526 MW; 05B7F47182870973 CRC64; MAEFATIARP YAKALFGLAQ EKNQIESWLG GLEKLAAVVQ EGKVASLIDR PETNASEKAD ILIDLVGLKD KELKNFVIVL AGQKRLSILP EVYAQYQDLT LSFNHIKSAV IYSAYPLTDK QVGELVQMLN KRFDSELKIS VEIEPELIGG IKVEVGDQVL DLSVQGKLSA LYTTMTN // ID ATPF_NEIMB Reviewed; 156 AA. AC Q7DD66; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; GN OrderedLocusNames=NMB1938; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000255|HAMAP-Rule:MF_01398}. CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC {ECO:0000255|HAMAP-Rule:MF_01398}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42267.1; -; Genomic_DNA. DR PIR; C81025; C81025. DR RefSeq; NP_274932.1; NC_003112.2. DR RefSeq; WP_002214796.1; NC_003112.2. DR ProteinModelPortal; Q7DD66; -. DR STRING; 122586.NMB1938; -. DR PaxDb; Q7DD66; -. DR EnsemblBacteria; AAF42267; AAF42267; NMB1938. DR GeneID; 904214; -. DR KEGG; nme:NMB1938; -. DR PATRIC; 20359923; VBINeiMen85645_2466. DR eggNOG; ENOG4107Z6K; Bacteria. DR eggNOG; COG0711; LUCA. DR HOGENOM; HOG000015378; -. DR KO; K02109; -. DR OMA; ILVWFTM; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; NMEN122586:GHGG-1995-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.5.620; -; 1. DR HAMAP; MF_01398; ATP_synth_b_bact; 1. DR InterPro; IPR028987; ATPase_B-like_membr. DR InterPro; IPR002146; ATPase_F0-cplx_b/b'su_bac. DR InterPro; IPR005864; ATPase_F0-cplx_bsu_bac. DR Pfam; PF00430; ATP-synt_B; 1. DR SUPFAM; SSF81573; SSF81573; 1. DR TIGRFAMs; TIGR01144; ATP_synt_b; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 156 ATP synthase subunit b. FT /FTId=PRO_0000368622. FT TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. SQ SEQUENCE 156 AA; 17139 MW; 3DE2A468D7D4121E CRC64; MNINATLFAQ IIVFFGLVWF TMKFVWPPIA KALDERAAKV AEGLAAAERG KSDFEQAEKK VAELLAEGRN QVSEMVANAE KRAAKIVEEA KEQASSEAAR IAAQAKADVE QELFRARESL REQVAVLAVK GAESILRSEV DASKHAKLLD TLKQEL // ID ATPG_NEIMB Reviewed; 291 AA. AC Q9JXQ1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; DE AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815}; GN Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; GN OrderedLocusNames=NMB1935; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The gamma chain is believed to be CC important in regulating ATPase activity and the flow of protons CC through the CF(0) complex. {ECO:0000255|HAMAP-Rule:MF_00815}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. {ECO:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00815}. CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. CC {ECO:0000255|HAMAP-Rule:MF_00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42264.1; -; Genomic_DNA. DR PIR; H81024; H81024. DR RefSeq; NP_274929.1; NC_003112.2. DR RefSeq; WP_002225829.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ1; -. DR STRING; 122586.NMB1935; -. DR PaxDb; Q9JXQ1; -. DR EnsemblBacteria; AAF42264; AAF42264; NMB1935. DR GeneID; 904217; -. DR KEGG; nme:NMB1935; -. DR PATRIC; 20359917; VBINeiMen85645_2463. DR eggNOG; ENOG4105J80; Bacteria. DR eggNOG; COG0224; LUCA. DR HOGENOM; HOG000215912; -. DR KO; K02115; -. DR OMA; DRGMCGG; -. DR OrthoDB; EOG6R5C97; -. DR BioCyc; NMEN122586:GHGG-1992-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1. DR InterPro; IPR000131; ATPase_F1-cplx_gsu. DR InterPro; IPR023632; ATPase_F1_gsu_CS. DR InterPro; IPR023633; ATPase_F1_gsu_dom. DR PANTHER; PTHR11693; PTHR11693; 1. DR Pfam; PF00231; ATP-synt; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; SSF52943; 1. DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 291 ATP synthase gamma chain. FT /FTId=PRO_0000073329. SQ SEQUENCE 291 AA; 32556 MW; 916B46CFA584A7B0 CRC64; MAVGKEILTK IRSVQNTQKI TKAMQMVSTS KMRKTQERMR LARPYAEKVR MVMSHLAQTN TDHGIPLLES HREIRRVGFI LITSDKGLCG GLNANVLKKF LAQVQEYRNQ GIEEEIVCFG SKGLMACQSI GLNVVASAVN LGDTPKMEML LGPLTELFQR YEKHEIDRIH LVYSGFVNTM RQEPRMEVLL PIGENVIGDS APKSPFSWEY RYEPTALAVL EYLVRRYLES VVYQALSDNM ASEQAARMVA MKAATDNAGN AIKELRLVYN KSRQAAITTE LSEIVAGAAA V // ID BAMD_NEIMB Reviewed; 267 AA. AC Q9K0B1; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=Outer membrane protein assembly factor BamD {ECO:0000255|HAMAP-Rule:MF_00922}; DE AltName: Full=Competence lipoprotein ComL; DE Flags: Precursor; GN Name=bamD {ECO:0000255|HAMAP-Rule:MF_00922}; Synonyms=comL; GN OrderedLocusNames=NMB0703; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. Required for efficient CC transformation of Neisseria meningitidis by species-related DNA. CC {ECO:0000255|HAMAP-Rule:MF_00922}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_00922}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_00922}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00922}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the BamD family. {ECO:0000255|HAMAP- CC Rule:MF_00922}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41120.1; -; Genomic_DNA. DR PIR; H81167; H81167. DR RefSeq; NP_273745.1; NC_003112.2. DR RefSeq; WP_002244053.1; NC_003112.2. DR STRING; 122586.NMB0703; -. DR PaxDb; Q9K0B1; -. DR PRIDE; Q9K0B1; -. DR EnsemblBacteria; AAF41120; AAF41120; NMB0703. DR GeneID; 902815; -. DR KEGG; nme:NMB0703; -. DR PATRIC; 20356747; VBINeiMen85645_0895. DR eggNOG; ENOG4106SNF; Bacteria. DR eggNOG; COG4105; LUCA. DR HOGENOM; HOG000260923; -. DR KO; K05807; -. DR OMA; IHVADYY; -. DR OrthoDB; EOG6WHNPP; -. DR BioCyc; NMEN122586:GHGG-731-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR Gene3D; 1.25.40.10; -; 1. DR HAMAP; MF_00922; OM_assembly_BamD; 1. DR InterPro; IPR017689; BamD. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR03302; OM_YfiO; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Competence; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Reference proteome; Signal. FT SIGNAL 1 16 {ECO:0000255|HAMAP-Rule:MF_00922}. FT CHAIN 17 267 Outer membrane protein assembly factor FT BamD. FT /FTId=PRO_0000036223. FT LIPID 17 17 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_00922}. FT LIPID 17 17 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_00922}. SQ SEQUENCE 267 AA; 30915 MW; 26B4588A67A7E223 CRC64; MKKILLTVSL GLALSACATQ GTVDKDAQIT QDWSVEKLYA EAQDELNSSN YTRAVKLYEI LESRFPTSRH AQQSQLDTAY AYYKDDEKDK ALAAIDRFRR LHPQHPNMDY ALYLRGLVLF NEDQSFLNKL ASQDWSDRDP KANREAYQAF AELVQRFPNS KYAADATARM VKLVDALGGN EMSVARYYMK RGAYIAAANR AQKIIGSYQN TRYVEESLAI LELAYKKLDK PRLAADTRRV LETNFPKSPF LKQPWRSDDM PWWRYWH // ID BAME_NEIMB Reviewed; 125 AA. AC Q9K1F0; DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Outer membrane protein assembly factor BamE {ECO:0000255|HAMAP-Rule:MF_00925}; DE Flags: Precursor; GN Name=bamE {ECO:0000255|HAMAP-Rule:MF_00925}; GN OrderedLocusNames=NMB0204; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_00925}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00925}. CC -!- SIMILARITY: Belongs to the BamE family. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40661.1; -; Genomic_DNA. DR PIR; F81226; F81226. DR RefSeq; NP_273262.1; NC_003112.2. DR RefSeq; WP_002218608.1; NC_003112.2. DR ProteinModelPortal; Q9K1F0; -. DR STRING; 122586.NMB0204; -. DR PaxDb; Q9K1F0; -. DR EnsemblBacteria; AAF40661; AAF40661; NMB0204. DR GeneID; 902312; -. DR KEGG; nme:NMB0204; -. DR PATRIC; 20355449; VBINeiMen85645_0253. DR eggNOG; COG2913; LUCA. DR HOGENOM; HOG000256181; -. DR OMA; HYPSRFA; -. DR OrthoDB; EOG6J48RK; -. DR BioCyc; NMEN122586:GHGG-215-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00925; OM_assembly_BamE; 1. DR InterPro; IPR026592; BamE. DR InterPro; IPR007450; Lipoprotein_SmpA/OmlA. DR Pfam; PF04355; SmpA_OmlA; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 17 {ECO:0000255|HAMAP-Rule:MF_00925}. FT CHAIN 18 125 Outer membrane protein assembly factor FT BamE. FT /FTId=PRO_0000417865. FT LIPID 18 18 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_00925}. FT LIPID 18 18 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_00925}. SQ SEQUENCE 125 AA; 13902 MW; 8E3B891FA7EB1576 CRC64; MNKTLILALS ALLGLAACSA ERVSLFPSYK LKIIQGNELE PRAVAALRPG MTKDQVLLLL GSPILRDAFH TDRWDYTFNT SRNGIIKERS NLTVYFENGV LVRTEGDVLQ NAAEALKDRQ NTDKP // ID ATPB_NEIMB Reviewed; 465 AA. AC Q9JXQ2; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; DE EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01347}; DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; GN OrderedLocusNames=NMB1934; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01347}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42263.1; -; Genomic_DNA. DR PIR; G81024; G81024. DR RefSeq; NP_274928.1; NC_003112.2. DR RefSeq; WP_002219871.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ2; -. DR SMR; Q9JXQ2; 2-464. DR STRING; 122586.NMB1934; -. DR PaxDb; Q9JXQ2; -. DR PRIDE; Q9JXQ2; -. DR EnsemblBacteria; AAF42263; AAF42263; NMB1934. DR GeneID; 904218; -. DR KEGG; nme:NMB1934; -. DR PATRIC; 20359915; VBINeiMen85645_2462. DR eggNOG; ENOG4105C4J; Bacteria. DR eggNOG; COG0055; LUCA. DR HOGENOM; HOG000009605; -. DR KO; K02112; -. DR OMA; AEFGIYP; -. DR OrthoDB; EOG6HQSP3; -. DR BioCyc; NMEN122586:GHGG-1991-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1140.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR005722; ATPase_F1-cplx_bsu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR024034; ATPase_F1_bsu/V1_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 465 ATP synthase subunit beta. FT /FTId=PRO_0000254313. FT NP_BIND 148 155 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 465 AA; 50391 MW; CA03154CADAD6D7E CRC64; MSQGKIVQII GAVVDVEFPR DMIPRVYDAL KLDENGLTLE VQQLLGDGVV RAIAMGSSDG LKRGMTVSNT GAPITVPVGK GTLGRIVDVL GTPVDEAGPI DTDKSRAIHQ AAPKFDELSS TTELLETGIK VIDLLCPFAK GGKVGLFGGA GVGKTVNMME LINNIAKAHS GLSVFAGVGE RTREGNDFYH EMKDSNVLDK VAMVYGQMNE PPGNRLRVAL TGLTMAEYFR DEKDENGKGR DVLFFVDNIY RYTLAGTEVS ALLGRMPSAV GYQPTLAEEM GRLQERITST QTGSITSIQA VYVPADDLTD PSPATTFAHL DATVVLSRDI ASLGIYPAVD PLDSTSRQLD PMVLGQEHYD VARGVQSTLQ KYKELRDIIA ILGMDELSDE DKLTVMRARK IQRFLSQPFH VAEVFTGSPG KYVALRDTIA GFKAILNGEY DHLPEQAFYM VGSIEEAVEK AKTLN // ID ATPE_NEIMB Reviewed; 140 AA. AC Q9JXQ3; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530}; DE AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530}; DE AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530}; GN Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; GN OrderedLocusNames=NMB1933; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00530}. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. CC {ECO:0000255|HAMAP-Rule:MF_00530}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42262.1; -; Genomic_DNA. DR PIR; F81024; F81024. DR RefSeq; NP_274927.1; NC_003112.2. DR RefSeq; WP_002225828.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ3; -. DR STRING; 122586.NMB1933; -. DR PaxDb; Q9JXQ3; -. DR EnsemblBacteria; AAF42262; AAF42262; NMB1933. DR GeneID; 904221; -. DR KEGG; nme:NMB1933; -. DR PATRIC; 20359913; VBINeiMen85645_2461. DR eggNOG; ENOG410825K; Bacteria. DR eggNOG; COG0355; LUCA. DR HOGENOM; HOG000216025; -. DR KO; K02114; -. DR OMA; HHRAEVA; -. DR OrthoDB; EOG690MN9; -. DR BioCyc; NMEN122586:GHGG-1990-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.15.10; -; 1. DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1. DR InterPro; IPR001469; ATPase_F1-cplx_dsu/esu. DR InterPro; IPR020546; ATPase_F1-cplx_dsu/esu_N. DR InterPro; IPR020547; ATPase_F1_dsu/esu_C. DR PANTHER; PTHR13822; PTHR13822; 1. DR Pfam; PF02823; ATP-synt_DE_N; 1. DR ProDom; PD000944; ATPase_F1-cplx_dsu/esu; 1. DR SUPFAM; SSF46604; SSF46604; 1. DR SUPFAM; SSF51344; SSF51344; 1. DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 140 ATP synthase epsilon chain. FT /FTId=PRO_0000188168. SQ SEQUENCE 140 AA; 15031 MW; 31E5A7366D0AA56B CRC64; MSIMQVEVVS SEQKIYSGEA TFIVVPTVQG ELGIYPRHEP IMSLVRPGAL RLTVPGEDKE VLVAVSGGVL EVQPDKVTVL ADVAVRSAEM DRARAEEAKK AAEAGISQAK DDKALAEAHK VLAAAIAQLK TLDYIRSHKK // ID BAMA_NEIMB Reviewed; 797 AA. AC Q9K1H0; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000255|HAMAP-Rule:MF_01430}; DE AltName: Full=Outer membrane protein Omp85; DE Flags: Precursor; GN Name=bamA {ECO:0000255|HAMAP-Rule:MF_01430}; Synonyms=omp85; GN OrderedLocusNames=NMB0182; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the BamA family. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SIMILARITY: Contains 5 POTRA domains. {ECO:0000255|PROSITE- CC ProRule:PRU01115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40639.1; -; Genomic_DNA. DR PIR; G81228; G81228. DR RefSeq; NP_273240.1; NC_003112.2. DR RefSeq; WP_002243947.1; NC_003112.2. DR ProteinModelPortal; Q9K1H0; -. DR STRING; 122586.NMB0182; -. DR TCDB; 1.B.33.1.1; the outer membrane protein insertion porin (bam complex) (ompip) family. DR PaxDb; Q9K1H0; -. DR EnsemblBacteria; AAF40639; AAF40639; NMB0182. DR GeneID; 902289; -. DR KEGG; nme:NMB0182; -. DR PATRIC; 20355389; VBINeiMen85645_0224. DR eggNOG; ENOG4105E1Z; Bacteria. DR eggNOG; COG4775; LUCA. DR HOGENOM; HOG000261767; -. DR KO; K07277; -. DR OMA; NLDRGYF; -. DR OrthoDB; EOG6F81K6; -. DR BioCyc; NMEN122586:GHGG-192-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01430; OM_assembly_BamA; 1. DR InterPro; IPR000184; Bac_surfAg_D15. DR InterPro; IPR023707; OM_assembly_BamA. DR InterPro; IPR010827; Surface_Ag_variable_number. DR Pfam; PF01103; Bac_surface_Ag; 1. DR Pfam; PF07244; POTRA; 5. DR PIRSF; PIRSF006076; OM_assembly_OMP85; 1. DR TIGRFAMs; TIGR03303; OM_YaeT; 1. DR PROSITE; PS51779; POTRA; 5. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 21 {ECO:0000255|HAMAP-Rule:MF_01430}. FT CHAIN 22 797 Outer membrane protein assembly factor FT BamA. FT /FTId=PRO_0000349887. FT DOMAIN 23 90 POTRA 1. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 91 171 POTRA 2. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 174 262 POTRA 3. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 265 344 POTRA 4. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 347 421 POTRA 5. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 797 AA; 88437 MW; B68BFC5A43D22EE8 CRC64; MKLKQIASAL MMLGISPLAL ADFTIQDIRV EGLQRTEPST VFNYLPVKVG DTYNDTHGSA IIKSLYATGF FDDVRVETAD GQLLLTVIER PTIGSLNITG AKMLQNDAIK KNLESFGLAQ SQYFNQATLN QAVAGLKEEY LGRGKLNIQI TPKVTKLARN RVDIDITIDE GKSAKITDIE FEGNQVYSDR KLMRQMSLTE GGIWTWLTRS NQFNEQKFAQ DMEKVTDFYQ NNGYFDFRIL DTDIQTNEDK TKQTIKITVH EGGRFRWGKV SIEGDTNEVP KAELEKLLTM KPGKWYERQQ MTAVLGEIQN RMGSAGYAYS EISVQPLPNA ETKTVDFVLH IEPGRKIYVN EIHITGNNKT RDEVVRRELR QMESAPYDTS KLQRSKERVE LLGYFDNVQF DAVPLAGTPD KVDLNMSLTE RSTGSLDLSA GWVQDTGLVM SAGVSQDNLF GTGKSAALRA SRSKTTLNGS LSFTDPYFTA DGVSLGYDVY GKAFDPRKAS TSIKQYKTTT AGAGIRMSVP VTEYDRVNFG LVAEHLTVNT YNKAPKHYAD FIKKYGKTDG TDGSFKGWLY KGTVGWGRNK TDSALWPTRG YLTGVNAEIA LPGSKLQYYS ATHNQTWFFP LSKTFTLMLG GEVGIAGGYG RTKEIPFFEN FYGGGLGSVR GYESGTLGPK VYDEYGEKIS YGGNKKANVS AELLFPMPGA KDARTVRLSL FADAGSVWDG KTYDDNSSSA TGGRVQNIYG AGNTHKSTFT NELRYSAGGA VTWLSPLGPM KFSYAYPLKK KPEDEIQRFQ FQLGTTF // ID BFRA_NEIMB Reviewed; 154 AA. AC P0A0R1; P72080; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Bacterioferritin A; DE Short=BFR A; DE EC=1.16.3.1; GN Name=bfrA; OrderedLocusNames=NMB1207; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds CC Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates CC in the subsequent Fe(3+) oxide mineral core formation within the CC central cavity of the protein complex. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000305}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron- CC binding site within each subunit is known as the ferroxidase CC center. {ECO:0000250}; CC -!- SUBUNIT: Oligomer of 24 subunits, arranged as 12 dimers, that are CC packed together to form an approximately spherical molecule with a CC central cavity, in which large amounts of iron can be deposited. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41589.1; -; Genomic_DNA. DR PIR; F81110; F81110. DR RefSeq; NP_274232.1; NC_003112.2. DR RefSeq; WP_002217177.1; NC_003112.2. DR ProteinModelPortal; P0A0R1; -. DR STRING; 122586.NMB1207; -. DR PaxDb; P0A0R1; -. DR PRIDE; P0A0R1; -. DR EnsemblBacteria; AAF41589; AAF41589; NMB1207. DR GeneID; 903629; -. DR KEGG; nme:NMB1207; -. DR PATRIC; 20358003; VBINeiMen85645_1514. DR eggNOG; ENOG4108YRX; Bacteria. DR eggNOG; COG2193; LUCA. DR HOGENOM; HOG000262383; -. DR KO; K03594; -. DR OMA; HEMQDET; -. DR OrthoDB; EOG6WDSKP; -. DR BioCyc; NMEN122586:GHGG-1244-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF002560; Bacterioferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR00754; bfr; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Heme; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 154 Bacterioferritin A. FT /FTId=PRO_0000192604. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 18 18 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 48 48 Iron (heme axial ligand); shared with FT dimeric partner. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 51 51 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 51 51 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 54 54 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 93 93 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 127 127 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 127 127 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 130 130 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. SQ SEQUENCE 154 AA; 17961 MW; 15136D10DDA4346A CRC64; MQGNQAVVDY MNELLSGELA ARDQYFIHSR LYSEWGYTKL FERLNHEMEE ETTHAEDFIR RILMLGGTPK MARAELNIGT DVVSCLKADL QTEYEVRDAL KKGIKLCEEA QDYVTRDLMV AQLKDTEEDH AHWLEQQLRL IELIGEGNYY QSQL // ID BFRB_NEIMB Reviewed; 157 AA. AC P63700; P56999; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Putative bacterioferritin B; DE Short=BFR B; GN Name=bfrB; OrderedLocusNames=NMB1206; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Iron-storage protein. {ECO:0000250}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000250}; CC -!- SUBUNIT: Oligomer of 24 subunits, arranged as 12 dimers, that are CC packed together to form an approximately spherical molecule with a CC central cavity, in which large amounts of iron can be deposited. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41588.1; -; Genomic_DNA. DR PIR; E81110; E81110. DR RefSeq; NP_274231.1; NC_003112.2. DR RefSeq; WP_002213535.1; NC_003112.2. DR ProteinModelPortal; P63700; -. DR SMR; P63700; 1-152. DR STRING; 122586.NMB1206; -. DR PaxDb; P63700; -. DR PRIDE; P63700; -. DR EnsemblBacteria; AAF41588; AAF41588; NMB1206. DR GeneID; 903628; -. DR KEGG; nme:NMB1206; -. DR PATRIC; 20358001; VBINeiMen85645_1513. DR eggNOG; COG2193; LUCA. DR HOGENOM; HOG000262383; -. DR KO; K03594; -. DR OMA; EMKHADQ; -. DR OrthoDB; EOG6WDSKP; -. DR BioCyc; NMEN122586:GHGG-1243-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002024; Bacterioferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF002560; Bacterioferritin; 1. DR PRINTS; PR00601; BACFERRITIN. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR00754; bfr; 1. DR PROSITE; PS00549; BACTERIOFERRITIN; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Heme; Iron; Iron storage; Metal-binding; KW Reference proteome. FT CHAIN 1 157 Putative bacterioferritin B. FT /FTId=PRO_0000192608. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 51 51 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 52 52 Iron (heme axial ligand); shared with FT dimeric partner. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 94 94 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 130 130 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. SQ SEQUENCE 157 AA; 18016 MW; FCB8A28F19EEAD40 CRC64; MKGDRLVIRE LNKNLGLLLV TINQYFLHAR ILKNWGFEEL GEHFFKQSIV EMKAADDLIE RILFLEGLPN LQELGKLLIG ESTEEIIACD LTKEQEKHEA LLAAIATAEA QQDYVSRDLL EKQKDTNEEH IDWLETQQEL IGKIGLPNYL QTAAQED // ID BICOA_NEIMB Reviewed; 592 AA. AC Q9JXF1; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Bifunctional enzyme BirA/CoaX; DE Includes: DE RecName: Full=Biotin--[acetyl-CoA-carboxylase] synthetase; DE EC=6.3.4.15; DE AltName: Full=Biotin--protein ligase; DE Includes: DE RecName: Full=Type III pantothenate kinase; DE EC=2.7.1.33; DE AltName: Full=PanK-III; DE AltName: Full=Pantothenic acid kinase; GN Name=birA/coaX; OrderedLocusNames=NMB2075; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Activates biotin to form biotinyl-5'-adenylate and CC transfers the biotin moiety to biotin-accepting proteins. CC {ECO:0000250}. CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the CC first step in CoA biosynthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide CC ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon- CC dioxide ligase (ADP-forming)]. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. CC -!- COFACTOR: CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000250}; CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 1/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the biotin-- CC protein ligase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the type III CC pantothenate kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 BPL/LPL catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42394.1; -; Genomic_DNA. DR PIR; B81009; B81009. DR RefSeq; NP_275065.1; NC_003112.2. DR RefSeq; WP_002225711.1; NC_003112.2. DR ProteinModelPortal; Q9JXF1; -. DR STRING; 122586.NMB2075; -. DR PaxDb; Q9JXF1; -. DR EnsemblBacteria; AAF42394; AAF42394; NMB2075. DR GeneID; 903989; -. DR KEGG; nme:NMB2075; -. DR PATRIC; 20360310; VBINeiMen85645_2655. DR eggNOG; ENOG4108EKN; Bacteria. DR eggNOG; COG0340; LUCA. DR eggNOG; COG1521; LUCA. DR HOGENOM; HOG000220772; -. DR KO; K01947; -. DR OMA; RPAGKRY; -. DR OrthoDB; EOG6G20K0; -. DR BioCyc; NMEN122586:GHGG-2138-MONOMER; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01274; Pantothen_kinase_3; 1. DR InterPro; IPR004408; Biotin_CoA_COase_ligase. DR InterPro; IPR003142; BPL_C. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR008988; Transcriptional_repressor_C. DR InterPro; IPR004619; Type_III_PanK. DR PANTHER; PTHR12835; PTHR12835; 1. DR Pfam; PF02237; BPL_C; 1. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR Pfam; PF03309; Pan_kinase; 1. DR SUPFAM; SSF50037; SSF50037; 1. DR TIGRFAMs; TIGR00671; baf; 1. DR TIGRFAMs; TIGR00121; birA_ligase; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Kinase; Ligase; Multifunctional enzyme; Nucleotide-binding; KW Potassium; Reference proteome; Transferase. FT CHAIN 1 592 Bifunctional enzyme BirA/CoaX. FT /FTId=PRO_0000270884. FT DOMAIN 83 259 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT NP_BIND 344 351 ATP. {ECO:0000250}. FT REGION 1 329 Biotin--protein ligase. FT REGION 336 592 Type III pantothenate kinase. FT REGION 433 436 Substrate binding. {ECO:0000250}. FT ACT_SITE 435 435 Proton acceptor. {ECO:0000255}. FT BINDING 426 426 Substrate. {ECO:0000250}. FT BINDING 458 458 ATP. {ECO:0000255}. FT BINDING 508 508 Substrate. {ECO:0000250}. SQ SEQUENCE 592 AA; 64701 MW; 9E27421DA2B41DE3 CRC64; MTVLKLSHWR VLAELADGLP QHVSQLARMA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR LVRPLAVFDA EGLRELGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK GRGRQGRKWS HRLGECLMFS FGWVFDRPQY ELGSLSPVAA VACRRALSRL GLDVQIKWPN DLVVGRDKLG GILIETVRTG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA AVLLETLLVE LDAVLLQYAR DGFAPFVAEY QAANRDHGKA VLLLRDGETV FEGTVKGVDG QGVLHLETAE GKQTVVSGEI SLRSDDRPVS VPKRRDSERF LLLDGGNSRL KWAWVENGTF ATVGSAPYRD LSPLGAEWAE KADGNVRIVG CAVCGEFKKA QVQEQLARKI EWLPSSAQAL GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF HLMKESLAVR TANLNRHAGK RYPFPTTTGN AVASGMMDAV CGSVMMMHGR LKEKTGAGKP VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIYGLLN MIAAEGREYE HI // ID BIOF_NEIMB Reviewed; 380 AA. AC Q9K0U0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative 8-amino-7-oxononanoate synthase; DE Short=AONS; DE EC=2.3.1.47; DE AltName: Full=7-keto-8-amino-pelargonic acid synthase; DE Short=7-KAP synthase; DE AltName: Full=8-amino-7-ketopelargonate synthase; GN Name=bioF; OrderedLocusNames=NMB0472; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl- CC [acyl-carrier protein] and L-alanine to produce 8-amino-7- CC oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] + L-alanine = CC 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein]. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. BioF subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40909.1; -; Genomic_DNA. DR PIR; C81194; C81194. DR RefSeq; NP_273519.1; NC_003112.2. DR RefSeq; WP_002224951.1; NC_003112.2. DR ProteinModelPortal; Q9K0U0; -. DR STRING; 122586.NMB0472; -. DR PaxDb; Q9K0U0; -. DR EnsemblBacteria; AAF40909; AAF40909; NMB0472. DR GeneID; 902588; -. DR KEGG; nme:NMB0472; -. DR PATRIC; 20356196; VBINeiMen85645_0619. DR eggNOG; ENOG4107EEK; Bacteria. DR eggNOG; COG0156; LUCA. DR HOGENOM; HOG000221021; -. DR KO; K00652; -. DR OMA; RDGARKH; -. DR OrthoDB; EOG6PZX7V; -. DR BioCyc; NMEN122586:GHGG-496-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004723; AONS_Archaea/Proteobacteria. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00858; bioF; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Biotin biosynthesis; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 380 Putative 8-amino-7-oxononanoate synthase. FT /FTId=PRO_0000381052. FT REGION 106 107 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 205 208 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 236 239 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 18 18 Substrate. {ECO:0000250}. FT BINDING 131 131 Substrate. {ECO:0000250}. FT BINDING 179 179 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 352 352 Substrate. {ECO:0000250}. FT MOD_RES 239 239 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 380 AA; 43260 MW; C7FA8E887D9D3DA5 CRC64; MKVFKQQLEQ LGAQNQYRSI PDLIHQGRYI TRENRKMLNM SSNDYLGLAS DENLRRSFLQ QYGGNFPSFT SSSSRLLTGN FPIYTDLEEL VAQRFQRESA LLFNSGYHAN LGILPALTTT KSLILADKFV HASMIDGIRL SRCAFFRYRH NDYEHLKNLL EKNVGKFDRT FIVTESVFSM DGDVADLKQL VQLKKQFPNT YLYVDEAHAI GVYGQNGLGI AERDNLIAEI DLLVGTFGKA LASVGAYAVC NQVLKECLIN QMRPLIFSTA LPPFNVAWTY FIFERLPQFS KERSHLEQLS AFLRREVAHR TQIMPSQTCI VPYILGGNEA TLAKAEYLQR QGYYCLPIRP STVPKNTSRI RLSLTADMTT DEVRQFAACL // ID BIOD_NEIMB Reviewed; 215 AA. AC Q9K085; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000255|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase {ECO:0000255|HAMAP-Rule:MF_00336}; DE Short=DTBS {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase {ECO:0000255|HAMAP-Rule:MF_00336}; GN Name=bioD {ECO:0000255|HAMAP-Rule:MF_00336}; GN OrderedLocusNames=NMB0733; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP + CC phosphate + dethiobiotin. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41146.1; -; Genomic_DNA. DR PIR; E81164; E81164. DR RefSeq; NP_273775.1; NC_003112.2. DR RefSeq; WP_002225454.1; NC_003112.2. DR ProteinModelPortal; Q9K085; -. DR STRING; 122586.NMB0733; -. DR PaxDb; Q9K085; -. DR EnsemblBacteria; AAF41146; AAF41146; NMB0733. DR GeneID; 902846; -. DR KEGG; nme:NMB0733; -. DR PATRIC; 20356825; VBINeiMen85645_0933. DR eggNOG; ENOG4105E78; Bacteria. DR eggNOG; COG0132; LUCA. DR HOGENOM; HOG000275033; -. DR KO; K01935; -. DR OMA; CINHAVL; -. DR OrthoDB; EOG66B3XT; -. DR BioCyc; NMEN122586:GHGG-762-MONOMER; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00347; bioD; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 215 ATP-dependent dethiobiotin synthetase FT BioD. FT /FTId=PRO_0000187979. FT NP_BIND 13 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 115 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 175 176 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT METAL 13 13 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 17 17 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 50 50 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 115 115 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 42 42 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 50 50 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. SQ SEQUENCE 215 AA; 23701 MW; E1F98EB99D5DEE90 CRC64; MKGVYFVSGI DTDIGKTVAT GVLAKQLLQQ GKSVITQKPV QTGCQNIADD IAVHRKIMGI PMQEADKRRL TMPEIFSYPA SPHLAARLDG RALDLDKIRT ATQELAAQYE VVLVEGAGGL MVPLTENLLT IDYIRQQGYP VILVTSGRLG SINHTLLSFA ALKQYGIRLH SLVFNHIHDS RDAHIAQDSL SYLKCRLKAD FSEAEWMELA KTDAV // ID BIOH_NEIMB Reviewed; 258 AA. AC Q9K197; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 11-NOV-2015, entry version 87. DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000255|HAMAP-Rule:MF_01260}; DE EC=3.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01260}; DE AltName: Full=Biotin synthesis protein BioH {ECO:0000255|HAMAP-Rule:MF_01260}; DE AltName: Full=Carboxylesterase BioH {ECO:0000255|HAMAP-Rule:MF_01260}; GN Name=bioH {ECO:0000255|HAMAP-Rule:MF_01260}; GN OrderedLocusNames=NMB0270; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The physiological role of BioH is to remove the methyl CC group introduced by BioC when the pimeloyl moiety is complete. It CC allows to synthesize pimeloyl-ACP via the fatty acid synthetic CC pathway through the hydrolysis of the ester bonds of pimeloyl-ACP CC esters. {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] methyl ester + CC H(2)O = pimeloyl-[acyl-carrier protein] + methanol. CC {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. CC Carboxylesterase BioH family. {ECO:0000255|HAMAP-Rule:MF_01260}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40724.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40724.1; ALT_INIT; Genomic_DNA. DR PIR; G81218; G81218. DR RefSeq; NP_273326.1; NC_003112.2. DR ProteinModelPortal; Q9K197; -. DR STRING; 122586.NMB0270; -. DR ESTHER; neime-NMA2216; BioH. DR PaxDb; Q9K197; -. DR EnsemblBacteria; AAF40724; AAF40724; NMB0270. DR GeneID; 902381; -. DR KEGG; nme:NMB0270; -. DR PATRIC; 20355624; VBINeiMen85645_0336. DR eggNOG; ENOG4105D3C; Bacteria. DR eggNOG; COG0596; LUCA. DR HOGENOM; HOG000028062; -. DR KO; K02170; -. DR OMA; QRERKSM; -. DR OrthoDB; EOG6FJNH9; -. DR BioCyc; NMEN122586:GHGG-285-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB. DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; -; 1. DR HAMAP; MF_01260; Carboxylester; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR010076; BioH. DR Pfam; PF00561; Abhydrolase_1; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01738; bioH; 1. PE 3: Inferred from homology; KW Biotin biosynthesis; Complete proteome; Cytoplasm; Hydrolase; KW Reference proteome; Serine esterase. FT CHAIN 1 258 Pimeloyl-[acyl-carrier protein] methyl FT ester esterase. FT /FTId=PRO_0000204484. FT REGION 83 84 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01260}. FT REGION 145 149 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01260}. FT ACT_SITE 83 83 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01260}. FT ACT_SITE 207 207 {ECO:0000255|HAMAP-Rule:MF_01260}. FT ACT_SITE 235 235 {ECO:0000255|HAMAP-Rule:MF_01260}. FT BINDING 23 23 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01260}. FT BINDING 235 235 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01260}. SQ SEQUENCE 258 AA; 28208 MW; E276CAF32714D04E CRC64; MRRQRERKSM PDAVKKVYLI HGWGANRHMF DDLMPRLPAT WPVSAVDLPG HGDAPFVRPF DIAAAADGIA AQIDAPADIL GWSLGGLVAL YLAARHPDKV RSLCLTASFA RLTADEDYPE GLAAPALGKM VGAFRSDYAK HIKQFLQLQL LHTPDADGII GRILPDLARC GTPQALQEAL DAAERADARH LLDKIDVPVL LVFGGKDAIT PPRMGEYLHR RLKGSRLVVM EKAAHAPFLS HAEAFAALYR DFVEGGLR // ID BIOB_NEIMB Reviewed; 350 AA. AC Q9JRW7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694}; DE EC=2.8.1.6 {ECO:0000255|HAMAP-Rule:MF_01694}; GN Name=bioB1 {ECO:0000255|HAMAP-Rule:MF_01694}; GN OrderedLocusNames=NMB1146; GN and GN Name=bioB2 {ECO:0000255|HAMAP-Rule:MF_01694}; GN OrderedLocusNames=NMB1184; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin CC by the insertion of a sulfur atom into dethiobiotin via a radical- CC based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S- CC adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + CC (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. {ECO:0000255|HAMAP-Rule:MF_01694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41533.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41568.1; -; Genomic_DNA. DR PIR; A81117; A81117. DR RefSeq; NP_274174.1; NC_003112.2. DR RefSeq; NP_274210.1; NC_003112.2. DR RefSeq; WP_002217196.1; NC_003112.2. DR ProteinModelPortal; Q9JRW7; -. DR SMR; Q9JRW7; 23-330. DR STRING; 122586.NMB1184; -. DR PaxDb; Q9JRW7; -. DR EnsemblBacteria; AAF41533; AAF41533; NMB1146. DR EnsemblBacteria; AAF41568; AAF41568; NMB1184. DR GeneID; 903567; -. DR GeneID; 903604; -. DR KEGG; nme:NMB1146; -. DR KEGG; nme:NMB1184; -. DR PATRIC; 20357869; VBINeiMen85645_1450. DR eggNOG; ENOG4105CZF; Bacteria. DR eggNOG; COG0502; LUCA. DR HOGENOM; HOG000239957; -. DR KO; K01012; -. DR OMA; PFDFIRM; -. DR OrthoDB; EOG622PMP; -. DR BioCyc; NMEN122586:GHGG-1182-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1219-MONOMER; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01694; BioB; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR002684; Biotin_synth/BioAB. DR InterPro; IPR024177; Biotin_synthase. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF001619; Biotin_synth; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 350 Biotin synthase. FT /FTId=PRO_0000381497. FT METAL 69 69 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 73 73 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 76 76 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 113 113 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 144 144 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 204 204 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 276 276 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. SQ SEQUENCE 350 AA; 38793 MW; C01D0E11020FFED5 CRC64; MTVSPVALRR KTECKPHPTA RYWKKCDVEA LFGLPFLDLI YQAAEIHRQN FNPREIQLST LLSIKTGGCP EDCAYCPQSA HHNTNLGKEQ MMDVDEIVEK AKIAKSRGAS RFCMGAAWRG PKPKDVETVS AIIKAVKGLG METCGTFGML EEGMAEDLKE AGLDYYNHNL DTDPDRYNDI IHTRQHEDRM DTLGKVRNAG LKVCCGGIVG MNETRAERAG LIASLANLDP QPESVPINRL VKVEGTPLAD AEDLDWTEFV RTIAVARITM PQSYVRLSAG RSNMPEAMQA MCFMAGANSI FYGDKLLTTG NPDEDGDRIL MEKLNLYPLQ FEPEGEVAEV EKASGIKVDY // ID CARA_NEIMB Reviewed; 377 AA. AC Q9JXX4; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209}; DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209}; GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; GN OrderedLocusNames=NMB1849; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP- CC Rule:MF_01209}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42183.1; -; Genomic_DNA. DR PIR; F81034; F81034. DR RefSeq; NP_274845.1; NC_003112.2. DR RefSeq; WP_002244304.1; NC_003112.2. DR ProteinModelPortal; Q9JXX4; -. DR SMR; Q9JXX4; 5-368. DR STRING; 122586.NMB1849; -. DR PaxDb; Q9JXX4; -. DR EnsemblBacteria; AAF42183; AAF42183; NMB1849. DR GeneID; 903249; -. DR KEGG; nme:NMB1849; -. DR PATRIC; 20359721; VBINeiMen85645_2366. DR eggNOG; ENOG4105C1M; Bacteria. DR eggNOG; COG0505; LUCA. DR HOGENOM; HOG000038087; -. DR KO; K01956; -. DR OMA; VDTRYIT; -. DR OrthoDB; EOG61ZTH6; -. DR BioCyc; NMEN122586:GHGG-1905-MONOMER; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.50.30.20; -; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SUPFAM; SSF52021; SSF52021; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 377 Carbamoyl-phosphate synthase small chain. FT /FTId=PRO_0000112299. FT DOMAIN 190 377 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01209}. FT REGION 1 186 CPSase. FT ACT_SITE 266 266 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01209}. FT ACT_SITE 350 350 {ECO:0000255|HAMAP-Rule:MF_01209}. FT ACT_SITE 352 352 {ECO:0000255|HAMAP-Rule:MF_01209}. SQ SEQUENCE 377 AA; 40587 MW; 36733FC0806B1670 CRC64; MSTPALLVLA DGSVFHGTSI GYEGSTSGEV VFNTSMTGYQ EILTDPSYCK QIVTLTYPHI GNTGTNAEDE ESRSVYAAGL IIRDLPLLHS NFRASESLHD YLVRNKTVAI ADIDTRRLTT LLREKGAQGG AILTGADATI EKAQELIAAF GSMVGKDLAK EVSCTETYEW TEGEWALGKG FVTPDEQPYH VVAYDFGVKT NILRMLASRG CRLTVVPAQT SAEDVLALNP DGVFLSNGPG DPEPCTYAIK AVQKLIESGK PIFGICLGHQ LISLAIGAKT LKMRFSHHGA NHPVQDLDSG KVVITSQNHG FAVDADTLPA NARITHKSLF DNTLQGIELT DKPVFCFQGH PEASPGPQDV GYLFDKFIGN MKAAKRA // ID CAPP_NEIMB Reviewed; 900 AA. AC Q9JXG5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595}; DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595}; DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595}; DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595}; GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=NMB2061; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid CC source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP- CC Rule:MF_00595}. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP- CC Rule:MF_00595}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595}; CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. CC {ECO:0000255|HAMAP-Rule:MF_00595}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42380.1; -; Genomic_DNA. DR PIR; A81010; A81010. DR RefSeq; NP_275051.1; NC_003112.2. DR RefSeq; WP_002244350.1; NC_003112.2. DR ProteinModelPortal; Q9JXG5; -. DR STRING; 122586.NMB2061; -. DR PaxDb; Q9JXG5; -. DR EnsemblBacteria; AAF42380; AAF42380; NMB2061. DR GeneID; 904019; -. DR KEGG; nme:NMB2061; -. DR PATRIC; 20360278; VBINeiMen85645_2639. DR eggNOG; ENOG4105CCA; Bacteria. DR eggNOG; COG2352; LUCA. DR HOGENOM; HOG000238647; -. DR KO; K01595; -. DR OMA; FTSNWEL; -. DR OrthoDB; EOG6TJ7T8; -. DR BioCyc; NMEN122586:GHGG-2124-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR HAMAP; MF_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR033129; PEPCASE_His_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; SSF51621; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 3: Inferred from homology; KW Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; KW Reference proteome. FT CHAIN 1 900 Phosphoenolpyruvate carboxylase. FT /FTId=PRO_0000166604. FT ACT_SITE 140 140 {ECO:0000255|HAMAP-Rule:MF_00595}. FT ACT_SITE 568 568 {ECO:0000255|HAMAP-Rule:MF_00595}. SQ SEQUENCE 900 AA; 101210 MW; 489B26F74AA06012 CRC64; MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ LDEQQTHDLT LACGLFAQIL NIAEDVHHER RRQIHEEAGR GGAEGSLTET VRRLKAGKAD GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL SFNRRIRALL PQRERCTNAD ALARLRREID TILLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRKMEHDFQ TAYPGVRVPD ILKIGGWIGG DRDGNPFVSA ETLRFAFRRH ADAVFRFYRG ELDKLYRELP LSIRRVKVNG DVTALSDKSP DEEIARAEEP YRRAIAYIMA RAMGKARALG LGMGCKFGFL EPYASAQEFL DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA GLEDYNRLNE EQKQTALLRE LSHQRPLYSP FITYSDHTRH ELAIFNEARK IKDEFGEDAV TQSIISNCEQ PSDLLALALL LKETGLLAVE NGKPHSRINI VPLFETIEAL ENACPVMETM FRLDWYDALL ESRGNIQEIM LGYSDSNKDG GYVTSSWCLY QAELGLVELF KKYDVRMRLF HGRGGSVGRG GGPSYQAILA QPAGSVAGQI RITEQGEVIT AKYADPGNAQ RNLETLVAAT LEASILPDKK DPDAKLMQAL SDVSFKYYRE LITHPDFIDY FLQTSPIQEI ATLNLGSRPA SRKTLARIQD LRAIPWVFSW MQNRLMLPAW YGFGSAVETL CEDKPETLAA LREHAQSNPF FQAMLSNMEQ VMAKTDITLA ENYAGLSESP DKAKIIFGMI KEEYRRSRKA LLDLLQTEEL LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG // ID CCA_NEIMB Reviewed; 417 AA. AC Q9JZ88; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Multifunctional CCA protein {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2'-nucleotidase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=Phosphatase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261}; GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01261}; OrderedLocusNames=NMB1241; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'- CC terminal CCA sequence in tRNAs without using a nucleic acid CC template. Adds these three nucleotides in the order of C, C, and A CC to the tRNA nucleotide-73, using CTP and ATP as substrates and CC producing inorganic pyrophosphate. Also shows phosphatase, 2'- CC nucleotidase and 2',3'-cyclic phosphodiesterase activities. These CC phosphohydrolase activities are probably involved in the repair of CC the tRNA 3'-CCA terminus degraded by intracellular RNases. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a CC 3' CCA end + 3 diphosphate. {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261}; CC Note=Magnesium is required for nucleotidyltransferase activity. CC {ECO:0000255|HAMAP-Rule:MF_01261}; CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261}; CC Note=Nickel for phosphatase activity. {ECO:0000255|HAMAP- CC Rule:MF_01261}; CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the CC nucleotidyltransferase activity and a C-terminal HD domain CC associated with both phosphodiesterase and phosphatase activities. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- MISCELLANEOUS: A single active site specifically recognizes both CC ATP and CTP and is responsible for their addition. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. Bacterial CCA-adding enzyme type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41622.1; -; Genomic_DNA. DR PIR; F81105; F81105. DR RefSeq; NP_274265.1; NC_003112.2. DR RefSeq; WP_002225191.1; NC_003112.2. DR ProteinModelPortal; Q9JZ88; -. DR STRING; 122586.NMB1241; -. DR PaxDb; Q9JZ88; -. DR EnsemblBacteria; AAF41622; AAF41622; NMB1241. DR GeneID; 903663; -. DR KEGG; nme:NMB1241; -. DR PATRIC; 20358079; VBINeiMen85645_1552. DR eggNOG; ENOG4105D4J; Bacteria. DR eggNOG; COG0617; LUCA. DR HOGENOM; HOG000007368; -. DR KO; K00974; -. DR OMA; APRECQE; -. DR OrthoDB; EOG651SRP; -. DR BioCyc; NMEN122586:GHGG-1278-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW. DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01261; CCA_bact_type1; 1. DR HAMAP; MF_01262; CCA_bact_type2; 1. DR InterPro; IPR012006; CCA_bact. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR Pfam; PF01966; HD; 1. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR PIRSF; PIRSF000813; CCA_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nickel; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding; KW Transferase; tRNA processing. FT CHAIN 1 417 Multifunctional CCA protein. FT /FTId=PRO_0000138988. FT METAL 21 21 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT METAL 23 23 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 8 8 ATP or CTP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01261}. FT BINDING 11 11 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 91 91 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 137 137 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 140 140 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. SQ SEQUENCE 417 AA; 46875 MW; 0E37948AF827BC1C CRC64; MQTYLVGGAV RDYLLGLPVK DRDWVVVGAD AQTMLAQGFQ PVGKDFPVFL HPETHEEYAL ARTERKTAKG YVGFSFHADK DVTLEQDLMR RDLTINAMAQ DADGKIIDPF GGQRDLAAGI LRHVSPAFAE DPVRILRTAR FAARYKFEIA EETIKLMRQM VENGEADALV AERVWQEFAK GLMEKNPRKM IEVLRECGAL KVLLPEVNAL FGVPQRADYH PEIDSGIHTL MTLQRAADMG LSLPERYAAL LHDLGKAKTP SDILPRHHGH DLAGVEPVRE VNQRLRAPKH CAELAELVCR WHIIFHQVGQ LKSQTILNVL KKTDAFRRPE RFQTALNVCI ADTQGRLNRE HTPYPQRAHW LALLEAANQA DSGKIAAECR AQGKAHLIAE QIDRARLAQI APLQKAFRAA QDKTEKH // ID CARB_NEIMB Reviewed; 1071 AA. AC Q9JXW8; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; GN OrderedLocusNames=NMB1855; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42189.1; -; Genomic_DNA. DR PIR; D81035; D81035. DR RefSeq; NP_274851.1; NC_003112.2. DR RefSeq; WP_002225779.1; NC_003112.2. DR ProteinModelPortal; Q9JXW8; -. DR STRING; 122586.NMB1855; -. DR PaxDb; Q9JXW8; -. DR PRIDE; Q9JXW8; -. DR EnsemblBacteria; AAF42189; AAF42189; NMB1855. DR GeneID; 903243; -. DR KEGG; nme:NMB1855; -. DR PATRIC; 20359733; VBINeiMen85645_2372. DR eggNOG; ENOG4105CU6; Bacteria. DR eggNOG; COG0458; LUCA. DR HOGENOM; HOG000234582; -. DR KO; K01955; -. DR OMA; AVFPFNK; -. DR OrthoDB; EOG6J1DC6; -. DR BioCyc; NMEN122586:GHGG-1911-MONOMER; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR Gene3D; 3.40.50.20; -; 2. DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 2. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 2. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; KW Repeat. FT CHAIN 1 1071 Carbamoyl-phosphate synthase large chain. FT /FTId=PRO_0000145026. FT DOMAIN 133 328 ATP-grasp 1. {ECO:0000255|HAMAP- FT Rule:MF_01210}. FT DOMAIN 673 864 ATP-grasp 2. {ECO:0000255|HAMAP- FT Rule:MF_01210}. FT NP_BIND 159 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}. FT NP_BIND 699 756 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}. FT REGION 1 403 Carboxyphosphate synthetic domain. FT REGION 404 548 Oligomerization domain. FT REGION 549 930 Carbamoyl phosphate synthetic domain. FT REGION 931 1071 Allosteric domain. FT METAL 285 285 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 299 299 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 299 299 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 301 301 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 823 823 Magnesium or manganese 3. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 835 835 Magnesium or manganese 3. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 835 835 Magnesium or manganese 4. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 837 837 Magnesium or manganese 4. FT {ECO:0000255|HAMAP-Rule:MF_01210}. SQ SEQUENCE 1071 AA; 117376 MW; 6BBE498935B974EE CRC64; MPKRTDLKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVILVNSN PATIMTDPEM ADVTYIEPIM WQTVEKIIAK ERPDAILPTM GGQTALNCAL DLARNGVLAK YNVELIGATE DAIDKAEDRG RFKEAMEKIG LSCPKSFVCH TMNEALAAQE QVGFPTLIRP SFTMGGSGGG IAYNKDEFLA ICERGFDASP THELLIEQSV LGWKEYEMEV VRDKNDNCII ICSIENFDPM GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVDTG GSNVQFAVNP ANGEMIVIEM NPRVSRSSAL ASKATGFPIA KVAAKLAVGF TLDELRNDIT GGKTPASFEP SIDYVVTKIP RFAFEKFPAA DDRLTTQMKS VGEVMAMGRT IQESFQKALR GLETGLCGFN PRSEDKAEIR RELANPGPER MLFVADAFRA GFTLEEIHEI CAIDPWFLAQ IEDLMKEEKA VSDGILSDLD FAALRRLKRK GFSDKRLAQL LNVSEKEVRE HRYALKLHPV YKRVDTCAAE FATETAYLYS TYEEECESRP SDRKKVMILG GGPNRIGQGI EFDYCCVHAA LALRESGFET IMVNCNPETV STDFDTSDRL YFEPLTLEDV LEIVRTENPW GVIVHYGGQT PLKLANALVE NGVNIIGTSA DSIDAAEDRE RFQKVLNDLG LRQPPNRIAH NEEEALVKAE EIGYPLVVRP SYVLGGRAMQ VVHSAEELQK YMREAVQVSE DSPVLLDFFL NNAIEVDVDC VSDGKDVVIG GIMQHVEQAG IHSGDSGCSL PPYSLSEEIQ DEIRRQTKAM AYALGVVGLM NVQFAVQDGV VFVLEVNPRA SRTVPFVSKA TGVPLAKVGA RCMAGISLKE QGVEKEVVPD FYAVKEAVFP FIKFPGVDTI LGPEMRSTGE VMGVGASFGE AYYKAQLGAG ERLNPTGKIF LSVREEDKER VIKTAKNFQV LGYGICATRG TAQYLTEHGL IVQTINKVPE GRPHIGDALK NGEIALVVNT VSSDPQSVSD SHIIRQSALQ QRVPQYTTTA GGEAMSEGAK SRDHLGVYSV QELHGRLKNR N // ID CH10_NEIMB Reviewed; 96 AA. AC Q9JXM4; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580}; DE AltName: Full=GroES protein {ECO:0000255|HAMAP-Rule:MF_00580}; DE AltName: Full=Protein Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580}; GN Name=groS {ECO:0000255|HAMAP-Rule:MF_00580}; GN Synonyms=groES {ECO:0000255|HAMAP-Rule:MF_00580}; GN OrderedLocusNames=NMB1973; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses CC the ATPase activity of the latter. {ECO:0000255|HAMAP- CC Rule:MF_00580}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. CC {ECO:0000255|HAMAP-Rule:MF_00580}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}. CC -!- SIMILARITY: Belongs to the GroES chaperonin family. CC {ECO:0000255|HAMAP-Rule:MF_00580}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42302.1; -; Genomic_DNA. DR PIR; G81019; G81019. DR RefSeq; NP_274967.1; NC_003112.2. DR RefSeq; WP_002235240.1; NC_003112.2. DR ProteinModelPortal; Q9JXM4; -. DR SMR; Q9JXM4; 1-95. DR STRING; 122586.NMB1973; -. DR PaxDb; Q9JXM4; -. DR EnsemblBacteria; AAF42302; AAF42302; NMB1973. DR GeneID; 904167; -. DR KEGG; nme:NMB1973; -. DR PATRIC; 20360021; VBINeiMen85645_2515. DR eggNOG; ENOG4105K5Y; Bacteria. DR eggNOG; COG0234; LUCA. DR HOGENOM; HOG000133897; -. DR KO; K04078; -. DR OMA; EEYYLFR; -. DR OrthoDB; EOG6GFGSD; -. DR BioCyc; NMEN122586:GHGG-2030-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.33.40; -; 1. DR HAMAP; MF_00580; CH10; 1. DR InterPro; IPR020818; Chaperonin_GroES. DR InterPro; IPR018369; Chaprnonin_Cpn10_CS. DR InterPro; IPR011032; GroES-like. DR PANTHER; PTHR10772; PTHR10772; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 96 10 kDa chaperonin. FT /FTId=PRO_0000174793. SQ SEQUENCE 96 AA; 10331 MW; A244C8EA1DE4AFA4 CRC64; MTIRPLHDRV VVKRLEAEEK TASGIVLPGA AAEKPDMGEV IAVGAGKIGK DGSRRPLDVK VGDKIIFGKY SGQTVKADGE ELLVMREEDI FGIVEK // ID CLPB_NEIMB Reviewed; 859 AA. AC Q9JYQ8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 83. DE RecName: Full=Chaperone protein ClpB; GN Name=clpB; OrderedLocusNames=NMB1472; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is CC involved in the recovery of the cell from heat-induced damage, in CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the CC processing of protein aggregates. Protein binding stimulates the CC ATPase activity; ATP hydrolysis unfolds the denatured protein CC aggregates, which probably helps expose new hydrophobic binding CC sites on the surface of ClpB-bound aggregates, contributing to the CC solubilization and refolding of denatured protein aggregates by CC DnaK (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal domain probably functions as a substrate- CC discriminating domain, recruiting aggregated proteins to the ClpB CC hexamer and/or stabilizing bound proteins. The NBD2 domain is CC responsible for oligomerization, whereas the NBD1 domain CC stabilizes the hexamer probably in an ATP-dependent manner. The CC movement of the coiled-coil domain is essential for ClpB ability CC to rescue proteins from an aggregated state, probably by pulling CC apart large aggregated proteins, which are bound between the CC coiled-coils motifs of adjacent ClpB subunits in the functional CC hexamer (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41829.1; -; Genomic_DNA. DR PIR; F81078; F81078. DR RefSeq; NP_274481.1; NC_003112.2. DR RefSeq; WP_002225096.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ8; -. DR SMR; Q9JYQ8; 160-351. DR STRING; 122586.NMB1472; -. DR PaxDb; Q9JYQ8; -. DR EnsemblBacteria; AAF41829; AAF41829; NMB1472. DR GeneID; 903894; -. DR KEGG; nme:NMB1472; -. DR PATRIC; 20358709; VBINeiMen85645_1864. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR HOGENOM; HOG000218211; -. DR KO; K03695; -. DR OMA; PVERILM; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; NMEN122586:GHGG-1512-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016485; P:protein processing; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR017730; Chaperonin_ClpB. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR028299; ClpA/B_CS2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF10431; ClpB_D2-small; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1. DR PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; Repeat; Stress response. FT CHAIN 1 859 Chaperone protein ClpB. FT /FTId=PRO_0000191148. FT NP_BIND 206 213 ATP 1. {ECO:0000250}. FT NP_BIND 609 616 ATP 2. {ECO:0000250}. FT REGION 1 143 N-terminal. {ECO:0000250}. FT REGION 159 340 NBD1. {ECO:0000250}. FT REGION 341 549 Linker. {ECO:0000250}. FT REGION 559 768 NBD2. {ECO:0000250}. FT REGION 769 859 C-terminal. {ECO:0000250}. FT COILED 391 525 {ECO:0000250}. SQ SEQUENCE 859 AA; 95195 MW; 80B00D0E7CD119E8 CRC64; MRYDKLTAKF QQALAEAQSL ALAADGSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV KQRLQQHLNS LPKVSGQGGD ILPSRELQAV LNLMDKAATK RSDAYIASEL FLLALVQQND ATGKILKEAG ATEQNINAAI DAVRGGQNVN DANAEDQRDA LKKYTLDLTQ RARDGKLDPV IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLRNKRLLVL DLAALIAGAK YRGEFEERLK GVLNDLAKDD GNTLIFIDEI HTLVGAGKTD GAMDAGNMLK PALARGELHC IGATTLDEYR QYIEKDAALE RRFQKVLVGE PSVEDTIAIL RGLQERYEIH HGIDITDPAI VAAAELSDRY ITDRFLPDKA IDLIDEAASR VKMEKETKPE AMDKIDRRLI QLRMEKAHVE KEKDDASKKR LELIDEEING LQKEYADLDE IWKAEKAISD GAANIKKQID EVKIKIEQAK RQGDLALASK LMYEDLEHLE KQRAAAERAD TDSTKPANKL LRNNVGAEEI AEVVSRMTGI PVSKMMEGER DKLLKMEEVL HRRVVGQDEA VRAVSDAIRR SRSGLADPNK PYGSFLFLGP TGVGKTELCK ALAGFLFDSE DHLIRIDMSE YMEKHAVARL IGAPPGYVGY EEGGYLTEQV RRKPYSVILL DEVEKAHPDV FNILLQVLDD GRLTDGQGRT VDFKNTVIVM TSNIGSQHIQ QMGIQDYEAV KEVVMEDVKE HFRPEMINRI DEVVVFHGLD QDNIRNIAKI QLKGLEKRLE KQNLRLAVSD AALDIIAKAG FDPIYGARPL KRAIQSEIEN PLAKALLAGN YAPESEIRVE ADGDRLKFA // ID CLPX_NEIMB Reviewed; 414 AA. AC Q9JYY3; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN OrderedLocusNames=NMB1372; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. CC It directs the protease to specific substrates. Can perform CC chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP- CC Rule:MF_00175}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric CC ring that, in the presence of ATP, binds to fourteen ClpP subunits CC assembled into a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41746.1; -; Genomic_DNA. DR PIR; A81091; A81091. DR RefSeq; NP_274390.1; NC_003112.2. DR RefSeq; WP_002222327.1; NC_003112.2. DR ProteinModelPortal; Q9JYY3; -. DR SMR; Q9JYY3; 7-42. DR STRING; 122586.NMB1372; -. DR PaxDb; Q9JYY3; -. DR PRIDE; Q9JYY3; -. DR EnsemblBacteria; AAF41746; AAF41746; NMB1372. DR GeneID; 903794; -. DR KEGG; nme:NMB1372; -. DR PATRIC; 20358415; VBINeiMen85645_1719. DR eggNOG; ENOG4105CHN; Bacteria. DR eggNOG; COG1219; LUCA. DR HOGENOM; HOG000010093; -. DR KO; K03544; -. DR OMA; HYKRVQA; -. DR OrthoDB; EOG625JZK; -. DR BioCyc; NMEN122586:GHGG-1410-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00175; ClpX; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010603; Znf_CppX_C4. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR Pfam; PF06689; zf-C4_ClpX; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SMART; SM00994; zf-C4_ClpX; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00382; clpX; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 414 ATP-dependent Clp protease ATP-binding FT subunit ClpX. FT /FTId=PRO_0000160391. FT ZN_FING 8 33 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00175}. FT NP_BIND 120 127 ATP. {ECO:0000255|HAMAP-Rule:MF_00175}. SQ SEQUENCE 414 AA; 45099 MW; BC48D54586E085F1 CRC64; MSNENRTCSF CGKSKSHVKH LIEGENAFIC DECVSNCIEI LHEDGNDGTP SESAGGEPEE SGKLPTPAEI VANLNDHVIG QEQAKKALAV SVYNHYKRLR HPKAGANVEL SKSNILLIGP TGSGKTLLAQ SLARKLDVPF VMADATTLTE AGYVGEDVEQ IITKLLGKCD FDVEKAQRGI VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA SVPPQGGRKH PNQEFINVDT TNILFICGGA FAGLEKVIRQ RTEKGGIGFG ASVHSKDENA DITKLFGIVE PEDLIKFGLI PELIGRLPVI ATLEELDEDA LINILTEPKN ALVKQYQALF GMENVELEFE EGALRSIARQ AMERKTGARG LRSIVERCLL DTMYRLPDLK GLKKVVVGKA VIEEGREPEL VFES // ID CLPS_NEIMB Reviewed; 100 AA. AC Q9JZZ5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=ATP-dependent Clp protease adapter protein ClpS {ECO:0000255|HAMAP-Rule:MF_00302}; GN Name=clpS {ECO:0000255|HAMAP-Rule:MF_00302}; GN OrderedLocusNames=NMB0837; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the modulation of the specificity of the CC ClpAP-mediated ATP-dependent protein degradation. CC {ECO:0000255|HAMAP-Rule:MF_00302}. CC -!- SUBUNIT: Binds to the N-terminal domain of the chaperone ClpA. CC {ECO:0000255|HAMAP-Rule:MF_00302}. CC -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000255|HAMAP- CC Rule:MF_00302}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41248.1; -; Genomic_DNA. DR PIR; E81153; E81153. DR RefSeq; NP_273878.1; NC_003112.2. DR RefSeq; WP_002221161.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ5; -. DR STRING; 122586.NMB0837; -. DR PaxDb; Q9JZZ5; -. DR EnsemblBacteria; AAF41248; AAF41248; NMB0837. DR GeneID; 902951; -. DR KEGG; nme:NMB0837; -. DR PATRIC; 20357061; VBINeiMen85645_1049. DR eggNOG; ENOG4105KAE; Bacteria. DR eggNOG; COG2127; LUCA. DR HOGENOM; HOG000247049; -. DR KO; K06891; -. DR OMA; TENTTKM; -. DR OrthoDB; EOG67Q9F2; -. DR BioCyc; NMEN122586:GHGG-868-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1390.10; -; 1. DR HAMAP; MF_00302; ClpS; 1. DR InterPro; IPR022935; ClpS. DR InterPro; IPR003769; ClpS_core. DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like. DR Pfam; PF02617; ClpS; 1. DR SUPFAM; SSF54736; SSF54736; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 100 ATP-dependent Clp protease adapter FT protein ClpS. FT /FTId=PRO_0000215729. SQ SEQUENCE 100 AA; 11411 MW; FDAE3B7E77606DEC CRC64; MTAQHQSDTL LHRLNTLPPK RYGVFLLNDD YTTMEFVVEI LTEIFMLGQE QAVAVMLLVH HEGKGLCGTY TRDIAQTKQQ QVMQRAKAEG HPLQCIVEEI // ID CH60_NEIMB Reviewed; 544 AA. AC P42385; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=63 kDa stress protein; DE AltName: Full=GSP63; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=HSP60; DE AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp63, mopA; GN OrderedLocusNames=NMB1972; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 23106 / 2996 / Serogroup B / Serotype 2b; RX PubMed=7746149; DOI=10.1111/j.1365-2958.1995.tb02242.x; RA Pannekoek Y., Dankert J., van Putten J.P.M.; RT "Construction of recombinant neisserial Hsp60 proteins and mapping of RT antigenic domains."; RL Mol. Microbiol. 15:277-285(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Prevents misfolding and promotes the refolding and CC proper assembly of unfolded polypeptides generated under stress CC conditions. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of CC 7 subunits. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z22956; CAA80532.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42301.1; -; Genomic_DNA. DR PIR; C81021; C81021. DR PIR; S61303; S61303. DR RefSeq; NP_274966.1; NC_003112.2. DR RefSeq; WP_002214867.1; NC_003112.2. DR ProteinModelPortal; P42385; -. DR SMR; P42385; 2-525. DR STRING; 122586.NMB1972; -. DR PaxDb; P42385; -. DR PRIDE; P42385; -. DR EnsemblBacteria; AAF42301; AAF42301; NMB1972. DR GeneID; 904169; -. DR KEGG; nme:NMB1972; -. DR PATRIC; 20360019; VBINeiMen85645_2514. DR eggNOG; ENOG4105CJ9; Bacteria. DR eggNOG; COG0459; LUCA. DR HOGENOM; HOG000076290; -. DR KO; K04077; -. DR OMA; IHQGKIS; -. DR OrthoDB; EOG6JDWBZ; -. DR BioCyc; NMEN122586:GHGG-2029-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 544 60 kDa chaperonin. FT /FTId=PRO_0000063460. FT CONFLICT 129 129 D -> E (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 214 214 A -> G (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 224 224 D -> E (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 239 239 Q -> K (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 253 253 D -> N (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 299 299 V -> T (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 308 308 S -> F (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 316 316 D -> N (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 346 346 V -> F (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 396 396 V -> L (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 436 436 Q -> K (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 450 450 P -> S (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 527 527 D -> N (in Ref. 1; CAA80532). FT {ECO:0000305}. FT CONFLICT 531 531 V -> M (in Ref. 1; CAA80532). FT {ECO:0000305}. SQ SEQUENCE 544 AA; 57423 MW; BC619AAB9B5701C1 CRC64; MAAKDVQFGN EVRQKMVNGV NILANAVRVT LGPKGRNVVV DRAFGGPHIT KDGVTVAKEI ELKDKFENMG AQMVKEVASK TNDVAGDGTT TATVLAQSIV AEGMKYVTAG MNPTDLKRGI DKAVAALVDE LKNIAKPCDT SKEIAQVGSI SANSDEQVGA IIAEAMEKVG KEGVITVEDG KSLENELDVV EGMQFDRGYL SPYFINDAEK QIAALDNPFV LLFDKKISNI RDLLPVLEQV AKASRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKAMLQ DIAILTGGVV ISEEVGLSLE KATLDDLGQA KRIEIGKENT TIIDGFGDAA QIEARVAEIR QQIETATSDY DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVEDAL HATRAAVEEG VVAGGGVALL RARAALENLH TGNADQDAGV QIVLRAVESP LRQIVANAGG EPSVVVNKVL EGKGNYGYNA GSGEYGDMIE MGVLDPAKVT RSALQHAASI AGLMLTTDCM IAEIPEDKPA VPDMGGMGGM GGMM // ID COAD_NEIMB Reviewed; 170 AA. AC P63817; Q9JQY9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; Synonyms=kdtB; GN OrderedLocusNames=NMB2019; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC {ECO:0000255|HAMAP-Rule:MF_00151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42342.1; -; Genomic_DNA. DR PIR; F81014; F81014. DR RefSeq; NP_275011.1; NC_003112.2. DR RefSeq; WP_002218149.1; NC_003112.2. DR ProteinModelPortal; P63817; -. DR STRING; 122586.NMB2019; -. DR PaxDb; P63817; -. DR EnsemblBacteria; AAF42342; AAF42342; NMB2019. DR GeneID; 904092; -. DR KEGG; nme:NMB2019; -. DR PATRIC; 20360151; VBINeiMen85645_2575. DR eggNOG; ENOG4108ZEF; Bacteria. DR eggNOG; COG0669; LUCA. DR HOGENOM; HOG000006518; -. DR KO; K00954; -. DR OMA; RHKQKLG; -. DR OrthoDB; EOG6MH5J7; -. DR BioCyc; NMEN122586:GHGG-2081-MONOMER; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 170 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_0000156244. SQ SEQUENCE 170 AA; 19543 MW; 9AA14A7506B9B377 CRC64; MLPNTPRRAV YAGSFDPPTL GHLWMIRQAQ SMFDELIVAI GINPDKRSTY TVAERQDMLC DITKMFPNVR TDVFENRFLV HYAREVDAGF IVRGIRSASD YEYERSMRHI NSDLAPEIST VFLMPPREIA EVSSTMVKGL VGPEGWTETI HRYVPQAVYE KILAEHQHEN // ID CLPP_NEIMB Reviewed; 204 AA. AC Q9JZ38; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 11-MAY-2016, entry version 103. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444}; DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444}; DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; GN OrderedLocusNames=NMB1312; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cleaves peptides in various proteins in a process that CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a CC major role in the degradation of misfolded proteins. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- CC and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP- CC Rule:MF_00444}. CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings CC which stack back to back to give a disk-like structure with a CC central cavity, resembling the structure of eukaryotic CC proteasomes. {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41687.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41687.1; ALT_INIT; Genomic_DNA. DR PIR; F81098; F81098. DR RefSeq; NP_274331.1; NC_003112.2. DR RefSeq; WP_010980918.1; NC_003112.2. DR PDB; 5DKP; X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-204. DR PDBsum; 5DKP; -. DR ProteinModelPortal; Q9JZ38; -. DR SMR; Q9JZ38; 7-199. DR STRING; 122586.NMB1312; -. DR MEROPS; S14.001; -. DR PaxDb; Q9JZ38; -. DR EnsemblBacteria; AAF41687; AAF41687; NMB1312. DR GeneID; 903734; -. DR KEGG; nme:NMB1312; -. DR PATRIC; 20358269; VBINeiMen85645_1646. DR eggNOG; ENOG4105CCQ; Bacteria. DR eggNOG; COG0740; LUCA. DR HOGENOM; HOG000285833; -. DR KO; K01358; -. DR OMA; TAGAKGH; -. DR OrthoDB; EOG6Z3KQ0; -. DR BioCyc; NMEN122586:GHGG-1350-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00444; ClpP; 1. DR InterPro; IPR001907; ClpP. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR033135; ClpP_His_AS. DR InterPro; IPR018215; ClpP_Ser_AS. DR PANTHER; PTHR10381; PTHR10381; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Protease; KW Reference proteome; Serine protease. FT CHAIN 1 204 ATP-dependent Clp protease proteolytic FT subunit. FT /FTId=PRO_0000179602. FT ACT_SITE 102 102 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00444}. FT ACT_SITE 127 127 {ECO:0000255|HAMAP-Rule:MF_00444}. FT STRAND 10 13 {ECO:0000244|PDB:5DKP}. FT STRAND 20 23 {ECO:0000244|PDB:5DKP}. FT HELIX 24 29 {ECO:0000244|PDB:5DKP}. FT TURN 30 32 {ECO:0000244|PDB:5DKP}. FT STRAND 33 40 {ECO:0000244|PDB:5DKP}. FT HELIX 42 58 {ECO:0000244|PDB:5DKP}. FT STRAND 60 62 {ECO:0000244|PDB:5DKP}. FT STRAND 64 70 {ECO:0000244|PDB:5DKP}. FT HELIX 75 87 {ECO:0000244|PDB:5DKP}. FT STRAND 88 90 {ECO:0000244|PDB:5DKP}. FT STRAND 92 101 {ECO:0000244|PDB:5DKP}. FT HELIX 103 109 {ECO:0000244|PDB:5DKP}. FT STRAND 116 118 {ECO:0000244|PDB:5DKP}. FT STRAND 123 126 {ECO:0000244|PDB:5DKP}. FT HELIX 139 164 {ECO:0000244|PDB:5DKP}. FT HELIX 168 174 {ECO:0000244|PDB:5DKP}. FT STRAND 179 182 {ECO:0000244|PDB:5DKP}. FT HELIX 183 189 {ECO:0000244|PDB:5DKP}. FT STRAND 193 195 {ECO:0000244|PDB:5DKP}. SQ SEQUENCE 204 AA; 22704 MW; C99673795060F9C8 CRC64; MSFDNYLVPT VIEQSGRGER AFDIYSRLLK ERIVFLVGPV TDESANLVVA QLLFLESENP DKDIFFYINS PGGSVTAGMS IYDTMNFIKP DVSTLCLGQA ASMGAFLLSA GEKGKRFALP NSRIMIHQPL ISGGLGGQAS DIEIHARELL KIKEKLNRLM AKHCDRDLAD LERDTDRDNF MSAEEAKEYG LIDQILENRA SLRL // ID COAE_NEIMB Reviewed; 210 AA. AC Q4W580; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376}; DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376}; DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376}; GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; GN OrderedLocusNames=NMB0331; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group CC of dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP- CC Rule:MF_00376}. CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA. CC {ECO:0000255|HAMAP-Rule:MF_00376}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}. CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP- CC Rule:MF_00376}. CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain. CC {ECO:0000255|HAMAP-Rule:MF_00376}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52165.1; -; Genomic_DNA. DR RefSeq; NP_273380.1; NC_003112.2. DR RefSeq; WP_002224873.1; NC_003112.2. DR ProteinModelPortal; Q4W580; -. DR STRING; 122586.NMB0331; -. DR PaxDb; Q4W580; -. DR EnsemblBacteria; AAY52165; AAY52165; NMB0331. DR GeneID; 903204; -. DR KEGG; nme:NMB0331; -. DR PATRIC; 20355801; VBINeiMen85645_0419. DR eggNOG; ENOG4108ZQD; Bacteria. DR eggNOG; COG0237; LUCA. DR HOGENOM; HOG000020769; -. DR KO; K00859; -. DR OMA; GGKKRYP; -. DR OrthoDB; EOG6HTP3H; -. DR BioCyc; NMEN122586:GHGG-352-MONOMER; -. DR UniPathway; UPA00241; UER00356. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1. DR InterPro; IPR001977; Depp_CoAkinase. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01121; CoaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00152; TIGR00152; 1. DR PROSITE; PS51219; DPCK; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 210 Dephospho-CoA kinase. FT /FTId=PRO_0000172968. FT DOMAIN 4 202 DPCK. {ECO:0000255|HAMAP-Rule:MF_00376}. FT NP_BIND 9 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00376}. SQ SEQUENCE 210 AA; 22904 MW; 411B19655C2285F8 CRC64; MTVWVGLTGG IGSGKSAAAQ CFADLGVPRI DADAAAHSLT ASDGIALPEI RRLFGDTVFD TQGLLRRDIL RKEVFASPSR KALLESVMLP LIFSEIKKQQ ETFTDAAYGI VEIPLLTEKR QFISLIRRVL TISAPVEKRI GRVMARSGLT RGEVAAVISH QASESERLLL ADDVLLNDGS LKSLREKTMR LHAFYSGIFA SKPTQGKHND // ID CTRC_NEIMB Reviewed; 265 AA. AC P32015; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 97. DE RecName: Full=Capsule polysaccharide export inner-membrane protein CtrC; GN Name=ctrC; OrderedLocusNames=NMB0073; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=1659649; DOI=10.1111/j.1365-2958.1991.tb01899.x; RA Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C.; RT "Evidence for a common molecular origin of the capsule gene loci in RT Gram-negative bacteria expressing group II capsular polysaccharides."; RL Mol. Microbiol. 5:1251-1263(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May form an ATP-driven capsule polysaccharide export CC apparatus, in association with the CtrB and CtrD proteins. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57677; AAA25452.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40540.1; -; Genomic_DNA. DR PIR; G81241; G81241. DR PIR; S15222; S15222. DR RefSeq; NP_273137.1; NC_003112.2. DR RefSeq; WP_002215286.1; NC_003112.2. DR STRING; 122586.NMB0073; -. DR PaxDb; P32015; -. DR EnsemblBacteria; AAF40540; AAF40540; NMB0073. DR GeneID; 902179; -. DR KEGG; nme:NMB0073; -. DR PATRIC; 20355147; VBINeiMen85645_0107. DR eggNOG; ENOG4108RDB; Bacteria. DR eggNOG; COG1682; LUCA. DR HOGENOM; HOG000256597; -. DR KO; K09688; -. DR OMA; EMFRHGY; -. DR OrthoDB; EOG6S26CK; -. DR BioCyc; NMEN122586:GHGG-79-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR000412; ABC_2_transport. DR PANTHER; PTHR30413; PTHR30413; 1. DR Pfam; PF01061; ABC2_membrane; 1. DR PRINTS; PR00164; ABC2TRNSPORT. DR PROSITE; PS51012; ABC_TM2; 1. PE 3: Inferred from homology; KW Capsule biogenesis/degradation; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Polysaccharide transport; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 265 Capsule polysaccharide export inner- FT membrane protein CtrC. FT /FTId=PRO_0000182980. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 67 84 Helical. {ECO:0000255}. FT TRANSMEM 121 141 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT DOMAIN 37 258 ABC transmembrane type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00442}. FT CONFLICT 61 61 R -> K (in Ref. 1; AAA25452). FT {ECO:0000305}. SQ SEQUENCE 265 AA; 30196 MW; FD117A37E0B16A09 CRC64; MKALHKTSFW ESLAIQRRVI GALLMREIIT RYGRNNIGFL WLFVEPLLMT FVIVLMWKFL RADRYSTLNI VAFAITGYPM LMMWRNASKR AVGSISSNAS LLYHRNVRVL DTILARMILE IAGATIAQIV IMAVLIAIGW IEMPADMFYM LMAWLLMAFF AIGLGLVICS IAFNFEPFGK IWGTLTFVMM PLSGAFFFVH NLPPKVQEYA LMIPMVHGTE MFRAGYFGSD VITYENPWYI VLCNLVLLLF GLAMVSKFSK GVEPQ // ID CRCB_NEIMB Reviewed; 119 AA. AC Q9JZG6; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN Name=crcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=NMB1065; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Important for reducing fluoride concentration in the CC cell, thus reducing its toxicity. {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SIMILARITY: Belongs to the CrcB (TC 9.B.71) family. CC {ECO:0000255|HAMAP-Rule:MF_00454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41461.1; -; Genomic_DNA. DR PIR; C81125; C81125. DR RefSeq; NP_274098.1; NC_003112.2. DR RefSeq; WP_002225263.1; NC_003112.2. DR STRING; 122586.NMB1065; -. DR PaxDb; Q9JZG6; -. DR EnsemblBacteria; AAF41461; AAF41461; NMB1065. DR GeneID; 903482; -. DR KEGG; nme:NMB1065; -. DR PATRIC; 20357675; VBINeiMen85645_1354. DR eggNOG; ENOG41084A1; Bacteria. DR eggNOG; COG0239; LUCA. DR HOGENOM; HOG000052572; -. DR KO; K06199; -. DR OMA; IPWGTLA; -. DR OrthoDB; EOG6HXJC8; -. DR BioCyc; NMEN122586:GHGG-1102-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00454; CrcB; 1. DR InterPro; IPR003691; CrcB. DR Pfam; PF02537; CRCB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 119 Putative fluoride ion transporter CrcB. FT /FTId=PRO_0000110141. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 30 50 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 59 79 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 97 117 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. SQ SEQUENCE 119 AA; 12474 MW; D651C88215B9B80B CRC64; MLSNIIPLSI GAALGATARW LLNLAVPASI PPATGNLFAN WIGAFLIGIF AETVNHPQWK LLLITGFLGS LTTLSGFSLE TVTLLQLNRP ASALANIFLH TAGSLLLTWL GLKIGAAVK // ID CTRB_NEIMB Reviewed; 387 AA. AC P32014; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Capsule polysaccharide export inner-membrane protein CtrB; GN Name=ctrB; OrderedLocusNames=NMB0072; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=1659649; DOI=10.1111/j.1365-2958.1991.tb01899.x; RA Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C.; RT "Evidence for a common molecular origin of the capsule gene loci in RT Gram-negative bacteria expressing group II capsular polysaccharides."; RL Mol. Microbiol. 5:1251-1263(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May form an ATP-driven capsule polysaccharide export CC apparatus, in association with the CtrC and CtrD proteins. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the BexC/CtrB/KpsE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57677; AAA25451.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40539.1; -; Genomic_DNA. DR PIR; S15221; S15221. DR RefSeq; NP_273136.1; NC_003112.2. DR RefSeq; WP_002215287.1; NC_003112.2. DR STRING; 122586.NMB0072; -. DR TCDB; 8.A.4.2.1; the cytoplasmic membrane-periplasmic auxiliary-2 (mpa2) family. DR PaxDb; P32014; -. DR EnsemblBacteria; AAF40539; AAF40539; NMB0072. DR GeneID; 902178; -. DR KEGG; nme:NMB0072; -. DR PATRIC; 20355145; VBINeiMen85645_0106. DR eggNOG; ENOG4105ECX; Bacteria. DR eggNOG; COG3524; LUCA. DR HOGENOM; HOG000256608; -. DR KO; K10107; -. DR OMA; EHEIVEQ; -. DR OrthoDB; EOG6W19DX; -. DR BioCyc; NMEN122586:GHGG-78-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:GOC. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015542; F:sugar efflux transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006859; P:extracellular carbohydrate transport; IEA:InterPro. DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW. DR InterPro; IPR005705; BexC_CtrB_KpsE_VexD. DR TIGRFAMs; TIGR01010; BexC_CtrB_KpsE; 1. PE 3: Inferred from homology; KW Capsule biogenesis/degradation; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Polysaccharide transport; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 387 Capsule polysaccharide export inner- FT membrane protein CtrB. FT /FTId=PRO_0000079498. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. SQ SEQUENCE 387 AA; 43392 MW; 8C20C87431DF951E CRC64; MSEQLPVAVA TETKAERKKP KKKSWIKKLS PLFWVTVIIP TVISLVYFGF FASDRFTSQS SFVVRSPKSQ SSLNGLGAIL QGTGFARAQD DIYTVGEYMR SRSSLDELRK ILPVREFYET KGDAFSRFNG FGFRGEEEAF YQYYKNQVMI NFDTVSGIST LNVTSFDALE SKKINEALLK QGEALINQLN DRARADTVRY AEEVVKTAAE RVKEASQNLT DYRIANGVFD LKAQSEVQMG LVSKLQDELI VIQTQLDQVK AVTPENPQIP GLQAREQSLR KEIDQQLRAI SGGGHSSLSN QAAEYQRVYL ENQLAEQQLA AAMTSLESAK VEADRQQLYL EVISQPSLPD LAHEPKRLYN IVATLIIGLM VYGILSLLTA SIREHKN // ID CTRD_NEIMB Reviewed; 216 AA. AC P32016; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=Capsule polysaccharide export ATP-binding protein CtrD; DE EC=3.6.3.38; DE AltName: Full=Capsular-polysaccharide-transporting ATPase; GN Name=ctrD; OrderedLocusNames=NMB0074; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=1659649; DOI=10.1111/j.1365-2958.1991.tb01899.x; RA Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C.; RT "Evidence for a common molecular origin of the capsule gene loci in RT Gram-negative bacteria expressing group II capsular polysaccharides."; RL Mol. Microbiol. 5:1251-1263(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Putative ATP-binding protein, and an energy-coupling CC component of capsule polysaccharide export apparatus. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + capsular polysaccharide(In) = CC ADP + phosphate + capsular polysaccharide(Out). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57677; AAA25453.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40541.1; -; Genomic_DNA. DR PIR; H81241; H81241. DR PIR; S15223; S15223. DR RefSeq; NP_273138.1; NC_003112.2. DR RefSeq; WP_002224750.1; NC_003112.2. DR ProteinModelPortal; P32016; -. DR STRING; 122586.NMB0074; -. DR PaxDb; P32016; -. DR EnsemblBacteria; AAF40541; AAF40541; NMB0074. DR GeneID; 902180; -. DR KEGG; nme:NMB0074; -. DR PATRIC; 20355149; VBINeiMen85645_0108. DR eggNOG; ENOG4105EY8; Bacteria. DR eggNOG; COG1134; LUCA. DR KO; K09689; -. DR OMA; KEYHEET; -. DR OrthoDB; EOG6FBX10; -. DR BioCyc; NMEN122586:GHGG-80-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015436; F:capsular-polysaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Capsule biogenesis/degradation; Cell inner membrane; KW Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Polysaccharide transport; Reference proteome; KW Sugar transport; Transport. FT CHAIN 1 216 Capsule polysaccharide export ATP-binding FT protein CtrD. FT /FTId=PRO_0000092237. FT DOMAIN 2 215 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT CONFLICT 10 17 RYLTRQGW -> QYQMRGGM (in Ref. 1; FT AAA25453). {ECO:0000305}. FT CONFLICT 22 22 H -> D (in Ref. 1; AAA25453). FT {ECO:0000305}. FT CONFLICT 25 29 SFKME -> NFSLQ (in Ref. 1; AAA25453). FT {ECO:0000305}. FT CONFLICT 34 34 I -> V (in Ref. 1; AAA25453). FT {ECO:0000305}. FT CONFLICT 48 48 I -> V (in Ref. 1; AAA25453). FT {ECO:0000305}. FT CONFLICT 59 59 T -> S (in Ref. 1; AAA25453). FT {ECO:0000305}. SQ SEQUENCE 216 AA; 24802 MW; 5608DEB1CABBC909 CRC64; MISVEHVSKR YLTRQGWRTV LHDISFKMEK GEKIGILGRN GAGKSTLIRL ISGVEPPTTG EIKRTMSISW PLAFSGAFQG SLTGMDNLRF ICRIYNVDID YVKAFTEEFS ELGQYLYEPV KRYSSGMKAR LAFALSLAVE FDCYLIDEVI AVGDSRFADK CKYELFEKRK DRSIILVSHS HSAMKQYCDN AMVLEKGHMY QFEDMDKAYE YYNSLP // ID CYAY_NEIMB Reviewed; 107 AA. AC P56977; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Protein CyaY; GN Name=cyaY; OrderedLocusNames=NMB1978; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42306.1; -; Genomic_DNA. DR PIR; C81020; C81020. DR RefSeq; NP_274971.1; NC_003112.2. DR RefSeq; WP_002225851.1; NC_003112.2. DR ProteinModelPortal; P56977; -. DR STRING; 122586.NMB1978; -. DR PaxDb; P56977; -. DR EnsemblBacteria; AAF42306; AAF42306; NMB1978. DR GeneID; 904161; -. DR KEGG; nme:NMB1978; -. DR PATRIC; 20360031; VBINeiMen85645_2520. DR eggNOG; ENOG4105XQ6; Bacteria. DR eggNOG; COG1965; LUCA. DR HOGENOM; HOG000190728; -. DR KO; K06202; -. DR OMA; LHQIWVA; -. DR OrthoDB; EOG6GXTXM; -. DR BioCyc; NMEN122586:GHGG-2035-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR Gene3D; 3.30.920.10; -; 1. DR HAMAP; MF_00142; CyaY; 1. DR InterPro; IPR002908; Frataxin/CyaY. DR InterPro; IPR020895; Frataxin_CS. DR PANTHER; PTHR16821; PTHR16821; 1. DR Pfam; PF01491; Frataxin_Cyay; 1. DR SMART; SM01219; Frataxin_Cyay; 1. DR SUPFAM; SSF55387; SSF55387; 1. DR TIGRFAMs; TIGR03421; FeS_CyaY; 1. DR PROSITE; PS01344; FRATAXIN_1; 1. DR PROSITE; PS50810; FRATAXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 107 Protein CyaY. FT /FTId=PRO_0000193946. SQ SEQUENCE 107 AA; 11936 MW; 1107C77D2459C881 CRC64; MMTESEFIRA SEALFEHIED QIDENGWDFD CRFAGNVLTI EAGDGAQIIV NRHTPNQELW IAAKSGGYHF AEQNGKWLAT RDGRDFYDVL NEALSAASGE AVEIAEL // ID CYSI_NEIMB Reviewed; 589 AA. AC Q9JS33; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000255|HAMAP-Rule:MF_01540}; DE Short=SiR-HP {ECO:0000255|HAMAP-Rule:MF_01540}; DE Short=SiRHP {ECO:0000255|HAMAP-Rule:MF_01540}; DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01540}; GN Name=cysI1 {ECO:0000255|HAMAP-Rule:MF_01540}; Synonyms=cysI-1; GN OrderedLocusNames=NMB1151; GN and GN Name=cysI2 {ECO:0000255|HAMAP-Rule:MF_01540}; Synonyms=cysI-2; GN OrderedLocusNames=NMB1189; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the sulfite reductase complex that CC catalyzes the 6-electron reduction of sulfite to sulfide. This is CC one of several activities required for the biosynthesis of L- CC cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 CC NADPH. {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- COFACTOR: CC Name=siroheme; Xref=ChEBI:CHEBI:60052; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540}; CC Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01540}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01540}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; CC hydrogen sulfide from sulfite (NADPH route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01540}. CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, CC the beta component is a hemoprotein. {ECO:0000255|HAMAP- CC Rule:MF_01540}. CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. {ECO:0000255|HAMAP-Rule:MF_01540}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62325.1; -; Genomic_DNA. DR EMBL; AE002098; AAF62326.1; -; Genomic_DNA. DR RefSeq; NP_274179.1; NC_003112.2. DR RefSeq; NP_274215.1; NC_003112.2. DR RefSeq; WP_002225214.1; NC_003112.2. DR ProteinModelPortal; Q9JS33; -. DR SMR; Q9JS33; 83-579. DR STRING; 122586.NMB1189; -. DR PaxDb; Q9JS33; -. DR EnsemblBacteria; AAF62325; AAF62325; NMB1151. DR EnsemblBacteria; AAF62326; AAF62326; NMB1189. DR GeneID; 903572; -. DR GeneID; 903609; -. DR KEGG; nme:NMB1151; -. DR KEGG; nme:NMB1189; -. DR PATRIC; 20357881; VBINeiMen85645_1456. DR eggNOG; ENOG4105ET1; Bacteria. DR eggNOG; COG0155; LUCA. DR HOGENOM; HOG000218418; -. DR KO; K00381; -. DR OMA; MGMTHGD; -. DR OrthoDB; EOG6W9XFB; -. DR BioCyc; NMEN122586:GHGG-1187-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1224-MONOMER; -. DR UniPathway; UPA00140; UER00207. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.480.10; -; 2. DR HAMAP; MF_01540; CysI; 1. DR InterPro; IPR011786; CysI. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 2. DR PRINTS; PR00397; SIROHAEM. DR SUPFAM; SSF55124; SSF55124; 2. DR TIGRFAMs; TIGR02041; CysI; 1. DR PROSITE; PS00365; NIR_SIR; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; Complete proteome; KW Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 589 Sulfite reductase [NADPH] hemoprotein FT beta-component. FT /FTId=PRO_0000199902. FT METAL 443 443 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 449 449 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 488 488 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. FT METAL 492 492 Iron (siroheme axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01540}. FT METAL 492 492 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01540}. SQ SEQUENCE 589 AA; 65966 MW; 4D79962B7B7B0339 CRC64; MTVQTKTKGL AWQEKPLSDN ERLKTESNFL RGTILDDLKD PLTGGFKGDN FQLIRFHGMY EQDDRDIRAE RAEAKLEPLK FMLLRCRLPG GIIKPSQWIE LDKFARENSH YRSIRLTNRQ TFQFHGVPKA KLQTMHRLLH KLGLDSIATA ADMNRNVLCT SNPIESELHR QAYEYAKKIS EHLLPRTRGY LDVWVDGKKV QSSDDFLQED EPILGKTYLP RKFKTAVVIP PLNDVDCYGN DLDFVAVSDG NGQLAGFNVL AGGGLSMEHG NTKTYPNISL ELGFVPPEHA LKAAEAVVTT QRDFGNRSDR KNARTRYTIQ NMGLDNFRAE VERRMGMPFE PVRPFKFTGR GDRIGWVKGI DGNWHLTLFI ESGRLVDEGG KQLLTGVLEI AKIHKGDFRI TANQNLIVAN VAEADKAKIE EFARTYGLIR NDVSKLRENA MSCVSFPTCP LAMAEAERVL PDFIGELDKI MAKHGTSDDY IVTRITGCPN GCGRAMLAEI GLVGKAVGRY NLHIGGDREG VRIPRLYKEN ITLPEILAEL DDLIGKWAAE RNIGEGFGDF AIRTGIVKPV LNAPVDFWDA SKAVAIARA // ID CTRA_NEIMB Reviewed; 391 AA. AC P0A0V8; P32013; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Capsule polysaccharide export outer membrane protein CtrA; DE Flags: Precursor; GN Name=ctrA; OrderedLocusNames=NMB0071; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=1659649; DOI=10.1111/j.1365-2958.1991.tb01899.x; RA Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C.; RT "Evidence for a common molecular origin of the capsule gene loci in RT Gram-negative bacteria expressing group II capsular polysaccharides."; RL Mol. Microbiol. 5:1251-1263(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1936 / Serogroup B; RX PubMed=1371768; RA Frosch M., Mueller D., Bousset K., Mueller A.; RT "Conserved outer membrane protein of Neisseria meningitidis involved RT in capsule expression."; RL Infect. Immun. 60:798-803(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in transport of capsular polysaccharides to the CC cell surface. May function as a membrane anchor for capsular CC polysaccharides. Possible porin properties. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the BexD/CtrA/VexA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40538.1; -; Genomic_DNA. DR PIR; S15220; S15220. DR RefSeq; NP_273135.1; NC_003112.2. DR RefSeq; WP_002215290.1; NC_003112.2. DR ProteinModelPortal; P0A0V8; -. DR STRING; 122586.NMB0071; -. DR PaxDb; P0A0V8; -. DR EnsemblBacteria; AAF40538; AAF40538; NMB0071. DR GeneID; 902177; -. DR KEGG; nme:NMB0071; -. DR PATRIC; 20355143; VBINeiMen85645_0105. DR eggNOG; ENOG4107V52; Bacteria. DR eggNOG; COG1596; LUCA. DR HOGENOM; HOG000256585; -. DR KO; K01991; -. DR OMA; ISIWEAP; -. DR OrthoDB; EOG632D2Q; -. DR BioCyc; NMEN122586:GHGG-77-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR InterPro; IPR003715; Poly_export. DR Pfam; PF02563; Poly_export; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Capsule biogenesis/degradation; Cell outer membrane; KW Complete proteome; Ion transport; Lipoprotein; Membrane; Palmitate; KW Polysaccharide transport; Porin; Reference proteome; Signal; KW Sugar transport; Transmembrane; Transmembrane beta strand; Transport. FT SIGNAL 1 22 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 23 391 Capsule polysaccharide export outer FT membrane protein CtrA. FT /FTId=PRO_0000025218. FT TOPO_DOM 23 33 Periplasmic. {ECO:0000255}. FT TRANSMEM 34 43 Beta stranded. {ECO:0000255}. FT TOPO_DOM 44 57 Extracellular. {ECO:0000255}. FT TRANSMEM 58 67 Beta stranded. {ECO:0000255}. FT TOPO_DOM 68 83 Periplasmic. {ECO:0000255}. FT TRANSMEM 84 93 Beta stranded. {ECO:0000255}. FT TOPO_DOM 94 117 Extracellular. {ECO:0000255}. FT TRANSMEM 118 127 Beta stranded. {ECO:0000255}. FT TOPO_DOM 128 135 Periplasmic. {ECO:0000255}. FT TRANSMEM 136 145 Beta stranded. {ECO:0000255}. FT TOPO_DOM 146 148 Extracellular. {ECO:0000255}. FT TRANSMEM 149 158 Beta stranded. {ECO:0000255}. FT TOPO_DOM 159 161 Periplasmic. {ECO:0000255}. FT TRANSMEM 162 171 Beta stranded. {ECO:0000255}. FT TOPO_DOM 172 178 Extracellular. {ECO:0000255}. FT TRANSMEM 179 188 Beta stranded. {ECO:0000255}. FT TOPO_DOM 189 391 Periplasmic. {ECO:0000255}. FT LIPID 23 23 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 23 23 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 391 AA; 41949 MW; 0F9434CF247F9FAD CRC64; MFKVKFYIRH AVLLLCGSLI VGCSAIPSSG PSAKKIVSLG QQSEVQIPEV ELIDVNHTVA QLLYKAQINQ SFTQFGDGYA SAGTLNIGDV LDIMIWEAPP AVLFGGGLSS MGSGSAHQTK LPEQLVTARG TVSVPFVGDI SVVGKTPGQV QEIIKGRLKK MANQPQVMVR LVQNNAANVS VIRAGNSVRM PLTAAGERVL DAVAAVGGST ANVQDTNVQL TRGNVVRTVA LEDLVANPRQ NILLRRGDVV TMITNPYTFT SMGAVGRTQE IGFSARGLSL SEAIGRMGGL QDRRSDARGV FVFRYTPLVE LPAERQDKWI AQGYGSEAEI PTVYRVNMAD AHSLFSMQRF PVKNKDVLYV SNAPLAEVQK FLSFVFSPVT SGANSINNLT N // ID CYSA_NEIMB Reviewed; 357 AA. AC Q9JZW0; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000255|HAMAP-Rule:MF_01701}; DE EC=3.6.3.25 {ECO:0000255|HAMAP-Rule:MF_01701}; DE AltName: Full=Sulfate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01701}; GN Name=cysA {ECO:0000255|HAMAP-Rule:MF_01701}; GN OrderedLocusNames=NMB0879; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter complex CysAWTP involved in CC sulfate/thiosulfate import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01701}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + sulfate(Out) = ADP + phosphate + CC sulfate(In). {ECO:0000255|HAMAP-Rule:MF_01701}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (CysA), two transmembrane proteins (CysT and CysW) and a solute- CC binding protein (CysP). {ECO:0000255|HAMAP-Rule:MF_01701}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01701}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01701}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Sulfate/tungstate importer (TC 3.A.1.6) family. CC {ECO:0000255|HAMAP-Rule:MF_01701}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01701}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41290.1; -; Genomic_DNA. DR PIR; B81147; B81147. DR RefSeq; NP_273920.1; NC_003112.2. DR RefSeq; WP_002225369.1; NC_003112.2. DR ProteinModelPortal; Q9JZW0; -. DR STRING; 122586.NMB0879; -. DR PaxDb; Q9JZW0; -. DR EnsemblBacteria; AAF41290; AAF41290; NMB0879. DR GeneID; 902998; -. DR KEGG; nme:NMB0879; -. DR PATRIC; 20357163; VBINeiMen85645_1095. DR eggNOG; ENOG4108IJ6; Bacteria. DR eggNOG; COG1118; LUCA. DR KO; K02045; -. DR OMA; HDDMHIT; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-915-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015419; F:sulfate transmembrane-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR014769; ABC_CysA_ATP-bd_C. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005666; Sulph_transpt1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00968; 3a0106s01; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51237; CYSA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Sulfate transport; Transport. FT CHAIN 1 357 Sulfate/thiosulfate import ATP-binding FT protein CysA. FT /FTId=PRO_0000092278. FT DOMAIN 3 237 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01701}. FT NP_BIND 35 42 ATP. {ECO:0000255|HAMAP-Rule:MF_01701}. SQ SEQUENCE 357 AA; 40185 MW; 382448A08614EE67 CRC64; MSITIQNLNK HFGNFHALKN INLNVPTGKL VSLLGPSGCG KTTLLRIIAG LENADGGNIL FDGQDVTAKH VRERKVGFVF QHYALFRHMN VFDNVAFGLT VLPKSERPSK GQIRAKVEEL LKLVQLSHLA KSYPHQLSGG QRQRIALARA LAVEPKLLLL DEPFGALDAK VRKELRTWLR DIHHNLGVTS ILVTHDQEEA LEVSDEIVVM NHGKIEQTGS AEAIYRKPEN AFVTEFLGET DAFEGRIEKG FWHYNGFAWK LDAQYKWQEQ TATGYIRPHE WQIAAEHETP MICAEIEKIH AVGALTHILV KHDKQDVHIT LAGSDAARYP IAEGKELKLI PKQVYVFSQN ELIEYSI // ID DADA_NEIMB Reviewed; 418 AA. AC Q9K1H5; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=D-amino acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01202}; DE EC=1.4.99.- {ECO:0000255|HAMAP-Rule:MF_01202}; GN Name=dadA {ECO:0000255|HAMAP-Rule:MF_01202}; GN OrderedLocusNames=NMB0176; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Oxidative deamination of D-amino acids. CC {ECO:0000255|HAMAP-Rule:MF_01202}. CC -!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + acceptor = a 2-oxo CC acid + NH(3) + reduced acceptor. {ECO:0000255|HAMAP- CC Rule:MF_01202}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01202}; CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family. CC {ECO:0000255|HAMAP-Rule:MF_01202}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40633.1; -; Genomic_DNA. DR PIR; A81228; A81228. DR RefSeq; NP_273234.1; NC_003112.2. DR RefSeq; WP_002224779.1; NC_003112.2. DR ProteinModelPortal; Q9K1H5; -. DR STRING; 122586.NMB0176; -. DR PaxDb; Q9K1H5; -. DR EnsemblBacteria; AAF40633; AAF40633; NMB0176. DR GeneID; 902283; -. DR KEGG; nme:NMB0176; -. DR PATRIC; 20355377; VBINeiMen85645_0218. DR eggNOG; ENOG4105MWK; Bacteria. DR eggNOG; COG0665; LUCA. DR HOGENOM; HOG000217450; -. DR KO; K00285; -. DR OMA; NDLYPRG; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NMEN122586:GHGG-186-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 4. DR HAMAP; MF_01202; DadA; 1. DR InterPro; IPR023080; DadA. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 3. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome. FT CHAIN 1 418 D-amino acid dehydrogenase. FT /FTId=PRO_0000166136. FT NP_BIND 3 17 FAD. {ECO:0000255|HAMAP-Rule:MF_01202}. SQ SEQUENCE 418 AA; 46535 MW; E50C13F9DFBC214D CRC64; MKVLVLGAGV AGVSSAWYLA EAGHEVTVID RAEGVAMETS FANAGQLSYG YTTPWAAPGI PTKALKWLFK SHPPLLFRPD GSLYQIEWLW QMLQNCTAAH YQTNKERMVR ISEYSREMFR RFEAQTGMNF EGRKKGTLQI FRQTKEVEAA KQDIAVLERY GVPYRRLKPE ECAEFEPALA RVTAKIAGGL HLPADATGDC RLFTENLYKL CQEKGVRFHF NQNISRIDHN GLRIKTVETE TGRFEADAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV AITRFDNRIR VGGMAELSGY EIKLPEKRRE TLALVVNDLF PEGGDLSQAS FWSGLRPMTP DSTPLIGRTR FDNLFLNTGH GTLGWTMSLG SAKLTADIVS GKDTEIRSDD LSLSRYQA // ID DAPD_NEIMB Reviewed; 273 AA. AC Q9K152; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811}; DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811}; GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811}; GN OrderedLocusNames=NMB0335; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine- CC 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6- CC oxoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC {ECO:0000255|HAMAP-Rule:MF_00811}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40778.1; -; Genomic_DNA. DR PIR; B81211; B81211. DR RefSeq; NP_273384.1; NC_003112.2. DR RefSeq; WP_002224875.1; NC_003112.2. DR ProteinModelPortal; Q9K152; -. DR SMR; Q9K152; 3-273. DR STRING; 122586.NMB0335; -. DR PaxDb; Q9K152; -. DR EnsemblBacteria; AAF40778; AAF40778; NMB0335. DR GeneID; 902450; -. DR KEGG; nme:NMB0335; -. DR PATRIC; 20355811; VBINeiMen85645_0424. DR eggNOG; ENOG4105DMJ; Bacteria. DR eggNOG; COG2171; LUCA. DR HOGENOM; HOG000003295; -. DR KO; K00674; -. DR OMA; QVPCALI; -. DR OrthoDB; EOG68H8BV; -. DR BioCyc; NMEN122586:GHGG-356-MONOMER; -. DR UniPathway; UPA00034; UER00019. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.166.10; -; 1. DR HAMAP; MF_00811; DapD; 1. DR InterPro; IPR005664; DapD_Trfase_Hexpep_rpt_fam. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR023180; THP_succinylTrfase_dom1. DR InterPro; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR19136:SF52; PTHR19136:SF52; 1. DR Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF14805; THDPS_N_2; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR00965; dapD; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Complete proteome; KW Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; KW Reference proteome; Repeat; Transferase. FT CHAIN 1 273 2,3,4,5-tetrahydropyridine-2,6- FT dicarboxylate N-succinyltransferase. FT /FTId=PRO_0000196952. FT BINDING 104 104 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00811}. FT BINDING 141 141 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00811}. SQ SEQUENCE 273 AA; 29410 MW; EF4B07681932BE55 CRC64; MSLQNIIETA FENRADITPT TVTPEVKEAV LETIRQLDSG KLRVAERLGV GEWKVNEWAK KAVLLSFRIQ DNEVLNDGVN KYFDKVPTKF ADWSEDEFKN AGFRAVPGAV ARRGSFVAKN VVLMPSYVNI GAYVDEGAMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQAAPTIIED NCFIGARSEI VEGVIVEEGS VISMGVFIGQ STKIFDRTTG EIYQGRVPAG SVVVSGSMPS KDGSHSLYCA VIVKRVDAQT RAKTSVNELL RGI // ID DBHB_NEIMB Reviewed; 89 AA. AC P64389; Q9JRI6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=DNA-binding protein HU-beta; GN Name=hupB; OrderedLocusNames=NMB1230; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Histone-like DNA-binding protein which is capable of CC wrapping DNA to stabilize it, and thus to prevent its denaturation CC under extreme environmental conditions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41611.1; -; Genomic_DNA. DR PIR; G81106; G81106. DR RefSeq; NP_274254.1; NC_003112.2. DR RefSeq; WP_002213508.1; NC_003112.2. DR ProteinModelPortal; P64389; -. DR STRING; 122586.NMB1230; -. DR PaxDb; P64389; -. DR PRIDE; P64389; -. DR EnsemblBacteria; AAF41611; AAF41611; NMB1230. DR GeneID; 903652; -. DR KEGG; nme:NMB1230; -. DR PATRIC; 20358051; VBINeiMen85645_1538. DR eggNOG; ENOG4105K70; Bacteria. DR eggNOG; COG0776; LUCA. DR HOGENOM; HOG000043828; -. DR KO; K03530; -. DR OMA; GSWSVSK; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NMEN122586:GHGG-1267-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR Gene3D; 4.10.520.10; -; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA condensation; DNA-binding; Reference proteome. FT CHAIN 1 89 DNA-binding protein HU-beta. FT /FTId=PRO_0000104952. SQ SEQUENCE 89 AA; 9348 MW; 0C1F9926C51554CA CRC64; MNKSELIEAI AQEADISKAA AQKALDATTN AVTTALKQGD TVTLVGFGTF YVGERAERQG RNPKTGEPLT IAAAKTPKFR AGKALKDAL // ID DAPE_NEIMB Reviewed; 381 AA. AC Q9JYL2; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Succinyl-diaminopimelate desuccinylase; DE Short=SDAP desuccinylase; DE EC=3.5.1.18; DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase; GN Name=dapE; OrderedLocusNames=NMB1530; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L- CC diaminopimelic acid (SDAP), forming succinate and LL-2,6- CC diaminoheptanedioate (DAP), an intermediate involved in the CC bacterial biosynthesis of lysine and meso-diaminopimelic acid, an CC essential component of bacterial cell walls. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O CC = succinate + LL-2,6-diaminoheptanedioate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16021622}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41885.1; -; Genomic_DNA. DR PIR; F81073; F81073. DR RefSeq; NP_274537.1; NC_003112.2. DR RefSeq; WP_002225058.1; NC_003112.2. DR PDB; 1VGY; X-ray; 1.90 A; A/B=2-381. DR PDB; 4O23; X-ray; 2.09 A; A/B=1-381. DR PDB; 4PPZ; X-ray; 2.00 A; A=1-381. DR PDB; 4PQA; X-ray; 1.78 A; A=1-381. DR PDBsum; 1VGY; -. DR PDBsum; 4O23; -. DR PDBsum; 4PPZ; -. DR PDBsum; 4PQA; -. DR ProteinModelPortal; Q9JYL2; -. DR SMR; Q9JYL2; 2-376. DR STRING; 122586.NMB1530; -. DR MEROPS; M20.010; -. DR PaxDb; Q9JYL2; -. DR DNASU; 904046; -. DR EnsemblBacteria; AAF41885; AAF41885; NMB1530. DR GeneID; 904046; -. DR KEGG; nme:NMB1530; -. DR PATRIC; 20358866; VBINeiMen85645_1942. DR eggNOG; ENOG4105C9Y; Bacteria. DR eggNOG; COG0624; LUCA. DR HOGENOM; HOG000243770; -. DR KO; K01439; -. DR OMA; QNDPFDA; -. DR OrthoDB; EOG60651W; -. DR BioCyc; NMEN122586:GHGG-1571-MONOMER; -. DR UniPathway; UPA00034; UER00021. DR EvolutionaryTrace; Q9JYL2; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.360; -; 1. DR HAMAP; MF_01690; DapE; 1. DR InterPro; IPR005941; DapE_proteobac. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01246; dapE_proteo; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cobalt; Complete proteome; KW Diaminopimelate biosynthesis; Hydrolase; Lysine biosynthesis; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 381 Succinyl-diaminopimelate desuccinylase. FT /FTId=PRO_0000375624. FT ACT_SITE 70 70 {ECO:0000250}. FT ACT_SITE 135 135 Proton acceptor. {ECO:0000250}. FT METAL 68 68 Cobalt or zinc 1. {ECO:0000250}. FT METAL 101 101 Cobalt or zinc 1. {ECO:0000250}. FT METAL 101 101 Cobalt or zinc 2. {ECO:0000250}. FT METAL 136 136 Cobalt or zinc 2. {ECO:0000250}. FT METAL 164 164 Cobalt or zinc 1. {ECO:0000250}. FT METAL 350 350 Cobalt or zinc 2. {ECO:0000250}. FT HELIX 5 14 {ECO:0000244|PDB:4PQA}. FT HELIX 26 35 {ECO:0000244|PDB:4PQA}. FT TURN 36 38 {ECO:0000244|PDB:4PQA}. FT STRAND 40 43 {ECO:0000244|PDB:4PQA}. FT STRAND 51 56 {ECO:0000244|PDB:4PQA}. FT STRAND 58 68 {ECO:0000244|PDB:4PQA}. FT HELIX 77 79 {ECO:0000244|PDB:4PQA}. FT STRAND 80 82 {ECO:0000244|PDB:4PQA}. FT STRAND 88 90 {ECO:0000244|PDB:4PQA}. FT STRAND 93 96 {ECO:0000244|PDB:4PQA}. FT TURN 97 102 {ECO:0000244|PDB:4PQA}. FT HELIX 103 119 {ECO:0000244|PDB:4PQA}. FT STRAND 124 133 {ECO:0000244|PDB:4PQA}. FT STRAND 135 137 {ECO:0000244|PDB:4PQA}. FT STRAND 140 142 {ECO:0000244|PDB:4PPZ}. FT HELIX 143 152 {ECO:0000244|PDB:4PQA}. FT STRAND 157 162 {ECO:0000244|PDB:4PQA}. FT STRAND 167 170 {ECO:0000244|PDB:4PQA}. FT STRAND 173 179 {ECO:0000244|PDB:4PQA}. FT STRAND 181 190 {ECO:0000244|PDB:4PQA}. FT HELIX 199 201 {ECO:0000244|PDB:4PQA}. FT HELIX 205 218 {ECO:0000244|PDB:4PQA}. FT STRAND 232 240 {ECO:0000244|PDB:4PQA}. FT STRAND 250 260 {ECO:0000244|PDB:4PQA}. FT HELIX 266 279 {ECO:0000244|PDB:4PQA}. FT STRAND 284 292 {ECO:0000244|PDB:4PQA}. FT HELIX 301 314 {ECO:0000244|PDB:4PQA}. FT STRAND 319 321 {ECO:0000244|PDB:4PQA}. FT HELIX 329 332 {ECO:0000244|PDB:4PQA}. FT TURN 333 335 {ECO:0000244|PDB:4PQA}. FT STRAND 336 341 {ECO:0000244|PDB:4PQA}. FT TURN 347 350 {ECO:0000244|PDB:4PQA}. FT STRAND 355 357 {ECO:0000244|PDB:4PQA}. FT HELIX 360 375 {ECO:0000244|PDB:4PQA}. SQ SEQUENCE 381 AA; 41325 MW; EA64C393977C48E7 CRC64; MTETQSLELA KELISRPSVT PDDRDCQKLL AERLHKIGFA AEELHFGDTK NIWLRRGTKA PVVCFAGHTD VVPTGPVEKW DSPPFEPAER DGRLYGRGAA DMKTSIACFV TACERFVAKH PNHQGSIALL ITSDEEGDAL DGTTKVVDVL KARDELIDYC IVGEPTAVDK LGDMIKNGRR GSLSGNLTVK GKQGHIAYPH LAINPVHTFA PALLELTQEV WDEGNEYFPP TSFQISNING GTGATNVIPG ELNVKFNFRF STESTEAGLK QRVHAILDKH GVQYDLQWSC SGQPFLTQAG KLTDVARAAI AETCGIEAEL STTGGTSDGR FIKAIAQELI ELGPSNATIH QINENVRLND IPKLSAVYEG ILARLLAGNA V // ID CYSG_NEIMB Reviewed; 483 AA. AC P95370; Q9JQK6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 09-DEC-2015, entry version 120. DE RecName: Full=Siroheme synthase {ECO:0000255|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01646}; DE Short=Urogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646}; DE EC=2.1.1.107 {ECO:0000255|HAMAP-Rule:MF_01646}; DE AltName: Full=SUMT {ECO:0000255|HAMAP-Rule:MF_01646}; DE AltName: Full=Uroporphyrinogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646}; DE Short=UROM {ECO:0000255|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Precorrin-2 dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01646}; DE EC=1.3.1.76 {ECO:0000255|HAMAP-Rule:MF_01646}; DE Includes: DE RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000255|HAMAP-Rule:MF_01646}; DE EC=4.99.1.4 {ECO:0000255|HAMAP-Rule:MF_01646}; GN Name=cysG {ECO:0000255|HAMAP-Rule:MF_01646}; Synonyms=cysG1; GN OrderedLocusNames=NMB1156; GN and GN Name=cysG2 {ECO:0000255|HAMAP-Rule:MF_01646}; GN OrderedLocusNames=NMB1194; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RA McVeigh T., Wilkie S.E., Woodcock S.C., Mortuza G., Peters S.E., RA Warren M.J.; RT "Sirohaem synthase from Neisseria meningitidis."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent CC methylations of uroporphyrinogen III at position C-2 and C-7 to CC form precorrin-2 via precorrin-1. Then it catalyzes the NAD- CC dependent ring dehydrogenation of precorrin-2 to yield CC sirohydrochlorin. Finally, it catalyzes the ferrochelation of CC sirohydrochlorin to yield siroheme. {ECO:0000255|HAMAP- CC Rule:MF_01646}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III CC = S-adenosyl-L-homocysteine + precorrin-1. {ECO:0000255|HAMAP- CC Rule:MF_01646}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S- CC adenosyl-L-homocysteine + precorrin-2. {ECO:0000255|HAMAP- CC Rule:MF_01646}. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; siroheme from sirohydrochlorin: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2 CC dehydrogenase / sirohydrochlorin ferrochelatase family. CC {ECO:0000255|HAMAP-Rule:MF_01646}. CC -!- SIMILARITY: In the C-terminal section; belongs to the precorrin CC methyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01646}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y10177; CAA71251.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41542.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41577.1; -; Genomic_DNA. DR PIR; D81111; D81111. DR PIR; T46867; T46867. DR RefSeq; NP_274184.1; NC_003112.2. DR RefSeq; NP_274220.1; NC_003112.2. DR RefSeq; WP_002225211.1; NC_003112.2. DR ProteinModelPortal; P95370; -. DR SMR; P95370; 1-458. DR STRING; 122586.NMB1194; -. DR PaxDb; P95370; -. DR EnsemblBacteria; AAF41542; AAF41542; NMB1156. DR EnsemblBacteria; AAF41577; AAF41577; NMB1194. DR GeneID; 903577; -. DR GeneID; 903614; -. DR KEGG; nme:NMB1156; -. DR KEGG; nme:NMB1194; -. DR PATRIC; 20357891; VBINeiMen85645_1461. DR eggNOG; ENOG4105CB8; Bacteria. DR eggNOG; COG0007; LUCA. DR eggNOG; COG1648; LUCA. DR HOGENOM; HOG000290518; -. DR KO; K02302; -. DR OMA; VPQHETN; -. DR OrthoDB; EOG6DRPFR; -. DR BioCyc; NMEN122586:GHGG-1192-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1229-MONOMER; -. DR UniPathway; UPA00148; UER00211. DR UniPathway; UPA00148; UER00222. DR UniPathway; UPA00262; UER00211. DR UniPathway; UPA00262; UER00222. DR UniPathway; UPA00262; UER00376. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC. DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.8.210; -; 1. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01646; Siroheme_synth; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR006366; CobA/CysG_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR012409; Sirohaem_synth. DR InterPro; IPR028281; Sirohaem_synthase_central. DR InterPro; IPR019478; Sirohaem_synthase_dimer_dom. DR InterPro; IPR006367; Sirohaem_synthase_N. DR InterPro; IPR003043; Uropor_MeTrfase_CS. DR Pfam; PF10414; CysG_dimeriser; 1. DR Pfam; PF13241; NAD_binding_7; 1. DR Pfam; PF14824; Sirohm_synth_M; 1. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036426; Sirohaem_synth; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1. DR TIGRFAMs; TIGR01470; cysG_Nterm; 1. DR PROSITE; PS00839; SUMT_1; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase; KW Multifunctional enzyme; NAD; Oxidoreductase; Phosphoprotein; KW Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 483 Siroheme synthase. FT /FTId=PRO_0000150382. FT NP_BIND 22 23 NAD. {ECO:0000255|HAMAP-Rule:MF_01646}. FT NP_BIND 43 44 NAD. {ECO:0000255|HAMAP-Rule:MF_01646}. FT REGION 1 203 precorrin-2 dehydrogenase / FT sirohydrochlorin ferrochelatase. FT {ECO:0000255|HAMAP-Rule:MF_01646}. FT REGION 217 483 Uroporphyrinogen-III C-methyltransferase. FT {ECO:0000255|HAMAP-Rule:MF_01646}. FT REGION 302 304 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01646}. FT REGION 332 333 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01646}. FT ACT_SITE 249 249 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT ACT_SITE 271 271 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT BINDING 226 226 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT BINDING 307 307 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT BINDING 384 384 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT BINDING 413 413 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01646}. FT MOD_RES 128 128 Phosphoserine. {ECO:0000255|HAMAP- FT Rule:MF_01646}. FT CONFLICT 475 483 GLNAGQRAA -> D (in Ref. 1; CAA71251). FT {ECO:0000305}. SQ SEQUENCE 483 AA; 52111 MW; 279C4F458B19582F CRC64; MNYFPIFANL AGRPVLVVGG GAVAARKISL LLKAGAEVRV AAKHLNAELS ALAAENKILW LAEEFRAEHI RTVFLIIAAS SDQALNRRVF HLAESCQKPV NVVDDRDHCS FIFPSVIDRN PVQIAVSSSG SAPVLARLLR ERLEALLPPS LGDMAEISGR WRDAVKGKLK SVTERRRFWE KQFNGRFAAL VKNRQNTLAE RELAGQLEQS RQNDQGGSVS LVGAGPGDAG LLTLKGLQEI QQADVVLYDA LVSDGILSLV RRDAERIFVG KRARGERTPQ EDTNALMVRL AREGRRVVRL KGGDPFVFGR GGEELETLAR HQIPFSVVPG ITAAVGATAY AGIPLTHRDY AQSAVFVTGH RKADAPDIEW QTLARSRQTL VIYMGALKAA LIAERLQQHG RSPDTPAAVI SQGTLPAQKT ATGTLANLAE LAETAPNPAL IVIGEVVGLH EKLAWFGENG EGENRVGQTY PALGGLNAGQ RAA // ID DAPB_NEIMB Reviewed; 269 AA. AC Q9K1F1; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 102. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; GN OrderedLocusNames=NMB0203; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy- CC tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6- CC dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5- CC tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC reductase (DHDPR), catalyzing the conversion of CC dihydrodipicolinate to tetrahydrodipicolinate. However, it was CC shown in E.coli that the substrate of the enzymatic reaction is CC not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy- CC 2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by CC the DapA-catalyzed reaction. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40660.1; -; Genomic_DNA. DR PIR; E81226; E81226. DR RefSeq; NP_273261.1; NC_003112.2. DR RefSeq; WP_002236618.1; NC_003112.2. DR ProteinModelPortal; Q9K1F1; -. DR SMR; Q9K1F1; 4-268. DR STRING; 122586.NMB0203; -. DR PaxDb; Q9K1F1; -. DR EnsemblBacteria; AAF40660; AAF40660; NMB0203. DR GeneID; 902311; -. DR KEGG; nme:NMB0203; -. DR PATRIC; 20355447; VBINeiMen85645_0252. DR eggNOG; ENOG4105DUK; Bacteria. DR eggNOG; COG0289; LUCA. DR HOGENOM; HOG000227153; -. DR KO; K00215; -. DR OMA; EAHHRMK; -. DR OrthoDB; EOG6SV5DS; -. DR BioCyc; NMEN122586:GHGG-214-MONOMER; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00102; DapB; 1. DR InterPro; IPR022663; DapB_C. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR022664; DapB_N_CS. DR InterPro; IPR023940; DHDPR_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR20836; PTHR20836; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF51735; SSF51735; 2. DR TIGRFAMs; TIGR00036; dapB; 1. DR PROSITE; PS01298; DAPB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 269 4-hydroxy-tetrahydrodipicolinate FT reductase. FT /FTId=PRO_0000141460. FT NP_BIND 10 15 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 99 101 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 123 126 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT REGION 166 167 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT ACT_SITE 156 156 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00102}. FT ACT_SITE 160 160 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT BINDING 36 36 NAD. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 157 157 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00102}. SQ SEQUENCE 269 AA; 28328 MW; FE180213A9C85EFF CRC64; MTPLKIAIAG ANGRMGRVLV EAVNNHPDTV LSGALEHSGS EALGLDAGYA VGLKTGIAIS DDVDAVLAQS DVLIDFTRPE PTLKHLQKCV EKQVNIIIGT TGFDDTGKAA IHTAAEKTGI VFAANFSVGV NLTFHILDTV ARVLNEGYDI EIIEGHHRHK VDAPSGTALR MGEVIAGALG RDLKQCAVYG REGHTGPRDP STIGFATVRA GDIVGDHTAL FATDGERVEI THKASSRMTF AAGAVRAAVW VNGKTGLYDM QDVLGLNNR // ID DAPF_NEIMB Reviewed; 283 AA. AC Q9K060; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Diaminopimelate epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197}; GN Name=dapF {ECO:0000255|HAMAP-Rule:MF_00197}; GN OrderedLocusNames=NMB0760; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6- CC diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- CC DAP), a precursor of L-lysine and an essential component of the CC bacterial peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000255|HAMAP-Rule:MF_00197}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41173.1; -; Genomic_DNA. DR PIR; E81161; E81161. DR RefSeq; NP_273802.1; NC_003112.2. DR RefSeq; WP_002237817.1; NC_003112.2. DR ProteinModelPortal; Q9K060; -. DR SMR; Q9K060; 4-281. DR STRING; 122586.NMB0760; -. DR PaxDb; Q9K060; -. DR EnsemblBacteria; AAF41173; AAF41173; NMB0760. DR GeneID; 902875; -. DR KEGG; nme:NMB0760; -. DR PATRIC; 20356893; VBINeiMen85645_0965. DR eggNOG; ENOG4105E4Z; Bacteria. DR eggNOG; COG0253; LUCA. DR HOGENOM; HOG000220466; -. DR KO; K01778; -. DR OMA; RFTKMQG; -. DR OrthoDB; EOG6ND0M5; -. DR BioCyc; NMEN122586:GHGG-791-MONOMER; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00197; DAP_epimerase; 1. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR PANTHER; PTHR31689; PTHR31689; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR TIGRFAMs; TIGR00652; DapF; 1. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Disulfide bond; KW Isomerase; Lysine biosynthesis; Reference proteome. FT CHAIN 1 283 Diaminopimelate epimerase. FT /FTId=PRO_0000149856. FT REGION 11 12 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 76 78 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 215 216 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 225 226 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT ACT_SITE 76 76 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT ACT_SITE 224 224 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT BINDING 14 14 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 47 47 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 67 67 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 197 197 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT SITE 166 166 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT SITE 215 215 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT DISULFID 76 224 SQ SEQUENCE 283 AA; 30393 MW; 08606A71DACED40B CRC64; MNTLKFTKMH GLGNDFMVID AVSQDFTPED APIAEWADRF RGVGFDQLLV VGRSETEGVD FRYRIFNADG SEVGQCGNGA RCFARFVADK GLTDKKEICV ETANGVIFPK LSDNGMVTVN MGKPKFMPSE IPFVPESGEG DDACIYGVHL ESGIQPVSCV NMGNPHAVIV VDDVECAPVR ETGSLIEPHR QFPERVNVGF MQVVGRTAIR LRVFERGVGE TQACGTGACA AVVAGIRLGL LDEGKTVEVV LPGGTLYIEW ACGGDVMMTG PAEAVFEGEL AYS // ID DDL_NEIMB Reviewed; 304 AA. AC Q9K0Y0; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; OrderedLocusNames=NMB0424; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D- CC alanyl-D-alanine. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00047}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40862.1; -; Genomic_DNA. DR PIR; C81201; C81201. DR RefSeq; NP_273472.1; NC_003112.2. DR RefSeq; WP_002223420.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y0; -. DR STRING; 122586.NMB0424; -. DR PaxDb; Q9K0Y0; -. DR EnsemblBacteria; AAF40862; AAF40862; NMB0424. DR GeneID; 902540; -. DR KEGG; nme:NMB0424; -. DR PATRIC; 20356046; VBINeiMen85645_0538. DR eggNOG; ENOG4105CPF; Bacteria. DR eggNOG; COG1181; LUCA. DR HOGENOM; HOG000011592; -. DR KO; K01921; -. DR OMA; NREIRFR; -. DR OrthoDB; EOG6ND0KB; -. DR BioCyc; NMEN122586:GHGG-448-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 304 D-alanine--D-alanine ligase. FT /FTId=PRO_0000177846. FT DOMAIN 103 299 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00047}. FT NP_BIND 129 184 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 253 253 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 266 266 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 266 266 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 268 268 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. SQ SEQUENCE 304 AA; 32554 MW; 66EFFD137C2B0BB0 CRC64; MQNFGKVAVL MGGFSSEREI SLDSGTAILN ALKSKGIDAY AFDPKETPLS ELKAQGFQTA FNILHGTYGE DGAVQGALEL LGIPYTGSGV AASAIGMDKY RCKLIWQALG LPVPEFAVLH DDTDFDAVEE KLGLPMFVKP AAEGSSVGVV KVKGKGRLKS VYEELKHLQG EIIAERFIGG GEYSCPVLNG KGLPGIHIIP ATEFYDYEAK YNRDDTIYQC PSEDLTEAEE SLMRELAVRG AQAIGAEGCV RVDFLKDTDG KLYLLEINTL PGMTSHSLVP KSAAVTGVGF ADLCIEILKT AHVG // ID CYSH_NEIMB Reviewed; 246 AA. AC Q9JRT1; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063}; DE EC=1.8.4.8 {ECO:0000255|HAMAP-Rule:MF_00063}; DE AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063}; DE AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000255|HAMAP-Rule:MF_00063}; DE AltName: Full=PAPS sulfotransferase {ECO:0000255|HAMAP-Rule:MF_00063}; DE AltName: Full=PAdoPS reductase {ECO:0000255|HAMAP-Rule:MF_00063}; GN Name=cysH1 {ECO:0000255|HAMAP-Rule:MF_00063}; GN OrderedLocusNames=NMB1155; GN and GN Name=cysH2 {ECO:0000255|HAMAP-Rule:MF_00063}; GN OrderedLocusNames=NMB1193; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Reduction of activated sulfate into sulfite. CC {ECO:0000255|HAMAP-Rule:MF_00063}. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + sulfite + CC thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. CC {ECO:0000255|HAMAP-Rule:MF_00063}. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00063}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063}. CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00063}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41541.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41576.1; -; Genomic_DNA. DR PIR; C81111; C81111. DR RefSeq; NP_274183.1; NC_003112.2. DR RefSeq; NP_274219.1; NC_003112.2. DR RefSeq; WP_002232454.1; NC_003112.2. DR ProteinModelPortal; Q9JRT1; -. DR STRING; 122586.NMB1193; -. DR PaxDb; Q9JRT1; -. DR EnsemblBacteria; AAF41541; AAF41541; NMB1155. DR EnsemblBacteria; AAF41576; AAF41576; NMB1193. DR GeneID; 903576; -. DR GeneID; 903613; -. DR KEGG; nme:NMB1155; -. DR KEGG; nme:NMB1193; -. DR PATRIC; 20357889; VBINeiMen85645_1460. DR eggNOG; ENOG4105ET3; Bacteria. DR eggNOG; COG0175; LUCA. DR HOGENOM; HOG000249395; -. DR KO; K00390; -. DR OMA; HLINQVN; -. DR OrthoDB; EOG6V1M7D; -. DR BioCyc; NMEN122586:GHGG-1191-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1228-MONOMER; -. DR UniPathway; UPA00140; UER00206. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00063; CysH; 1. DR InterPro; IPR011798; APS_reductase. DR InterPro; IPR004511; PAPS/APS_Rdtase. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01507; PAPS_reduct; 1. DR PIRSF; PIRSF000857; PAPS_reductase; 1. DR TIGRFAMs; TIGR02055; APS_reductase; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Oxidoreductase; Reference proteome. FT CHAIN 1 246 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_0000100636. SQ SEQUENCE 246 AA; 28091 MW; FAD0206EF23FEB98 CRC64; METTLFKPAL WQIPHIGSGG ETALAEKTET LKQRLHRIVG SHRDARFASS LAAEDMVITD LIAGENLNIG IFTLDTGLLH TETLNLLDRL GRAYPHLRIK RFRPVREDAD RYVESKGRFA FYDSVEARRE CCRIRKTEPL NRAIAGADAW LTGQRREQSA TRTELPFAEY DAGRGIGKYN PIFDWSEHDV WAYILANNVP YNDLYRQGFP SIGCDPCTRP VKAGEDIRAG RWWWEGRNSK ECGLHK // ID DCD_NEIMB Reviewed; 188 AA. AC P63904; Q9JRE8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146}; DE Short=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146}; DE EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146}; GN Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; OrderedLocusNames=NMB0849; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: dCTP + H(2)O = dUTP + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. CC {ECO:0000255|HAMAP-Rule:MF_00146}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41260.1; -; Genomic_DNA. DR PIR; D81149; D81149. DR RefSeq; NP_273890.1; NC_003112.2. DR RefSeq; WP_002224592.1; NC_003112.2. DR ProteinModelPortal; P63904; -. DR STRING; 122586.NMB0849; -. DR PaxDb; P63904; -. DR EnsemblBacteria; AAF41260; AAF41260; NMB0849. DR GeneID; 902963; -. DR KEGG; nme:NMB0849; -. DR PATRIC; 20357089; VBINeiMen85645_1063. DR eggNOG; ENOG4105DHP; Bacteria. DR eggNOG; COG0717; LUCA. DR HOGENOM; HOG000228600; -. DR KO; K01494; -. DR OMA; MEYFRIP; -. DR OrthoDB; EOG67DPKR; -. DR BioCyc; NMEN122586:GHGG-880-MONOMER; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. DR InterPro; IPR011962; dCTP_deam. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR008180; dUTPase/dCTP_deaminase. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR02274; dCTP_deam; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Nucleotide metabolism; KW Reference proteome. FT CHAIN 1 188 Deoxycytidine triphosphate deaminase. FT /FTId=PRO_0000155999. SQ SEQUENCE 188 AA; 21295 MW; 2CA4459F4E78FDF6 CRC64; MSIKSDKWIR RMSEEFGMID PFEPNQIKEA DGKRIISYGT SSYGYDIRCA NEFKIFTNIN STIVDPKNFD PKNFVTVEDD CCIIPPNSFA LARTVEYFRI PRNVLTVCLG KSTYARCGII VNVTPFEPEW EGYVTLEFSN TTPLPAKIYA GEGVAQVLFF ESDEICETSY KDRNGKYMGQ TGVTLPKA // ID DEF_NEIMB Reviewed; 167 AA. AC P63916; Q9JQN0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Peptide deformylase {ECO:0000255|HAMAP-Rule:MF_00163}; DE Short=PDF {ECO:0000255|HAMAP-Rule:MF_00163}; DE EC=3.5.1.88 {ECO:0000255|HAMAP-Rule:MF_00163}; DE AltName: Full=Polypeptide deformylase {ECO:0000255|HAMAP-Rule:MF_00163}; GN Name=def {ECO:0000255|HAMAP-Rule:MF_00163}; OrderedLocusNames=NMB0110; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Removes the formyl group from the N-terminal Met of CC newly synthesized proteins. Requires at least a dipeptide for an CC efficient rate of reaction. N-terminal L-methionine is a CC prerequisite for activity but the enzyme has broad specificity at CC other positions. {ECO:0000255|HAMAP-Rule:MF_00163}. CC -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate + CC methionyl peptide. {ECO:0000255|HAMAP-Rule:MF_00163}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00163}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000255|HAMAP-Rule:MF_00163}; CC -!- SIMILARITY: Belongs to the polypeptide deformylase family. CC {ECO:0000255|HAMAP-Rule:MF_00163}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40569.1; -; Genomic_DNA. DR PIR; E81238; E81238. DR RefSeq; NP_273168.1; NC_003112.2. DR RefSeq; WP_002216218.1; NC_003112.2. DR ProteinModelPortal; P63916; -. DR SMR; P63916; 2-165. DR STRING; 122586.NMB0110; -. DR PaxDb; P63916; -. DR EnsemblBacteria; AAF40569; AAF40569; NMB0110. DR GeneID; 902214; -. DR KEGG; nme:NMB0110; -. DR PATRIC; 20355233; VBINeiMen85645_0150. DR eggNOG; ENOG4108Z02; Bacteria. DR eggNOG; COG0242; LUCA. DR HOGENOM; HOG000243509; -. DR KO; K01462; -. DR OMA; FDTMYEE; -. DR OrthoDB; EOG664CMF; -. DR BioCyc; NMEN122586:GHGG-116-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.45.10; -; 1. DR HAMAP; MF_00163; Pep_deformylase; 1. DR InterPro; IPR000181; Fmet_deformylase. DR InterPro; IPR023635; Peptide_deformylase. DR PANTHER; PTHR10458; PTHR10458; 1. DR Pfam; PF01327; Pep_deformylase; 1. DR PIRSF; PIRSF004749; Pep_def; 1. DR PRINTS; PR01576; PDEFORMYLASE. DR SUPFAM; SSF56420; SSF56420; 1. DR TIGRFAMs; TIGR00079; pept_deformyl; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Iron; Metal-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 167 Peptide deformylase. FT /FTId=PRO_0000082808. FT ACT_SITE 134 134 {ECO:0000255|HAMAP-Rule:MF_00163}. FT METAL 91 91 Iron. {ECO:0000255|HAMAP-Rule:MF_00163}. FT METAL 133 133 Iron. {ECO:0000255|HAMAP-Rule:MF_00163}. FT METAL 137 137 Iron. {ECO:0000255|HAMAP-Rule:MF_00163}. SQ SEQUENCE 167 AA; 19115 MW; F579BEAFD6AFA4B5 CRC64; MALLNILQYP DERLHTVAKP VEQVDERIRK LIADMFETMY ESRGIGLAAT QVDVHERVVV MDLTEDRSEP RVFINPVIVE KDGETTYEEG CLSVPGIYDT VTRAERVKVE ALNEKGEKFT LEADGLLAIC VQHELDHLMG IVFVERLSQL KQGRIKTKLK KRQKHTI // ID DCUP_NEIMB Reviewed; 354 AA. AC Q9K041; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000255|HAMAP-Rule:MF_00218}; DE Short=UPD {ECO:0000255|HAMAP-Rule:MF_00218}; DE Short=URO-D {ECO:0000255|HAMAP-Rule:MF_00218}; DE EC=4.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00218}; GN Name=hemE {ECO:0000255|HAMAP-Rule:MF_00218}; GN OrderedLocusNames=NMB0781; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of CC uroporphyrinogen-III to yield coproporphyrinogen-III. CC {ECO:0000255|HAMAP-Rule:MF_00218}. CC -!- CATALYTIC ACTIVITY: Uroporphyrinogen III = coproporphyrinogen + 4 CC CO(2). {ECO:0000255|HAMAP-Rule:MF_00218}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 4/4. {ECO:0000255|HAMAP-Rule:MF_00218}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00218}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00218}. CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family. CC {ECO:0000255|HAMAP-Rule:MF_00218}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41194.1; -; Genomic_DNA. DR PIR; B81158; B81158. DR RefSeq; NP_273823.1; NC_003112.2. DR RefSeq; WP_002222724.1; NC_003112.2. DR ProteinModelPortal; Q9K041; -. DR STRING; 122586.NMB0781; -. DR PaxDb; Q9K041; -. DR EnsemblBacteria; AAF41194; AAF41194; NMB0781. DR GeneID; 902896; -. DR KEGG; nme:NMB0781; -. DR PATRIC; 20356941; VBINeiMen85645_0989. DR eggNOG; ENOG4105CFZ; Bacteria. DR eggNOG; COG0407; LUCA. DR HOGENOM; HOG000253896; -. DR KO; K01599; -. DR OMA; GSSKDFR; -. DR OrthoDB; EOG6VXF6H; -. DR BioCyc; NMEN122586:GHGG-812-MONOMER; -. DR UniPathway; UPA00251; UER00321. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00218; URO_D; 1. DR InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE. DR InterPro; IPR000257; Uroporphyrinogen_deCOase. DR Pfam; PF01208; URO-D; 1. DR TIGRFAMs; TIGR01464; hemE; 1. DR PROSITE; PS00906; UROD_1; 1. DR PROSITE; PS00907; UROD_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Decarboxylase; Lyase; KW Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 354 Uroporphyrinogen decarboxylase. FT /FTId=PRO_0000187618. FT REGION 27 31 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT BINDING 46 46 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT BINDING 153 153 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT BINDING 208 208 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT BINDING 326 326 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00218}. FT SITE 77 77 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00218}. SQ SEQUENCE 354 AA; 39105 MW; 83502DF9125E4E12 CRC64; MISLKNDTFL RALLKQPVEY TPIWMMRQAG RYLPEYKATR AKAGSFLDLC KNTELATEVT IQPLERFDLD AAILFSDILT VPDAMGLGLY FAEGEGPKFK RALQHEADIA KLHVPDMEKL QYVFDAVTSI RKALDGRVPL IGFSGSPFTL ACYMVEGGGS KEFRTIKTMM YSRPDLLHKI LDTNAQAVTA YLNAQIDAGA QAVQIFDTWG GVLSDAAFKE FSLKYIRQIV AGLKRESEGR RVPVIVFAKG GGLWLESMAQ IGADALGLDW TCNIGEARRR VGKQVALQGN FDPFALFGTP ESIRTEVARI LADYGHGSGH VFNLGHGINQ HADPEHAKIL VDTVHELSRQ YHGG // ID CYSJ_NEIMB Reviewed; 604 AA. AC Q9JS45; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541}; DE Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541}; DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541}; GN Name=cysJ1 {ECO:0000255|HAMAP-Rule:MF_01541}; Synonyms=cysJ-1; GN OrderedLocusNames=NMB1152; GN and GN Name=cysJ2 {ECO:0000255|HAMAP-Rule:MF_01541}; Synonyms=cysJ-2; GN OrderedLocusNames=NMB1190; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the sulfite reductase complex that CC catalyzes the 6-electron reduction of sulfite to sulfide. This is CC one of several activities required for the biosynthesis of L- CC cysteine from sulfate. The flavoprotein component catalyzes the CC electron flow from NADPH -> FAD -> FMN to the hemoprotein CC component. {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 CC NADPH. {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541}; CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; CC hydrogen sulfide from sulfite (NADPH route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, CC the beta component is a hemoprotein. {ECO:0000255|HAMAP- CC Rule:MF_01541}. CC -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase CC flavoprotein subunit CysJ family. {ECO:0000255|HAMAP- CC Rule:MF_01541}. CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin CC family. {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000255|HAMAP-Rule:MF_01541}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. {ECO:0000255|HAMAP- CC Rule:MF_01541}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41573.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41538.1; -; Genomic_DNA. DR PIR; H81110; H81110. DR RefSeq; NP_274180.1; NC_003112.2. DR RefSeq; NP_274216.1; NC_003112.2. DR RefSeq; WP_010980903.1; NC_003112.2. DR ProteinModelPortal; Q9JS45; -. DR SMR; Q9JS45; 228-604. DR STRING; 122586.NMB1190; -. DR PaxDb; Q9JS45; -. DR EnsemblBacteria; AAF41538; AAF41538; NMB1152. DR EnsemblBacteria; AAF41573; AAF41573; NMB1190. DR GeneID; 903573; -. DR GeneID; 903610; -. DR KEGG; nme:NMB1152; -. DR KEGG; nme:NMB1190; -. DR PATRIC; 20357883; VBINeiMen85645_1457. DR eggNOG; ENOG4107EER; Bacteria. DR eggNOG; COG0369; LUCA. DR HOGENOM; HOG000282025; -. DR KO; K00380; -. DR OMA; GVWYEND; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; NMEN122586:GHGG-1188-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1225-MONOMER; -. DR UniPathway; UPA00140; UER00207. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.990.10; -; 1. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_01541; CysJ; 1. DR InterPro; IPR010199; CysJ. DR InterPro; IPR029758; CysJ_Proteobact. DR InterPro; IPR003097; FAD-binding_1. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00667; FAD_binding_1; 1. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000207; SiR-FP_CysJ; 1. DR PRINTS; PR00369; FLAVODOXIN. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR TIGRFAMs; TIGR01931; cysJ; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; KW Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase; KW Reference proteome; Transport. FT CHAIN 1 604 Sulfite reductase [NADPH] flavoprotein FT alpha-component. FT /FTId=PRO_0000199929. FT DOMAIN 66 204 Flavodoxin-like. {ECO:0000255|HAMAP- FT Rule:MF_01541}. FT DOMAIN 239 453 FAD-binding FR-type. {ECO:0000255|HAMAP- FT Rule:MF_01541}. FT NP_BIND 72 77 FMN. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 119 122 FMN. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 155 164 FMN. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 391 394 FAD. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 409 411 FAD. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 424 427 FAD. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 524 525 NADP. {ECO:0000255|HAMAP-Rule:MF_01541}. FT NP_BIND 530 534 NADP. {ECO:0000255|HAMAP-Rule:MF_01541}. FT BINDING 327 327 FAD. {ECO:0000255|HAMAP-Rule:MF_01541}. FT BINDING 361 361 FAD; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01541}. FT BINDING 566 566 NADP. {ECO:0000255|HAMAP-Rule:MF_01541}. FT BINDING 604 604 FAD. {ECO:0000255|HAMAP-Rule:MF_01541}. SQ SEQUENCE 604 AA; 66386 MW; 33BDC8B846E56264 CRC64; MSEHDMQNTN PPLPPLPPEI TQLLSGLDAA QWAWLSGYAW AKAGNGASAG LPALQTALPA AEPFSVTVLS ASQTGNAKSV ADKAADSLEA AGIQVSRAEL KDYKAKNIAG ERRLLLVTST QGEGEPPKEA VVLHKLLNGK KAPKLDKLQF AVLGLGDSSY PNFCQAGKDF DRRFEELGAK RLLERVDADL DFTASANAWT DNIAALLKEE AAKNRATPAP QTTPPAGLQT APDGRYCKAA PFPAALLANQ KITARQSDKD VRHIEIDLSG SDLHYLPGDA LGVWFDNDPA LVREILDLLG IDPATEIQAG GKMMPVARAL SSHFELTQNT PAFVKGYAAF AHYEELDKII ADNAVLQDFV QNTPIVDVLH RFPASLTAEQ FIRLLRPLAP RLYSISSAQA EVGDEVHLTV GVVRFEHEGR ARTGGASGFL ADRLEEDGTV RVFVERNDGF RLPEDSRKPI VMIGSGTGVA PFRAFVQQRA AENAEGKNWL IFGNPHFARD FLYQTEWQQF AKDGFLHRYD FAWSRDQEEK IYVQDKIREQ AEGLWQWLQE GAHIYVCGDA AKMAKDVEAA LLDVIIGAGH LDEEGAEEYL DMLREEKRYQ RDVY // ID CYSK_NEIMB Reviewed; 310 AA. AC Q7DDL5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Cysteine synthase; DE Short=CSase; DE EC=2.5.1.47; DE AltName: Full=O-acetylserine (thiol)-lyase; DE Short=OAS-TL; DE AltName: Full=O-acetylserine sulfhydrylase; GN Name=cysK; OrderedLocusNames=NMB0763; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L- CC cysteine + acetate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L- CC cysteine from L-serine: step 2/2. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41176.1; -; Genomic_DNA. DR PIR; H81161; H81161. DR RefSeq; NP_273805.1; NC_003112.2. DR RefSeq; WP_002217611.1; NC_003112.2. DR ProteinModelPortal; Q7DDL5; -. DR SMR; Q7DDL5; 1-307. DR STRING; 122586.NMB0763; -. DR PaxDb; Q7DDL5; -. DR PRIDE; Q7DDL5; -. DR EnsemblBacteria; AAF41176; AAF41176; NMB0763. DR GeneID; 902878; -. DR KEGG; nme:NMB0763; -. DR PATRIC; 20356897; VBINeiMen85645_0967. DR eggNOG; ENOG4105C6T; Bacteria. DR eggNOG; COG0031; LUCA. DR HOGENOM; HOG000217394; -. DR KO; K01738; -. DR OMA; VKCRIGS; -. DR OrthoDB; EOG6Q2SP8; -. DR BioCyc; NMEN122586:GHGG-794-MONOMER; -. DR UniPathway; UPA00136; UER00200. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR InterPro; IPR005856; Cys_synth. DR InterPro; IPR005859; CysK. DR InterPro; IPR001216; P-phosphate_BS. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01139; cysK; 1. DR TIGRFAMs; TIGR01136; cysKM; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 310 Cysteine synthase. FT /FTId=PRO_0000320266. FT REGION 179 183 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 74 74 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 267 267 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 44 44 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 310 AA; 32821 MW; FE9C74BF7C2AFD7A CRC64; MKIANSITEL IGNTPLVKLN RLTEGLKAEV AVKLEFFNPG SSVKDRIAEA MIEGAEKAGK INKNTVIVEA TSGNTGVGLA MVCAARGYKL AITMPESMSK ERKMLLRAFG AELILTPAAE GMAGAIAKAK SLVDAHPDTY FMPRQFDNEA NPEVHRKTTA EEIWRDTDGK VDVFVAGVGT GGTITGVGEV LKKYKPEVKV VAVEPEASPV LSGGEKGPHP IQGIGAGFIP TVLNTKIYDS ITKVSNEAAF ETARAIAEKE GILVGISSGA AVWSALQLAK QPENEGKLIV VLLPSYGERY LSTPLFADLA // ID DCDA_NEIMB Reviewed; 414 AA. AC Q9JXM2; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120}; DE EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120}; GN Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120}; GN OrderedLocusNames=NMB1976; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso- CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP- CC Rule:MF_02120}. CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine + CC CO(2). {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02120}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42304.1; -; Genomic_DNA. DR PIR; A81020; A81020. DR RefSeq; NP_274969.1; NC_003112.2. DR RefSeq; WP_002225849.1; NC_003112.2. DR ProteinModelPortal; Q9JXM2; -. DR STRING; 122586.NMB1976; -. DR PaxDb; Q9JXM2; -. DR EnsemblBacteria; AAF42304; AAF42304; NMB1976. DR GeneID; 904163; -. DR KEGG; nme:NMB1976; -. DR PATRIC; 20360027; VBINeiMen85645_2518. DR eggNOG; ENOG4105CU5; Bacteria. DR eggNOG; COG0019; LUCA. DR HOGENOM; HOG000045070; -. DR KO; K01586; -. DR OMA; LKGNKFG; -. DR OrthoDB; EOG6Z9B18; -. DR BioCyc; NMEN122586:GHGG-2033-MONOMER; -. DR UniPathway; UPA00034; UER00027. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_02120; LysA; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR002986; DAP_deCOOHase_LysA. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01181; DAPDCRBXLASE. DR PRINTS; PR01179; ODADCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR01048; lysA; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase; KW Lysine biosynthesis; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 414 Diaminopimelate decarboxylase. FT /FTId=PRO_0000149932. FT REGION 265 268 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_02120}. FT ACT_SITE 334 334 Proton donor. {ECO:0000255}. FT BINDING 231 231 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02120}. FT BINDING 268 268 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 304 304 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 308 308 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 335 335 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 362 362 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 362 362 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT MOD_RES 52 52 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_02120}. SQ SEQUENCE 414 AA; 44698 MW; A8AE27C1B81D6CB2 CRC64; MTLFCEQVPY PRLAEAFGTP LYVYSQSALT EAFEHYQTAF AALNPLVCYA VKANGNLSII KHFASLGSGF DIVSGGELAR VLAAGGDAAK TIFSGVGKSE AEIEFALNAG VKCFNMESIP EIDRIQKVAA RLGKTAPVSL RINPDVDAKT HPYISTGLKA NKFGIAYADA LEAYHYAAQQ PNLKIIGIDC HIGSQLTDLS PLVEACERIL ILVDALAAEG IVLEHLDLGG GVGIVYQDEN VPDLGAYAQA VQKLIGTRRL KLILEPGRSL VGNAGSLLTR VEFVKYGEEK NFVMVDAAMN DLMRPALYDA YHHIEAVETK DIATLTANIV GPICETGDFL GKDRTIACEE GDLLLIRSAG AYGASMASNY NARNRAAEVL VDGNEYRLIR RRETLEQQMA NELACLQAEH QNAV // ID DAPA_NEIMB Reviewed; 291 AA. AC Q9JZR4; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=NMB0929; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, KINETIC PARAMETERS, RP ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT. RC STRAIN=MC58; RX PubMed=19236959; DOI=10.1016/j.bbapap.2009.02.003; RA Devenish S.R., Huisman F.H., Parker E.J., Hadfield A.T., Gerrard J.A.; RT "Cloning and characterisation of dihydrodipicolinate synthase from the RT pathogen Neisseria meningitidis."; RL Biochim. Biophys. Acta 1794:1168-1174(2009). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:19236959}. CC -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)- CC 4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- ENZYME REGULATION: Is allosterically feedback inhibited by lysine; CC the N.meningitidis enzyme is significantly more sensitive to CC lysine than the E.coli enzyme. Shows substrate inhibition by (S)- CC ASA, with a Ki of 1.7 mM. {ECO:0000269|PubMed:19236959}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.50 mM for pyruvate {ECO:0000269|PubMed:19236959}; CC KM=0.052 mM for L-aspartate-4-semialdehyde CC {ECO:0000269|PubMed:19236959}; CC Note=kcat is 46.7 sec(-1).; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19236959}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC synthase (DHDPS), catalyzing the condensation of (S)-aspartate- CC beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate CC (DHDP). However, it was shown in E.coli that the product of the CC enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4- CC hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that CC the consecutive dehydration reaction leading to DHDP is not CC spontaneous but catalyzed by DapB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41336.1; -; Genomic_DNA. DR PIR; D81141; D81141. DR RefSeq; NP_273968.1; NC_003112.2. DR RefSeq; WP_002225337.1; NC_003112.2. DR PDB; 3FLU; X-ray; 2.00 A; A/B/C/D=1-291. DR PDBsum; 3FLU; -. DR ProteinModelPortal; Q9JZR4; -. DR STRING; 122586.NMB0929; -. DR PaxDb; Q9JZR4; -. DR EnsemblBacteria; AAF41336; AAF41336; NMB0929. DR GeneID; 903050; -. DR KEGG; nme:NMB0929; -. DR PATRIC; 20357327; VBINeiMen85645_1178. DR eggNOG; ENOG4105CDP; Bacteria. DR eggNOG; COG0329; LUCA. DR HOGENOM; HOG000173604; -. DR KO; K01714; -. DR OMA; GMDACVP; -. DR OrthoDB; EOG6W7235; -. DR BioCyc; NMEN122586:GHGG-967-MONOMER; -. DR BRENDA; 4.3.3.7; 3593. DR UniPathway; UPA00034; UER00017. DR EvolutionaryTrace; Q9JZR4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00418; DapA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Complete proteome; Cytoplasm; Diaminopimelate biosynthesis; Lyase; KW Lysine biosynthesis; Reference proteome; Schiff base. FT CHAIN 1 291 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_0000103131. FT ACT_SITE 133 133 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT ACT_SITE 161 161 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT BINDING 45 45 Pyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00418}. FT BINDING 203 203 Pyruvate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 44 44 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 107 107 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT STRAND 4 8 {ECO:0000244|PDB:3FLU}. FT HELIX 21 33 {ECO:0000244|PDB:3FLU}. FT STRAND 38 43 {ECO:0000244|PDB:3FLU}. FT TURN 44 47 {ECO:0000244|PDB:3FLU}. FT HELIX 48 50 {ECO:0000244|PDB:3FLU}. FT HELIX 53 67 {ECO:0000244|PDB:3FLU}. FT STRAND 73 76 {ECO:0000244|PDB:3FLU}. FT HELIX 82 94 {ECO:0000244|PDB:3FLU}. FT STRAND 98 103 {ECO:0000244|PDB:3FLU}. FT HELIX 112 125 {ECO:0000244|PDB:3FLU}. FT STRAND 130 134 {ECO:0000244|PDB:3FLU}. FT HELIX 136 139 {ECO:0000244|PDB:3FLU}. FT HELIX 145 151 {ECO:0000244|PDB:3FLU}. FT STRAND 157 162 {ECO:0000244|PDB:3FLU}. FT HELIX 167 176 {ECO:0000244|PDB:3FLU}. FT STRAND 182 185 {ECO:0000244|PDB:3FLU}. FT HELIX 188 190 {ECO:0000244|PDB:3FLU}. FT HELIX 191 196 {ECO:0000244|PDB:3FLU}. FT STRAND 201 205 {ECO:0000244|PDB:3FLU}. FT HELIX 206 208 {ECO:0000244|PDB:3FLU}. FT HELIX 211 223 {ECO:0000244|PDB:3FLU}. FT HELIX 226 240 {ECO:0000244|PDB:3FLU}. FT TURN 241 244 {ECO:0000244|PDB:3FLU}. FT STRAND 245 247 {ECO:0000244|PDB:3FLU}. FT HELIX 250 258 {ECO:0000244|PDB:3FLU}. FT HELIX 275 287 {ECO:0000244|PDB:3FLU}. SQ SEQUENCE 291 AA; 30880 MW; AD5AF175BF32D842 CRC64; MLQGSLVALI TPMNQDGSIH YEQLRDLIDW HIENGTDGIV AVGTTGESAT LSVEEHTAVI EAVVKHVAKR VPVIAGTGAN NTVEAIALSQ AAEKAGADYT LSVVPYYNKP SQEGIYQHFK TIAEATSIPM IIYNVPGRTV VSMTNDTILR LAEIPNIVGV KEASGNIGSN IELINRAPEG FVVLSGDDHT ALPFMLCGGH GVITVAANAA PKLFADMCRA ALQGDIALAR ELNDRLIPIY DTMFCEPSPA APKWAVSALG RCEPHVRLPL VPLTENGQAK VRAALKASGQ L // ID DHAS_NEIMB Reviewed; 371 AA. AC P30903; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 09-DEC-2015, entry version 110. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000255|HAMAP-Rule:MF_02121}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=NMB2079; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140. RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a; RX PubMed=8101504; DOI=10.1016/0378-1119(93)90707-A; RA Hatten L., Wang L., Schryvers A.B., Schweizer H.P.; RT "Cloning and characterization of the Neisseria meningitidis asd RT gene."; RL Gene 129:123-128(1993). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_02121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42397.1; -; Genomic_DNA. DR EMBL; Z14063; CAA78444.1; -; Genomic_DNA. DR PIR; E81009; E81009. DR RefSeq; NP_275068.1; NC_003112.2. DR RefSeq; WP_002225714.1; NC_003112.2. DR ProteinModelPortal; P30903; -. DR SMR; P30903; 1-369. DR STRING; 122586.NMB2079; -. DR PaxDb; P30903; -. DR PRIDE; P30903; -. DR EnsemblBacteria; AAF42397; AAF42397; NMB2079. DR GeneID; 903977; -. DR KEGG; nme:NMB2079; -. DR PATRIC; 20360326; VBINeiMen85645_2660. DR eggNOG; ENOG4107QJH; Bacteria. DR eggNOG; COG0136; LUCA. DR HOGENOM; HOG000161376; -. DR KO; K00133; -. DR OMA; SCQGGDY; -. DR OrthoDB; EOG67X1PS; -. DR BioCyc; NMEN122586:GHGG-2145-MONOMER; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR011534; Asp_ADH_gamma-type. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01745; asd_gamma; 1. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome; KW Threonine biosynthesis. FT CHAIN 1 371 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141385. FT NP_BIND 9 12 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}. FT NP_BIND 37 38 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}. FT NP_BIND 165 166 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}. FT ACT_SITE 135 135 Acyl-thioester intermediate. FT {ECO:0000255|HAMAP-Rule:MF_02121}. FT ACT_SITE 275 275 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 73 73 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}. FT BINDING 102 102 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 162 162 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 193 193 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_02121}. FT BINDING 241 241 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 244 244 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 268 268 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 351 351 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}. FT CONFLICT 44 44 A -> R (in Ref. 2; CAA78444). FT {ECO:0000305}. FT CONFLICT 117 119 DVL -> NVI (in Ref. 2; CAA78444). FT {ECO:0000305}. SQ SEQUENCE 371 AA; 39858 MW; F36BF70BB80075AA CRC64; MKVGFVGWRG MVGSVLMQRM KEENDFAHIP EAFFFTTSNV GGAAPDFGQA AKTLLDANNV AELAKMDIIV TCQGGDYTKS VFQALRDSGW NGYWIDAASS LRMKDDAIIV LDPVNRDVLD NGLKNGVKNY IGGNCTVSLM LMALGGLFQN DLVEWATSMT YQAASGAGAK NMRELISGMG AVHAQVADAL ADPAGSILDI DRKVSDFLRS EDYPKANFGV PLAGSLIPWI DVDLGNGQSK EEWKGGVETN KILGRSDNPT VIDGLCVRVG AMRCHSQAIT LKLKKDLPVS EIETILAGAN DWVKVIPNEK EASIHELTPA KVTGTLSVPV GRIRKLGMGG EYISAFTVGD QLLWGAAEPL RRVLRIVLGS L // ID DNAK_NEIMB Reviewed; 642 AA. AC Q9K0N4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Chaperone protein DnaK; DE AltName: Full=HSP70; DE AltName: Full=Heat shock 70 kDa protein; DE AltName: Full=Heat shock protein 70; GN Name=dnaK; OrderedLocusNames=NMB0554; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}. CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity). CC {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40982.1; -; Genomic_DNA. DR PIR; H81185; H81185. DR RefSeq; NP_273598.1; NC_003112.2. DR RefSeq; WP_002225573.1; NC_003112.2. DR ProteinModelPortal; Q9K0N4; -. DR SMR; Q9K0N4; 1-606. DR STRING; 122586.NMB0554; -. DR PaxDb; Q9K0N4; -. DR PRIDE; Q9K0N4; -. DR EnsemblBacteria; AAF40982; AAF40982; NMB0554. DR GeneID; 902669; -. DR KEGG; nme:NMB0554; -. DR PATRIC; 20356379; VBINeiMen85645_0709. DR eggNOG; ENOG4105CFG; Bacteria. DR eggNOG; COG0443; LUCA. DR HOGENOM; HOG000228136; -. DR KO; K04043; -. DR OMA; EKMAPPQ; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; NMEN122586:GHGG-580-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 2.60.34.10; -; 1. DR HAMAP; MF_00332; DnaK; 1. DR InterPro; IPR012725; Chaperone_DnaK. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C. DR InterPro; IPR029047; HSP70_peptide-bd. DR InterPro; IPR013126; Hsp_70_fam. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. DR SUPFAM; SSF100934; SSF100934; 1. DR TIGRFAMs; TIGR02350; prok_dnaK; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Stress response. FT CHAIN 1 642 Chaperone protein DnaK. FT /FTId=PRO_0000078503. FT MOD_RES 200 200 Phosphothreonine; by autocatalysis. FT {ECO:0000250}. SQ SEQUENCE 642 AA; 68792 MW; 235696C763BD5805 CRC64; MAKVIGIDLG TTNSCLAISE NGQTKVIENA EGARTTPSVI AYLDGGEILV GAPAKRQAVT NAKNTIYAAK RLIGHKFEDK EVQRDIESMP FEIIKANNGD AWVKAQGKEL SPPQISAEVL RKMKEAAEAY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG MDKGDNKDRK VAVYDLGGGT FDISIIEIAN LDGDKQFEVL ATNGDTFLGG EDFDQRLIDH IIAEFKKEQG IDLKQDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLAMK ITRAKFESLV EDLITRSIEP CKIALKDAGL STGDIDDVIL VGGQSRMPKV QEAVKAFFGK EPRKDVNPDE AVAVGAAIQG EVLSGGRSDV LLLDVTPLSL GIETMGGVMT KLIQKNTTIP TKASQVFSTA EDNQSAVTIH VLQGERERAS ANKSLGQFNL GDIAPAPRGM PQIEVTFDID ANGILHVSAK DKGTGKAANI TIQGSSGLSE EEIERMVKDA EANAEEDKKL TELVASRNQA EALIHSVKKS LADYGDKLDA AEKEKIEAAL KEAEEAVKGD DKAAIDAKTE ALGAASQKLG EMVYAQAQAE AQAGESEQAN ASAKKDDDVV DADFEEVKDD KK // ID DHPS_NEIMB Reviewed; 285 AA. AC Q51161; Q51157; Q51158; Q51159; Q51160; Q57214; Q60395; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 20-JAN-2016, entry version 114. DE RecName: Full=Dihydropteroate synthase; DE Short=DHPS; DE EC=2.5.1.15; DE AltName: Full=Dihydropteroate pyrophosphorylase; GN Name=folP; Synonyms=dhpS; OrderedLocusNames=NMB1691; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=952 / Serogroup B / Serotype NT, RC BT490 / Serogroup B / Serotype 15, and RC MO035 / Serogroup B / Serotype 15; RX PubMed=1400191; RA Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O., RA Swedberg G.; RT "Transformational exchanges in the dihydropteroate synthase gene of RT Neisseria meningitidis: a novel mechanism for acquisition of RT sulfonamide resistance."; RL J. Bacteriol. 174:6386-6393(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=3976 / Serogroup B / Serotype NT; RX PubMed=7642493; RA Fermer C., Kristiansen B.E., Skoeld O., Swedberg G.; RT "Sulfonamide resistance in Neisseria meningitidis as defined by site- RT directed mutagenesis could have its origin in other species."; RL J. Bacteriol. 177:4669-4675(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) CC with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to CC form 7,8-dihydropteroate (H2Pte), the immediate precursor of CC folate derivatives. {ECO:0000250|UniProtKB:P0AC13}. CC -!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate CC + 4-aminobenzoate = diphosphate + dihydropteroate. CC {ECO:0000250|UniProtKB:P0AC13}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0AC13}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8- CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X68062; CAA48199.1; -; Genomic_DNA. DR EMBL; X68066; CAA48203.1; -; Genomic_DNA. DR EMBL; X68069; CAA48206.1; -; Genomic_DNA. DR EMBL; X87405; CAA60855.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42039.1; -; Genomic_DNA. DR PIR; A57423; A57423. DR PIR; S25611; S25611. DR PIR; S65832; S65832. DR PIR; S65839; S65839. DR RefSeq; NP_274695.1; NC_003112.2. DR RefSeq; WP_002224358.1; NC_003112.2. DR ProteinModelPortal; Q51161; -. DR STRING; 122586.NMB1691; -. DR PaxDb; Q51161; -. DR EnsemblBacteria; AAF42039; AAF42039; NMB1691. DR GeneID; 903415; -. DR KEGG; nme:NMB1691; -. DR PATRIC; 20359335; VBINeiMen85645_2174. DR eggNOG; ENOG4105EEI; Bacteria. DR eggNOG; COG0294; LUCA. DR KO; K00796; -. DR OMA; SIDTYHA; -. DR OrthoDB; EOG67T5P5; -. DR BioCyc; NMEN122586:GHGG-1746-MONOMER; -. DR UniPathway; UPA00077; UER00156. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.20; -; 1. DR InterPro; IPR006390; DHP_synth. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR01496; DHPS; 1. DR PROSITE; PS00792; DHPS_1; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome; Folate biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1 285 Dihydropteroate synthase. FT /FTId=PRO_0000168218. FT DOMAIN 18 276 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT REGION 264 266 6-hydroxymethyl-7,8-dihydropterin FT diphosphate binding. FT {ECO:0000250|UniProtKB:P0AC13}. FT METAL 25 25 Magnesium. FT {ECO:0000250|UniProtKB:P9WND1}. FT BINDING 66 66 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 99 99 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 119 119 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 190 190 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 229 229 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT VARIANT 2 4 ARH -> VGC (in strain: 3976 / Serogroup B FT / Serotype NT). FT VARIANT 31 31 F -> L (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 36 36 V -> A (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 42 42 Q -> R (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 50 50 Q -> R (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 68 68 S -> P (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 69 69 G -> C (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 84 84 P -> S (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 96 96 I -> V (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 102 102 R -> H (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 105 105 I -> V (in strain: 952 / Serogroup B / FT Serotype NT and 3976 / Serogroup B / FT Serotype NT). FT VARIANT 125 125 N -> T (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 130 130 V -> L (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 135 135 R -> C (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 137 137 A -> T (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 147 147 Q -> R (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 151 151 K -> E (in strain: BT490 / Serogroup B / FT Serotype 15 and 952 / Serogroup B / FT Serotype NT). FT VARIANT 152 152 T -> N (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 172 172 A -> T (in strain: 952 / Serogroup B / FT Serotype NT). FT VARIANT 174 174 S -> A (in strain: BT490 / Serogroup B / FT Serotype 15 and 3976 / Serogroup B / FT Serotype NT). FT VARIANT 175 178 AECI -> ETCV (in strain: 952 / Serogroup FT B / Serotype NT). FT VARIANT 188 188 I -> T (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 194 195 Missing (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 196 196 G -> C (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 200 200 P -> T (in strain: 952 / Serogroup B / FT Serotype NT and 3976 / Serogroup B / FT Serotype NT). FT VARIANT 206 206 A -> T (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 208 208 M -> V (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 220 220 F -> Y (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 230 230 S -> R (in strain: 952 / Serogroup B / FT Serotype NT and BT490 / Serogroup B / FT Serotype 15). FT VARIANT 231 231 T -> M (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 232 232 I -> V (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 239 239 A -> S (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 239 239 A -> T (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 240 240 N -> D (in strain: BT490 / Serogroup B / FT Serotype 15, 952 / Serogroup B / Serotype FT NT and 3976 / Serogroup B / Serotype NT). FT VARIANT 243 243 E -> A (in strain: BT490 / Serogroup B / FT Serotype 15 and 3976 / Serogroup B / FT Serotype NT). FT VARIANT 245 245 V -> G (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 253 253 L -> V (in strain: BT490 / Serogroup B / FT Serotype 15). FT VARIANT 255 255 S -> A (in strain: BT490 / Serogroup B / FT Serotype 15 and 3976 / Serogroup B / FT Serotype NT). FT VARIANT 261 261 Q -> K (in strain: 3976 / Serogroup B / FT Serotype NT). FT VARIANT 277 277 V -> A (in strain: 3976 / Serogroup B / FT Serotype NT). SQ SEQUENCE 285 AA; 30313 MW; C56518F61CF98A4E CRC64; MARHVWQAGR FEIGLDKPKI MGIVNLTPDS FSDGGVYSQN AQTALAHAEQ LLKEGADILD IGGESTRSGA DYVSPEEEWA RVEPVLAEVA GWGVPISLDT RRTVIMEKAL ALGGIDIIND VAALNDEGAV ELLARQADTG ICLMHMQGLP KTMQINPKYQ DVVGEVARYL KARSAECIAA GIAPQRIILD PGFGSGFGKP LQHNIALMRH LPELMAETGF PLLIGVSRKS TIGELTGEAN AAERVHGSVA AALASVARGA QIVRVHDVKA TADALKVWEA LGINL // ID DER_NEIMB Reviewed; 485 AA. AC Q9JZY1; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195}; DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195}; GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA; GN OrderedLocusNames=NMB0852; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngA (Der) GTPase family. CC {ECO:0000255|HAMAP-Rule:MF_00195}. CC -!- SIMILARITY: Contains 2 EngA-type G (guanine nucleotide-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00195}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41263.1; -; Genomic_DNA. DR PIR; G81149; G81149. DR RefSeq; NP_273893.1; NC_003112.2. DR RefSeq; WP_002225394.1; NC_003112.2. DR ProteinModelPortal; Q9JZY1; -. DR STRING; 122586.NMB0852; -. DR PaxDb; Q9JZY1; -. DR EnsemblBacteria; AAF41263; AAF41263; NMB0852. DR GeneID; 902966; -. DR KEGG; nme:NMB0852; -. DR PATRIC; 20357095; VBINeiMen85645_1066. DR eggNOG; ENOG4105DKZ; Bacteria. DR eggNOG; COG1160; LUCA. DR HOGENOM; HOG000242862; -. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; NMEN122586:GHGG-883-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00195; GTPase_Der; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR031166; G_ENGA. DR InterPro; IPR016484; GTP-bd_EngA. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR032859; KH_dom-like. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11649:SF5; PTHR11649:SF5; 1. DR Pfam; PF14714; KH_dom-like; 1. DR Pfam; PF01926; MMR_HSR1; 2. DR PIRSF; PIRSF006485; GTP-binding_EngA; 1. DR PRINTS; PR00326; GTP1OBG. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03594; GTPase_EngA; 1. DR TIGRFAMs; TIGR00231; small_GTP; 2. DR PROSITE; PS51712; G_ENGA; 2. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome; Repeat; Ribosome biogenesis. FT CHAIN 1 485 GTPase Der. FT /FTId=PRO_0000179021. FT DOMAIN 3 167 EngA-type G 1. FT DOMAIN 176 349 EngA-type G 2. FT DOMAIN 350 434 KH-like. {ECO:0000255|HAMAP- FT Rule:MF_00195}. FT NP_BIND 9 16 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 56 60 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 119 122 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 182 189 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 229 233 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 294 297 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. SQ SEQUENCE 485 AA; 54063 MW; 300DF75F7A30519C CRC64; MKPTIALVGR PNVGKSTLFN RLTRTKDALV HDLPGLTRDR HYGHGKVGSK PYLVIDTGGF EPVVDSGILH EMAKQTLQAV DEADAVVFLV DGRTGLTPQD KIIADRLRQS PRPVYLAVNK GEGGNRAVLA AEFYELALGD PYVISGAHGD GVYYLIEDIL EKFPEPEAEE ADARHPVFAV IGRPNVGKST LVNAILGEER VITFDMAGTT RDSIHIDFER EGKPFTIIDT AGVRRRGKVD EAVEKFSVIK AMQAVEAANV AVLVLDAQQD IADQDATIAG FALEAGRALV VAVNKWDGIS EERREQVKRD INRKLYFLDF AKFHFISALK ERGIDGLFDS IQAAYNAAMI KMPTPKITRV LQSAIERQQP PRAGLVRPKM RYAHQGGMNP PVIVVHGNSL HAISDSYTRY LTQTFRKAFN LQGTPLRIQY NVSENPYENA EDKPKKKPLR RVSLSNRIEK REGRKEEKNR FKKKTKVSVK KQFSK // ID DNLJ_NEIMB Reviewed; 841 AA. AC Q9K0E3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588}; DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; GN OrderedLocusNames=NMB0666; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA ligase that catalyzes the formation of CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl CC groups in double-stranded DNA using NAD as a coenzyme and as the CC energy source for the reaction. It is essential for DNA CC replication and repair of damaged DNA. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D- CC ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}. CC -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41084.1; -; Genomic_DNA. DR PIR; F81172; F81172. DR RefSeq; NP_273708.1; NC_003112.2. DR RefSeq; WP_002214202.1; NC_003112.2. DR ProteinModelPortal; Q9K0E3; -. DR SMR; Q9K0E3; 25-349, 767-840. DR STRING; 122586.NMB0666; -. DR PaxDb; Q9K0E3; -. DR EnsemblBacteria; AAF41084; AAF41084; NMB0666. DR GeneID; 902777; -. DR KEGG; nme:NMB0666; -. DR PATRIC; 20356631; VBINeiMen85645_0834. DR eggNOG; ENOG4105C77; Bacteria. DR eggNOG; COG0272; LUCA. DR HOGENOM; HOG000218459; -. DR KO; K01972; -. DR OMA; IEIHETV; -. DR OrthoDB; EOG6TTVM9; -. DR BioCyc; NMEN122586:GHGG-693-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR033136; DNA_ligase_CS. DR InterPro; IPR001679; DNAligase. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004150; NAD_DNA_ligase_OB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR004149; Znf_DNAligase_C4. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 1. DR Pfam; PF03119; DNA_ligase_ZBD; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS01055; DNA_LIGASE_N1; 1. DR PROSITE; PS01056; DNA_LIGASE_N2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; KW Magnesium; Manganese; Metal-binding; NAD; Reference proteome; Zinc. FT CHAIN 1 841 DNA ligase. FT /FTId=PRO_0000313332. FT DOMAIN 764 841 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 54 58 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 103 104 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 145 145 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 471 471 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 474 474 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 489 489 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 495 495 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 143 143 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 166 166 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 203 203 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 321 321 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 345 345 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. SQ SEQUENCE 841 AA; 92360 MW; BC9209F2BDB88185 CRC64; MNPNSKHNTN FTNLLKPSDS DIKQFAAQHI CRLTDLLNRY AYEYYTLDAP SVPDAEYDKL FRELEALELN HPELKLPDSP TQRVGGEPLA GFAEVRHEVP MLSLTNAFSP QDENGVFDHA EMYAFDQRVR DGLDGGNPEY VIEPKFDGLA ISLLYRDGVL VQAATRGDGT TGEDVTQNIK TVSNIPLRLH GENTPELIEV RGEVLMLKAD FVALNKRQAE NGQKPFANPR NAAAGSLRQL DSRITAQRKL HFFPYSVARQ QDGFVAEEHI QELAYFQALG FSLPNGNFGC FKNIDEVLAF YEHMQQKRPE LPYEIDGMVV KVNSLAQQHE LGFISRAPRW AVAHKFPAEE ALTIVEAIDV QIGRTGAVTP VARLQPVFVG GVTVTNATLH NQDEVSRKDV RVGDTVVVRR AGDVIPEVVR VIFERRPMRE TAVAVSDGIG HRQDDLFAET PSANQTQSVP LHKPYRLPTH CPICRSEIER EEGEAVARCS GGMLCQAQRA QGLIHFASRK AMDIDGLGEK QIEQLVAQDL VRHFADLYRL DIPTLQKMKE TADKTVAESD QMPSEGSSVG ASGKHKKQPV KWAENILAGI EASKTPELAR FLFALGIRHV GERTAKTLAQ AFGTLERVRR APEPVLACLP DIGTVVARSI AHFFAQAEQQ AMIDELLAAG VAPQTQAVTI PPARHAEPQR WIARLPGFKI SENKAQALWE LAGKNIEGLQ TDKALPTDWQ AWRSEPQNAA LLENLKTFFA QMPSEDEAAQ GSDGINKAVA GKTFVLTGTL PTLKRDQAQS LIEAAGGKVS GSVSKKTDYV VAGEAAGSKL EKANALGVSV LSEAELLTLL G // ID DPO3A_NEIMB Reviewed; 1144 AA. AC Q9JXZ2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE RecName: Full=DNA polymerase III subunit alpha; DE EC=2.7.7.7; GN Name=dnaE; OrderedLocusNames=NMB1827; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. CC This DNA polymerase also exhibits 3' to 5' exonuclease activity. CC The alpha chain is the DNA polymerase (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, CC epsilon and theta chains) that associates with a tau subunit. This CC core dimerizes to form the PolIII' complex. PolIII' associates CC with the gamma complex (composed of gamma, delta, delta', psi and CC chi chains) and with the beta chain to form the complete DNA CC polymerase III complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42162.1; -; Genomic_DNA. DR PIR; H81037; H81037. DR RefSeq; NP_274824.1; NC_003112.2. DR RefSeq; WP_002225661.1; NC_003112.2. DR ProteinModelPortal; Q9JXZ2; -. DR STRING; 122586.NMB1827; -. DR PaxDb; Q9JXZ2; -. DR EnsemblBacteria; AAF42162; AAF42162; NMB1827. DR GeneID; 903273; -. DR KEGG; nme:NMB1827; -. DR PATRIC; 20359641; VBINeiMen85645_2326. DR eggNOG; ENOG4105C0B; Bacteria. DR eggNOG; COG0587; LUCA. DR HOGENOM; HOG000021784; -. DR KO; K02337; -. DR OMA; DFCMDGR; -. DR OrthoDB; EOG6CZQGR; -. DR BioCyc; NMEN122586:GHGG-1882-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR InterPro; IPR004805; PolC_alpha. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF14579; HHH_6; 1. DR Pfam; PF02811; PHP; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. DR TIGRFAMs; TIGR00594; polc; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 1144 DNA polymerase III subunit alpha. FT /FTId=PRO_0000103332. SQ SEQUENCE 1144 AA; 127136 MW; 4CEABB86F90DD7EA CRC64; MTEPTYIPLR LHTEFSITDG MVRIKKLIAK AQEYGLPALG ISDLMNEFGL VKFYKACRSA GIKPIGAADV RIGNPDAPDK PFRAMLIIRN DAGYLRLSEL LTAAYVGKDR NVHHAELNPE WLENGDNSGL ICLSGAHYGE VGVNLLNGNE DAARTAALKY AAWFPDAFYM ELQRLPERPE WEACVSGSVK LAEELGLPVV ATHPTQFMSR DDFNAHEARV CIAGGWVLTD KKRPRDFTPG QFFIPPETMA ERFADLPEAL ENTVEIAKRC NLHITLGKNF LPLFPTPDGL SLDDYLIKLS NEGLQERMVQ LYPDEAERAA KMPEYQERLD FELNIIIQMK FPGYFLIVQD FINWAKTHGC PVGPGRGSGA GSLVAYSLKI TDLDPLKYAL LFERFLNPER VSMPDFDVDF CQSNRGRVIE YVREKYGAEA VSQIVTFGTM SSKAVIRDVG RVLELPFMLC DKLSKLIPLE ANKPLSLEKA METEPQIQEL IEAEEADELI TLAKKLEDLT RGLGMHAGGV LIAPGKISDY SPVYQADESA SPVSMYDKGD VEDVGLVKFD FLGLRNLTII EMAQNNIKNT TGDIIDVGKI PLDDQVAYQI FRDANTTAVF QFESTGMKKM LKTAHTTKFE ELIAFVSLYR PGPMDNIPDF VARMKGQEFQ YIHPLLEGIL APTYGIMVYQ EQVMQAAQII GGYSLGGADL LRRAMGKKKP EEMVKHREIF AEGAAKQGIS REKSDEIFNY MEKFAGYGFN KSHAAAYALI SYQTAWLKAH YPAEFMAATM SSELDNTDQL KHFYDDCRAN GIEFLPPDIN ESDYRFTPYP DMKIRYALGA IKGTGEAAVE SITAARQSGG KFTGLLDFCE RVGKEHMNRR TLEALIRGGA FDSIEPNRAM LLANIDLAMD NADQKAANAN QGGLFDMMED AIEPVRLIDA PMWSESEKLA EEKTVIGFYL SGHPFGPYAQ EVRQIAPTKL DRLKPQDSVR LAGFVTAVRT MMGKRGKIAF VSLEDLSGQV EIMVGGQTLE NCADCLKADQ VLIIESKVSR DDYGGGDGLR ILANQVMTLQ TARERYARSL SLALAPHHDI GGLVRLLAAH QLPDTPRIPL QLSYANEKAS GRLQVPPKWT VTPSSALFGE LETLLGSRSV RVNW // ID DSBB_NEIMB Reviewed; 162 AA. AC Q9JYC6; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Disulfide bond formation protein B {ECO:0000255|HAMAP-Rule:MF_00286}; DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00286}; GN Name=dsbB {ECO:0000255|HAMAP-Rule:MF_00286}; GN OrderedLocusNames=NMB1649; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for disulfide bond formation in some CC periplasmic proteins. Acts by oxidizing the DsbA protein. CC {ECO:0000255|HAMAP-Rule:MF_00286}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00286}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00286}. CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000255|HAMAP- CC Rule:MF_00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41998.1; -; Genomic_DNA. DR PIR; H81058; H81058. DR RefSeq; NP_274654.1; NC_003112.2. DR RefSeq; WP_002216721.1; NC_003112.2. DR ProteinModelPortal; Q9JYC6; -. DR STRING; 122586.NMB1649; -. DR PaxDb; Q9JYC6; -. DR EnsemblBacteria; AAF41998; AAF41998; NMB1649. DR GeneID; 903467; -. DR KEGG; nme:NMB1649; -. DR PATRIC; 20359218; VBINeiMen85645_2121. DR eggNOG; COG1495; LUCA. DR HOGENOM; HOG000027866; -. DR KO; K03611; -. DR OMA; PLFDWFE; -. DR OrthoDB; EOG615VM4; -. DR BioCyc; NMEN122586:GHGG-1698-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1550.10; -; 1. DR HAMAP; MF_00286; DsbB; 1. DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC. DR InterPro; IPR022920; Disulphide_bond_form_DsbB. DR InterPro; IPR023380; DsbB-like_dom. DR Pfam; PF02600; DsbB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Disulfide bond; Electron transport; Membrane; Oxidoreductase; KW Redox-active center; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 162 Disulfide bond formation protein B. FT /FTId=PRO_0000059348. FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 9 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 26 43 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 44 60 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 61 67 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 68 85 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 86 141 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 142 160 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 161 162 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT DISULFID 35 38 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT DISULFID 101 128 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00286}. SQ SEQUENCE 162 AA; 17701 MW; CC02718FC7166B77 CRC64; MTPLFRKAVW LLFAVSVCAF AGSLAAQYVL GMEPCVLCIS QRLCVLATAL CTAIVLMCRP RRRAGGLFGA VFISIPAVTG ISVAAYQLWL QSLPPGTAPS CGAPWTFRLK GWPLFDWFEP VVRGFGNCAE PDYLLGIALP VWSVAYFLAV VLTVWWAWAR AK // ID DUT_NEIMB Reviewed; 150 AA. AC Q9JZU7; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00116}; DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00116}; DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00116}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00116}; GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00116}; OrderedLocusNames=NMB0893; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it CC produces dUMP, the immediate precursor of thymidine nucleotides CC and it decreases the intracellular concentration of dUTP so that CC uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP- CC Rule:MF_00116}. CC -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00116}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00116}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00116}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41302.1; -; Genomic_DNA. DR PIR; C81146; C81146. DR RefSeq; NP_273934.1; NC_003112.2. DR RefSeq; WP_002225353.1; NC_003112.2. DR ProteinModelPortal; Q9JZU7; -. DR SMR; Q9JZU7; 1-134. DR STRING; 122586.NMB0893; -. DR PaxDb; Q9JZU7; -. DR EnsemblBacteria; AAF41302; AAF41302; NMB0893. DR GeneID; 903012; -. DR KEGG; nme:NMB0893; -. DR PATRIC; 20357207; VBINeiMen85645_1119. DR eggNOG; ENOG4108Z1K; Bacteria. DR eggNOG; COG0756; LUCA. DR HOGENOM; HOG000028968; -. DR KO; K01520; -. DR OMA; MVSAWNR; -. DR OrthoDB; EOG689HXK; -. DR BioCyc; NMEN122586:GHGG-929-MONOMER; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046080; P:dUTP metabolic process; IEA:InterPro. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00116; dUTPase_bact; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR008180; dUTPase/dCTP_deaminase. DR InterPro; IPR008181; dUTPase_1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR00576; dut; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Nucleotide metabolism; Reference proteome. FT CHAIN 1 150 Deoxyuridine 5'-triphosphate FT nucleotidohydrolase. FT /FTId=PRO_0000182886. FT REGION 69 71 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT REGION 86 88 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT BINDING 82 82 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT BINDING 96 96 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00116}. SQ SEQUENCE 150 AA; 16129 MW; 120F426E74D37A7E CRC64; MNIEVEMKVL DERMADVVPV YATEGSAGLD LRACLDEEVV LQPGETFLVP TGLAIYLANP AYAAVLLPRS GLGHKHGIVL GNLVGLIDSD YQGELKVSLW NRSSEPFTVK PFERIAQMVV VPIVQAGFKR VEEFVGSSRG EGGFGSTGSH // ID DNAJ_NEIMB Reviewed; 373 AA. AC P63969; P57107; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=NMB0059; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates actively in the response to hyperosmotic CC and heat shock by preventing the aggregation of stress-denatured CC proteins and by disaggregating proteins, also in an autonomous, CC DnaK-independent fashion. Unfolded proteins bind initially to CC DnaJ; upon interaction with the DnaJ-bound protein, DnaK CC hydrolyzes its bound ATP, resulting in the formation of a stable CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers CC the release of the substrate protein, thus completing the reaction CC cycle. Several rounds of ATP-dependent interactions between DnaJ, CC DnaK and GrpE are required for fully efficient folding. Also CC involved, together with DnaK and GrpE, in the DNA replication of CC plasmids through activation of initiation proteins. CC {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01152}; CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_01152}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK CC ATPase activity. Zinc center 1 plays an important role in the CC autonomous, DnaK-independent chaperone activity of DnaJ. Zinc CC center 2 is essential for interaction with DnaK and for DnaJ CC activity. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40528.1; -; Genomic_DNA. DR PIR; D81242; D81242. DR RefSeq; NP_273124.1; NC_003112.2. DR RefSeq; WP_002215274.1; NC_003112.2. DR ProteinModelPortal; P63969; -. DR SMR; P63969; 2-78, 134-208. DR STRING; 122586.NMB0059; -. DR PaxDb; P63969; -. DR EnsemblBacteria; AAF40528; AAF40528; NMB0059. DR GeneID; 902166; -. DR KEGG; nme:NMB0059; -. DR PATRIC; 20355123; VBINeiMen85645_0095. DR eggNOG; ENOG4105BZ5; Bacteria. DR eggNOG; COG0484; LUCA. DR HOGENOM; HOG000226717; -. DR KO; K03686; -. DR OMA; IKDPCNS; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; NMEN122586:GHGG-65-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 2.10.230.10; -; 1. DR HAMAP; MF_01152; DnaJ; 1. DR InterPro; IPR012724; DnaJ. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR008971; HSP40/DnaJ_pept-bd. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF49493; SSF49493; 3. DR SUPFAM; SSF57938; SSF57938; 1. DR TIGRFAMs; TIGR02349; DnaJ_bact; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51188; ZF_CR; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; DNA replication; KW Metal-binding; Reference proteome; Repeat; Stress response; Zinc; KW Zinc-finger. FT CHAIN 1 373 Chaperone protein DnaJ. FT /FTId=PRO_0000070840. FT DOMAIN 5 70 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 147 154 CXXCXGXG motif. FT REPEAT 164 171 CXXCXGXG motif. FT REPEAT 186 193 CXXCXGXG motif. FT REPEAT 200 207 CXXCXGXG motif. FT ZN_FING 134 212 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 77 117 Gly-rich. FT METAL 147 147 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 150 150 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 164 164 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 167 167 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 186 186 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 189 189 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 200 200 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 203 203 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 373 AA; 40585 MW; 4D881E20A5D831CF CRC64; MSNQDFYATL GVARTATDDE IKKAYRKLAM KYHPDRNPDN KEAEEKFKEV QKAYETLSDK EKRAMYDQYG HAAFEGGGQG GFGGFGGFGG AQGFDFGDIF SQMFGGGSGR AQPDYQGEDV QVGIEITLEE AAKGVKKRIN IPTYEACDVC NGSGAKPGTS PETCPTCKGS GTVHIQQAIF RMQQTCPTCH GAGKHIKEPC VKCRGAGRNK AVKTVEVNIP AGIDDGQRIR LSGEGGPGMH GAPAGDLYVT VRIRAHKIFQ RDGLDLHCEL PISFATAALG GELEVPTLDG KVKLTVPKET QTGRRMRVKG KGVKSLRSSA TGDLYCHIVV ETPVNLTDRQ KELLEEFERI STGLENQTPR KKSFLDKLRD LFD // ID DNAA_NEIMB Reviewed; 518 AA. AC Q9JXS7; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Chromosomal replication initiator protein DnaA; GN Name=dnaA; OrderedLocusNames=NMB1903; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Plays an important role in the initiation and regulation CC of chromosomal replication. Binds to the origin of replication; it CC binds specifically double-stranded DNA at a 9 bp consensus (dnaA CC box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic CC phospholipids (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42233.1; -; Genomic_DNA. DR PIR; F81027; F81027. DR RefSeq; NP_274897.1; NC_003112.2. DR RefSeq; WP_002223060.1; NC_003112.2. DR ProteinModelPortal; Q9JXS7; -. DR STRING; 122586.NMB1903; -. DR PaxDb; Q9JXS7; -. DR EnsemblBacteria; AAF42233; AAF42233; NMB1903. DR GeneID; 904267; -. DR KEGG; nme:NMB1903; -. DR PATRIC; 20359849; VBINeiMen85645_2429. DR eggNOG; ENOG4105CI4; Bacteria. DR eggNOG; COG0593; LUCA. DR HOGENOM; HOG000235659; -. DR KO; K02313; -. DR OMA; AVGNSIM; -. DR OrthoDB; EOG689HR1; -. DR BioCyc; NMEN122586:GHGG-1960-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1750.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00377; DnaA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001957; Chromosome_initiator_DnaA. DR InterPro; IPR020591; Chromosome_initiator_DnaA-like. DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS. DR InterPro; IPR013317; DnaA. DR InterPro; IPR013159; DnaA_C. DR InterPro; IPR024633; DnaA_N_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR Pfam; PF00308; Bac_DnaA; 1. DR Pfam; PF08299; Bac_DnaA_C; 1. DR Pfam; PF11638; DnaA_N; 1. DR PRINTS; PR00051; DNAA. DR SMART; SM00382; AAA; 1. DR SMART; SM00760; Bac_DnaA_C; 1. DR SUPFAM; SSF48295; SSF48295; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00362; DnaA; 1. DR PROSITE; PS01008; DNAA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 518 Chromosomal replication initiator protein FT DnaA. FT /FTId=PRO_0000114221. FT NP_BIND 222 229 ATP. {ECO:0000255}. SQ SEQUENCE 518 AA; 58028 MW; 1B1BD0C49BE71E9D CRC64; MTLAEFWPLC LRRLHDMLPQ GQFAQWIAPL TVGEEGGVWV VYGKNQFACN MLKSQFAGKI EAVREELAAG RSAFVFKPGE GVRYEMAAVE GAVEPAEPSL HAVSEGMPVQ EVLLDELPSE EPVKPAASKT AADILAERMK NLPHEPRQAA GSASRPESVA VAKARTDVQR DAEEARYEQT NLSPDYTFDT LVEGKGNRLA AAAAQAIAES PGQSYNPFFL YGSTGLGKTH LVQAVGNELL KNRPDAKVRY MHSDDYIRSF MKAVRNNTYD VFKQQYKQYD LLIIDDIQFI KGKDRTMEEF FYLYNHFHNE KKQLILTCDV LPAKIEGMDD RLKSRFSWGL TLELEPPELE MRIAILQKKA EAAGISIEDE AALFIANLIR SNVRELEGAF NRVGASSRFM NRPVIDIDLA RTALQDIIAE KHKVITADII IDAVAKYYRI KISDVLGKKR TRNIARPRQV AMSLTKELTT LSLPSIGDSF GGRDHTTVMH GIRAVAKLRE EDPELAQDYE KLLILIQN // ID DNAG_NEIMB Reviewed; 590 AA. AC P57029; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974}; GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; GN OrderedLocusNames=NMB1537; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA CC molecules used as primers for DNA polymerase during DNA CC replication. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core CC domain that contains the primase activity, and a C-terminal DnaB- CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Belongs to the DnaG primase family. CC {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41892.1; -; Genomic_DNA. DR PIR; E81072; E81072. DR RefSeq; NP_274544.1; NC_003112.2. DR RefSeq; WP_002225052.1; NC_003112.2. DR ProteinModelPortal; P57029; -. DR STRING; 122586.NMB1537; -. DR PaxDb; P57029; -. DR EnsemblBacteria; AAF41892; AAF41892; NMB1537. DR GeneID; 904069; -. DR KEGG; nme:NMB1537; -. DR PATRIC; 20358878; VBINeiMen85645_1948. DR eggNOG; ENOG4105C9G; Bacteria. DR eggNOG; COG0358; LUCA. DR HOGENOM; HOG000014483; -. DR KO; K02316; -. DR OMA; PARENTG; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; NMEN122586:GHGG-1578-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.90.580.10; -; 1. DR Gene3D; 3.90.980.10; -; 1. DR HAMAP; MF_00974; DNA_primase_DnaG; 1. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR InterPro; IPR013264; DNA_primase_core_N. DR InterPro; IPR019475; DNA_primase_DnaB-bd. DR InterPro; IPR006295; DNA_primase_DnaG. DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom. DR InterPro; IPR030846; DnaG_bac. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR002694; Znf_CHC2. DR Pfam; PF10410; DnaB_bind; 1. DR Pfam; PF08278; DnaG_DnaB_bind; 1. DR Pfam; PF08275; Toprim_N; 1. DR Pfam; PF01807; zf-CHC2; 1. DR PIRSF; PIRSF002811; DnaG; 1. DR SMART; SM00766; DnaG_DnaB_bind; 1. DR SMART; SM00493; TOPRIM; 1. DR SMART; SM00400; ZnF_CHCC; 1. DR TIGRFAMs; TIGR01391; dnaG; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Primosome; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 590 DNA primase. FT /FTId=PRO_0000180510. FT DOMAIN 255 337 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT ZN_FING 37 61 CHC2-type. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 261 261 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 305 305 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 305 305 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 307 307 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. SQ SEQUENCE 590 AA; 65915 MW; 36DFCEAD470A1019 CRC64; MIPSDFIDEL LAKTDIVDII DEQVPLKKGG ANYMACCPFH KEKTPSFSVS PTKQFYHCFS CGAHGSAIGF VMEHQGLSFP EAVQFLADRV GMVVPKVHGQ NDNPEVRAER KKKQQTLEET TAAAADFYAQ QLKFNPAAKA YLDKRGLSAE VIAHYGLGYA PDGWQPLTQV FQPYPNTALV DTGMVIDNEG RHYDRFRHRI MFPIRNPRGQ VIGFGGRVLD DSKPKYLNSP DTPLFDKGKN LYGLYEGRAA VKEAGRILVV EGYMDVVALA QFGVGYGVAA LGTATTAEHV KILMRQADSI YFCFDGDSAG RKAAWRALEN ALPQLKDDKS LHFLFLPEEH DPDSYIRAYG KAQFEDALLN QSKPLSEYFW EHLSDGIHLN TQEGKAELVK TSSPLLAQIT APALAYLLKQ RLSELVGIDP DNLAQLLGQE APKRHVKQKN YKLPPISVKQ PVMLTLVQRQ IRSLLINPDW AAYIDLPDYL ALDGDFACLA NLAESIKNHA AVPETAQVLE YMRGSPYEET ITRIFHSTHQ SEEMNSSSEE DCENFQIGMK KLLNELKYSQ IETLKQKSLQ SGLNESEKKL LLSLLTAKQN // ID DPO4_NEIMB Reviewed; 318 AA. AC Q9JYS8; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=DNA polymerase IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE Short=Pol IV {ECO:0000255|HAMAP-Rule:MF_01113}; DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01113}; GN Name=dinB {ECO:0000255|HAMAP-Rule:MF_01113}; GN OrderedLocusNames=NMB1448; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved CC in untargeted mutagenesis. Copies undamaged DNA at stalled CC replication forks, which arise in vivo from mismatched or CC misaligned primer ends. These misaligned primers can be extended CC by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. CC May be involved in translesional synthesis, in conjunction with CC the beta clamp from PolIII. {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01113}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01113}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000255|HAMAP-Rule:MF_01113}. CC -!- SIMILARITY: Contains 1 umuC domain. {ECO:0000255|HAMAP- CC Rule:MF_01113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41808.1; -; Genomic_DNA. DR PIR; A81083; A81083. DR RefSeq; NP_274460.1; NC_003112.2. DR RefSeq; WP_010980939.1; NC_003112.2. DR ProteinModelPortal; Q9JYS8; -. DR STRING; 122586.NMB1448; -. DR PaxDb; Q9JYS8; -. DR EnsemblBacteria; AAF41808; AAF41808; NMB1448. DR GeneID; 903868; -. DR KEGG; nme:NMB1448; -. DR PATRIC; 20358627; VBINeiMen85645_1825. DR eggNOG; ENOG4105CQ3; Bacteria. DR eggNOG; COG0389; LUCA. DR HOGENOM; HOG000082707; -. DR KO; K02346; -. DR OMA; WIAQEIR; -. DR OrthoDB; EOG6FZ4D8; -. DR BioCyc; NMEN122586:GHGG-1486-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.100; -; 1. DR HAMAP; MF_01113; DNApol_IV; 1. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. DR InterPro; IPR022880; DNApol_IV. DR InterPro; IPR024728; PolY_HhH_motif. DR InterPro; IPR001126; UmuC. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR Pfam; PF11798; IMS_HHH; 1. DR SUPFAM; SSF100879; SSF100879; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication; KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; KW Mutator protein; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 318 DNA polymerase IV. FT /FTId=PRO_0000173929. FT DOMAIN 6 186 UmuC. {ECO:0000255|HAMAP-Rule:MF_01113}. FT ACT_SITE 105 105 {ECO:0000255|HAMAP-Rule:MF_01113}. FT METAL 10 10 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01113}. FT METAL 104 104 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01113}. FT SITE 15 15 Substrate discrimination. FT {ECO:0000255|HAMAP-Rule:MF_01113}. SQ SEQUENCE 318 AA; 35966 MW; A8D75AFDCDDAB9CB CRC64; MSSRKIIHID MDAFYASVEL REQPHLKGRP VVVAWEGARS VICAASYEAR QFGLHSAMSV ATAKRLCPQA VYVPPHFDLY RQVSAQIHAV FRRYTDLIEP LSLDEAYLDV TRNFKNIPYA GDVAKEIRAA IFAETGLTAS AGIAPNKFLA KIASDWRKPN GQFVLPPHKV MAFLETLPLG KIPGVGKVTL KKMQSLGMRT AGDLRRFERG ELLNHFGRYG YRLYDLVRGT DERPVKAERE RLQISTEITL PEDLPLEQAA GHLPHLAEDL WRQITRKNVE AQSVTLKLKT YDFRIITRTL TYSSVLPDCA LCCRLRKC // ID DTD_NEIMB Reviewed; 163 AA. AC Q9K143; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518}; DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase; GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=NMB0347; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate CC specificity. By recycling D-aminoacyl-tRNA to D-amino acids and CC free tRNA molecules, this enzyme counteracts the toxicity CC associated with the formation of D-aminoacyl-tRNA entities in CC vivo. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid + CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP- CC Rule:MF_00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40790.1; -; Genomic_DNA. DR PIR; A81210; A81210. DR RefSeq; NP_273396.1; NC_003112.2. DR RefSeq; WP_002224881.1; NC_003112.2. DR ProteinModelPortal; Q9K143; -. DR STRING; 122586.NMB0347; -. DR PaxDb; Q9K143; -. DR EnsemblBacteria; AAF40790; AAF40790; NMB0347. DR GeneID; 902462; -. DR KEGG; nme:NMB0347; -. DR PATRIC; 20355841; VBINeiMen85645_0439. DR eggNOG; ENOG4108YYA; Bacteria. DR eggNOG; COG1490; LUCA. DR HOGENOM; HOG000113982; -. DR KO; K07560; -. DR OMA; VFGADMK; -. DR OrthoDB; EOG6C2WM2; -. DR BioCyc; NMEN122586:GHGG-368-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.80.10; -; 1. DR HAMAP; MF_00518; Deacylase_Dtd; 1. DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD. DR InterPro; IPR023509; DTD-like_dom. DR PANTHER; PTHR10472; PTHR10472; 1. DR Pfam; PF02580; Tyr_Deacylase; 1. DR SUPFAM; SSF69500; SSF69500; 1. DR TIGRFAMs; TIGR00256; TIGR00256; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 163 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_0000164565. FT ACT_SITE 84 84 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00518}. SQ SEQUENCE 163 AA; 17639 MW; 0E06CA8A927A130D CRC64; MRAVIQKTVG AKVDVVSEAG TETCGKIDGG FVVLLGVTHS DTEKDARYIA DKIAHLRVFE DEAGKLNLSL KDVGGAVLLV SQFTLYADAA SGRRPSFSQA APAEQAQQLY LRTAELLRGH GIHVETGRFR THMQVSLCND GPVTILLDSF MTRISPKMKV VPD // ID DXR_NEIMB Reviewed; 394 AA. AC Q9K1G8; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183}; GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=NMB0184; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction CC of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol CC 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00183}. CC -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) CC = 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40641.1; -; Genomic_DNA. DR PIR; A81229; A81229. DR RefSeq; NP_273242.1; NC_003112.2. DR RefSeq; WP_002243949.1; NC_003112.2. DR ProteinModelPortal; Q9K1G8; -. DR SMR; Q9K1G8; 4-393. DR STRING; 122586.NMB0184; -. DR PaxDb; Q9K1G8; -. DR EnsemblBacteria; AAF40641; AAF40641; NMB0184. DR GeneID; 902291; -. DR KEGG; nme:NMB0184; -. DR PATRIC; 20355393; VBINeiMen85645_0226. DR eggNOG; ENOG4105CEA; Bacteria. DR eggNOG; COG0743; LUCA. DR HOGENOM; HOG000007221; -. DR KO; K00099; -. DR OMA; GFCPLSE; -. DR OrthoDB; EOG6R2H04; -. DR BioCyc; NMEN122586:GHGG-194-MONOMER; -. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070402; F:NADPH binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00183; DXP_reductoisom; 1. DR InterPro; IPR003821; DXP_reductoisomerase. DR InterPro; IPR013644; DXP_reductoisomerase_C. DR InterPro; IPR013512; DXP_reductoisomerase_N. DR InterPro; IPR026877; DXPR_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR30525; PTHR30525; 1. DR Pfam; PF08436; DXP_redisom_C; 1. DR Pfam; PF02670; DXP_reductoisom; 1. DR Pfam; PF13288; DXPR_C; 1. DR PIRSF; PIRSF006205; Dxp_reductismrs; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69055; SSF69055; 1. DR TIGRFAMs; TIGR00243; Dxr; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Metal-binding; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 394 1-deoxy-D-xylulose 5-phosphate FT reductoisomerase. FT /FTId=PRO_0000163683. FT NP_BIND 9 38 NADP. {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 152 152 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 154 154 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 228 228 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT BINDING 127 127 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 154 154 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 183 183 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 206 206 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 228 228 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. SQ SEQUENCE 394 AA; 41920 MW; AA85397E5BE7BD2E CRC64; MTPQVLTILG STGSIGESTL DVVSRHPEKF RVFALAGHKQ VEKLAAQCQT FHPEYAVVAD AEHAARLEAL LKRDGTATQV LHGAQALVDV ASADEVSGVM CAIVGAVGLP SALAAAQKGK TIYLANKETL VVSGALFMET ARANGAAVLP VDSEHNAVFQ VLPRDYAGRL NEHGIASIIL TASGGPFLTA DLNTFDRITP AQAVKHPNWR MGRKISVDSA TMMNKGLELI EAHWLFNCPP DKLEVVIHPQ SVIHSMVRYR DGSVLAQLGN PDMRTPIAYC LGLPERIDSG VGDLDFDALS ALTFQKPDFD RFPCLRLAYE AMNAGGAAPC VLNAANEAAV AAFLDGQIKF TDIAKTVAHC LAQDFSDGIG DIGGLLAQDA RTRAQARAFI GTLR // ID DSBD_NEIMB Reviewed; 601 AA. AC Q9JYM0; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=Thiol:disulfide interchange protein DsbD; DE EC=1.8.1.8; DE AltName: Full=Protein-disulfide reductase; DE Short=Disulfide reductase; DE Flags: Precursor; GN Name=dsbD; OrderedLocusNames=NMB1519; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required to facilitate the formation of correct CC disulfide bonds in some periplasmic proteins and for the assembly CC of the periplasmic c-type cytochromes. Acts by transferring CC electrons from cytoplasmic thioredoxin to the periplasm. This CC transfer involves a cascade of disulfide bond formation and CC reduction steps (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein CC disulfide + NAD(P)H. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41875.1; -; Genomic_DNA. DR PIR; F81074; F81074. DR RefSeq; NP_274527.1; NC_003112.2. DR RefSeq; WP_002244193.1; NC_003112.2. DR PDB; 2K0R; NMR; -; A=20-146. DR PDB; 2K9F; NMR; -; B=20-146. DR PDBsum; 2K0R; -. DR PDBsum; 2K9F; -. DR ProteinModelPortal; Q9JYM0; -. DR STRING; 122586.NMB1519; -. DR PaxDb; Q9JYM0; -. DR EnsemblBacteria; AAF41875; AAF41875; NMB1519. DR GeneID; 904002; -. DR KEGG; nme:NMB1519; -. DR PATRIC; 20358834; VBINeiMen85645_1927. DR eggNOG; ENOG4105CSG; Bacteria. DR eggNOG; COG4232; LUCA. DR HOGENOM; HOG000254982; -. DR KO; K04084; -. DR OMA; YISQTRD; -. DR OrthoDB; EOG69D3B9; -. DR BioCyc; NMEN122586:GHGG-1559-MONOMER; -. DR EvolutionaryTrace; Q9JYM0; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.40.1250; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00399; DbsD; 1. DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom. DR InterPro; IPR028250; DsbDN. DR InterPro; IPR022910; Thiol_diS_interchange_DbsD. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 2. DR Pfam; PF11412; DsbC; 1. DR Pfam; PF02683; DsbD; 1. DR Pfam; PF00085; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF74863; SSF74863; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Disulfide bond; Electron transport; KW Membrane; NAD; Oxidoreductase; Redox-active center; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 601 Thiol:disulfide interchange protein DsbD. FT /FTId=PRO_0000007378. FT TOPO_DOM 21 191 Periplasmic. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. FT TOPO_DOM 213 242 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. FT TOPO_DOM 264 266 Periplasmic. {ECO:0000255}. FT TRANSMEM 267 287 Helical. {ECO:0000255}. FT TOPO_DOM 288 310 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TOPO_DOM 332 346 Periplasmic. {ECO:0000255}. FT TRANSMEM 347 367 Helical. {ECO:0000255}. FT TOPO_DOM 368 380 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 381 401 Helical. {ECO:0000255}. FT TOPO_DOM 402 406 Periplasmic. {ECO:0000255}. FT TRANSMEM 407 427 Helical. {ECO:0000255}. FT TOPO_DOM 428 437 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 438 458 Helical. {ECO:0000255}. FT TOPO_DOM 459 601 Periplasmic. {ECO:0000255}. FT DOMAIN 467 601 Thioredoxin. FT DISULFID 120 126 Redox-active. {ECO:0000250}. FT DISULFID 207 328 Redox-active. {ECO:0000250}. FT DISULFID 519 522 Redox-active. {ECO:0000250}. FT HELIX 24 26 {ECO:0000244|PDB:2K0R}. FT TURN 29 31 {ECO:0000244|PDB:2K0R}. FT STRAND 32 39 {ECO:0000244|PDB:2K0R}. FT STRAND 41 50 {ECO:0000244|PDB:2K0R}. FT STRAND 54 57 {ECO:0000244|PDB:2K0R}. FT TURN 58 60 {ECO:0000244|PDB:2K0R}. FT STRAND 62 69 {ECO:0000244|PDB:2K0R}. FT STRAND 80 83 {ECO:0000244|PDB:2K0R}. FT STRAND 85 87 {ECO:0000244|PDB:2K0R}. FT STRAND 89 95 {ECO:0000244|PDB:2K0R}. FT STRAND 98 102 {ECO:0000244|PDB:2K0R}. FT STRAND 111 117 {ECO:0000244|PDB:2K0R}. FT STRAND 119 121 {ECO:0000244|PDB:2K0R}. FT TURN 122 124 {ECO:0000244|PDB:2K0R}. FT STRAND 130 138 {ECO:0000244|PDB:2K0R}. FT STRAND 140 142 {ECO:0000244|PDB:2K0R}. SQ SEQUENCE 601 AA; 64925 MW; AC19CBBF9E763A04 CRC64; MKKLICLFAV FLMLCGRAFA LDANDLLPPE KAFVPELAVA DDGVNVRFRI ADGYYMYQAK IVGKTDPADL LGQPSFSKGE EKEDEFFGRQ TVYHHEAQVA FPYAKAVGEP YKLVLTYQGC AEAGVCYPPV DTEFDIFGNG TYHPQTDEPA SAKDRFLQPS SQNGSGALPP PKGDEGGDSR FKLSWDTLNA NLLAFFLAGL GLSFTACMYP LLPIVSSIVV GDKKAGKARA FVLSVVYVQG LALTYTLVGI VAGLTGALLT VWLQQAWVVL AASALMVVLA LSMFGLFNIQ LPNAVQSYFQ NQSSRLSGGK IVSVFIMGIL SALIVGPCVA PPLAFALGYI GQTGDAVLGG LALYTLALGT GVPLIAIGTF GGHILPKAGD WMNAVKYAFG FILLAVAVYL ATPHLPYYLV VALYTLLMLV PAFMLLVNGR RQKRRPKAVA FALGGILLIG GAWFGWQGAN GKTTALHHFL TLNPPAEAGK SSEHGKMFAD TAALKAAMDT ALKEHPDKPV VLDFYADWCI SCKEMAAYTL NQPEVHQAVD MERFFQIDVT ANTPEHQALL KEYGLFGPPG VFVVRSDGSR SEPLLGFVKA DKFIEWYEQN R // ID DUSC_NEIMB Reviewed; 333 AA. AC Q9JZL5; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000255|HAMAP-Rule:MF_02043}; DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02043}; DE AltName: Full=U16-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02043}; DE Short=U16-specific Dus {ECO:0000255|HAMAP-Rule:MF_02043}; DE AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000255|HAMAP-Rule:MF_02043}; GN Name=dusC {ECO:0000255|HAMAP-Rule:MF_02043}; GN OrderedLocusNames=NMB0999; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. Specifically modifies CC U16 in tRNAs. {ECO:0000255|HAMAP-Rule:MF_02043}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(16) in tRNA + NAD(P)(+) = CC uracil(16) in tRNA + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_02043}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02043}; CC -!- SIMILARITY: Belongs to the Dus family. DusC subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41402.1; -; Genomic_DNA. DR PIR; G81132; G81132. DR RefSeq; NP_274035.1; NC_003112.2. DR RefSeq; WP_002225293.1; NC_003112.2. DR ProteinModelPortal; Q9JZL5; -. DR STRING; 122586.NMB0999; -. DR PaxDb; Q9JZL5; -. DR DNASU; 903134; -. DR EnsemblBacteria; AAF41402; AAF41402; NMB0999. DR GeneID; 903134; -. DR KEGG; nme:NMB0999; -. DR PATRIC; 20357517; VBINeiMen85645_1275. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR HOGENOM; HOG000217854; -. DR KO; K05541; -. DR OMA; GYKPPAH; -. DR OrthoDB; EOG6VHZFQ; -. DR BioCyc; NMEN122586:GHGG-1036-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02043; DusC_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR032886; DusC. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase; KW Reference proteome; RNA-binding; tRNA processing; tRNA-binding. FT CHAIN 1 333 tRNA-dihydrouridine(16) synthase. FT /FTId=PRO_0000162115. FT NP_BIND 19 21 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT NP_BIND 211 213 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT NP_BIND 235 236 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT ACT_SITE 110 110 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT BINDING 80 80 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT BINDING 151 151 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 47 47 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 107 107 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT SITE 188 188 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT SITE 289 289 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 291 291 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 312 312 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. SQ SEQUENCE 333 AA; 37258 MW; E59E122B820E9D7C CRC64; MIDRQTNEPK QKTRIILAPM QGLVDDVMRD LLTRIGGYDE CVSEFVRITH TVHSRSIWLK YVPEIANGNK TFSGTPCTVQ LLGSDADNMA ANALEAVRFG ANKIDLNFGC PAPTVNKHKG GAILLKEPEL IFHIVKTLRG RLPAHIPLTA KMRLGYEDKS RALECACAIA EGGACGLTVH ARTKAEGYEP PAHWEWIRKI RDSVNIPVTA NGDVFSLQDY IGIKTISGCN SVMLGRGAVI RPDLARQIKQ YENGGPVKDT DFAEVSKWIR QFFELCLTKE ANNKYPLARL KQWLGMMKKE FAAAQNLFDR VRTVKDADEV RNILAEFERE MNT // ID EFEMO_NEIMB Reviewed; 388 AA. AC Q9K1P6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Efem/EfeO family lipoprotein NMB0035; DE Flags: Precursor; GN OrderedLocusNames=NMB0035; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the EfeM/EfeO family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40506.1; -; Genomic_DNA. DR PIR; E81244; E81244. DR RefSeq; NP_273101.1; NC_003112.2. DR RefSeq; WP_002215233.1; NC_003112.2. DR STRING; 122586.NMB0035; -. DR PaxDb; Q9K1P6; -. DR PRIDE; Q9K1P6; -. DR EnsemblBacteria; AAF40506; AAF40506; NMB0035. DR GeneID; 902138; -. DR KEGG; nme:NMB0035; -. DR PATRIC; 20355023; VBINeiMen85645_0048. DR eggNOG; ENOG410650H; Bacteria. DR eggNOG; COG2822; LUCA. DR HOGENOM; HOG000236929; -. DR KO; K07224; -. DR OMA; PQLQKEN; -. DR OrthoDB; EOG696C0D; -. DR BioCyc; NMEN122586:GHGG-36-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR028096; EfeO_Cupredoxin. DR Pfam; PF13473; Cupredoxin_1; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 388 Efem/EfeO family lipoprotein NMB0035. FT /FTId=PRO_0000320326. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 388 AA; 42251 MW; ECF95AC5A74499C4 CRC64; MRKFNLTALS VMLALGLTAC QPPEAEKAAP AASGEAQTAN EGGSVSIAVN DNACEPMELT VPSGQVVFNI KNNSGRKLEW EILKGVMVVD ERENIAPGLS DKMTVTLLPG EYEMTCGLLT NPRGKLVVTD SGFKDTANEA DLEKLSQPLA DYKAYVQGEV KELVAKTKTF TEAVKAGDIE KAKSLFADTR VHYERIEPIA ELFSELDPVI DAREDDFKDG AKDAGFTGFH RIEYALWVEK DVSGVKEIAA KLMTDVEALQ KEIDALAFPP GKVVGGASEL IEEVAGSKIS GEEDRYSHTD LSDFQANVDG SKKIVDLFRP LIEAKNKALL EKTDTNFKQV NEILAKYRTK DGFETYDKLG EADRKALQAS INALAEDLAQ LRGILGLK // ID DXS_NEIMB Reviewed; 637 AA. AC Q9JXV7; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315}; DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315}; GN Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=NMB1867; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C CC atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield CC 1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1- CC deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00315}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00315}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose CC 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D- CC glyceraldehyde 3-phosphate and pyruvate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42201.1; -; Genomic_DNA. DR PIR; D81034; D81034. DR RefSeq; NP_274863.1; NC_003112.2. DR RefSeq; WP_002225782.1; NC_003112.2. DR ProteinModelPortal; Q9JXV7; -. DR SMR; Q9JXV7; 1-631. DR STRING; 122586.NMB1867; -. DR PaxDb; Q9JXV7; -. DR EnsemblBacteria; AAF42201; AAF42201; NMB1867. DR GeneID; 904321; -. DR KEGG; nme:NMB1867; -. DR PATRIC; 20359763; VBINeiMen85645_2387. DR eggNOG; ENOG4105C2V; Bacteria. DR eggNOG; COG1154; LUCA. DR HOGENOM; HOG000012986; -. DR KO; K01662; -. DR OMA; HKLTHEV; -. DR OrthoDB; EOG6BKJ6P; -. DR BioCyc; NMEN122586:GHGG-1923-MONOMER; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 3. DR HAMAP; MF_00315; DXP_synth; 1. DR InterPro; IPR005477; Dxylulose-5-P_synthase. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR020826; Transketolase_BS. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF13292; DXP_synthase_N; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 3. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00204; dxs; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate; KW Transferase. FT CHAIN 1 637 1-deoxy-D-xylulose-5-phosphate synthase. FT /FTId=PRO_0000189134. FT REGION 117 119 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT REGION 149 150 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT METAL 148 148 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT METAL 177 177 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT BINDING 76 76 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 177 177 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 294 294 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 381 381 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. SQ SEQUENCE 637 AA; 68750 MW; DF5FD396CF6FAF51 CRC64; MNPSPLLDLI DSPQDLRRLD KKQLPRLAGE LRTFLLESVG QTGGHFASNL GAVELTIALH YVYDTPEDKL VWDVGHQSYP HKILTGRKNQ MHTMRQYGGL AGFPKRCESE YDAFGVGHSS TSIGAALGMA AADKLLGSDR RSVAIIGDGA MTAGQAFEAL NCAGDMDVDL LVVLNDNEMS ISPNVGALPK YLASNVVRDM HGLLSTVKAQ TGKVLDKIPG AMEFAQKVEH KIKTLAEEAE HAKQSLSLFE NFGFRYTGPV DGHNVENLVD VLKDLRSRKG PQLLHVITKK GNGYKLAEND PVKYHAVANL PKESAAQMPS EKEPKPAAKP TYTQVFGKWL CDRAAADSRL VAITPAMREG SGLVEFEQRF PDRYFDVGIA EQHAVTFAGG LACEGMKPVV AIYSTFLQRA YDQLVHDIAL QNLPVLFAVD RAGIVGADGP THAGLYDLSF LRCVPNMIVA APSDENECRL LLSTCYQADA PAAVRYPRGT GTGAPVSDGM ETVEIGKGII RREGEKTAFI AFGSMVAPAL AVAEKLNATV ADMRFVKPID EELIVRLARS HDRIVTLEEN AEQGGAGGAV LEVLAKHGIC KPVLLLGVAD TVTGHGDPKK LLDDLGLSAE AVERRVRAWL SDRDAAN // ID EFTS_NEIMB Reviewed; 284 AA. AC P64051; Q9JRH4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050}; DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050}; GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=NMB2102; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_00050}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}. CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP- CC Rule:MF_00050}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42419.1; -; Genomic_DNA. DR PIR; G81006; G81006. DR RefSeq; NP_275090.1; NC_003112.2. DR RefSeq; WP_002218222.1; NC_003112.2. DR ProteinModelPortal; P64051; -. DR STRING; 122586.NMB2102; -. DR PaxDb; P64051; -. DR PRIDE; P64051; -. DR EnsemblBacteria; AAF42419; AAF42419; NMB2102. DR GeneID; 903937; -. DR KEGG; nme:NMB2102; -. DR PATRIC; 20360374; VBINeiMen85645_2684. DR eggNOG; ENOG4105CU7; Bacteria. DR eggNOG; COG0264; LUCA. DR HOGENOM; HOG000220986; -. DR KO; K02357; -. DR OMA; FIMEPKK; -. DR OrthoDB; EOG66B42N; -. DR BioCyc; NMEN122586:GHGG-2167-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.479.20; -; 3. DR HAMAP; MF_00050; EF_Ts; 1. DR InterPro; IPR001816; Transl_elong_EFTs/EF1B. DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer. DR InterPro; IPR018101; Transl_elong_Ts_CS. DR InterPro; IPR009060; UBA-like. DR PANTHER; PTHR11741; PTHR11741; 1. DR Pfam; PF00889; EF_TS; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR SUPFAM; SSF54713; SSF54713; 2. DR TIGRFAMs; TIGR00116; tsf; 1. DR PROSITE; PS01126; EF_TS_1; 1. DR PROSITE; PS01127; EF_TS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 284 Elongation factor Ts. FT /FTId=PRO_0000161162. FT REGION 80 83 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000255|HAMAP-Rule:MF_00050}. SQ SEQUENCE 284 AA; 30330 MW; 129F171D8B7E4630 CRC64; MAEITAKMVA DLRAATGLGM MECKKALVEA EGNFDKAEEI LRIKSGAKAG KLAGRTAAEG VLAYAINGNV GALVEVNCET DFVAKDAGFV EFANFVAKTA AEKKPASVEE LSELVEAERK AIIAKLGENM SVRRFQVIDT ANQLVAYIHG ALATEGVLVE YKGSEDVARK IGMHIVAAKP QCVSEAEVDA ETVEKERHIY TEQAIASGKP ADIAAKMVEG RIRKFLAEIT LNGQAFVMNP DQTVAQFSKE NGTEVISFVR YKVGDGIEKK AVDYAAEVAA AAKV // ID DYR_NEIMB Reviewed; 162 AA. AC Q9K168; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; OrderedLocusNames=NMB0308; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential CC reaction for de novo glycine and purine synthesis, and for DNA CC precursor synthesis (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660}. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00660}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40754.1; -; Genomic_DNA. DR PIR; G81214; G81214. DR RefSeq; NP_273358.1; NC_003112.2. DR RefSeq; WP_002218701.1; NC_003112.2. DR ProteinModelPortal; Q9K168; -. DR STRING; 122586.NMB0308; -. DR PaxDb; Q9K168; -. DR EnsemblBacteria; AAF40754; AAF40754; NMB0308. DR GeneID; 902424; -. DR KEGG; nme:NMB0308; -. DR PATRIC; 20355727; VBINeiMen85645_0383. DR eggNOG; ENOG4108YYV; Bacteria. DR eggNOG; COG0262; LUCA. DR HOGENOM; HOG000040234; -. DR KO; K00287; -. DR OMA; MCITHVE; -. DR OrthoDB; EOG6KT2V2; -. DR BioCyc; NMEN122586:GHGG-328-MONOMER; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR012259; DHFR. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR017925; DHFR_CS. DR InterPro; IPR001796; DHFR_dom. DR Pfam; PF00186; DHFR_1; 1. DR PIRSF; PIRSF000194; DHFR; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS00075; DHFR_1; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; One-carbon metabolism; Oxidoreductase; KW Reference proteome. FT CHAIN 1 162 Dihydrofolate reductase. FT /FTId=PRO_0000186403. FT DOMAIN 3 161 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT NP_BIND 8 9 NADP. {ECO:0000250}. FT NP_BIND 16 21 NADP. {ECO:0000250}. FT NP_BIND 45 48 NADP. {ECO:0000250}. FT NP_BIND 65 68 NADP. {ECO:0000250}. FT NP_BIND 98 103 NADP. {ECO:0000250}. FT REGION 7 9 Substrate binding. {ECO:0000250}. FT BINDING 29 29 Substrate. {ECO:0000250}. FT BINDING 60 60 Substrate. {ECO:0000250}. FT BINDING 117 117 Substrate. {ECO:0000250}. SQ SEQUENCE 162 AA; 17752 MW; B5EBB53CEABB8F62 CRC64; MLKITLIAAC AENLCIGAGN AMPWHIPEDF AFFKAYTLGK PVIMGRKTWE SLPVKPLPGR RNIVISRQAD YCAAGAETAA SLEAALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD LSVEGDAFFP AIDRTHWKEA ERTERRVSSK GTRYAFVHYL RY // ID EFG_NEIMB Reviewed; 701 AA. AC Q9K1I8; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054}; DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054}; GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; GN OrderedLocusNames=NMB0138; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step CC during translation elongation. During this step, the ribosome CC changes from the pre-translocational (PRE) to the post- CC translocational (POST) state as the newly formed A-site-bound CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E CC sites, respectively. Catalyzes the coordinated movement of the two CC tRNA molecules, the mRNA and conformational changes in the CC ribosome. {ECO:0000255|HAMAP-Rule:MF_00054}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40597.1; -; Genomic_DNA. DR PIR; C81234; C81234. DR RefSeq; NP_273196.1; NC_003112.2. DR RefSeq; WP_002218568.1; NC_003112.2. DR ProteinModelPortal; Q9K1I8; -. DR STRING; 122586.NMB0138; -. DR PaxDb; Q9K1I8; -. DR PRIDE; Q9K1I8; -. DR EnsemblBacteria; AAF40597; AAF40597; NMB0138. DR GeneID; 902246; -. DR KEGG; nme:NMB0138; -. DR PATRIC; 20355297; VBINeiMen85645_0178. DR eggNOG; ENOG4105CEJ; Bacteria. DR eggNOG; COG0480; LUCA. DR HOGENOM; HOG000231585; -. DR KO; K02355; -. DR OMA; GDTFCDP; -. DR OrthoDB; EOG6X6RBF; -. DR BioCyc; NMEN122586:GHGG-148-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004540; Transl_elong_EFG/EF2. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_II; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00484; EF-G; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 701 Elongation factor G. FT /FTId=PRO_0000091168. FT DOMAIN 8 290 tr-type G. FT NP_BIND 17 24 GTP. {ECO:0000255|HAMAP-Rule:MF_00054}. FT NP_BIND 88 92 GTP. {ECO:0000255|HAMAP-Rule:MF_00054}. FT NP_BIND 142 145 GTP. {ECO:0000255|HAMAP-Rule:MF_00054}. SQ SEQUENCE 701 AA; 77244 MW; 27FF7781B4A40B0D CRC64; MARKTPISLY RNIGISAHID AGKTTTTERI LFYTGLTHKL GEVHDGAATT DYMEQEQERG ITITSAAVTS YWSGMAKQFP EHRFNIIDTP GHVDFTVEVE RSMRVLDGAV MVYCAVGGVQ PQSETVWRQA NKYQVPRLAF VNKMDRQGAN FFRVVEQMKT RLRANPVPIV IPVGAEDNFS GVVDLLKMKS IIWNEVDKGT TFTYGDIPAE LVETAEEWRQ NMIEAAAEAS EELMDKYLGG DELTEEEIVG ALRQRTLAGE IQPMLCGSAF KNKGVQRMLD AVVELLPAPT DIPPVQGVNP NTEEADSRQA SDEEKFSALA FKMLNDKYVG QLTFIRVYSG VVKSGDTVLN SVKGTRERIG RLVQMTAADR TEIEEVRAGD IAAAIGLKDV TTGETLCAES APIILERMEF PEPVIHIAVE PKTKADQEKM GIALNRLAKE DPSFRVRTDE ESGQTIISGM GELHLEIIVD RMKREFGVEA NIGAPQVAYR ETIRKAVKAE YKHAKQSGGK GQYGHVVIEM EPMEPGGEGY EFIDEIKGGV IPREFIPSVD KGIRDTLPNG IVAGYPVVDV RIRLVFGSYH DVDSSQLAFE LAASQAFKEG MRQASPALLE PIMAVEVETP EEYMGDVMGD LNRRRGVVLG MDDDGIGGKK VRAEVPLAEM FGYSTDLRSA TQGRATYSME FKKYSEAPAH IAAAVTEARK G // ID EFTU_NEIMB Reviewed; 394 AA. AC P64027; Q9JRI5; Q9K1I7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA1; GN OrderedLocusNames=NMB0124; GN and GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA2; GN OrderedLocusNames=NMB0139; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40583.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40598.1; -; Genomic_DNA. DR PIR; A81235; A81235. DR PIR; D81234; D81234. DR RefSeq; NP_273182.1; NC_003112.2. DR RefSeq; NP_273197.1; NC_003112.2. DR RefSeq; WP_002215366.1; NC_003112.2. DR ProteinModelPortal; P64027; -. DR SMR; P64027; 2-394. DR STRING; 122586.NMB0124; -. DR PaxDb; P64027; -. DR PRIDE; P64027; -. DR EnsemblBacteria; AAF40583; AAF40583; NMB0124. DR EnsemblBacteria; AAF40598; AAF40598; NMB0139. DR GeneID; 902231; -. DR GeneID; 902247; -. DR KEGG; nme:NMB0124; -. DR KEGG; nme:NMB0139; -. DR PATRIC; 20355267; VBINeiMen85645_0164. DR eggNOG; ENOG4105CGV; Bacteria. DR eggNOG; COG0050; LUCA. DR HOGENOM; HOG000229290; -. DR KO; K02358; -. DR OMA; GMVICKP; -. DR OrthoDB; EOG6R5C6X; -. DR BioCyc; NMEN122586:GHGG-133-MONOMER; -. DR BioCyc; NMEN122586:GHGG-149-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00485; EF-Tu; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 394 Elongation factor Tu. FT /FTId=PRO_0000091357. FT DOMAIN 10 204 tr-type G. FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT REGION 19 26 G1. {ECO:0000250}. FT REGION 60 64 G2. {ECO:0000250}. FT REGION 81 84 G3. {ECO:0000250}. FT REGION 136 139 G4. {ECO:0000250}. FT REGION 174 176 G5. {ECO:0000250}. FT VARIANT 37 37 A -> S (in TufB). SQ SEQUENCE 394 AA; 42909 MW; 0C571C3D20CBE944 CRC64; MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTTILAKKF GGAAKAYDQI DNAPEEKARG ITINTSHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLARQVGVPY IIVFMNKCDM VDDAELLELV EMEIRDLLSS YDFPGDDCPI VQGSALKALE GDAAYEEKIF ELAAALDSYI PTPERAVDKP FLLPIEDVFS ISGRGTVVTG RVERGIIHVG DEIEIVGLKE TQKTTCTGVE MFRKLLDEGQ AGDNVGVLLR GTKREDVERG QVLAKPGTIT PHTKFKAEVY VLSKEEGGRH TPFFANYRPQ FYFRTTDVTG AVTLEEGVEM VMPGENVTIT VELIAPIAME EGLRFAIREG GRTVGAGVVS SVIA // ID ENO_NEIMB Reviewed; 428 AA. AC Q9JZ53; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=NMB1285; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible conversion of 2- CC phosphoglycerate into phosphoenolpyruvate. It is essential for the CC degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; CC -!- ENZYME REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for CC the export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. The export CC of enolase possibly depends on the covalent binding to the CC substrate; once secreted, it remains attached to the cell surface. CC {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41661.1; -; Genomic_DNA. DR PIR; D81100; D81100. DR RefSeq; NP_274305.1; NC_003112.2. DR RefSeq; WP_002222383.1; NC_003112.2. DR ProteinModelPortal; Q9JZ53; -. DR SMR; Q9JZ53; 2-426. DR STRING; 122586.NMB1285; -. DR PaxDb; Q9JZ53; -. DR PRIDE; Q9JZ53; -. DR EnsemblBacteria; AAF41661; AAF41661; NMB1285. DR GeneID; 903707; -. DR KEGG; nme:NMB1285; -. DR PATRIC; 20358197; VBINeiMen85645_1610. DR eggNOG; ENOG4105C70; Bacteria. DR eggNOG; COG0148; LUCA. DR HOGENOM; HOG000072174; -. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR BioCyc; NMEN122586:GHGG-1323-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR InterPro; IPR029017; Enolase_N-like. DR PANTHER; PTHR11902; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; KW Metal-binding; Reference proteome; Secreted. FT CHAIN 1 428 Enolase. FT /FTId=PRO_0000133935. FT REGION 364 367 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 205 205 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 337 337 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 242 242 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 285 285 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 312 312 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 155 155 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 285 285 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 312 312 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 337 337 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 388 388 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. SQ SEQUENCE 428 AA; 46134 MW; 08D0B6E661AF85EB CRC64; MSAIVDIFAR EILDSRGNPT VECDVLLESG VMGRAAVPSG ASTGQKEALE LRDGDKSRYS GKGVLKAVEH VNNQIAQALI GIDANEQSYI DQIMIELDGT ENKGNLGANA TLAVSMAVAR AAAEDSGLPL YRYLGGAGPM SLPVPMMNVI NGGEHANNSL NIQEFMIMPV GAKSFREALR CGAEIFHALK KLCDSKGFPT TVGDEGGFAP NLNSHKEALQ LMVEATEAAG YKAGEDVLFA LDCASSEFYK DGKYHLEAEG RSYTNAEFAE YLEGLVNEFP IISIEDGMDE NDWEGWKLLT EKLGGRVQLV GDDLFVTNPK ILAEGIEKGV ANALLVKVNQ IGTLSETLKA VDLAKRNRYA SVMSHRSGET EDSTIADLAV ATNCMQIKTG SLSRSDRMAK YNQLLRIEEE LAEAADYPSK AAFYQLGK // ID EFP_NEIMB Reviewed; 186 AA. AC Q9JZQ8; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141}; DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141}; GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141}; OrderedLocusNames=NMB0937; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient CC translation and peptide-bond synthesis on native or reconstituted CC 70S ribosomes in vitro. Probably functions indirectly by altering CC the affinity of the ribosome for aminoacyl-tRNA, thus increasing CC their reactivity as acceptors for peptidyl transferase. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41343.1; -; Genomic_DNA. DR PIR; F81139; F81139. DR RefSeq; NP_273975.1; NC_003112.2. DR RefSeq; WP_002219406.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ8; -. DR STRING; 122586.NMB0937; -. DR PaxDb; Q9JZQ8; -. DR EnsemblBacteria; AAF41343; AAF41343; NMB0937. DR GeneID; 23783072; -. DR GeneID; 903057; -. DR KEGG; nme:NMB0937; -. DR PATRIC; 20357347; VBINeiMen85645_1188. DR eggNOG; ENOG4105FUQ; Bacteria. DR eggNOG; COG0231; LUCA. DR HOGENOM; HOG000010047; -. DR KO; K02356; -. DR OMA; DRRDYQY; -. DR OrthoDB; EOG6JQH6Q; -. DR BioCyc; NMEN122586:GHGG-974-MONOMER; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 2. DR HAMAP; MF_00141; EF_P; 1. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR020599; Transl_elong_fac_P/YeiP. DR InterPro; IPR013185; Transl_elong_KOW-like. DR InterPro; IPR001059; Transl_elong_P/YeiP_cen. DR InterPro; IPR011768; Transl_elongation_fac_P. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF01132; EFP; 1. DR Pfam; PF08207; EFP_N; 1. DR Pfam; PF09285; Elong-fact-P_C; 1. DR PIRSF; PIRSF005901; EF-P; 1. DR SMART; SM01185; EFP; 1. DR SMART; SM00841; Elong-fact-P_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 2. DR TIGRFAMs; TIGR00038; efp; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 186 Elongation factor P. FT /FTId=PRO_0000094295. SQ SEQUENCE 186 AA; 20880 MW; 3502433BE9D8E189 CRC64; MKTAQELRAG NVFMVGNDPM VVQKTEYIKG GRSSAKVSMK LKNLLTGAAS ETIYKADDKF DVVILSRKNC TYSYFADPMY VFMDEEFNQY EIEADNIGDA LKFIVDGMED QCEVTFYEGN PISVELPTII VREVEYTEPA VKGDTSGKVM KTARLVGGTE IQVMSYIENG DKVEIDTRTG EFRKRA // ID ENGB_NEIMB Reviewed; 209 AA. AC Q9JY03; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-MAY-2016, entry version 88. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; GN OrderedLocusNames=NMB1806; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Necessary for normal cell division and for the CC maintenance of normal septation. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321}; CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- SIMILARITY: Contains 1 EngB-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_00321}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42143.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42143.1; ALT_INIT; Genomic_DNA. DR PIR; G81040; G81040. DR RefSeq; NP_274803.1; NC_003112.2. DR ProteinModelPortal; Q9JY03; -. DR STRING; 122586.NMB1806; -. DR PaxDb; Q9JY03; -. DR EnsemblBacteria; AAF42143; AAF42143; NMB1806. DR GeneID; 903292; -. DR KEGG; nme:NMB1806; -. DR PATRIC; 20359581; VBINeiMen85645_2296. DR eggNOG; ENOG4105WHM; Bacteria. DR eggNOG; COG0218; LUCA. DR HOGENOM; HOG000009832; -. DR KO; K03978; -. DR OMA; NKHESMV; -. DR OrthoDB; EOG6ND0NG; -. DR BioCyc; NMEN122586:GHGG-1861-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00321; GTPase_EngB; 1. DR InterPro; IPR030393; G_ENGB_dom. DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1. DR PROSITE; PS51706; G_ENGB; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; GTP-binding; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 209 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157768. FT DOMAIN 22 198 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 37 37 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 59 59 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. SQ SEQUENCE 209 AA; 23543 MW; BDBBBF9AA120D15B CRC64; MNLFQNAKFF TTINHLKDLP DTPLEIAFVG RSNAGKSSAI NTLTNHVRLA YVSKTPGRTQ HINFFELQNG NFMVDLPGYG YAQVPEAVRA HWVNLLGDYL QQRKQLIGLV LIMDARHPLK ELDIRMLDFF HTTGRPVHIL LSKADKLSKN EQIKTLSQVK KLLKPYSDRQ NISVQLFSSL KKQGIDEANR TVGSWLDAAD AAASSPEEN // ID EX7L_NEIMB Reviewed; 451 AA. AC Q9JYZ2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378}; DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; GN OrderedLocusNames=NMB1363; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41737.1; -; Genomic_DNA. DR PIR; D81092; D81092. DR RefSeq; NP_274381.1; NC_003112.2. DR RefSeq; WP_002225145.1; NC_003112.2. DR STRING; 122586.NMB1363; -. DR PaxDb; Q9JYZ2; -. DR EnsemblBacteria; AAF41737; AAF41737; NMB1363. DR GeneID; 903785; -. DR KEGG; nme:NMB1363; -. DR PATRIC; 20358389; VBINeiMen85645_1706. DR eggNOG; ENOG4105DVS; Bacteria. DR eggNOG; COG1570; LUCA. DR HOGENOM; HOG000229265; -. DR KO; K03601; -. DR OMA; PFMPKVI; -. DR OrthoDB; EOG64R65J; -. DR BioCyc; NMEN122586:GHGG-1401-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00378; Exonuc_7_L; 1. DR InterPro; IPR003753; Exonuc_VII_L. DR InterPro; IPR020579; Exonuc_VII_lsu_C. DR InterPro; IPR025824; OB-fold_nuc-bd_dom. DR Pfam; PF02601; Exonuc_VII_L; 1. DR Pfam; PF13742; tRNA_anti_2; 1. DR TIGRFAMs; TIGR00237; xseA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 451 Exodeoxyribonuclease 7 large subunit. FT /FTId=PRO_0000197863. SQ SEQUENCE 451 AA; 50080 MW; 28C5C55DDEA02471 CRC64; MSDFFHSDVL SVSELNAFAK SLLENHLAGL WIAGEVSNLT RAASGHYYFS LKDSRAQVRC AMFKGAAVRL AKPLKEGDHI EVSGKISIYE ARGEFQITVN EVRLKGLGQL YEAYERLKAQ LQAEGAFAAE RKKPLPVRPQ CIGIVTSLAA AALRDVVTTL KRRAPEIPVI VYPTPVQGAG SELQIAQAIK TASQRAECDV LIVCRGGGSI EDLWAFNEEP VVRAIESCTV PVVSGVGHET DFTLADFVAD MRAPTPTGAA ELVSPNRQES LHRLAQAQCR LKTVLEQRYF DASQKLDWLA RQIRHPRQKL DEQRASIGKL AQTLSYSMTQ NVRTHTARFE RQTQALKHCR PDVSVCKKNI DRFQTALSHA FHQLLTHRRQ SLTAQAALLE AVSPQHILER GFSVVKNTRG QVIRNADVLK QGQKLHIIFA DGETDVRVSK EQGQQDLFDC I // ID EX7S_NEIMB Reviewed; 74 AA. AC Q9K1A5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Exodeoxyribonuclease 7 small subunit; DE EC=3.1.11.6; DE AltName: Full=Exodeoxyribonuclease VII small subunit; DE Short=Exonuclease VII small subunit; GN Name=xseB; OrderedLocusNames=NMB0262; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40716.1; -; Genomic_DNA. DR PIR; G81217; G81217. DR RefSeq; NP_273318.1; NC_003112.2. DR RefSeq; WP_002221918.1; NC_003112.2. DR ProteinModelPortal; Q9K1A5; -. DR STRING; 122586.NMB0262; -. DR PaxDb; Q9K1A5; -. DR EnsemblBacteria; AAF40716; AAF40716; NMB0262. DR GeneID; 902373; -. DR KEGG; nme:NMB0262; -. DR PATRIC; 20355602; VBINeiMen85645_0325. DR eggNOG; ENOG41086UY; Bacteria. DR eggNOG; COG1722; LUCA. DR HOGENOM; HOG000228798; -. DR KO; K03602; -. DR OMA; VEQQVQV; -. DR OrthoDB; EOG69KV31; -. DR BioCyc; NMEN122586:GHGG-277-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.1040; -; 1. DR HAMAP; MF_00337; Exonuc_7_S; 1. DR InterPro; IPR003761; Exonuc_VII_S. DR Pfam; PF02609; Exonuc_VII_S; 1. DR PIRSF; PIRSF006488; Exonuc_VII_S; 1. DR ProDom; PD028235; Exonuc_VII_S; 1. DR TIGRFAMs; TIGR01280; xseB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 74 Exodeoxyribonuclease 7 small subunit. FT /FTId=PRO_0000206978. SQ SEQUENCE 74 AA; 8375 MW; 47E041B46AB775FF CRC64; MKKNAPKSFE EALSRLESLT QSMQGEMPLE DALAAYQEGN ELVRYCQTKL AQVEQKLQVL DTDGLKELNL ESDE // ID F16PA_NEIMB Reviewed; 324 AA. AC Q9JZH1; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855}; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=NMB1060; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01855}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01855}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SIMILARITY: Belongs to the FBPase class 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01855}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41456.1; -; Genomic_DNA. DR PIR; F81126; F81126. DR RefSeq; NP_274093.1; NC_003112.2. DR RefSeq; WP_002244111.1; NC_003112.2. DR ProteinModelPortal; Q9JZH1; -. DR STRING; 122586.NMB1060; -. DR PaxDb; Q9JZH1; -. DR EnsemblBacteria; AAF41456; AAF41456; NMB1060. DR GeneID; 903477; -. DR KEGG; nme:NMB1060; -. DR PATRIC; 20357663; VBINeiMen85645_1348. DR eggNOG; ENOG4105CZI; Bacteria. DR eggNOG; COG0158; LUCA. DR HOGENOM; HOG000191264; -. DR KO; K03841; -. DR OMA; YTTRYIG; -. DR OrthoDB; EOG6X10TR; -. DR BioCyc; NMEN122586:GHGG-1097-MONOMER; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01855; FBPase_class1; 1. DR InterPro; IPR000146; FBPase_class-1. DR InterPro; IPR033391; FBPase_N. DR InterPro; IPR028343; FBPtase. DR PANTHER; PTHR11556; PTHR11556; 1. DR Pfam; PF00316; FBPase; 1. DR PIRSF; PIRSF500210; FBPtase; 1. DR PIRSF; PIRSF000904; FBPtase_SBPase; 1. DR PRINTS; PR00115; F16BPHPHTASE. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 324 Fructose-1,6-bisphosphatase class 1. FT /FTId=PRO_0000364608. FT REGION 110 113 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 88 88 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 107 107 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 107 107 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 109 109 Magnesium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01855}. FT METAL 110 110 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 271 271 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT BINDING 199 199 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT BINDING 265 265 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01855}. SQ SEQUENCE 324 AA; 35581 MW; B69F83DCC4D42487 CRC64; MDTLTRFLPE HLQQNQLPEA LGGVLLSVVS ACTEINAKVR LGALAGVLGM AGTGNIQGED QKKLDVIANN IMIDTLKANS AVAGLASEEE DTFVNAGENG RYLVLFDPLD GSSNIDVNIS VGTIFSILEK PEGALATESF LQTGRQQLAA GYVLYGPQTQ LVFTFGHGVY MFTLNAENEF VLTKENPKVP ESTKEFAINM SNRRHWLPPV QQYIDELLAG ETGTRGKNYN MRWVASMVAE IHRILMRGGV FMYPQDKRDP AKPGKLRLMY EANPMSLILE QAGASASNAY QAMLDIQPEN LHQRVAVFMG SSEEVAYLDR LHAK // ID ERA_NEIMB Reviewed; 307 AA. AC Q9K0C7; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 16-MAR-2016, entry version 98. DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367}; GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=NMB0687; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with CC rapid nucleotide exchange. Plays a role in 16S rRNA processing and CC 30S ribosomal subunit biogenesis and possibly also in cell cycle CC regulation and energy metabolism. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Contains 1 Era-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41105.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41105.1; ALT_INIT; Genomic_DNA. DR PIR; F81169; F81169. DR RefSeq; NP_273729.1; NC_003112.2. DR ProteinModelPortal; Q9K0C7; -. DR STRING; 122586.NMB0687; -. DR PaxDb; Q9K0C7; -. DR EnsemblBacteria; AAF41105; AAF41105; NMB0687. DR GeneID; 902799; -. DR KEGG; nme:NMB0687; -. DR PATRIC; 20356687; VBINeiMen85645_0861. DR eggNOG; ENOG4105CWT; Bacteria. DR eggNOG; COG1159; LUCA. DR HOGENOM; HOG000245597; -. DR KO; K03595; -. DR OMA; FDDITHN; -. DR OrthoDB; EOG68DD1Q; -. DR BioCyc; NMEN122586:GHGG-715-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00367; GTPase_Era; 1. DR InterPro; IPR030388; G_ERA_dom. DR InterPro; IPR005662; GTP-bd_Era. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF07650; KH_2; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR TIGRFAMs; TIGR00436; era; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51713; G_ERA; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; KW Ribosome biogenesis; RNA-binding; rRNA-binding. FT CHAIN 1 307 GTPase Era. FT /FTId=PRO_0000180034. FT DOMAIN 17 186 Era-type G. FT DOMAIN 217 293 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_00367}. FT NP_BIND 25 32 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 72 76 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 133 136 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. SQ SEQUENCE 307 AA; 34617 MW; EAD0B680C6DA9D2A CRC64; MDIETFLAGE RAAGGYRCGF VAIVGRPNVG KSTLMNHLIG QKISITSKKA QTTRNRVTGI YTDDTAQFVF VDTPGFQTDH RNALNDRLNQ NVTEALGGVD VVVFVVEAMR FTDADRVVLK QLPKHTPVIL VVNKIDKDKA KDRYALEAFV AQVRAEFEFA AAEAVSAKHG LRIANLLELI KPYLPESVPM YPEDMVTDKS ARFLAMEIVR EKLFRYLGEE LPYAMNVEVE QFEEEDGLNR IYIAVLVDKE SQKAILIGKG GERLKKISTE ARLDMEKLFD TKVFLKVWVK VKSGWADDIR FLRELGL // ID ERPA_NEIMB Reviewed; 112 AA. AC Q7DDN1; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Putative iron-sulfur cluster insertion protein ErpA {ECO:0000255|HAMAP-Rule:MF_01380}; GN Name=erpA {ECO:0000255|HAMAP-Rule:MF_01380}; GN OrderedLocusNames=NMB0557; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for insertion of 4Fe-4S clusters. CC {ECO:0000255|HAMAP-Rule:MF_01380}. CC -!- COFACTOR: CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01380}; CC Note=Binds 1 iron-sulfur cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01380}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01380}. CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000255|HAMAP- CC Rule:MF_01380}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40985.1; -; Genomic_DNA. DR PIR; H81183; H81183. DR RefSeq; NP_273601.1; NC_003112.2. DR RefSeq; WP_002219692.1; NC_003112.2. DR ProteinModelPortal; Q7DDN1; -. DR SMR; Q7DDN1; 6-112. DR STRING; 122586.NMB0557; -. DR PaxDb; Q7DDN1; -. DR EnsemblBacteria; AAF40985; AAF40985; NMB0557. DR GeneID; 902672; -. DR KEGG; nme:NMB0557; -. DR PATRIC; 20356385; VBINeiMen85645_0712. DR eggNOG; ENOG4108YX9; Bacteria. DR eggNOG; COG0316; LUCA. DR HOGENOM; HOG000228313; -. DR KO; K15724; -. DR OMA; FDENVND; -. DR OrthoDB; EOG6VXF8J; -. DR BioCyc; NMEN122586:GHGG-583-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.300.12; -; 1. DR HAMAP; MF_01380; Fe_S_insert_ErpA; 1. DR InterPro; IPR000361; FeS_biogenesis. DR InterPro; IPR016092; FeS_cluster_insertion. DR InterPro; IPR017870; FeS_cluster_insertion_CS. DR InterPro; IPR023063; FeS_cluster_insertion_RrpA. DR Pfam; PF01521; Fe-S_biosyn; 1. DR SUPFAM; SSF89360; SSF89360; 1. DR TIGRFAMs; TIGR00049; TIGR00049; 1. DR PROSITE; PS01152; HESB; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 112 Putative iron-sulfur cluster insertion FT protein ErpA. FT /FTId=PRO_0000311509. FT METAL 40 40 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. FT METAL 104 104 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. FT METAL 106 106 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. SQ SEQUENCE 112 AA; 12291 MW; C2EFE747CB58D182 CRC64; MSDESPIIFT DSCCAKVADL IAEENNPDLK LRVFVNGGGC SGFQYGFTFD EIKNDDDFEI EKNGLVFLVD PMSYQYLVGA EIDYTESLQG SQFVIRNPNA ETTCGCGSSF SV // ID EXBB_NEIMB Reviewed; 220 AA. AC P64100; P57027; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Biopolymer transport protein ExbB; GN Name=exbB; OrderedLocusNames=NMB1729; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the TonB-dependent energy-dependent CC transport of various receptor-bound substrates. Protects ExbD from CC proteolytic degradation and functionally stabilizes TonB (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a CC complex with TonB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the ExbB/TolQ family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42074.1; -; Genomic_DNA. DR PIR; H81048; H81048. DR RefSeq; NP_274732.1; NC_003112.2. DR RefSeq; WP_002216612.1; NC_003112.2. DR STRING; 122586.NMB1729; -. DR PaxDb; P64100; -. DR EnsemblBacteria; AAF42074; AAF42074; NMB1729. DR GeneID; 903370; -. DR KEGG; nme:NMB1729; -. DR PATRIC; 20359421; VBINeiMen85645_2216. DR eggNOG; ENOG4108PAU; Bacteria. DR eggNOG; COG0811; LUCA. DR HOGENOM; HOG000134792; -. DR KO; K03561; -. DR OMA; SQAINHQ; -. DR OrthoDB; EOG6JDWB5; -. DR BioCyc; NMEN122586:GHGG-1784-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR InterPro; IPR002898; MotA_ExbB_proton_chnl. DR Pfam; PF01618; MotA_ExbB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 220 Biopolymer transport protein ExbB. FT /FTId=PRO_0000145807. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. SQ SEQUENCE 220 AA; 24144 MW; 9B5D5183CDD11D7D CRC64; MNLKLVFESG DPVLIGVFVL MLLMSIVTWC LVVLRCIKLY RARKGNAAVK RHMRDTLSLN DAVEKVRAVD APLSKLAQEA LQSYRNYRRN EASELAQALP LNEYLVIQIR NSMAQIMRRF DYGMTALASI GATAPFIGLF GTVWGIYHAL INIGQSGQMS IAAVAGPIGE ALVATAAGLF VAIPAVLAYN FLNRGTKILT QDLDAMAHDL HVRLLNQKDS // ID EXBD_NEIMB Reviewed; 144 AA. AC P0A0R9; P95376; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE RecName: Full=Biopolymer transport protein ExbD; GN Name=exbD; OrderedLocusNames=NMB1728; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the TonB-dependent energy-dependent CC transport of various receptor-bound substrates. {ECO:0000250}. CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a CC complex with TonB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass type II membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ExbD/TolR family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42073.1; -; Genomic_DNA. DR PIR; G81048; G81048. DR RefSeq; NP_274731.1; NC_003112.2. DR RefSeq; WP_002212592.1; NC_003112.2. DR ProteinModelPortal; P0A0R9; -. DR STRING; 122586.NMB1728; -. DR PaxDb; P0A0R9; -. DR EnsemblBacteria; AAF42073; AAF42073; NMB1728. DR GeneID; 903371; -. DR KEGG; nme:NMB1728; -. DR PATRIC; 20359419; VBINeiMen85645_2215. DR eggNOG; ENOG4105M8F; Bacteria. DR eggNOG; COG0848; LUCA. DR HOGENOM; HOG000134906; -. DR KO; K03559; -. DR OMA; RAMASIE; -. DR OrthoDB; EOG6TJ80C; -. DR BioCyc; NMEN122586:GHGG-1783-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003400; ExbD. DR Pfam; PF02472; ExbD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 144 Biopolymer transport protein ExbD. FT /FTId=PRO_0000129126. FT TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TOPO_DOM 40 144 Periplasmic. {ECO:0000255}. SQ SEQUENCE 144 AA; 15514 MW; 96DCD7A142DAC370 CRC64; MAFGSMNSGD DSPMSDINVT PLVDVMLVLL IVFMITMPVL THSIPLELPT ASEQTNKQDK QPKDPLRLTI DANGGYYVGG DSASKVEIGE VESRLKAAKE QNENVIVAIA ADKAVEYDYV NKALEAARQA GITKIGFVTE TKAQ // ID FABZ_NEIMB Reviewed; 149 AA. AC P95378; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406}; DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; GN Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; GN OrderedLocusNames=NMB0179; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=9197543; DOI=10.1016/S0378-1119(97)00005-X; RA Steeghs L., Jennings M.P., Poolman J.T., Der Ley P.; RT "Isolation and characterization of the Neisseria meningitidis lpxD- RT fabZ-lpxA gene cluster involved in lipid A biosynthesis."; RL Gene 190:263-270(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. CC Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and CC long chain saturated and unsaturated beta-hydroxyacyl-ACPs. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U79481; AAC45423.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40636.1; -; Genomic_DNA. DR PIR; D81228; D81228. DR RefSeq; NP_273237.1; NC_003112.2. DR RefSeq; WP_002218583.1; NC_003112.2. DR ProteinModelPortal; P95378; -. DR STRING; 122586.NMB0179; -. DR PaxDb; P95378; -. DR EnsemblBacteria; AAF40636; AAF40636; NMB0179. DR GeneID; 902286; -. DR KEGG; nme:NMB0179; -. DR PATRIC; 20355383; VBINeiMen85645_0221. DR eggNOG; ENOG4108YXN; Bacteria. DR eggNOG; COG0764; LUCA. DR HOGENOM; HOG000277829; -. DR KO; K02372; -. DR OMA; AMIKDKS; -. DR OrthoDB; EOG6JTCGM; -. DR BioCyc; NMEN122586:GHGG-189-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.129.10; -; 1. DR HAMAP; MF_00406; FabZ; 1. DR InterPro; IPR013114; FabA_FabZ. DR InterPro; IPR010084; FabZ. DR InterPro; IPR029069; HotDog_dom. DR Pfam; PF07977; FabA; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR01750; fabZ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome. FT CHAIN 1 149 3-hydroxyacyl-[acyl-carrier-protein] FT dehydratase FabZ. FT /FTId=PRO_0000091703. FT ACT_SITE 53 53 {ECO:0000255|HAMAP-Rule:MF_00406}. SQ SEQUENCE 149 AA; 16627 MW; 8B3D7B544D56C10E CRC64; MDVQLPIEAK DIQKLIPHRY PFLQLDRITA FEPMKTLTAI KNVTINEPQF QGHFPDLPVM PGVLIIEAMA QACGTLAILS EGGRKENEFF FFAGIDEARF KRQVIPGDQL VFEVELLTSR RGIGKFNAVA KVDGQVAVEA IIMCAKRVV // ID FBPC_NEIMB Reviewed; 352 AA. AC Q4W575; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC {ECO:0000255|HAMAP-Rule:MF_01706}; DE EC=3.6.3.30 {ECO:0000255|HAMAP-Rule:MF_01706}; GN Name=fbpC {ECO:0000255|HAMAP-Rule:MF_01706}; GN OrderedLocusNames=NMB0632; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter complex FbpABC involved in CC Fe(3+) ions import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + Fe(3+)(Out) = ADP + phosphate + CC Fe(3+)(In). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01706}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion CC importer (TC 3.A.1.10) family. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52135.1; -; Genomic_DNA. DR RefSeq; NP_273675.1; NC_003112.2. DR RefSeq; WP_002219640.1; NC_003112.2. DR ProteinModelPortal; Q4W575; -. DR STRING; 122586.NMB0632; -. DR PaxDb; Q4W575; -. DR EnsemblBacteria; AAY52135; AAY52135; NMB0632. DR GeneID; 903196; -. DR KEGG; nme:NMB0632; -. DR PATRIC; 20356561; VBINeiMen85645_0800. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR KO; K02010; -. DR OMA; AINICID; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-658-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015408; F:ferric-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015853; ABC_transpr_FbpC. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51242; FBPC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Ion transport; Iron; Iron transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 352 Fe(3+) ions import ATP-binding protein FT FbpC. FT /FTId=PRO_0000272041. FT DOMAIN 5 239 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01706}. FT NP_BIND 37 44 ATP. {ECO:0000255|HAMAP-Rule:MF_01706}. SQ SEQUENCE 352 AA; 37881 MW; 7648115E055FF3FA CRC64; MTAALHIGHL SKSFQNTPVL NDISLSLDPG EILFIVGASG CGKTTLLRCL AGFEQPDFGE ISLSGRTIFS KNTNLPVRER RLGYVVQEGV LFPHLTVYRN TAYGLGNGKG KTAQERQRIE AMLELTGISE LAGRYPHELS GGQQQRVALA RALAPDPELI LLDEPFSALD EQLRRQIRED MIAALRANGK SAVFVSHDRE EALQYADRIA VMKQGRILQT ASPHELYRQP ADLDAALFIG EGIVFPAALN ADGTADCGLG RLPVQSGAPA GTRGTLLIRP EQFSLHPHSA PTASIHAVVL KTTPKARHTE ISLRVGQTVL TLNLPSAPTL SDGISAVLHL DGPALFFPGN TL // ID FABH_NEIMB Reviewed; 320 AA. AC Q9JXR6; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815}; DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815}; GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; GN OrderedLocusNames=NMB1916; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. Catalyzes the first condensation reaction which CC initiates fatty acid synthesis and may therefore play a role in CC governing the total rate of fatty acid production. Possesses both CC acetoacetyl-ACP synthase and acetyl transacylase activities. Its CC substrate specificity determines the biosynthesis of branched- CC chain and/or straight-chain of fatty acids. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + malonyl-[acyl-carrier-protein] = CC acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential CC for the weak association between ACP/AcpP and FabH. CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SIMILARITY: Belongs to the FabH family. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42246.1; -; Genomic_DNA. DR PIR; C81029; C81029. DR RefSeq; NP_274910.1; NC_003112.2. DR RefSeq; WP_002225817.1; NC_003112.2. DR ProteinModelPortal; Q9JXR6; -. DR SMR; Q9JXR6; 3-320. DR STRING; 122586.NMB1916; -. DR PaxDb; Q9JXR6; -. DR EnsemblBacteria; AAF42246; AAF42246; NMB1916. DR GeneID; 904246; -. DR KEGG; nme:NMB1916; -. DR PATRIC; 20359879; VBINeiMen85645_2444. DR eggNOG; ENOG4105CCZ; Bacteria. DR eggNOG; COG0332; LUCA. DR HOGENOM; HOG000246674; -. DR KO; K00648; -. DR OMA; ESGMYEN; -. DR OrthoDB; EOG6J74XN; -. DR BioCyc; NMEN122586:GHGG-1973-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.47.10; -; 2. DR HAMAP; MF_01815; FabH; 1. DR InterPro; IPR013751; ACP_syn_III. DR InterPro; IPR013747; ACP_syn_III_C. DR InterPro; IPR004655; FabH_synth. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF08545; ACP_syn_III; 1. DR Pfam; PF08541; ACP_syn_III_C; 1. DR SUPFAM; SSF53901; SSF53901; 1. DR TIGRFAMs; TIGR00747; fabH; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Multifunctional enzyme; Reference proteome; KW Transferase. FT CHAIN 1 320 3-oxoacyl-[acyl-carrier-protein] synthase FT 3. FT /FTId=PRO_0000110446. FT REGION 248 252 ACP-binding. {ECO:0000255|HAMAP- FT Rule:MF_01815}. FT ACT_SITE 114 114 {ECO:0000255|HAMAP-Rule:MF_01815}. FT ACT_SITE 247 247 {ECO:0000255|HAMAP-Rule:MF_01815}. FT ACT_SITE 277 277 {ECO:0000255|HAMAP-Rule:MF_01815}. SQ SEQUENCE 320 AA; 33789 MW; 5B0B51F622CCF5A4 CRC64; MQYAKISGTG SYLPANRVSN DDLAQKVDTS DEWITARTGI KFRHIAAENE KTSDLAAEAA HRALDAAGLD SGEIDLIIVA TATPDMQFPS TATIVQQKLG ITNGCPAFDV QAVCAGFMYA LTTANAYIKS GMAKNALVIG AETFSRIVDW NDRTTCVLFG DGAGAVVLSA SDTPGIIHSK LKADGNYLKL LNVPGQIACG KVSGSPYISM DGPGVFKFAV KMLSKIADDV IEEAGYTAAQ IDWIVPHQAN RRIIESTAKH LGLSMDKVVL TVQDHGNTSA ASIPLALDTG IRSGQIKRGQ NLLLEGIGGG FAWGAVLLQY // ID FBPA_NEIMB Reviewed; 331 AA. AC P0A0Y4; P17940; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Major ferric iron-binding protein; DE Short=FBP; DE AltName: Full=Iron(III) periplasmic-binding protein; DE AltName: Full=Major iron-regulated protein; DE Short=MIRP; DE Flags: Precursor; GN Name=fbpA; Synonyms=fbp; OrderedLocusNames=NMB0634; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: This protein may be a central component in the iron- CC acquisition system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41057.1; -; Genomic_DNA. DR PIR; D81177; D81177. DR RefSeq; NP_273677.1; NC_003112.2. DR RefSeq; WP_002214250.1; NC_003112.2. DR ProteinModelPortal; P0A0Y4; -. DR SMR; P0A0Y4; 23-331. DR STRING; 122586.NMB0634; -. DR PaxDb; P0A0Y4; -. DR EnsemblBacteria; AAF41057; AAF41057; NMB0634. DR GeneID; 902745; -. DR KEGG; nme:NMB0634; -. DR PATRIC; 20356565; VBINeiMen85645_0802. DR eggNOG; ENOG4107QKW; Bacteria. DR eggNOG; COG1840; LUCA. DR HOGENOM; HOG000238625; -. DR KO; K02012; -. DR OMA; FTAYKGN; -. DR OrthoDB; EOG625JVF; -. DR BioCyc; NMEN122586:GHGG-660-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-4149-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR InterPro; IPR026045; Ferric-bd. DR InterPro; IPR006061; SBP_1_CS. DR InterPro; IPR006059; SBP_1_dom. DR Pfam; PF01547; SBP_bac_1; 1. DR PIRSF; PIRSF002825; CfbpA; 1. DR PROSITE; PS01037; SBP_BACTERIAL_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Ion transport; Iron; Iron transport; Metal-binding; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 22 {ECO:0000250}. FT CHAIN 23 331 Major ferric iron-binding protein. FT /FTId=PRO_0000031692. FT METAL 31 31 Iron. {ECO:0000250}. FT METAL 79 79 Iron. {ECO:0000250}. FT METAL 217 217 Iron. {ECO:0000250}. FT METAL 218 218 Iron. {ECO:0000250}. SQ SEQUENCE 331 AA; 35828 MW; 3FD53DFA251C7CE0 CRC64; MKTSIRYALL AAALTAATPA LADITVYNGQ HKEAAQAVAD AFTRATGIKV KLNSAKGDQL AGQIKEEGSR SPADVFYSEQ IPALATLSAA NLLEPLPAST INETRGKGVP VAAKKDWVAL SGRSRVVVYD TRKLSEKDLE KSVLNYATPK WKNRIGYAPT SGAFLEQVVA IVKLKGEAAA LKWLKGLKEY GKPYAKNSVA LQAVENGEID AALINNYYWH AFAREKGVQN VHTRLNFVRH RDPGALVTYS GAAVLKSSQN KDEAKKFVAF LASKEGQRAL TAVRAEYPLN PHVVSTFNLE PIAKLEAPQV SATTVSEKEH ATRLLEQAGM K // ID FABI_NEIMB Reviewed; 261 AA. AC Q9K151; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; DE Short=ENR; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; OrderedLocusNames=NMB0336; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond CC in an enoyl moiety that is covalently linked to an acyl carrier CC protein (ACP). Involved in the elongation cycle of fatty acid CC which are used in the lipid metabolism (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a CC trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. FabI subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40779.1; -; Genomic_DNA. DR PIR; C81211; C81211. DR RefSeq; NP_273385.1; NC_003112.2. DR RefSeq; WP_002223367.1; NC_003112.2. DR ProteinModelPortal; Q9K151; -. DR SMR; Q9K151; 2-258. DR STRING; 122586.NMB0336; -. DR PaxDb; Q9K151; -. DR PRIDE; Q9K151; -. DR EnsemblBacteria; AAF40779; AAF40779; NMB0336. DR GeneID; 902451; -. DR KEGG; nme:NMB0336; -. DR PATRIC; 20355813; VBINeiMen85645_0425. DR eggNOG; ENOG4105CSJ; Bacteria. DR eggNOG; COG0623; LUCA. DR KO; K00208; -. DR OMA; GILDMIH; -. DR OrthoDB; EOG6HF644; -. DR BioCyc; NMEN122586:GHGG-357-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PANTHER; PTHR24322:SF317; PTHR24322:SF317; 2. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 261 Enoyl-[acyl-carrier-protein] reductase FT [NADH] FabI. FT /FTId=PRO_0000320269. FT NP_BIND 19 20 NAD. {ECO:0000250}. FT NP_BIND 64 65 NAD. {ECO:0000250}. FT NP_BIND 193 197 NAD. {ECO:0000250}. FT ACT_SITE 147 147 Proton acceptor. {ECO:0000250}. FT ACT_SITE 157 157 Proton acceptor. {ECO:0000250}. FT BINDING 13 13 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 92 92 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 95 95 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000250}. FT BINDING 164 164 NAD. {ECO:0000250}. FT SITE 206 206 Involved in acyl-ACP binding. FT {ECO:0000250}. SQ SEQUENCE 261 AA; 27691 MW; AF2D0C70F550253D CRC64; MGFLQGKKIL ITGMISERSI AYGIAKACRE QGAELAFTYV VDKLEERVRK MAAELDSELV FRCDVASDDE INQVFADLGK HWDGLDGLVH SIGFAPKEAL SGDFLDSISR EAFNTAHEIS AYSLPALAKA ARPMMRGRNS AIVALSYLGA VRAIPNYNVM GMAKASLEAG IRFTAACLGK EGIRCNGISA GPIKTLAASG IADFGKLLGH VAAHNPLRRN VTIEEVGNTA AFLLSDLSSG ITGEITYVDG GYSINALSTE G // ID FKBA_NEIMB Reviewed; 272 AA. AC Q9JYI8; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Rotamase; DE Flags: Precursor; GN Name=fkpA; OrderedLocusNames=NMB1567; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41921.1; -; Genomic_DNA. DR PIR; C81068; C81068. DR RefSeq; NP_274574.1; NC_003112.2. DR RefSeq; WP_002212827.1; NC_003112.2. DR ProteinModelPortal; Q9JYI8; -. DR STRING; 122586.NMB1567; -. DR PaxDb; Q9JYI8; -. DR EnsemblBacteria; AAF41921; AAF41921; NMB1567. DR GeneID; 904149; -. DR KEGG; nme:NMB1567; -. DR PATRIC; 20358996; VBINeiMen85645_2017. DR eggNOG; ENOG4108V1T; Bacteria. DR eggNOG; COG0545; LUCA. DR HOGENOM; HOG000154888; -. DR KO; K03772; -. DR OMA; GRYIANT; -. DR OrthoDB; EOG6DRPKW; -. DR BioCyc; NMEN122586:GHGG-1608-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.10.287.460; -; 1. DR InterPro; IPR008104; INFPOTNTIATR. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR InterPro; IPR000774; PPIase_FKBP_N. DR PANTHER; PTHR10516; PTHR10516; 2. DR Pfam; PF00254; FKBP_C; 1. DR Pfam; PF01346; FKBP_N; 1. DR PRINTS; PR01730; INFPOTNTIATR. DR PROSITE; PS50059; FKBP_PPIASE; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Isomerase; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Rotamase; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 272 Probable FKBP-type peptidyl-prolyl cis- FT trans isomerase FkpA. FT /FTId=PRO_0000349891. FT DOMAIN 167 253 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. FT LIPID 21 21 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 21 21 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 272 AA; 28894 MW; 5BF9AD2A7A6217C8 CRC64; MNTIFKISAL TLSAALALSA CGKKEAAPAS ASEPAAASSA QGDTSSIGST MQQASYAMGV DIGRSLKQMK EQGAEIDLKV FTEAMQAVYD GKEIKMTEEQ AQEVMMKFLQ EQQAKAVEKH KADAKANKEK GEAFLKENAA KDGVKTTASG LQYKITKQGE GKQPTKDDIV TVEYEGRLID GTVFDSSKAN GGPVTFPLSQ VIPGWTEGVQ LLKEGGEATF YIPSNLAYRE QGAGDKIGPN ATLVFDVKLV KIGAPENAPA KQPAQVDIKK VN // ID FISL_NEIMB Reviewed; 79 AA. AC P64131; Q9JR42; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Putative Fis-like DNA-binding protein; GN OrderedLocusNames=NMB1420; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the transcriptional regulatory Fis family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41781.1; -; Genomic_DNA. DR PIR; F81085; F81085. DR RefSeq; NP_274432.1; NC_003112.2. DR RefSeq; WP_002213092.1; NC_003112.2. DR ProteinModelPortal; P64131; -. DR STRING; 122586.NMB1420; -. DR PaxDb; P64131; -. DR EnsemblBacteria; AAF41781; AAF41781; NMB1420. DR GeneID; 903842; -. DR KEGG; nme:NMB1420; -. DR PATRIC; 20358527; VBINeiMen85645_1775. DR eggNOG; ENOG4105VY0; Bacteria. DR eggNOG; COG2901; LUCA. DR HOGENOM; HOG000256331; -. DR KO; K03557; -. DR OMA; TECIETQ; -. DR OrthoDB; EOG67HJXZ; -. DR BioCyc; NMEN122586:GHGG-1458-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR005412; Fis_DNA-bd. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR Pfam; PF02954; HTH_8; 1. DR PIRSF; PIRSF002097; DNA-binding_Fis; 1. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; SSF46689; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 79 Putative Fis-like DNA-binding protein. FT /FTId=PRO_0000203906. FT DNA_BIND 55 74 H-T-H motif. {ECO:0000250}. SQ SEQUENCE 79 AA; 8937 MW; 6A21EBC40B2B8E95 CRC64; MPHTLPDISQ CIRQNLEQYF KDLNGTEPCG VYDMVLHQVE KPLLVCVMEQ CGGNQSKASV MLGLNRNTLR KKLIQHGLL // ID FMM1_NEIMB Reviewed; 170 AA. AC P05431; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-MAY-2016, entry version 125. DE RecName: Full=Fimbrial protein; DE AltName: Full=Pilin; DE Flags: Precursor; GN Name=pilE; OrderedLocusNames=NMB0018; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C311 / Serogroup B; RX PubMed=3141743; DOI=10.1111/j.1365-2958.1988.tb00073.x; RA Potts W.J., Saunders J.R.; RT "Nucleotide sequence of the structural gene for class I pilin from RT Neisseria meningitidis: homologies with the pilE locus of Neisseria RT gonorrhoeae."; RL Mol. Microbiol. 2:647-653(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP PROTEIN SEQUENCE OF 8-36, AND METHYLATION AT PHE-8. RC STRAIN=ATCC 13090; RX PubMed=413571; DOI=10.1021/bi00596a010; RA Hermodson M.A., Chen K.C., Buchanan T.M.; RT "Neisseria pili proteins: amino-terminal amino acid sequences and RT identification of an unusual amino acid."; RL Biochemistry 17:442-445(1978). RN [4] RP PROTEIN SEQUENCE OF 98-103, PHOSPHORYLATION AT SER-100, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=8645220; RA Stimson E., Virji M., Barker S., Panico M., Blench I., Saunders J., RA Payne G., Moxon E.R., Dell A., Morris H.R.; RT "Discovery of a novel protein modification: alpha-glycerophosphate is RT a substituent of meningococcal pilin."; RL Biochem. J. 316:29-33(1996). RN [5] RP STRUCTURE OF CARBOHYDRATE ON SER-70. RX PubMed=8993351; DOI=10.1111/j.1749-6632.1996.tb52949.x; RA Virji M., Stimson E., Makepeace K., Dell A., Morris H.R., Payne G., RA Saunders J.R., Moxon E.R.; RT "Posttranslational modifications of meningococcal pili. Identification RT of a common trisaccharide substitution on variant pilins of strain RT C311."; RL Ann. N. Y. Acad. Sci. 797:53-64(1996). RN [6] RP GLYCOSYLATION AT SER-70. RX PubMed=9515697; DOI=10.1046/j.1365-2958.1998.00706.x; RA Marceau M., Forest K., Beretti J.-L., Tainer J., Nassif X.; RT "Consequences of the loss of O-linked glycosylation of meningococcal RT type IV pilin on piliation and pilus-mediated adhesion."; RL Mol. Microbiol. 27:705-715(1998). CC -!- FUNCTION: This protein is the predominant Neisseria surface CC antigen, which allows adhesion of the bacterium to various host CC cells. CC -!- SUBUNIT: The pili are polar flexible filaments of about 5.4 CC nanometers diameter and 2.5 micrometers average length; they CC consist of only a single polypeptide chain arranged in a helical CC configuration of five subunits per turn in the assembled pilus. CC -!- SUBCELLULAR LOCATION: Fimbrium. CC -!- PTM: O-linked glycan has been reported to consist either of the CC Gal(alpha1-3) GlcNAc disaccharide, or the Gal(beta 1-4) Gal(alpha CC 1-3) 2,4-diacetamido-2,4,6-trideoxyhexose trisaccharide. CC {ECO:0000269|PubMed:9515697}. CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}. CC -!- CAUTION: In PubMed:413571 it is said that 50% of the peptides have CC N-methyl-Phe and 50% begin with Thr-9. N-terminal methylation CC produces preview during Edman degradation, which makes this appear CC to happen when the peptide is completely N-terminal methylated. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X07731; CAA30557.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40497.1; -; Genomic_DNA. DR PIR; F81246; F81246. DR PIR; S03091; S03091. DR RefSeq; NP_273084.1; NC_003112.2. DR RefSeq; WP_010980743.1; NC_003112.2. DR PDB; 4V1J; X-ray; 1.43 A; A=32-170. DR PDBsum; 4V1J; -. DR ProteinModelPortal; P05431; -. DR SMR; P05431; 8-169. DR STRING; 122586.NMB0018; -. DR UniCarbKB; P05431; -. DR PaxDb; P05431; -. DR EnsemblBacteria; AAF40497; AAF40497; NMB0018. DR GeneID; 902121; -. DR KEGG; nme:NMB0018; -. DR PATRIC; 20354975; VBINeiMen85645_0024. DR eggNOG; ENOG4108ZUW; Bacteria. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR KO; K02650; -. DR OMA; KSAVVEY; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-19-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR InterPro; IPR012902; N_methyl_site. DR InterPro; IPR001082; Pilin. DR Pfam; PF13633; N_methyl_3; 1. DR Pfam; PF00114; Pilin; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Complete proteome; KW Direct protein sequencing; Disulfide bond; Fimbrium; Glycoprotein; KW Methylation; Phosphoprotein; Reference proteome. FT PROPEP 1 7 {ECO:0000250}. FT /FTId=PRO_0000024164. FT CHAIN 8 170 Fimbrial protein. FT /FTId=PRO_0000024165. FT MOD_RES 8 8 N-methylphenylalanine. FT {ECO:0000269|PubMed:413571}. FT MOD_RES 100 100 O-(sn-1-glycerophosphoryl)serine. FT {ECO:0000269|PubMed:8645220}. FT CARBOHYD 70 70 O-linked (Gal...). FT {ECO:0000269|PubMed:9515697}. FT /FTId=CAR_000204. FT DISULFID 127 163 {ECO:0000250}. FT CONFLICT 97 105 QMASSNVNN -> TMLSSGVNK (in Ref. 1; FT CAA30557). {ECO:0000305}. FT CONFLICT 134 155 DKAKAANDDVTAAAAANGKKID -> NDTDDTVAAVAADNT FT GNIN (in Ref. 1; CAA30557). FT {ECO:0000305}. FT HELIX 32 48 {ECO:0000244|PDB:4V1J}. FT HELIX 51 61 {ECO:0000244|PDB:4V1J}. FT HELIX 68 71 {ECO:0000244|PDB:4V1J}. FT HELIX 76 78 {ECO:0000244|PDB:4V1J}. FT STRAND 82 90 {ECO:0000244|PDB:4V1J}. FT STRAND 93 98 {ECO:0000244|PDB:4V1J}. FT TURN 105 109 {ECO:0000244|PDB:4V1J}. FT STRAND 111 118 {ECO:0000244|PDB:4V1J}. FT STRAND 120 129 {ECO:0000244|PDB:4V1J}. FT HELIX 156 158 {ECO:0000244|PDB:4V1J}. SQ SEQUENCE 170 AA; 18072 MW; 037368DD1B26FA6F CRC64; MNTLQKGFTL IELMIVIAIV GILAAVALPA YQDYTARAQV SEAILLAEGQ KSAVTEYYLN HGEWPGNNTS AGVATSSEIK GKYVKSVEVK NGVVTAQMAS SNVNNEIKGK KLSLWAKRQN GSVKWFCGQP VTRDKAKAAN DDVTAAAAAN GKKIDTKHLP STCRDASDAS // ID FETP_NEIMB Reviewed; 88 AA. AC P67616; Q9JQP5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=Probable Fe(2+)-trafficking protein {ECO:0000255|HAMAP-Rule:MF_00686}; GN OrderedLocusNames=NMB2021; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Could be a mediator in iron transactions between iron CC acquisition and iron-requiring processes, such as synthesis and/or CC repair of Fe-S clusters in biosynthetic enzymes. CC {ECO:0000255|HAMAP-Rule:MF_00686}. CC -!- SIMILARITY: Belongs to the Fe(2+)-trafficking protein family. CC {ECO:0000255|HAMAP-Rule:MF_00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42344.1; -; Genomic_DNA. DR PIR; H81014; H81014. DR RefSeq; NP_275013.1; NC_003112.2. DR RefSeq; WP_002214948.1; NC_003112.2. DR ProteinModelPortal; P67616; -. DR STRING; 122586.NMB2021; -. DR PaxDb; P67616; -. DR EnsemblBacteria; AAF42344; AAF42344; NMB2021. DR GeneID; 904089; -. DR KEGG; nme:NMB2021; -. DR PATRIC; 20360157; VBINeiMen85645_2578. DR eggNOG; ENOG4105KMG; Bacteria. DR eggNOG; COG2924; LUCA. DR HOGENOM; HOG000137239; -. DR OMA; SKQTMLI; -. DR OrthoDB; EOG654P6H; -. DR BioCyc; NMEN122586:GHGG-2083-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00686; Fe_traffic_YggX; 1. DR InterPro; IPR007457; Fe_traffick_prot_YggX. DR Pfam; PF04362; Iron_traffic; 1. DR PIRSF; PIRSF029827; Fe_traffic_YggX; 1. DR ProDom; PD029191; Fe_traffick_prot_YggX; 1. DR SUPFAM; SSF111148; SSF111148; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Reference proteome. FT CHAIN 1 88 Probable Fe(2+)-trafficking protein. FT /FTId=PRO_0000214493. SQ SEQUENCE 88 AA; 10180 MW; EBC6F2FBF097F2F1 CRC64; MARMVFCVKL NKEAEGMKFP PLPNELGKRI FENVSQEAWA AWTRHQTMLI NENRLSLADP RAREYLAQQM EQYFFGDGAD AVQGYVPQ // ID FMT_NEIMB Reviewed; 308 AA. AC Q9K1K6; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182}; DE EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182}; GN Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182}; OrderedLocusNames=NMB0111; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Modifies the free amino group of the aminoacyl moiety of CC methionyl-tRNA(fMet). The formyl group appears to play a dual role CC in the initiator identity of N-formylmethionyl-tRNA by: (I) CC promoting its recognition by IF2 and (II) impairing its binding to CC EFTu-GTP. {ECO:0000255|HAMAP-Rule:MF_00182}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl- CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). CC {ECO:0000255|HAMAP-Rule:MF_00182}. CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP- CC Rule:MF_00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40570.1; -; Genomic_DNA. DR PIR; F81238; F81238. DR RefSeq; NP_273169.1; NC_003112.2. DR RefSeq; WP_002224762.1; NC_003112.2. DR ProteinModelPortal; Q9K1K6; -. DR STRING; 122586.NMB0111; -. DR PaxDb; Q9K1K6; -. DR EnsemblBacteria; AAF40570; AAF40570; NMB0111. DR GeneID; 902215; -. DR KEGG; nme:NMB0111; -. DR PATRIC; 20355235; VBINeiMen85645_0151. DR eggNOG; ENOG4105CAE; Bacteria. DR eggNOG; COG0223; LUCA. DR HOGENOM; HOG000261177; -. DR KO; K00604; -. DR OMA; GCINSHA; -. DR OrthoDB; EOG6B09WV; -. DR BioCyc; NMEN122586:GHGG-117-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_00182; Formyl_trans; 1. DR InterPro; IPR005794; Fmt. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR001555; GART_AS. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00460; fmt; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 308 Methionyl-tRNA formyltransferase. FT /FTId=PRO_0000083004. FT REGION 110 113 Tetrahydrofolate (THF) binding. FT {ECO:0000255|HAMAP-Rule:MF_00182}. SQ SEQUENCE 308 AA; 32901 MW; FB4E816824BE0511 CRC64; MKVIFAGTPD FAAAALRAVA AAGFEIPLVL TQPDRPKGRG MQLTAPPVKQ AALELGLRVE QPEKLRNNAE ALQMLKEVEA DVMVVAAYGL ILPQEVLDTP KHGCLNIHAS LLPRWRGAAP IQRAIEAGDA ETGVCIMQMD IGLDTGDVVS EHRYAIQPTD TANEVHDALM EIGAAAVVAD LQQLQSKGRL NAVKQPEEGV TYAQKLSKEE ARIDWSKSAA VIERKIRAFN PVPAAWVEYQ GKPMKIRRAE VVAQQGAAGE VLSCSADGLV VACGENALKI TELQPAGGRR MNIAAFAAGR HIEAGAKL // ID FTSK1_NEIMB Reviewed; 812 AA. AC Q9JZ36; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=DNA translocase FtsK 1; GN Name=ftsK1; OrderedLocusNames=NMB1314; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein that coordinates cell CC division and chromosome segregation. The N-terminus is involved in CC assembly of the cell-division machinery. The C-terminus functions CC as a DNA motor that moves dsDNA in an ATP-dependent manner towards CC the dif recombination site, which is located within the CC replication terminus region. Translocation stops specifically at CC Xer-dif sites, where FtsK interacts with the Xer recombinase, CC allowing activation of chromosome unlinking by recombination. FtsK CC orienting polar sequences (KOPS) guide the direction of DNA CC translocation. FtsK can remove proteins from DNA as it CC translocates, but translocation stops specifically at XerCD-dif CC site, thereby preventing removal of XerC and XerD from dif (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. Note=Located at the septum. CC {ECO:0000250}. CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for CC the localization to the septal ring and is required for cell CC division, followed by a linker domain, and a C-terminal domain, CC which forms the translocation motor involved in chromosome CC segregation. The C-terminal domain can be further subdivided into CC alpha, beta and gamma subdomains. The alpha and beta subdomains CC multimerise to produce a hexameric ring, contain the nucleotide CC binding motif and form the DNA pump. The gamma subdomain is a CC regulatory subdomain that controls translocation of DNA by CC recognition of KOPS motifs and interacts with XerD recombinase (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FtsK domain. {ECO:0000255|PROSITE- CC ProRule:PRU00289}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41689.1; -; Genomic_DNA. DR PIR; A81096; A81096. DR RefSeq; NP_274333.1; NC_003112.2. DR RefSeq; WP_002225165.1; NC_003112.2. DR ProteinModelPortal; Q9JZ36; -. DR SMR; Q9JZ36; 328-731. DR STRING; 122586.NMB1314; -. DR PaxDb; Q9JZ36; -. DR EnsemblBacteria; AAF41689; AAF41689; NMB1314. DR GeneID; 903736; -. DR KEGG; nme:NMB1314; -. DR PATRIC; 20358273; VBINeiMen85645_1648. DR eggNOG; ENOG4105CNU; Bacteria. DR eggNOG; COG1674; LUCA. DR HOGENOM; HOG000010003; -. DR KO; K03466; -. DR OMA; ESSTEMP; -. DR OrthoDB; EOG6S52GD; -. DR BioCyc; NMEN122586:GHGG-1352-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025199; FtsK_4TM. DR InterPro; IPR002543; FtsK_dom. DR InterPro; IPR018541; Ftsk_gamma. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF13491; FtsK_4TM; 1. DR Pfam; PF09397; Ftsk_gamma; 1. DR Pfam; PF01580; FtsK_SpoIIIE; 1. DR SMART; SM00843; Ftsk_gamma; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50901; FTSK; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; KW Cell membrane; Chromosome partition; Complete proteome; DNA-binding; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 812 DNA translocase FtsK 1. FT /FTId=PRO_0000098274. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 184 204 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TOPO_DOM 231 812 Cytoplasmic. {ECO:0000255}. FT DOMAIN 461 670 FtsK. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. FT NP_BIND 481 486 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. SQ SEQUENCE 812 AA; 87958 MW; 0F5894CAD3704BB6 CRC64; MTEKSHKKTA KGRAGSPSPT SARNKKADNG ARGNKVSERL KAVKELQKTE TKKARPEHVV NLIGDALWLM GLAATLYLAI SLISFDMGDP SWSHSSPVVE DVANWGGLFG AYVADVGYYL FGWSFWWWIA AACVVLYKNF RLHAKQTENE AYNHKIAAAA LFVLTVFSPV LEYFVLGGKY ADSLPVGAGG MVGIRVGAVF AWLLGKSGSL LIILVVLLLS LSLLVQISWL EFLNGAGRAV QNRLSALSGK VMALGKRRPN TKTDGVDTQN TRRMVKEAKN ITAKPVALPE GSSSNRKSVA VSVAPPPKIQ VSLFEDDEPR QAGEYHKPTL NLLRIPDSEP VSINPAELER TAELIESKLA EFGIGVQVVS ATSGPVITRY EIEPAQGVKG SQIVALSKDL ARSMSLQSVR IVETIAGKNT MGIELPNDKR QDVMLSEILS SPVFAEAKSK LTVALGKDIA GTPVVGDLAK MPHLLVAGMT GSGKSVGVNG MIMSMLFKAT PDEVRFIMID PKMLELSIYD GIPHLLCPVV TDMREAGQAL NWCVAEMEKR YRLLSHAGVR NLEGFNQKVE AAKAAGKPLL NPFSLNPDEP EPLEKLPLIV VVIDELADLM MTERKAVEQQ IARLAQKARA AGIHMIVATQ RPSVDVVTGL IKANIPTRMA FTVQSKIDSR TILDQMGADE LLKYGDSLFL QPGSAEPTRL QGAFVSDDEV HQVVNYVKSQ APADYIEGLL SGEAALETAN IVNPNADSDE LFDQAVAYVL ESKKTSISSL QRQLRIGYNR AANLMEALEN AGVVSSTDLN GSRKILAHKD HL // ID FTSK2_NEIMB Reviewed; 1014 AA. AC Q9JZG4; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=DNA translocase FtsK 2; GN Name=ftsK2; OrderedLocusNames=NMB1067; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein that coordinates cell CC division and chromosome segregation. The N-terminus is involved in CC assembly of the cell-division machinery. The C-terminus functions CC as a DNA motor that moves dsDNA in an ATP-dependent manner towards CC the dif recombination site, which is located within the CC replication terminus region. Translocation stops specifically at CC Xer-dif sites, where FtsK interacts with the Xer recombinase, CC allowing activation of chromosome unlinking by recombination. FtsK CC orienting polar sequences (KOPS) guide the direction of DNA CC translocation. FtsK can remove proteins from DNA as it CC translocates, but translocation stops specifically at XerCD-dif CC site, thereby preventing removal of XerC and XerD from dif (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. Note=Located at the septum. CC {ECO:0000250}. CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for CC the localization to the septal ring and is required for cell CC division, followed by a linker domain, and a C-terminal domain, CC which forms the translocation motor involved in chromosome CC segregation. The C-terminal domain can be further subdivided into CC alpha, beta and gamma subdomains. The alpha and beta subdomains CC multimerise to produce a hexameric ring, contain the nucleotide CC binding motif and form the DNA pump. The gamma subdomain is a CC regulatory subdomain that controls translocation of DNA by CC recognition of KOPS motifs and interacts with XerD recombinase (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FtsK domain. {ECO:0000255|PROSITE- CC ProRule:PRU00289}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41463.1; -; Genomic_DNA. DR PIR; E81125; E81125. DR RefSeq; NP_274100.1; NC_003112.2. DR RefSeq; WP_002225260.1; NC_003112.2. DR ProteinModelPortal; Q9JZG4; -. DR SMR; Q9JZG4; 533-932, 946-1010. DR STRING; 122586.NMB1067; -. DR PaxDb; Q9JZG4; -. DR EnsemblBacteria; AAF41463; AAF41463; NMB1067. DR GeneID; 903485; -. DR KEGG; nme:NMB1067; -. DR PATRIC; 20357681; VBINeiMen85645_1357. DR eggNOG; ENOG4105CNU; Bacteria. DR eggNOG; COG1674; LUCA. DR HOGENOM; HOG000220743; -. DR KO; K03466; -. DR OMA; WIVMIVI; -. DR OrthoDB; EOG6S52GD; -. DR BioCyc; NMEN122586:GHGG-1104-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002543; FtsK_dom. DR InterPro; IPR018541; Ftsk_gamma. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF09397; Ftsk_gamma; 1. DR Pfam; PF01580; FtsK_SpoIIIE; 1. DR SMART; SM00843; Ftsk_gamma; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50901; FTSK; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; KW Cell membrane; Chromosome partition; Complete proteome; DNA-binding; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 1014 DNA translocase FtsK 2. FT /FTId=PRO_0000098275. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT DOMAIN 662 871 FtsK. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. FT NP_BIND 682 687 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. SQ SEQUENCE 1014 AA; 110965 MW; BFC7D6B7CE37DA86 CRC64; MFWIVLIVIL LLALAGLFFV RAQSEREWMR EVSAWQEKKG EKQAELPEIK DGMPDFPELA LMLFHAVKTA VYWLFVGVVR FCRNYLAHES EPDRPVPPAS ANRADVPTAS DGYSDSGNGT EEAETEEAEA AEEEAADTED IATAVIDNRR IPFDRSIAEG LMPSESEISP VRPVFKEITL EEATRALNSA ALRETKKRYI DAFEKNETAV PKVRVSDTPM EGLQIIGLDD PVLQRTYSHM FDADKEAFSE SADYGFEPYF EKQHPSAFSA VKAENARNAP FHRHAGQGKG QAEAKSPDVS QGQSVSDGTA VRDARRRVSV NLKEPNKATV SAEARISRLI PESQTVVGKR DVEMPSETEN VFTETVSSVG YGGPVYDETA DIHIEEPAAP DAWVVEPPEV PKVPMTAIDI QPPPPVSEIY NRTYEPPSGF EQVQRSRIAE TDHLADDVLN GGWQEETAAI ADDGSEGAAE RSSGQYLSET EAFGHDSQAV CPFENVPSER PSCRVSDTEA DEGAFPSEET GAVSEHLPTT DLLLPPLFNP EATQTEEELL ENSITIEEKL AEFKVKVKVV DSYSGPVITR YEIEPDVGVR GNSVLNLEKD LARSLGVASI RVVETIPGKT CMGLELPNPK RQMIRLSEIF NSPEFAESKS KLTLALGQDI TGQPVVTDLG KAPHLLVAGT TGSGKSVGVN AMILSMLFKA APEDVRMIMI DPKMLELSIY EGIPHLLAPV VTDMKLAANA LNWCVNEMEK RYRLMSFMGV RNLAGFNQKI AEAAARGEKI GNPFSLTPDD PEPLEKLPFI VVVVDEFADL MMTAGKKIEE LIARLAQKAR AAGIHLILAT QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE NLLGQGDMLF LLPGTAYPQR VHGAFASDEE VHRVVEYLKQ FGEPDYVDDI LSGGGSEELP GIGRSGDDET DPMYDEAVSV VLKTRKASIS GVQRALRIGY NRAARLIDQM EAEGIVSAPE HNGNRTILVP LDNA // ID FKBP_NEIMB Reviewed; 109 AA. AC P0A0W2; P25138; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=FK506-binding protein; DE EC=5.2.1.8; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE AltName: Full=Rotamase; GN Name=fbp; OrderedLocusNames=NMB0027; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=BNCV / Serogroup B; RX PubMed=1371354; DOI=10.1073/pnas.89.4.1164; RA Sampson B.A., Gotschlich E.C.; RT "Neisseria meningitidis encodes an FK506-inhibitable rotamase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1164-1168(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: PPIases accelerate the folding of proteins. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by FK506. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M97859; AAA25455.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40498.1; -; Genomic_DNA. DR PIR; F81245; F81245. DR RefSeq; NP_273093.1; NC_003112.2. DR RefSeq; WP_002216146.1; NC_003112.2. DR ProteinModelPortal; P0A0W2; -. DR SMR; P0A0W2; 19-107. DR STRING; 122586.NMB0027; -. DR PaxDb; P0A0W2; -. DR EnsemblBacteria; AAF40498; AAF40498; NMB0027. DR GeneID; 902130; -. DR KEGG; nme:NMB0027; -. DR PATRIC; 20355003; VBINeiMen85645_0038. DR eggNOG; ENOG4108V1T; Bacteria. DR eggNOG; COG0545; LUCA. DR HOGENOM; HOG000154887; -. DR KO; K01802; -. DR OMA; ERARLTC; -. DR OrthoDB; EOG6DRPKW; -. DR BioCyc; NMEN122586:GHGG-28-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PTHR10516; 1. DR Pfam; PF00254; FKBP_C; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Reference proteome; Rotamase. FT CHAIN 1 109 FK506-binding protein. FT /FTId=PRO_0000075351. FT DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. FT VARIANT 3 3 G -> S (in strain: BNCV / Serogroup B). FT VARIANT 12 12 G -> S (in strain: BNCV / Serogroup B). FT VARIANT 33 33 N -> D (in strain: BNCV / Serogroup B). SQ SEQUENCE 109 AA; 11789 MW; F90A625F4899AE4B CRC64; MGGLIIEDLQ EGFGKEAVKG KEITVHYTGW LENGTKFDSS LDRRQPLTIT LGVGQVIKGW DEGFGGMKEG GKRKLTIPSE MGYGAHGAGG VIPPHATLIF EVELLKVYE // ID FTHS_NEIMB Reviewed; 558 AA. AC Q9JXY2; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543}; DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543}; DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543}; GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=NMB1839; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP + CC phosphate + 10-formyltetrahydrofolate. {ECO:0000255|HAMAP- CC Rule:MF_01543}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01543}. CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase CC family. {ECO:0000255|HAMAP-Rule:MF_01543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42174.1; -; Genomic_DNA. DR PIR; E81037; E81037. DR RefSeq; NP_274836.1; NC_003112.2. DR RefSeq; WP_002225668.1; NC_003112.2. DR ProteinModelPortal; Q9JXY2; -. DR SMR; Q9JXY2; 8-556. DR STRING; 122586.NMB1839; -. DR PaxDb; Q9JXY2; -. DR EnsemblBacteria; AAF42174; AAF42174; NMB1839. DR GeneID; 903260; -. DR KEGG; nme:NMB1839; -. DR PATRIC; 20359685; VBINeiMen85645_2348. DR eggNOG; ENOG4105CKU; Bacteria. DR eggNOG; COG2759; LUCA. DR HOGENOM; HOG000040280; -. DR KO; K01938; -. DR OMA; CGEIMTM; -. DR OrthoDB; EOG6PCPSP; -. DR BioCyc; NMEN122586:GHGG-1894-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01543; FTHFS; 1. DR InterPro; IPR000559; Formate_THF_ligase. DR InterPro; IPR020628; Formate_THF_ligase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01268; FTHFS; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW One-carbon metabolism; Reference proteome. FT CHAIN 1 558 Formate--tetrahydrofolate ligase. FT /FTId=PRO_0000199365. FT NP_BIND 66 73 ATP. {ECO:0000255|HAMAP-Rule:MF_01543}. SQ SEQUENCE 558 AA; 59062 MW; 93F4C203B39C7CDC CRC64; MSFKTDAEIA QSSTMRPIGE IAAKLGLNAD NIEPYGHYKA KINPAEAFKL PQKQGRLILV TAINPTPAGE GKTTVTIGLA DALRHIGKDA VIALREPSLG PVFGVKGGAA GGGYAQVLPM EDINLHFTGD FHAIGAANNL LAAMLDNHIY QGNELNIDPK RVLWRRVVDM NDRQLRNIID GMGKPVDGVM RPDGFDITVA SEVMAVFCLA KDISDLKERL GNILVAYAKD GSPVYAKDLK ANGAMAALLK DAIKPNLVQT IEGTPAFVHG GPFANIAHGC NSVTATRLAK HLADYAVTEA GFGADLGAEK FCDIKCRLAG LKPDAAVVVA TVRALKYNGG VERANLGEEN LDALEKGLPN LLKHISNLKN VFGLPVVVAL NRFVSDADAE LAMIEKACAE HGVEVSLTEV WGKGGAGGAD LARKVVNAIE SQTNNFGFAY DVELGIKDKI RAIAQKVYGA EDVDFSAEAS AEIASLEKLG LDKMPICMAK TQYSLSDNAK LLGCPEDFRI AVRGITVSAG AGFIVALCGN MMKMPGLPKV PAAEKIDVDA EGVIHGLF // ID FTSA_NEIMB Reviewed; 414 AA. AC Q9K0X8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033}; GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; GN OrderedLocusNames=NMB0426; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Cell division protein that is involved in the assembly CC of the Z ring. May serve as a membrane anchor for the Z ring. CC {ECO:0000255|HAMAP-Rule:MF_02033}. CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000255|HAMAP- CC Rule:MF_02033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_02033}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent CC manner. Targeted to the membrane through a conserved C-terminal CC amphiphatic helix. {ECO:0000255|HAMAP-Rule:MF_02033}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP- CC Rule:MF_02033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40864.1; -; Genomic_DNA. DR PIR; E81201; E81201. DR RefSeq; NP_273474.1; NC_003112.2. DR RefSeq; WP_002216537.1; NC_003112.2. DR ProteinModelPortal; Q9K0X8; -. DR STRING; 122586.NMB0426; -. DR PaxDb; Q9K0X8; -. DR EnsemblBacteria; AAF40864; AAF40864; NMB0426. DR GeneID; 902542; -. DR KEGG; nme:NMB0426; -. DR PATRIC; 20356050; VBINeiMen85645_0540. DR eggNOG; ENOG4105CIT; Bacteria. DR eggNOG; COG0849; LUCA. DR HOGENOM; HOG000049205; -. DR KO; K03590; -. DR OMA; HTAVIPF; -. DR OrthoDB; EOG6TR0B6; -. DR BioCyc; NMEN122586:GHGG-450-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_02033; FtsA; 1. DR InterPro; IPR020823; Cell_div_FtsA. DR InterPro; IPR003494; SHS2_FtsA. DR Pfam; PF02491; SHS2_FTSA; 1. DR PIRSF; PIRSF003101; FtsA; 1. DR SMART; SM00842; FtsA; 1. DR TIGRFAMs; TIGR01174; ftsA; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Complete proteome; Membrane; Reference proteome. FT CHAIN 1 414 Cell division protein FtsA. FT /FTId=PRO_0000320267. SQ SEQUENCE 414 AA; 44061 MW; 729655580466026F CRC64; MEQQQRYISV LDIGTSKVLA LIGEVQDDDK INIVGLGQAP SRGLRAGMVT NIDATVQAIR QAVNDAELMA DTKITHVTTG IAGNHIRSLN SQGVVKIKDG EVTQADIDRA IETAKAINIP PDQKILDAVV QDYIIDTQLG VREPIGMSGV RLDTRVHIIT GASTAVQNVQ KCIERCGLKS DQIMLQPLAS GQAVLTEDEK DLGVCVIDIG GGTTDIAVYM NGAIRHTSVI PAGGNLITKD LSKSLRTPLD AAEYIKIHYG VASCDTEGLG EMIEVPGVGD RTSRQVSSKV LAAIISARIQ EIFGVVLGEL QKSGFPKEVL NAGIVLTGGV SMMTGIVEFA EKIFDLPVRT GAPQEMGGLS DRVRTPRFST AIGLLHAACK LEGNLPQPEN GAVQEREGGG GLLARLKRWI ENSF // ID FPG_NEIMB Reviewed; 275 AA. AC P55044; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 11-MAY-2016, entry version 121. DE RecName: Full=Formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM; DE Short=AP lyase MutM; DE EC=4.2.99.18; GN Name=mutM; Synonyms=fpg; OrderedLocusNames=NMB1295; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8586265; DOI=10.1111/j.1574-6968.1995.tb07933.x; RA Swartley J.S., Stephens D.S.; RT "Co-transcription of a homologue of the formamidopyrimidine-DNA RT glycosylase (fpg) and lysophosphatidic acid acyltransferase (nlaA) in RT Neisseria meningitidis."; RL FEMS Microbiol. Lett. 134:171-176(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in base excision repair of DNA damaged by CC oxidation or by mutagenic agents. Acts as DNA glycosylase that CC recognizes and removes damaged bases. Has a preference for CC oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has CC AP (apurinic/apyrimidinic) lyase activity and introduces nicks in CC the DNA strand. Cleaves the DNA backbone by beta-delta elimination CC to generate a single-strand break at the site of the removed base CC with both 3'- and 5'-phosphates (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7- CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N- CC methyl)formamidopyrimidine. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U21808; AAB01505.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41671.1; -; Genomic_DNA. DR PIR; B81099; B81099. DR RefSeq; NP_274315.1; NC_003112.2. DR RefSeq; WP_002225172.1; NC_003112.2. DR ProteinModelPortal; P55044; -. DR SMR; P55044; 2-275. DR STRING; 122586.NMB1295; -. DR PaxDb; P55044; -. DR EnsemblBacteria; AAF41671; AAF41671; NMB1295. DR GeneID; 903717; -. DR KEGG; nme:NMB1295; -. DR PATRIC; 20358219; VBINeiMen85645_1621. DR eggNOG; ENOG4105ERD; Bacteria. DR eggNOG; COG0266; LUCA. DR HOGENOM; HOG000020881; -. DR KO; K10563; -. DR OMA; WHRRGKY; -. DR OrthoDB; EOG6QP131; -. DR BioCyc; NMEN122586:GHGG-1333-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR HAMAP; MF_00103; Fapy_DNA_glycosyl; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF01149; Fapy_DNA_glyco; 1. DR Pfam; PF06831; H2TH; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR SMART; SM00898; Fapy_DNA_glyco; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR SUPFAM; SSF81624; SSF81624; 1. DR TIGRFAMs; TIGR00577; fpg; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS01242; ZF_FPG_1; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase; KW Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; KW Reference proteome; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 275 Formamidopyrimidine-DNA glycosylase. FT /FTId=PRO_0000170843. FT ZN_FING 241 275 FPG-type. FT ACT_SITE 2 2 Schiff-base intermediate with DNA. FT {ECO:0000250}. FT ACT_SITE 3 3 Proton donor. {ECO:0000250}. FT ACT_SITE 58 58 Proton donor; for beta-elimination FT activity. {ECO:0000250}. FT ACT_SITE 265 265 Proton donor; for delta-elimination FT activity. {ECO:0000250}. FT BINDING 95 95 DNA. {ECO:0000250}. FT BINDING 114 114 DNA. {ECO:0000250}. FT CONFLICT 61 62 LI -> IV (in Ref. 1; AAB01505). FT {ECO:0000305}. FT CONFLICT 66 68 TGV -> KGI (in Ref. 1; AAB01505). FT {ECO:0000305}. FT CONFLICT 151 151 A -> V (in Ref. 1; AAB01505). FT {ECO:0000305}. FT CONFLICT 213 213 Q -> R (in Ref. 1; AAB01505). FT {ECO:0000305}. FT CONFLICT 252 252 R -> Q (in Ref. 1; AAB01505). FT {ECO:0000305}. SQ SEQUENCE 275 AA; 30856 MW; 29A38C945C5EC559 CRC64; MPELPEVETT LRGIAPHIEG KTVEAVVLRQ LKLRWQINPD LGEILSGRQV LSCGRRAKYL LIRFQTGVLL IHLGMSGSLR IFTPSDGRIG RPDRHDHVDI VFSDGTVMRY RDPRKFGAIL WYEGIEEHHP LLEKLGPEPL SEAFCADYLY ARLKAQKRAV KLALMDNAVV VGVGNIYANE SLFRAGISPH RPANRLKKKE CALLVETVKA VLQRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC PRCGGLVVKE TLGQRGTFYC PNCQK // ID FTSQ_NEIMB Reviewed; 235 AA. AC Q9K0X9; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Cell division protein FtsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN Name=ftsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN OrderedLocusNames=NMB0425; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. May control correct divisome assembly. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00911}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00911}. Note=Localizes to the division CC septum. {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SIMILARITY: Contains 1 POTRA domain. {ECO:0000255|PROSITE- CC ProRule:PRU01115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40863.1; -; Genomic_DNA. DR PIR; D81201; D81201. DR RefSeq; NP_273473.1; NC_003112.2. DR RefSeq; WP_010980792.1; NC_003112.2. DR ProteinModelPortal; Q9K0X9; -. DR STRING; 122586.NMB0425; -. DR PaxDb; Q9K0X9; -. DR EnsemblBacteria; AAF40863; AAF40863; NMB0425. DR GeneID; 902541; -. DR KEGG; nme:NMB0425; -. DR PATRIC; 20356048; VBINeiMen85645_0539. DR eggNOG; ENOG4105K7E; Bacteria. DR eggNOG; COG1589; LUCA. DR HOGENOM; HOG000255873; -. DR KO; K03589; -. DR OMA; WHATLGN; -. DR OrthoDB; EOG6XM7B0; -. DR BioCyc; NMEN122586:GHGG-449-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:InterPro. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00911; FtsQ_subfam; 1. DR InterPro; IPR005548; Cell_div_FtsQ/DivIB. DR InterPro; IPR026579; FtsQ. DR InterPro; IPR013685; POTRA_FtsQ_type. DR Pfam; PF03799; FtsQ; 1. DR Pfam; PF08478; POTRA_1; 1. DR PROSITE; PS51779; POTRA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 235 Cell division protein FtsQ. FT /FTId=PRO_0000414682. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TRANSMEM 7 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TOPO_DOM 26 235 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT DOMAIN 30 99 POTRA. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 235 AA; 27135 MW; B7E605926BD5E9FF CRC64; MERLTRWLLV MMAMLLAASG LVWFYNSNHL PVKQVSLKGN LVYSDKKTLG SLAKEYIHGN ILRTDINGAQ EAYRRYPWIA SVMVRRRFPD TVEVVLTERK PVARWGDHAL VDGEGNVFEA RLDRPGMPVF RGAEGTSAEM LRRYDEFSTV LAKQGLGIKE MTYTARSAWI VVLDNGITVR LGRENEMKRL RLFTEAWQHL LRKNKNRLSY VDMRYKDGFS VRYASDGLPE KESEE // ID FTSZ_NEIMB Reviewed; 392 AA. AC P0A0S6; Q51130; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 71. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=NMB0427; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NMB / Serogroup B; RA Ribot E.M., Quinn F.D., Stephens D.S., Raymond N.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U43329; AAB18147.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40865.1; -; Genomic_DNA. DR PIR; E81199; E81199. DR RefSeq; NP_273475.1; NC_003112.2. DR RefSeq; WP_002212501.1; NC_003112.2. DR ProteinModelPortal; P0A0S6; -. DR SMR; P0A0S6; 14-321. DR STRING; 122586.NMB0427; -. DR PaxDb; P0A0S6; -. DR EnsemblBacteria; AAF40865; AAF40865; NMB0427. DR GeneID; 902543; -. DR KEGG; nme:NMB0427; -. DR PATRIC; 20356052; VBINeiMen85645_0541. DR eggNOG; ENOG4105CDK; Bacteria. DR eggNOG; COG0206; LUCA. DR HOGENOM; HOG000049094; -. DR KO; K03531; -. DR OMA; AQVIWGI; -. DR OrthoDB; EOG6S7XZG; -. DR BioCyc; NMEN122586:GHGG-451-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 392 Cell division protein FtsZ. FT /FTId=PRO_0000114369. FT NP_BIND 24 28 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 111 113 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 142 142 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 145 145 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 189 189 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT CONFLICT 30 30 I -> S (in Ref. 1; AAB18147). FT {ECO:0000305}. FT CONFLICT 352 392 MIRTNRGIRTMNLTAADFDNQSVLDDFEIPAILRRQHNSDK FT -> RSAPIAVSAR (in Ref. 1; AAB18147). FT {ECO:0000305}. SQ SEQUENCE 392 AA; 41487 MW; 4900B04AF6138221 CRC64; MEFVYDVAES AVSPAVIKVI GLGGGGCNAI NNMVANNVRG VEFISANTDA QSLAKNHAAK RIQLGTNLTR GLGAGANPDI GRAAAQEDRE AIEEAIRGAN MLFITTGMGG GTGTGSAPVV AEIAKSLGIL TVAVVTRPFA YEGKRVHVAQ AGLEQLKEHV DSLIIIPNDK LMTALGEDVT MREAFRAADN VLRDAVAGIS EVVTCPSEII NLDFADVKTV MSNRGIAMMG SGYAQGIDRA RMATDQAISS PLLDDVTLDG ARGVLVNITT APGCLKMSEL SEVMKIVNQS AHPDLECKFG AAEDETMSED AIRITIIATG LKEKGAVDFV PAREVEAVAP SKQEQSHNVE GMIRTNRGIR TMNLTAADFD NQSVLDDFEI PAILRRQHNS DK // ID FTSB_NEIMB Reviewed; 92 AA. AC P64161; Q9JR95; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Cell division protein FtsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN Name=ftsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN OrderedLocusNames=NMB1286; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00599}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00599}. Note=Localizes to the division CC septum. {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000255|HAMAP- CC Rule:MF_00599}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41662.1; -; Genomic_DNA. DR PIR; E81100; E81100. DR RefSeq; NP_274306.1; NC_003112.2. DR RefSeq; WP_002213385.1; NC_003112.2. DR STRING; 122586.NMB1286; -. DR PaxDb; P64161; -. DR EnsemblBacteria; AAF41662; AAF41662; NMB1286. DR GeneID; 903708; -. DR KEGG; nme:NMB1286; -. DR PATRIC; 20358199; VBINeiMen85645_1611. DR eggNOG; ENOG4105XX3; Bacteria. DR eggNOG; COG2919; LUCA. DR HOGENOM; HOG000262021; -. DR KO; K05589; -. DR OMA; DYVRVKD; -. DR OrthoDB; EOG6P5ZC4; -. DR BioCyc; NMEN122586:GHGG-1324-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00599; FtsB; 1. DR InterPro; IPR023081; Cell_div_FtsB. DR InterPro; IPR007060; FtsL/DivIC. DR Pfam; PF04977; DivIC; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Coiled coil; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 92 Cell division protein FtsB. FT /FTId=PRO_0000214450. FT TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT TRANSMEM 4 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT TOPO_DOM 22 92 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT COILED 28 50 {ECO:0000255|HAMAP-Rule:MF_00599}. SQ SEQUENCE 92 AA; 10563 MW; 48F5E3DE7AFE02B6 CRC64; MKWVTVVLSF ALVCCQYSLW FGKGSIGRNS SLREQIAVQE EKNQTLALRN HSLAAEVYDL ENGQEAISEI ARVELGYIQD GETFYRLIRH NR // ID FUR_NEIMB Reviewed; 144 AA. AC P0A0S8; Q57298; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 69. DE RecName: Full=Ferric uptake regulation protein; DE Short=Ferric uptake regulator; GN Name=fur; OrderedLocusNames=NMB0205; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a; RX PubMed=8163167; DOI=10.1016/0378-1119(94)90143-0; RA Karkhoff-Schweizer R.R., Schryvers A.B., Schweizer H.P.; RT "Cloning and sequence analysis of the fur gene encoding an iron- RT regulatory protein of Neisseria meningitidis."; RL Gene 141:139-140(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Acts as a global negative controlling element, employing CC Fe(2+) as a cofactor to bind the operator of the repressed genes. CC Regulates the expression of the fbp protein. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U01151; AAC13744.1; -; Unassigned_DNA. DR EMBL; AE002098; AAF40662.1; -; Genomic_DNA. DR PIR; G81226; G81226. DR RefSeq; NP_273263.1; NC_003112.2. DR RefSeq; WP_002218609.1; NC_003112.2. DR ProteinModelPortal; P0A0S8; -. DR STRING; 122586.NMB0205; -. DR PaxDb; P0A0S8; -. DR EnsemblBacteria; AAF40662; AAF40662; NMB0205. DR GeneID; 902313; -. DR KEGG; nme:NMB0205; -. DR PATRIC; 20355451; VBINeiMen85645_0254. DR eggNOG; ENOG41090R7; Bacteria. DR eggNOG; COG0735; LUCA. DR HOGENOM; HOG000014144; -. DR KO; K03711; -. DR OMA; DERSDIG; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; NMEN122586:GHGG-216-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR CollecTF; EXPREG_000006e0; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002481; FUR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01475; FUR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Iron; Metal-binding; KW Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc. FT CHAIN 1 144 Ferric uptake regulation protein. FT /FTId=PRO_0000095565. FT REGION 1 86 DNA-binding. {ECO:0000250}. FT REGION 87 144 Dimerization. {ECO:0000250}. FT COMPBIAS 89 92 His-rich. FT METAL 35 35 Zinc. {ECO:0000250}. FT METAL 83 83 Zinc. {ECO:0000250}. FT METAL 89 89 Iron. {ECO:0000250}. FT METAL 91 91 Iron. {ECO:0000250}. FT METAL 92 92 Zinc. {ECO:0000250}. FT METAL 95 95 Zinc. {ECO:0000250}. FT METAL 98 98 Zinc. {ECO:0000250}. FT METAL 103 103 Zinc. {ECO:0000250}. FT METAL 110 110 Iron. {ECO:0000250}. FT METAL 127 127 Iron. {ECO:0000250}. FT VARIANT 5 5 N -> S (in strain: CCUG 37603). SQ SEQUENCE 144 AA; 16411 MW; B37489E92856AC02 CRC64; MEKFNNIAQL KDSGLKVTGP RLKILDLFET HAEEHLSAED VYRILLEEGV EIGVATIYRV LTQFEQAGIL QRHHFETGKA VYELDKGDHH DHIVCVKCGE VTEFHNPEIE ALQDKIAEEN GYRIVDHALY MYGVCSDCQA KGKR // ID G6PI2_NEIMB Reviewed; 547 AA. AC Q9K153; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Glucose-6-phosphate isomerase 2; DE Short=GPI 2; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase 2; DE Short=PGI 2; DE AltName: Full=Phosphohexose isomerase 2; DE Short=PHI 2; GN Name=pgi2; OrderedLocusNames=NMB0334; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40777.1; -; Genomic_DNA. DR PIR; A81211; A81211. DR RefSeq; NP_273383.1; NC_003112.2. DR RefSeq; WP_002224874.1; NC_003112.2. DR ProteinModelPortal; Q9K153; -. DR STRING; 122586.NMB0334; -. DR PaxDb; Q9K153; -. DR EnsemblBacteria; AAF40777; AAF40777; NMB0334. DR GeneID; 902449; -. DR KEGG; nme:NMB0334; -. DR PATRIC; 20355807; VBINeiMen85645_0422. DR eggNOG; ENOG4107QP8; Bacteria. DR eggNOG; COG0166; LUCA. DR HOGENOM; HOG000261370; -. DR KO; K01810; -. DR OMA; EQPAVEW; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; NMEN122586:GHGG-355-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1390.10; -; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR023096; G6P_Isomerase_C. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 547 Glucose-6-phosphate isomerase 2. FT /FTId=PRO_0000180694. FT ACT_SITE 351 351 Proton donor. {ECO:0000250}. FT ACT_SITE 382 382 {ECO:0000250}. FT ACT_SITE 508 508 {ECO:0000250}. SQ SEQUENCE 547 AA; 60199 MW; 54B0CC7FB74BA028 CRC64; MNAFTRAWYA LERHYQDTRH VLLRDRFACE PDRFERMHER LDGMLFDYSK NRLGEDTLQL LCNLADAADL EGKMRALRTG AKVNGSEGRA ALHTALRLPD GADAVYVDGR DVLPEIRREL NRALKFAHSL DDGSYQGITG KRITDFVHIG IGGSDLGPAM CVQALEPFRR HITVHFAANA DPACLDAVLC RLNPETTVFC VASKSFKTPE TLLNAQAVKA WYRGAGFSES ETACHFCAVS ADTAAAAAFG IAAERVFAMY DWVGGRYSVW SPVGLPVMVA VGGARFRELL AGAHAMDRHF FSTPTRHNIP VLMALIAVWY NNFQHADGQT AVPYSHNLRL LPAWLNQLDM ESLGKSRASD GSPAVCKTGG IVFGGEGVNC QHAYFQLLHQ GTRLIPCDFI VPMTAQGRED GRSRFTVANA FAQAEALMKG KTLDEARAEL ADLPEAERER LAPHKEFPGN RPSNSILIDR LTPYNLGMLM AAYEHKTFVQ GAIWNVNPFD QWGVEYGKQL AKTIIGELEG GTSVHDASTE GLMAFYRECR LKGGGAA // ID GALE_NEIMB Reviewed; 339 AA. AC P56985; Q59617; Q59624; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=UDP-glucose 4-epimerase; DE EC=5.1.3.2; DE AltName: Full=Galactowaldenase; DE AltName: Full=UDP-galactose 4-epimerase; GN Name=galE; OrderedLocusNames=NMB0064; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=MC58; RX PubMed=7934827; DOI=10.1111/j.1365-2958.1993.tb01962.x; RA Jennings M.P., van der Ley P., Wilks K.E., Maskell D.J., Poolman J.T., RA Moxon E.R.; RT "Cloning and molecular analysis of the galE gene of Neisseria RT meningitidis and its role in lipopolysaccharide biosynthesis."; RL Mol. Microbiol. 10:361-369(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the metabolism of galactose. Plays an CC essential role in the incorporation of galactose into CC meningococcal lipopolysaccharide surface molecules, which are CC important for pathogenesis. Catalyzes the conversion of UDP- CC galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism CC involving the transient reduction of NAD. CC {ECO:0000269|PubMed:7934827}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L20495; AAA65535.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40532.1; -; Genomic_DNA. DR PIR; S39638; S39638. DR RefSeq; NP_273128.1; NC_003112.2. DR RefSeq; WP_002249104.1; NC_003112.2. DR ProteinModelPortal; P56985; -. DR SMR; P56985; 1-339. DR STRING; 122586.NMB0064; -. DR PaxDb; P56985; -. DR EnsemblBacteria; AAF40532; AAF40532; NMB0064. DR GeneID; 902171; -. DR KEGG; nme:NMB0064; -. DR PATRIC; 20355133; VBINeiMen85645_0100. DR eggNOG; ENOG4105CMR; Bacteria. DR eggNOG; COG1087; LUCA. DR HOGENOM; HOG000168001; -. DR KO; K01784; -. DR OMA; SDPSWNI; -. DR OrthoDB; EOG6WHNS9; -. DR BioCyc; NMEN122586:GHGG-70-MONOMER; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01179; galE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Isomerase; NAD; Reference proteome. FT CHAIN 1 339 UDP-glucose 4-epimerase. FT /FTId=PRO_0000183213. FT NP_BIND 12 13 NAD. {ECO:0000250}. FT NP_BIND 32 37 NAD. {ECO:0000250}. FT NP_BIND 59 60 NAD. {ECO:0000250}. FT NP_BIND 81 85 NAD. {ECO:0000250}. FT REGION 200 201 Substrate binding. {ECO:0000250}. FT REGION 217 219 Substrate binding. {ECO:0000250}. FT REGION 293 296 Substrate binding. {ECO:0000250}. FT ACT_SITE 150 150 Proton acceptor. {ECO:0000250}. FT BINDING 100 100 NAD. {ECO:0000250}. FT BINDING 125 125 NAD. {ECO:0000250}. FT BINDING 125 125 Substrate. {ECO:0000250}. FT BINDING 150 150 NAD. {ECO:0000250}. FT BINDING 150 150 Substrate. {ECO:0000250}. FT BINDING 154 154 NAD. {ECO:0000250}. FT BINDING 179 179 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 180 180 Substrate. {ECO:0000250}. FT BINDING 232 232 Substrate. {ECO:0000250}. SQ SEQUENCE 339 AA; 37062 MW; 7D702C44F07DA99B CRC64; MKKILVTGGT GFIGSHTVVS LLKSGHQVVI LDNLCNSSIN ILPRLKTITG QEIPFYQGDI RDREILRRIF AENRIDSVIH FAGLKAVGES VAEPMKYYDN NVSGSLVLAE EMARAGVFSI VFSSSATVYG DPGKVPYTED MPPGDTTSPY GASKSMVERI LTDIQKADPR WSMILLRYFN PIGAHESGLI GEQPNGIPNN LLPYICQVAA GKLPQLAVFG DDYPTPDGTG MRDYIHVMDL AEGHVAAMQA KSNVAGTHLL NLGSGRASSV LEIIRAFEAA SGLTIPYEVK PRRAGDLACF YADPSYTKAQ IGWQTQRDLT QMMEDSWRWV SNNPNGYDD // ID GATC_NEIMB Reviewed; 96 AA. AC Q9JZ00; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 77. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C; DE Short=Glu-ADT subunit C; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122}; GN Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; GN OrderedLocusNames=NMB1355; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00122}. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP- CC Rule:MF_00122}. CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP- CC Rule:MF_00122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41729.1; -; Genomic_DNA. DR PIR; D81091; D81091. DR RefSeq; NP_274373.1; NC_003112.2. DR RefSeq; WP_002219137.1; NC_003112.2. DR ProteinModelPortal; Q9JZ00; -. DR STRING; 122586.NMB1355; -. DR PaxDb; Q9JZ00; -. DR EnsemblBacteria; AAF41729; AAF41729; NMB1355. DR GeneID; 903777; -. DR KEGG; nme:NMB1355; -. DR PATRIC; 20358367; VBINeiMen85645_1695. DR eggNOG; ENOG41080G2; Bacteria. DR eggNOG; COG0721; LUCA. DR HOGENOM; HOG000017522; -. DR KO; K02435; -. DR OMA; SVTPMAM; -. DR OrthoDB; EOG61S35Z; -. DR BioCyc; NMEN122586:GHGG-1393-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00122; GatC; 1. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR Pfam; PF02686; Glu-tRNAGln; 1. DR SUPFAM; SSF141000; SSF141000; 1. DR TIGRFAMs; TIGR00135; gatC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 96 Glutamyl-tRNA(Gln) amidotransferase FT subunit C. FT /FTId=PRO_0000105315. SQ SEQUENCE 96 AA; 10958 MW; EECAEC185A42D335 CRC64; MALTLADVDK IARLSRLHLT AEEKEKSLQE LNDIFTMVEQ MQTINTDGIE PMAHPHEAAL RLREDEVTET DRAAEYQAGA PEVRNRLYIV PQVIEE // ID FOLD_NEIMB Reviewed; 284 AA. AC P0C277; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576}; GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; GN OrderedLocusNames=NMB2077; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidation of 5,10- CC methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and CC then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- CC formyltetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) = CC 5,10-methenyltetrahydrofolate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_01576}. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP- CC Rule:MF_01576}. CC -!- SEQUENCE CAUTION: CC Sequence=AE002098; Type=Frameshift; Positions=33; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P0C277; -. DR SMR; P0C277; 2-283. DR OMA; AHERPGX; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020867; THF_DH/CycHdrlase_CS. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00766; THF_DHG_CYH_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 284 Bifunctional protein FolD. FT /FTId=PRO_0000268416. FT NP_BIND 166 168 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 191 191 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 232 232 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01576}. SQ SEQUENCE 284 AA; 30145 MW; 6435AA7AFD4B2263 CRC64; MSAQLINGKE VSQKRLQAVA EAVAQRQQNN LHHPCLAVVL VGGDPASAVY VRNKKTACQK CGIKSLSYEL PESTSQEELL ALVDRLNADS EVDGILVQLP LPKHLDSQAV LERISPDKDV DGFHPYNVGR LAVKMPLMRP CTPKGVMTLL EAYGIDPKGK KAVVVGASNI VGRPQALELL LARATVTVCH SATENLTDEV AGADILVVGV GIPNFVKGEW IKPGAVVIDV GINRLDDGSL CGDVEFETAK ERAAMITPVP GGVGPMTIAT LMENTLHAAS LHDA // ID FRPA_NEIMB Reviewed; 1302 AA. AC Q9K0K9; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Iron-regulated protein FrpA; GN Name=frpA; OrderedLocusNames=NMB0585; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May participate in the pathogenesis of meningococcal CC disease. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000250}. CC -!- DOMAIN: The Gly-rich region is probably involved in binding CC calcium, which is required for target cell-binding or cytolytic CC activity. CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 12 hemolysin-type calcium-binding repeats. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41013.1; -; Genomic_DNA. DR PIR; C81182; C81182. DR RefSeq; NP_273629.1; NC_003112.2. DR RefSeq; WP_010980816.1; NC_003112.2. DR ProteinModelPortal; Q9K0K9; -. DR SMR; Q9K0K9; 942-988. DR STRING; 122586.NMB0585; -. DR PaxDb; Q9K0K9; -. DR EnsemblBacteria; AAF41013; AAF41013; NMB0585. DR GeneID; 902700; -. DR KEGG; nme:NMB0585; -. DR PATRIC; 20356455; VBINeiMen85645_0747. DR eggNOG; ENOG4105DDI; Bacteria. DR eggNOG; COG2931; LUCA. DR HOGENOM; HOG000219011; -. DR OMA; YIFDLGH; -. DR OrthoDB; EOG690MC5; -. DR BioCyc; NMEN122586:GHGG-611-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR Gene3D; 2.150.10.10; -; 3. DR InterPro; IPR010566; Haemolys_ca-bd. DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS. DR InterPro; IPR001343; Hemolysn_Ca-bd. DR InterPro; IPR003995; RTX_toxin_determinant-A. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. DR Pfam; PF06594; HCBP_related; 3. DR Pfam; PF00353; HemolysinCabind; 12. DR PRINTS; PR01488; RTXTOXINA. DR SUPFAM; SSF51120; SSF51120; 3. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 9. PE 3: Inferred from homology; KW Calcium; Cell outer membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Secreted; Toxin. FT CHAIN 1 1302 Iron-regulated protein FrpA. FT /FTId=PRO_0000196242. FT REPEAT 742 759 Hemolysin-type calcium-binding 1. FT REPEAT 760 777 Hemolysin-type calcium-binding 2. FT REPEAT 888 905 Hemolysin-type calcium-binding 3. FT REPEAT 906 923 Hemolysin-type calcium-binding 4. FT REPEAT 924 941 Hemolysin-type calcium-binding 5. FT REPEAT 942 959 Hemolysin-type calcium-binding 6. FT REPEAT 960 977 Hemolysin-type calcium-binding 7. FT REPEAT 1088 1105 Hemolysin-type calcium-binding 8. FT REPEAT 1106 1123 Hemolysin-type calcium-binding 9. FT REPEAT 1124 1141 Hemolysin-type calcium-binding 10. FT REPEAT 1142 1159 Hemolysin-type calcium-binding 11. FT REPEAT 1160 1177 Hemolysin-type calcium-binding 12. SQ SEQUENCE 1302 AA; 141398 MW; 21D058C56C98BDE8 CRC64; MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DDAAAIVGKD ANLNGLNLWM KKGVENLWDD TVGKKTRLEK FDRVALQHFS QYVDLINENN GRLPNTSEIE RSYYKAVTEN GVSSSAAIDL VINRSLPDMA DGYWALGLGI EAERIHNEQA VNNPNGSERD NRKQLISALD KGFDGSFKEK HFTFLQSVIM DVTKLGVEYT IDGWQKIGGW GNGIINDLYK SVVKREWTGI FEIVNNNIKQ FRDLFPNPEG WIDDGHQCFA PWVKETKKRN GKYHVYDPLA LDLDGDGIET VAAKGFSGSL FDHTNNGIRT ATGWVSADDG LLVRDLNGNG IIDNGAELFG DNTKLADGSF AKHGYAALAE LDSNGDNIIN AADAAFQSLR VWQDLNQDGI SQANELRTLE ELGIQSLDLA YKDVNKNLGN GNTLAQQGSY TKTDGTTAKM GDLLLAADNL HSRFKDKVEL TAEQAKAANL AGIGRLRDLR EAAALSGDLA NMLKAYSAAE TKEAQLALLD NLIHKWAETD SNWGKKSPMR LSTDWTQTAN EGIALTPSQV AQLKKNALVS LSDKAKAAID AARDRIAVLD AYTGQDSNTL YYMSEEDALN IVKVTNDTYD HLAKNIYQNL LFQTRLQPYL NQISFKMEND TFTLDFSGLV QAFNHVKETN PQKAFVDLAE MLAYGELRSW YEGRRLMTDY VEEAKKAGKF EDYQKVLGQE TVALLAKTSG TQADDILQNV GFGHNKNVSL YGNDGNDTLI GGAGNDYLEG GSGSDTYVFG EGFGQDTVYN YDYATGRKDI IRFTDGITAD MLTFTREGNH LLIKAKDGSG QVTVQSYFQN DGSGAYRIDE IHFDNGKVLD VATVKELVQQ STDGSDRLYA YQSGNTLNGG LGDDYLYGAD GDDLLNGDAG NDSIYSGNGN DTLDGGEGND ALYGYNGNDA LNGGEGNDHL NGEDGNDTLI GGAGNDYLEG GSGSDTYVFG KGFGQDAVYN YDYATGRKDI IRFTDGITAD MLTFTREGNH LLIKAKDGSG QVTVQSYFQN DGSGAYRIDE IHFDNGKVLD VATVKELVQQ STDGSDRLYA YQSGNTLNGG LGDDYLYGAD GDDLLNGDAG NDSIYSGNGN DTLDGGEGND ALYGYNGNDA LNGGEGNDHL NGEDGNDTLI GGAGNDYLEG GSGSDTYVFG EGFGQDTVYN YHVDKNSDTM HFKGFKAADV HFIRSGSDLV LSASEQDNVR ISGFFYGENH RVDTFVFDDA AISNPDFAKY INAGNNLVQS MSVFGSNTAA TGGNVDANIQ SVQQPLLVTP SA // ID FRPC_NEIMB Reviewed; 1829 AA. AC Q9JYV5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Iron-regulated protein FrpC; GN Name=frpC; OrderedLocusNames=NMB1415; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May participate in the pathogenesis of meningococcal CC disease. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000250}. CC -!- DOMAIN: The Gly-rich region is probably involved in binding CC calcium, which is required for target cell-binding or cytolytic CC activity. CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 22 hemolysin-type calcium-binding repeats. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41776.1; -; Genomic_DNA. DR PIR; E81086; E81086. DR RefSeq; NP_274427.1; NC_003112.2. DR RefSeq; WP_010980934.1; NC_003112.2. DR ProteinModelPortal; Q9JYV5; -. DR SMR; Q9JYV5; 1070-1116. DR STRING; 122586.NMB1415; -. DR PaxDb; Q9JYV5; -. DR EnsemblBacteria; AAF41776; AAF41776; NMB1415. DR GeneID; 903837; -. DR KEGG; nme:NMB1415; -. DR PATRIC; 20358511; VBINeiMen85645_1767. DR eggNOG; ENOG4105DDI; Bacteria. DR eggNOG; COG2931; LUCA. DR HOGENOM; HOG000219011; -. DR OMA; IKARVIT; -. DR OrthoDB; EOG690MC5; -. DR BioCyc; NMEN122586:GHGG-1453-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR Gene3D; 2.150.10.10; -; 5. DR InterPro; IPR010566; Haemolys_ca-bd. DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS. DR InterPro; IPR001343; Hemolysn_Ca-bd. DR InterPro; IPR003995; RTX_toxin_determinant-A. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. DR Pfam; PF06594; HCBP_related; 5. DR Pfam; PF00353; HemolysinCabind; 22. DR PRINTS; PR01488; RTXTOXINA. DR SUPFAM; SSF51120; SSF51120; 5. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 17. PE 3: Inferred from homology; KW Calcium; Cell outer membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Secreted; Toxin. FT CHAIN 1 1829 Iron-regulated protein FrpC. FT /FTId=PRO_0000196244. FT REPEAT 869 886 Hemolysin-type calcium-binding 1. FT REPEAT 887 904 Hemolysin-type calcium-binding 2. FT REPEAT 1015 1032 Hemolysin-type calcium-binding 3. FT REPEAT 1033 1050 Hemolysin-type calcium-binding 4. FT REPEAT 1051 1068 Hemolysin-type calcium-binding 5. FT REPEAT 1069 1086 Hemolysin-type calcium-binding 6. FT REPEAT 1087 1104 Hemolysin-type calcium-binding 7. FT REPEAT 1215 1232 Hemolysin-type calcium-binding 8. FT REPEAT 1233 1250 Hemolysin-type calcium-binding 9. FT REPEAT 1251 1268 Hemolysin-type calcium-binding 10. FT REPEAT 1269 1286 Hemolysin-type calcium-binding 11. FT REPEAT 1287 1304 Hemolysin-type calcium-binding 12. FT REPEAT 1415 1432 Hemolysin-type calcium-binding 13. FT REPEAT 1433 1450 Hemolysin-type calcium-binding 14. FT REPEAT 1451 1468 Hemolysin-type calcium-binding 15. FT REPEAT 1469 1486 Hemolysin-type calcium-binding 16. FT REPEAT 1487 1504 Hemolysin-type calcium-binding 17. FT REPEAT 1615 1632 Hemolysin-type calcium-binding 18. FT REPEAT 1633 1650 Hemolysin-type calcium-binding 19. FT REPEAT 1651 1668 Hemolysin-type calcium-binding 20. FT REPEAT 1669 1686 Hemolysin-type calcium-binding 21. FT REPEAT 1687 1704 Hemolysin-type calcium-binding 22. SQ SEQUENCE 1829 AA; 197446 MW; 8F63506E1F6D9B40 CRC64; MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DDAAAIVGKD ANLNGLNLWM KKGVENLWDD TVGKKTRLEK FDRVALQHFR QYARLINQNN GRLPNTSEIE RSYYKAVTDN GVSSSAAIDL VINRSLPDMA DGYWALGLGI EAERIHNEQA VNNPNGSERD NRKQLISALD KGFDGSFKEK HFTFLQSVMM DVTKLGVEYT IDGWQKIGGW GNGIINDLYK SVVKREWTGI FEIVNNNIKQ GNEAFKNEIN SLVHDMKAAG KEFGDDLNTQ WNNLTQAAEI IYNDIVDNTS QGIEKGVKAI KELSEKMKNA ASDLADGSAE KAKQVVEDLA QAAKEAYENA KSTAEKAAQA AREFFKGLPS FKDLAEKFRD LFPNPEGWID DGHQCLAPWV KETKKRNGKY HVYDPLALDL DGDGIETVAT KGFAGSLFDH TNNGIRTATG WVSADDGLLV RDLNGNGIID NGAELFGDNT KLADGSFAKH GYAALAELDS NGDNIINAAD AAFQTLRVWQ DLNQDGISQA NELRTLEELG IQSLDLAYKD VNKNLGNGNT LAQQGSYTKT DGTTAKMGDL LLAADNLHSR FKDKVELTAE QAKAANLAGI GRLRDLREAA ALSGDLANML KAYSAAETKE AQLALLDNLI HKWAETDSNW GKKSPMRLST DWTQTANEGI ALTPSQVAQL KKNALVSLSD KAKAAIDAAR DRIAVLDAYT GQDSNTLYYM SEEDALNIVK VTNDTYDHLA KNIYQNLLFQ TRLQPYLNQI SFKMENDTFT LDFSGLVQAF NHVKETNPQK AFVDLAEMLA YGELRSWYEG RRLMTDYVEE AKKAGKFEDY QKVLGQETVA LLAKTSGTQA DDILQNVGFG HNKNVSLYGN DGNDTLIGGA GNDYLEGGSG SDTYVFGEGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDTVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT VQYYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDAVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GNTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL NGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGKGF GQDAVYNYDY ATGRKDIIRF TDGITADMLT FTREGNHLLI KAKDGSGQVT VQSYFQNDGS GAYRIDEIHF DNGKVLDVAT VKELVQQSTD GSDRLYAYQS GSTLNGGLGD DYLYGADGDD LLNGDAGNDS IYSGNGNDTL DGGEGNDALY GYNGNDALNG GEGNDHLNGE DGNDTLIGGA GNDYLEGGSG SDTYVFGEGF GQDTVYNYHV DKNSDTMHFK GFKAADVHFI RSGSDLVLSA SEQDNVRISG FFYGENHRVD TFVFDDAAIS NPDFAKYINA GNNLVQSMSV FGSNTAATGG NVDANIQSVQ QPLLVTPSA // ID FTSL_NEIMB Reviewed; 89 AA. AC Q7DDQ4; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Cell division protein FtsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN Name=ftsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN OrderedLocusNames=NMB0412; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. {ECO:0000255|HAMAP-Rule:MF_00910}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00910}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00910}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00910}. Note=Localizes to the division CC septum where it forms a ring structure. {ECO:0000255|HAMAP- CC Rule:MF_00910}. CC -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000255|HAMAP- CC Rule:MF_00910}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40851.1; -; Genomic_DNA. DR PIR; A81202; A81202. DR RefSeq; NP_273461.1; NC_003112.2. DR RefSeq; WP_002216515.1; NC_003112.2. DR STRING; 122586.NMB0412; -. DR PaxDb; Q7DDQ4; -. DR EnsemblBacteria; AAF40851; AAF40851; NMB0412. DR GeneID; 902528; -. DR KEGG; nme:NMB0412; -. DR PATRIC; 20356013; VBINeiMen85645_0522. DR eggNOG; COG3117; LUCA. DR HOGENOM; HOG000219098; -. DR OrthoDB; EOG6WQD9T; -. DR BioCyc; NMEN122586:GHGG-436-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00910; FtsL; 1. DR InterPro; IPR011922; Cell_div_FtsL. DR Pfam; PF04999; FtsL; 1. DR TIGRFAMs; TIGR02209; ftsL_broad; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Coiled coil; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 89 Cell division protein FtsL. FT /FTId=PRO_0000414564. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TRANSMEM 7 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TOPO_DOM 25 89 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT COILED 33 73 {ECO:0000255}. SQ SEQUENCE 89 AA; 10186 MW; 9D313BEB0929DEB5 CRC64; MAMNKLNFLL LLAVCVSAFS VVMQQNQYRL NFTALDKAKK QEIALEQDYA QMRLQQARLA NHEAIRAAAE KQNLHPPVSG NTFMVEHQR // ID GATB_NEIMB Reviewed; 476 AA. AC Q9JYZ7; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; DE Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121}; GN Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121}; GN OrderedLocusNames=NMB1358; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). CC {ECO:0000255|HAMAP-Rule:MF_00121}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00121}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00121}. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP- CC Rule:MF_00121}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41732.1; -; Genomic_DNA. DR PIR; G81091; G81091. DR RefSeq; NP_274376.1; NC_003112.2. DR RefSeq; WP_002225147.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ7; -. DR STRING; 122586.NMB1358; -. DR PaxDb; Q9JYZ7; -. DR EnsemblBacteria; AAF41732; AAF41732; NMB1358. DR GeneID; 903780; -. DR KEGG; nme:NMB1358; -. DR PATRIC; 20358373; VBINeiMen85645_1698. DR eggNOG; ENOG4105CHT; Bacteria. DR eggNOG; COG0064; LUCA. DR HOGENOM; HOG000223743; -. DR KO; K02434; -. DR OMA; RAMRTKE; -. DR OrthoDB; EOG6RJV5B; -. DR BioCyc; NMEN122586:GHGG-1396-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.410; -; 1. DR HAMAP; MF_00121; GatB; 1. DR InterPro; IPR004413; Apn/Gln-ADT_bsu. DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E. DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat. DR InterPro; IPR018027; Asn/Gln_amidotransferase. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR023168; GatB_Yqey_C. DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS. DR PANTHER; PTHR11659; PTHR11659; 1. DR Pfam; PF02934; GatB_N; 1. DR Pfam; PF02637; GatB_Yqey; 1. DR SMART; SM00845; GatB_Yqey; 1. DR SUPFAM; SSF89095; SSF89095; 1. DR TIGRFAMs; TIGR00133; gatB; 1. DR PROSITE; PS01234; GATB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 476 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit B. FT /FTId=PRO_0000148817. SQ SEQUENCE 476 AA; 51911 MW; 198AB255E3E82A33 CRC64; MTWETVIGLE IHVQLNTKSK IFSGASTAFG AEPNAHASVV ECALPGVLPV MNREVVEKAI KLGLALDAKI NQKNVFDRKN YFYPDLPKGY QISQLDLPIV EHGKLEIVVG DDVKTINVTR AHMEEDAGKS VHEGLNGATG IDLNRAGTPL LEVVSEPEMR SAAEAVAYAK ALHSLVTWLD ICDGNMAEGS FRVDANVSVR PKGQEEFGTR REIKNLNSFR FLEQAINYEA EAQIEILEDG GKVQQATMLF DPEKGETRVM RLKEDAHDYR YFPDPDLLPV IISDAQMQKA KAEMPELPKE MAARFVADYG VSEYDARLLT ASRAQAAYFE EAAKESGQGK LTANWMNGEL AAALNKEGME LADSPITAPR LAALVGKIAD GTLSSKLAKK AFEAMWAEPE ATIAEIIEKH GLQQMTDTGE IEAMVDEVLA NNAKAVEQFK SGNEKALNAI VGQVMKASKG KANPAQVQEL IKAKLA // ID FTSY_NEIMB Reviewed; 421 AA. AC P57011; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; Synonyms=pilA; GN OrderedLocusNames=NMB0045; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Acts as a receptor for the CC complex formed by the signal recognition particle (SRP) and the CC ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to CC the transfer of the RNC complex to the Sec translocase for CC insertion into the membrane, the hydrolysis of GTP by both Ffh and CC FtsY, and the dissociation of the SRP-FtsY complex into the CC individual components. {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein; Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP- CC Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40516.1; -; Genomic_DNA. DR PIR; H81243; H81243. DR RefSeq; NP_273111.1; NC_003112.2. DR RefSeq; WP_002243928.1; NC_003112.2. DR ProteinModelPortal; P57011; -. DR SMR; P57011; 128-420. DR STRING; 122586.NMB0045; -. DR PaxDb; P57011; -. DR EnsemblBacteria; AAF40516; AAF40516; NMB0045. DR GeneID; 902148; -. DR KEGG; nme:NMB0045; -. DR PATRIC; 20355047; VBINeiMen85645_0060. DR eggNOG; ENOG4105CCP; Bacteria. DR eggNOG; COG0552; LUCA. DR HOGENOM; HOG000036278; -. DR KO; K03110; -. DR OMA; QIPIRFI; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; NMEN122586:GHGG-46-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00920; FtsY; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004390; SR_rcpt_FtsY. DR InterPro; IPR000897; SRP54_GTPase_dom. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW GTP-binding; Membrane; Nucleotide-binding; Receptor; KW Reference proteome. FT CHAIN 1 421 Signal recognition particle receptor FT FtsY. FT /FTId=PRO_0000101143. FT NP_BIND 228 235 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 309 313 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 373 376 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. SQ SEQUENCE 421 AA; 45143 MW; 22FB6D5D84A1E460 CRC64; MFSFFRRKKK QETPALEEAQ IQETAAKAES ELAQIVENIK EDAESLAESV KGQVESAVET VSGAVEQVKE TVAEMLSEAE EAAEKAAEQV EAAKEAVAET VGEAVGQVQE AVATTEEHKL GWAARLKQGL TKSRDKMAKS LAGVFGGGQI DEDLYEELET VLITSDMGME ATEYLMKDVR DRVSLKGLKD GNELRGALKE ALYDLIKPLE KPLVLPETKE PFVIMLAGIN GAGKTTSIGK LAKYFQAQGK SVLLAAGDTF RAAAREQLQA WGERNNVTVI SQTTGDSAAV CFDAVQAAKA RGIDIVLADT AGRLPTQLHL MEEIKKVKRV LQKAMPDAPH EIIVVLDANI GQNAVNQVKA FDDALGLTGL IVTKLDGTAK GGILAALASD RPVPVRYIGV GEGIDDLRPF DARAFVDALL D // ID G6PI1_NEIMB Reviewed; 548 AA. AC Q9JYX3; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Glucose-6-phosphate isomerase 1; DE Short=GPI 1; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase 1; DE Short=PGI 1; DE AltName: Full=Phosphohexose isomerase 1; DE Short=PHI 1; GN Name=pgi1; OrderedLocusNames=NMB1388; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41752.1; -; Genomic_DNA. DR PIR; C81089; C81089. DR RefSeq; NP_274402.1; NC_003112.2. DR RefSeq; WP_002225136.1; NC_003112.2. DR ProteinModelPortal; Q9JYX3; -. DR SMR; Q9JYX3; 3-545. DR STRING; 122586.NMB1388; -. DR PaxDb; Q9JYX3; -. DR EnsemblBacteria; AAF41752; AAF41752; NMB1388. DR GeneID; 903810; -. DR KEGG; nme:NMB1388; -. DR PATRIC; 20358457; VBINeiMen85645_1740. DR eggNOG; ENOG4107QP8; Bacteria. DR eggNOG; COG0166; LUCA. DR HOGENOM; HOG000261370; -. DR KO; K01810; -. DR OMA; CETQAML; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; NMEN122586:GHGG-1426-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1390.10; -; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR023096; G6P_Isomerase_C. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 548 Glucose-6-phosphate isomerase 1. FT /FTId=PRO_0000180693. FT ACT_SITE 353 353 Proton donor. {ECO:0000250}. FT ACT_SITE 384 384 {ECO:0000250}. FT ACT_SITE 512 512 {ECO:0000250}. SQ SEQUENCE 548 AA; 62084 MW; 28A85A19BFF174E1 CRC64; MKHLHDLPAW SKLWNHFDDS KTLHMREMFE QDPQRAERYW LQVGGLTLDY SKNRINDETM SLLFELAREA GVPERMRQMF HGEKINTTEN RAVLHVALRN RTNSPIVVDG EDVMPKVNRV LQRMGEFAHE VRSGSWLGYT NQVITDVVNI GIGGSDLGPL MMCTALKPFG HPRLNMHFVS NVDGSQLRDV LSKVHPETTL FIIASKTFTT QETLTNALTA REWFLNHAGD EEAVAKHFAA VSTNQKAVAE FGIDTANMFE FWDWVGGRYS LWSAIGLPIM LYLGEENFIE MLNGAHLMDQ HFINTPLERN LPVILALIGI WYINYYGGGS HVIAPYDQHL HRLPKFIQQL DMESNGKQVT LDGKAVGHET SPIIWGETGI NGQHAFFQLL HQGTHITPID LIASLEKRSN LPGHHEILLA NVFAQAEAFM RGKTPDEVRA ELKAQGMDEV RIEELVPHKT FSGNRPTNLI LMDKVNPRNM GSLIAMYEHK TFVQGIIWGI NSFDQWGVEL GKQLAKTILG ELTGETGPQK HDSSTERLIN LYLQTNRK // ID GATA_NEIMB Reviewed; 481 AA. AC Q9JYZ9; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120}; DE Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120}; DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120}; GN Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; GN OrderedLocusNames=NMB1356; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP- CC Rule:MF_00120}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00120}. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP- CC Rule:MF_00120}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00120}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41730.1; -; Genomic_DNA. DR PIR; E81091; E81091. DR RefSeq; NP_274374.1; NC_003112.2. DR RefSeq; WP_002225150.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ9; -. DR STRING; 122586.NMB1356; -. DR PaxDb; Q9JYZ9; -. DR EnsemblBacteria; AAF41730; AAF41730; NMB1356. DR GeneID; 903778; -. DR KEGG; nme:NMB1356; -. DR PATRIC; 20358369; VBINeiMen85645_1696. DR eggNOG; ENOG4105C3P; Bacteria. DR eggNOG; COG0154; LUCA. DR HOGENOM; HOG000116699; -. DR KO; K02433; -. DR OMA; KEYFGAG; -. DR OrthoDB; EOG61P6R9; -. DR BioCyc; NMEN122586:GHGG-1394-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1300.10; -; 1. DR HAMAP; MF_00120; GatA; 1. DR InterPro; IPR000120; Amidase. DR InterPro; IPR020556; Amidase_CS. DR InterPro; IPR023631; Amidase_dom. DR InterPro; IPR004412; GatA. DR PANTHER; PTHR11895; PTHR11895; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; SSF75304; 1. DR TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 481 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105183. FT ACT_SITE 76 76 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_00120}. FT ACT_SITE 151 151 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_00120}. FT ACT_SITE 175 175 Acyl-ester intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00120}. SQ SEQUENCE 481 AA; 51280 MW; 43698A67048D476D CRC64; MTQYTLKQAS VLLQSKQISA VELASAYLAA IAEKNPALNG YITIDQDKTL AEARAADERI AQGNASALTG VPVAYKDIFC QTGWRSACAS KMLDNFISPY TATVVQNLLD EGMVTLGRTN MDEFAMGSTN ENSFYGAAKN PWNLEHVPGG SSGGSAAVVA ARLAPAALGS DTGGSIRQPA SHCGITGIKP TYGTVSRFGM VAYASSFDQT GPMAQTAEDC AILLNAMAGF DPKDSTSLER EKEDYTRDLN QPLKGLKIGL PKEYFGEGNS ADVLTALQNT IDLLKAQGAE LIEVSLPQTK LSIPAYYVLA SAEASTNLSR YDGVRYGHRA AQFADLEEMY GKTRAEGFGS EVKRRIMIGT YVLSHGYYDA YYLKAQKLRR LVADDFQTAF ARCDLILAPT APTAAPKIGA DASPVETYLS DIYTIAVNLA GLPALTLPAG FSGGGLPVGV QLVGNYFAEA KILGAAHQIQ LNSDWHGKRP E // ID GLMM_NEIMB Reviewed; 444 AA. AC Q9JY89; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554}; DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554}; GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554}; GN OrderedLocusNames=NMB1690; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP- CC Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000255|HAMAP-Rule:MF_01554}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42038.1; -; Genomic_DNA. DR PIR; C81054; C81054. DR RefSeq; NP_274694.1; NC_003112.2. DR RefSeq; WP_002224978.1; NC_003112.2. DR ProteinModelPortal; Q9JY89; -. DR STRING; 122586.NMB1690; -. DR PaxDb; Q9JY89; -. DR EnsemblBacteria; AAF42038; AAF42038; NMB1690. DR GeneID; 903417; -. DR KEGG; nme:NMB1690; -. DR PATRIC; 20359333; VBINeiMen85645_2173. DR eggNOG; ENOG4107QJF; Bacteria. DR eggNOG; COG1109; LUCA. DR HOGENOM; HOG000268678; -. DR KO; K03431; -. DR OMA; FNLGGEQ; -. DR OrthoDB; EOG6TN467; -. DR BioCyc; NMEN122586:GHGG-1745-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR HAMAP; MF_01554_B; GlmM_B; 1. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR006352; GlmM_bact. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR TIGRFAMs; TIGR01455; glmM; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 444 Phosphoglucosamine mutase. FT /FTId=PRO_0000147921. FT ACT_SITE 104 104 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 104 104 Magnesium; via phosphate group. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 243 243 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 245 245 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 247 247 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT MOD_RES 104 104 Phosphoserine. {ECO:0000255|HAMAP- FT Rule:MF_01554}. SQ SEQUENCE 444 AA; 47688 MW; 7161B658FC03BBD1 CRC64; MAKKYFGTDG VRGEVGQFPI TPDFVLKLGY AAGQVLVQHD TDQKPTVLIG KDTRISGYML EAALVAGFTA AGVNVVQTGP LPTPGVAYLT RALRLSAGVM ISASHNAYSD NGIKFFAEGG VKLSDEVELE IEAKIDGEMK TQPSARLGRA RRISGADDRY IEFCKSTFPS HSDLRGLKLV VDTANGAGYG VAPKVFHELG AQVVSIGNEP NGYNINEKCG ATYTKTLQAA VLQHEADYGI ALDGDGDRLM MVDKNGQVYD GDSLIYVIAK ARAREGINIG GVVGTVMTNM AMEIALKEQG VDFCRAKVGD RYVLEQLNQR GWLIGGEASG HILCMDKHNT GDGIISALQV LAALQTLNQD LATVCADWQP YPQTMINVRI QKGQQWQEAS KDVLAEVEKE LEGKGRVVLR ASGTEPVVRV MVEARQADWA REGAERIAAA IGGI // ID GCH1L_NEIMB Reviewed; 249 AA. AC Q9JXG9; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog; GN OrderedLocusNames=NMB2054; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42374.1; -; Genomic_DNA. DR PIR; G81011; G81011. DR RefSeq; NP_275044.1; NC_003112.2. DR RefSeq; WP_002225699.1; NC_003112.2. DR ProteinModelPortal; Q9JXG9; -. DR STRING; 122586.NMB2054; -. DR PaxDb; Q9JXG9; -. DR EnsemblBacteria; AAF42374; AAF42374; NMB2054. DR GeneID; 904027; -. DR KEGG; nme:NMB2054; -. DR PATRIC; 20360264; VBINeiMen85645_2632. DR eggNOG; ENOG4107QNR; Bacteria. DR eggNOG; COG0327; LUCA. DR HOGENOM; HOG000014258; -. DR OMA; RVGWCTG; -. DR OrthoDB; EOG6N3CRB; -. DR BioCyc; NMEN122586:GHGG-2117-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002678; GTP_cyclohydrolase_I/Nif3. DR PANTHER; PTHR13799; PTHR13799; 1. DR Pfam; PF01784; NIF3; 1. DR SUPFAM; SSF102705; SSF102705; 1. DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 249 GTP cyclohydrolase 1 type 2 homolog. FT /FTId=PRO_0000147321. FT METAL 64 64 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 65 65 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 102 102 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 217 217 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 221 221 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 221 221 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. SQ SEQUENCE 249 AA; 27417 MW; 58EC0E47B6AE27B2 CRC64; MVLCRDFLTW CNETLQTALF KDYAPNGLQV EGREYIGKIV TSVTASRAAI DFAVEQKADL LLVHHGMFWK NELPTVTGWK KERIAALLRH DINMAGYHLP LDAHPTLGNN AQLADRLGFA TEKRFGEQNL LNSGSLKQAK TLGALAAHIE TVLQRKPVVI GNPEREIRRV AWCSGGAQGF FQTAIDEGVD LYLTGEISEA QYHLANETGT AFISAGHHAT ERYGVRALAE SAAEVFGLEV CHFDENNPA // ID GCH4_NEIMB Reviewed; 298 AA. AC Q9K023; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 11-NOV-2015, entry version 70. DE RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527}; DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527}; GN Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527}; GN OrderedLocusNames=NMB0803; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01527}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6- CC (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01527}. CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_01527}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000255|HAMAP-Rule:MF_01527}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41216.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41216.1; ALT_INIT; Genomic_DNA. DR PIR; B81155; B81155. DR RefSeq; NP_273845.1; NC_003112.2. DR STRING; 122586.NMB0803; -. DR PaxDb; Q9K023; -. DR EnsemblBacteria; AAF41216; AAF41216; NMB0803. DR GeneID; 902918; -. DR KEGG; nme:NMB0803; -. DR PATRIC; 20356993; VBINeiMen85645_1015. DR eggNOG; ENOG4105DZA; Bacteria. DR eggNOG; COG1469; LUCA. DR HOGENOM; HOG000280679; -. DR KO; K09007; -. DR OMA; INMYVDL; -. DR OrthoDB; EOG6X6RBH; -. DR BioCyc; NMEN122586:GHGG-834-MONOMER; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1. DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2. DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA. DR Pfam; PF02649; GCHY-1; 1. DR TIGRFAMs; TIGR00294; TIGR00294; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 298 GTP cyclohydrolase FolE2. FT /FTId=PRO_0000147716. FT SITE 188 188 May be catalytically important. FT {ECO:0000255|HAMAP-Rule:MF_01527}. SQ SEQUENCE 298 AA; 33280 MW; 023BFD2A015B7CB4 CRC64; MQLLKASDII SHLQIDGIFP GGNAIPCTHL NNYMNIKEKQ LMNTIADVQS SRDLRNLPIN QVGIKDLRFP ITLQTAEGIQ STIARLTMTV YLPAEQKGTH MSRFVALMEQ HAEALDFAQL RKLTTEMVAL LDSRAGKISV SFPFFRKKTA PVSGIRSLLD YDVCLTGEIK DGAYGHSMKV MIPVTSLCPC SKEISQYGAH NQRSHVTVSL TADAEVGIEE VIDYVEAQAS CQLYGLLKRP DEKYVTEKAY ENPKFVEDMV RDVATSLIAD KRIKSFVVES ENFESIHNHS AYAYIAYP // ID GCSH_NEIMB Reviewed; 128 AA. AC Q9K0L7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272}; GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; GN OrderedLocusNames=NMB0575; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The H protein shuttles the methylamine group of glycine CC from the P protein to the T protein. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00272}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|HAMAP- CC Rule:MF_00272}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00272}. CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41003.1; -; Genomic_DNA. DR PIR; B81183; B81183. DR RefSeq; NP_273619.1; NC_003112.2. DR RefSeq; WP_002222872.1; NC_003112.2. DR ProteinModelPortal; Q9K0L7; -. DR STRING; 122586.NMB0575; -. DR PaxDb; Q9K0L7; -. DR EnsemblBacteria; AAF41003; AAF41003; NMB0575. DR GeneID; 902690; -. DR KEGG; nme:NMB0575; -. DR PATRIC; 20356431; VBINeiMen85645_0735. DR eggNOG; ENOG4105KE9; Bacteria. DR eggNOG; COG0509; LUCA. DR HOGENOM; HOG000239392; -. DR KO; K02437; -. DR OMA; NTDPYGE; -. DR OrthoDB; EOG60CWTC; -. DR BioCyc; NMEN122586:GHGG-601-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00272; GcvH; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR002930; GCV_H. DR InterPro; IPR017453; GCV_H_sub. DR InterPro; IPR011053; Single_hybrid_motif. DR PANTHER; PTHR11715; PTHR11715; 1. DR Pfam; PF01597; GCV_H; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00527; gcvH; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Complete proteome; Lipoyl; Reference proteome. FT CHAIN 1 128 Glycine cleavage system H protein. FT /FTId=PRO_0000166230. FT DOMAIN 25 107 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT MOD_RES 66 66 N6-lipoyllysine. {ECO:0000255|HAMAP- FT Rule:MF_00272}. SQ SEQUENCE 128 AA; 13643 MW; 97FDC4E14E412579 CRC64; MSNNIPAELK YVASHEWLRL EEDGTITVGI THHAQELLGD IVFVELPEVG ANLAAEEQAG VVESVKAASD VYAPIAGEVV AVNEDLPSAP ETANSDPYGA GWFFKLKPAN VADYDSLLTA EQYAGEVD // ID GCST_NEIMB Reviewed; 366 AA. AC Q9K0L8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259}; DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259}; GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259}; GN OrderedLocusNames=NMB0574; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10- CC methylenetetrahydrofolate + NH(3). {ECO:0000255|HAMAP- CC Rule:MF_00259}. CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP- CC Rule:MF_00259}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41002.1; -; Genomic_DNA. DR PIR; A81183; A81183. DR RefSeq; NP_273618.1; NC_003112.2. DR RefSeq; WP_002222873.1; NC_003112.2. DR ProteinModelPortal; Q9K0L8; -. DR SMR; Q9K0L8; 7-364. DR STRING; 122586.NMB0574; -. DR PaxDb; Q9K0L8; -. DR EnsemblBacteria; AAF41002; AAF41002; NMB0574. DR GeneID; 902689; -. DR KEGG; nme:NMB0574; -. DR PATRIC; 20356429; VBINeiMen85645_0734. DR eggNOG; ENOG4105D43; Bacteria. DR eggNOG; COG0404; LUCA. DR HOGENOM; HOG000239381; -. DR KO; K00605; -. DR OMA; LGWLVHL; -. DR OrthoDB; EOG6T1WS5; -. DR BioCyc; NMEN122586:GHGG-600-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.30.110; -; 1. DR Gene3D; 3.30.1360.120; -; 2. DR HAMAP; MF_00259; GcvT; 1. DR InterPro; IPR006223; GCS_T. DR InterPro; IPR022903; GCS_T_bac. DR InterPro; IPR028896; GCST/DmdA. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR029043; GcvT/YgfZ_C. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR PANTHER; PTHR13847:SF5; PTHR13847:SF5; 1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR SUPFAM; SSF101790; SSF101790; 1. DR TIGRFAMs; TIGR00528; gcvT; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 366 Aminomethyltransferase. FT /FTId=PRO_0000122576. SQ SEQUENCE 366 AA; 39740 MW; 566A7BCD21691D91 CRC64; MTALKTTPFH QAHQDAGAKL VDFAGWELPI HYGSQIAEHE AVRTDAGMFD VSHMLVTDVA GANAKAFFRK LIANDVAKLA FVGKALYSAL LNDNGGVIDD LIVYRTNEAE TQYRIVSNGA TREKDTAQFH KVGQEFGVAF NPRYDLGMLA VQGPKAIEKL LTVKPEWADV VHNLKPFQGA DLGNDWFVAR TGYTGEDGVE VILPGTEAVA FFKALQQAGV QPCGLGARDT LRMEAGMNLY GNDMDDDTSP LEAGMGWTVD LKDESRDFVG KAALLALKEK GVAVKQVGLL LEKGGILRAH MEVLTDKGQG ETTSGVFSPS LKQSIAIARV PKDFDGDTAK VLMRGKEVDV RVLKLPFVRN GQKQFD // ID GLMS_NEIMB Reviewed; 612 AA. AC Q9K1P9; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 91. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164}; DE EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; GN OrderedLocusNames=NMB0031; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, CC converting fructose-6P into glucosamine-6P using glutamine as a CC nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40502.1; -; Genomic_DNA. DR PIR; B81246; B81246. DR RefSeq; NP_273097.1; NC_003112.2. DR RefSeq; WP_002225764.1; NC_003112.2. DR ProteinModelPortal; Q9K1P9; -. DR STRING; 122586.NMB0031; -. DR MEROPS; C44.971; -. DR PaxDb; Q9K1P9; -. DR EnsemblBacteria; AAF40502; AAF40502; NMB0031. DR GeneID; 902134; -. DR KEGG; nme:NMB0031; -. DR PATRIC; 20355011; VBINeiMen85645_0042. DR eggNOG; ENOG4105C46; Bacteria. DR eggNOG; COG0449; LUCA. DR HOGENOM; HOG000258896; -. DR KO; K00820; -. DR OMA; GEFFCAS; -. DR OrthoDB; EOG6KT2Q1; -. DR BioCyc; NMEN122586:GHGG-32-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00164; GlmS; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS. DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01135; glmS; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS51464; SIS; 2. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Reference proteome; Repeat; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000255|HAMAP- FT Rule:MF_00164}. FT CHAIN 2 612 Glutamine--fructose-6-phosphate FT aminotransferase [isomerizing]. FT /FTId=PRO_0000135361. FT DOMAIN 2 220 Glutamine amidotransferase type-2. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 288 428 SIS 1. {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 461 602 SIS 2. {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 2 2 Nucleophile; for GATase activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 607 607 For Fru-6P isomerization activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. SQ SEQUENCE 612 AA; 66619 MW; 0FE3788D70A19CF4 CRC64; MCGIVGAIRA HHNVVDFLTD GLKRLEYRGY DSSGIAVNTD GKIKRVRRVG RVQLMEDAAR EKGISGGIGI GHTRWATHGG VTEPNAHPHI SGGMIAVVHN GIIENFESER KRLEGLGYRF ESQTDTEVIA HSINHEYAQN GGRLFEAVQE AVKRFHGAYA IAVIAQDKPD ELVVARMGCP LLVALGDDET FIASDVSAVI AFTRRVAYLE DGDIALLASD GIKRLTDKNG LPAERKVKVS ELSLASLELG LYSHFMQKEI HEQPRAIADT AEVFLDGGFI PENFGKDAKS VFESIRSVKI LACGTSYYAA LTAKYWLESI AKIPSDVEIA SEYRYRSVIA DSDQLVITIS QSGETLDTME ALKYAKSLGH RHSLSICNVM ESALPRESSL VLYTRAGAEI GVASTKAFTT QLVALFGLAV TLAKVRGLVS EEDEARYTEE LRQLPGSVQH ALNLEPQIAA WAQQFAKKTS ALFLGRGIHY PIALEGALKL KEITYIHAEA YPAGELKHGP LALVDENMPV VVIAPNDSLL DKVKANMQEV GARGGELFVF ADLDSNFNAT EGVHVIRAPR HVGKLSPVVH TIPVQLLAYH TALARGTDVD KPRNLAKSVT VE // ID GLO2_NEIMB Reviewed; 252 AA. AC Q9JXK4; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000255|HAMAP-Rule:MF_01374}; DE EC=3.1.2.6 {ECO:0000255|HAMAP-Rule:MF_01374}; DE AltName: Full=Glyoxalase II {ECO:0000255|HAMAP-Rule:MF_01374}; DE Short=Glx II {ECO:0000255|HAMAP-Rule:MF_01374}; GN Name=gloB {ECO:0000255|HAMAP-Rule:MF_01374}; GN OrderedLocusNames=NMB1997; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D- CC lactoyl-glutathione to form glutathione and D-lactic acid. CC {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O = CC glutathione + a 2-hydroxy carboxylate. {ECO:0000255|HAMAP- CC Rule:MF_01374}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01374}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01374}; CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal CC degradation; (R)-lactate from methylglyoxal: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II family. {ECO:0000255|HAMAP-Rule:MF_01374}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42324.1; -; Genomic_DNA. DR PIR; H81017; H81017. DR RefSeq; NP_274989.1; NC_003112.2. DR RefSeq; WP_002219913.1; NC_003112.2. DR ProteinModelPortal; Q9JXK4; -. DR STRING; 122586.NMB1997; -. DR PaxDb; Q9JXK4; -. DR EnsemblBacteria; AAF42324; AAF42324; NMB1997. DR GeneID; 904130; -. DR KEGG; nme:NMB1997; -. DR PATRIC; 20360093; VBINeiMen85645_2551. DR eggNOG; ENOG4108RW0; Bacteria. DR eggNOG; COG0491; LUCA. DR HOGENOM; HOG000058041; -. DR KO; K01069; -. DR OMA; NYIWLLQ; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-2054-MONOMER; -. DR UniPathway; UPA00619; UER00676. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01374; Glyoxalase_2; 1. DR InterPro; IPR032282; HAGH_C. DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF16123; HAGH_C; 1. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR03413; GSH_gloB; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 252 Hydroxyacylglutathione hydrolase. FT /FTId=PRO_0000309664. FT METAL 52 52 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 54 54 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 56 56 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 57 57 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 107 107 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 128 128 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 128 128 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 166 166 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. SQ SEQUENCE 252 AA; 28155 MW; 89D5AFADC9018F87 CRC64; MKITPVKALT DNYIWMIQHG NHAVCVDPSE PSPVLEFLVR NRLMLAQTWV THPHPDHEGG AAALWRGYME SPVYGESDIE AATHTVTAGT QFTFGDGQVT VWATPGHTDR HTSYLLETSD GIHVFCGDTL FSAGCGRVFT GTIEQLYDSF QRFNRLPENT LFYPAHEYTA ANLRFAAHIE PDNADIQTAL KAAAHTPTLP VTLAHERRVN PFLRVDLPHV RDRAEALSGK TLNSSLDTFV ALRELKNQYR TK // ID GMHA_NEIMB Reviewed; 197 AA. AC P0A0Y6; Q9JQM1; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; DE EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067}; DE AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; GN Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067}; Synonyms=lpcA; GN OrderedLocusNames=NMB2090; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. RX PubMed=12101286; RA Valvano M.A., Messner P., Kosma P.; RT "Novel pathways for biosynthesis of nucleotide-activated glycero- RT manno-heptose precursors of bacterial glycoproteins and cell surface RT polysaccharides."; RL Microbiology 148:1979-1989(2002). CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate CC in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- CATALYTIC ACTIVITY: D-sedoheptulose 7-phosphate = D-glycero-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00067}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00067}; CC -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7- CC phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7- CC phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from CC sedoheptulose 7-phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- MISCELLANEOUS: The reaction produces a racemic mixture of D- CC glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42407.1; -; Genomic_DNA. DR PIR; H81007; H81007. DR RefSeq; NP_275078.1; NC_003112.2. DR RefSeq; WP_002219976.1; NC_003112.2. DR ProteinModelPortal; P0A0Y6; -. DR SMR; P0A0Y6; 4-195. DR STRING; 122586.NMB2090; -. DR PaxDb; P0A0Y6; -. DR EnsemblBacteria; AAF42407; AAF42407; NMB2090. DR GeneID; 903960; -. DR KEGG; nme:NMB2090; -. DR PATRIC; 20360350; VBINeiMen85645_2672. DR eggNOG; ENOG4105F55; Bacteria. DR eggNOG; COG0279; LUCA. DR HOGENOM; HOG000237572; -. DR KO; K03271; -. DR OMA; QHFRDSA; -. DR OrthoDB; EOG6384PC; -. DR BioCyc; NMEN122586:GHGG-2155-MONOMER; -. DR BRENDA; 5.3.1.28; 3593. DR UniPathway; UPA00041; UER00436. DR UniPathway; UPA00976; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00067; GmhA; 1. DR InterPro; IPR004515; Phosphoheptose_Isoase. DR InterPro; IPR001347; SIS. DR Pfam; PF13580; SIS_2; 1. DR TIGRFAMs; TIGR00441; gmhA; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 197 Phosphoheptose isomerase. FT /FTId=PRO_0000136539. FT DOMAIN 37 197 SIS. {ECO:0000255|HAMAP-Rule:MF_00067}. FT REGION 52 54 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 94 95 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 120 122 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT METAL 61 61 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 65 65 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 175 175 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 183 183 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 125 125 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 175 175 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. SQ SEQUENCE 197 AA; 20989 MW; FAE0DA549A085280 CRC64; MTTLQERVAA HFAESIRAKQ EAGKVLVEPT VQAAELMLQC LMNDGKILAC GNGGSAADAQ HFAAEMTGRF EKERMELAAV ALTTDTSALT AIGNDYGFDH VFSKQVRALG RAGDVLVGIS TSGNSANVIE AVKAAHERDM HVIALTGRDG GKIAAILKDT DVLLNVPHPR TARIQENHIL LIHAMCDCID SVLLEGM // ID GLNE_NEIMB Reviewed; 896 AA. AC Q9K1D5; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802}; DE EC=2.7.7.42 {ECO:0000255|HAMAP-Rule:MF_00802}; DE AltName: Full=Glutamine-synthetase adenylyltransferase; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_00802}; DE AltName: Full=[Glutamate--ammonia-ligase] adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802}; GN Name=glnE {ECO:0000255|HAMAP-Rule:MF_00802}; GN OrderedLocusNames=NMB0224; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Adenylation and deadenylation of glutamate--ammonia CC ligase. {ECO:0000255|HAMAP-Rule:MF_00802}. CC -!- CATALYTIC ACTIVITY: ATP + [L-glutamate:ammonia ligase (ADP- CC forming)]-L-tyrosine = diphosphate + [L-glutamate:ammonia ligase CC (ADP-forming)]-O(4)-(5'-adenylyl)-L-tyrosine. {ECO:0000255|HAMAP- CC Rule:MF_00802}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00802}; CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000255|HAMAP- CC Rule:MF_00802}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40680.1; -; Genomic_DNA. DR PIR; B81223; B81223. DR RefSeq; NP_273281.1; NC_003112.2. DR RefSeq; WP_002224816.1; NC_003112.2. DR ProteinModelPortal; Q9K1D5; -. DR STRING; 122586.NMB0224; -. DR PaxDb; Q9K1D5; -. DR EnsemblBacteria; AAF40680; AAF40680; NMB0224. DR GeneID; 902336; -. DR KEGG; nme:NMB0224; -. DR PATRIC; 20355522; VBINeiMen85645_0285. DR eggNOG; ENOG4105CE6; Bacteria. DR eggNOG; COG1391; LUCA. DR HOGENOM; HOG000256491; -. DR KO; K00982; -. DR OMA; EFMVQYA; -. DR OrthoDB; EOG651SRZ; -. DR BioCyc; NMEN122586:GHGG-239-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00802; GlnE; 1. DR InterPro; IPR023057; GlnE. DR InterPro; IPR005190; GlnE_rpt_dom. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR Pfam; PF08335; GlnD_UR_UTase; 2. DR Pfam; PF03710; GlnE; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1 896 Glutamate-ammonia-ligase FT adenylyltransferase. FT /FTId=PRO_0000209259. FT REGION 66 273 GlnE 1. FT REGION 575 779 GlnE 2. SQ SEQUENCE 896 AA; 101762 MW; 41490023A8A36662 CRC64; MSDNRLDTAR RHSLFLARQL DNGKLKPEIF LPMLDKVLTE ADFQAFADWG EIRAEENEEE LARQLRELRR YVVSQIIVRD INRISDLNEV TRTITLFADF AVNTALDFAY AYYRDMYGTP IGRYTKSPQH LSVVAMGKAG GYELNVSSDI DLIFVYPESG DTDGRRERGN QEFFTKVGQK LIALLNDITA DGQVFRVDMR LRPDGDSGAL VLSETALEQY LITQGREWER YAWCKGRVVT PYPNDIKALV RPFVFRKYLD YGAYEAMRKL HRQISSEVSK KGMADNIKLG AGGIREVEFI AQIFQMIRGG QMRALQLKGT QETLKKLAEL GIMLSEHVET LLAAYRFLRD VEHRLQYWDD QQTQTLPTSP EQRQLLAESM GFDSYSAFSD GLNVHRNKVN QLFNEILSEP EEQTQDNSEW QWAWQDKPDE EGRRCRLKAH GFDAETVAAR LDQIRHGHKY RHLSAHAQPR FDAVVPLFVQ AAAAQSNPTD TLMRLLDFLE NISRRSAYLA FLNEHPQTLA QLAQIMGQSS WVAAYLNKYP ILLDELISAQ LLDTAFDWQA LAAALSDDLK ACGGDTEAQM DTLRRFQHAQ VFRLAVQDLA GLWTVESLSD QLSALADTIL AAALLCAWAD MPKKHRDTPQ FAVVGYGKLG GKELGYASDL DLVYLYDDPH PDAGDVYSRL ARRLTNWLSA ATGAGSLYET DLRLRPNGDA GFLAHSIAAF EKYQRENAWT WEHQSLTRAR FICGTSEIQT AFDRIRTEIL TAERDQTALA GEIIEMREKM FPTHPPADSN VKYARGGVVD VEFIVQYLIL AHARQYPQLL DNYGNIALLN ISADCGLIDK TLAGQSRTAY RFYRRQQHNT KLRDAAKTEV TGELLAHYGN VRKLWREVFG EEAATV // ID GLXK_NEIMB Reviewed; 371 AA. AC P57099; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Glycerate kinase; DE EC=2.7.1.31; GN Name=glxK; OrderedLocusNames=NMB1268; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + D-glycerate = ADP + 3-phospho-D- CC glycerate. CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41645.1; -; Genomic_DNA. DR PIR; F81102; F81102. DR RefSeq; NP_274289.1; NC_003112.2. DR RefSeq; WP_002222399.1; NC_003112.2. DR ProteinModelPortal; P57099; -. DR SMR; P57099; 1-371. DR STRING; 122586.NMB1268; -. DR PaxDb; P57099; -. DR EnsemblBacteria; AAF41645; AAF41645; NMB1268. DR GeneID; 903690; -. DR KEGG; nme:NMB1268; -. DR PATRIC; 20358151; VBINeiMen85645_1587. DR eggNOG; ENOG4105BZW; Bacteria. DR eggNOG; COG1929; LUCA. DR HOGENOM; HOG000089298; -. DR KO; K00865; -. DR OMA; YGKTPMG; -. DR OrthoDB; EOG628F79; -. DR BioCyc; NMEN122586:GHGG-1306-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008887; F:glycerate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0031388; P:organic acid phosphorylation; IEA:InterPro. DR Gene3D; 3.90.1510.10; -; 1. DR InterPro; IPR018193; Glyc_kinase_flavodox-like-dom. DR InterPro; IPR004381; Glycerate_kinase. DR PANTHER; PTHR21599; PTHR21599; 1. DR Pfam; PF02595; Gly_kinase; 1. DR PIRSF; PIRSF006078; GlxK; 1. DR SUPFAM; SSF110738; SSF110738; 1. DR TIGRFAMs; TIGR00045; TIGR00045; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 371 Glycerate kinase. FT /FTId=PRO_0000071538. SQ SEQUENCE 371 AA; 39537 MW; 779AD64ADA322DDF CRC64; MKIVIAPDSF KESLTAQQVA EAIKRGFQQS IADVECLLCP VGDGGEGTVD AIRHSLDLEE KCLQVTGPFG QKEVMRYFQK EQLALFEVAD LVGLGKIPLE KRNPLQIQTR GIGELIRHLI SQEIKEIYIG VGGTASNDGG IGIAAGLGYQ FYDEDGNALP VCGQSLLNLA SVSTENRYEI PEDVHIRILA DVVSPLCGHQ GATYTFGKQK GLDSTMFEAV DQAIQDFYEK VSPATLKLKG AGAGGGIAGG LCAFAQASIV SGIDTCLDLI DFDKKVSDVD LVIVGEGRLD RQSLAGKAPI GVAKRTPVGV PVVAICGSLV EDLPSLPFEN IQAAFSILEK SEPLEDSLKN ASLYLEHTAS NIGHLLNMPK I // ID GLK_NEIMB Reviewed; 328 AA. AC P64254; Q9JQX3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Glucokinase {ECO:0000255|HAMAP-Rule:MF_00524}; DE EC=2.7.1.2 {ECO:0000255|HAMAP-Rule:MF_00524}; DE AltName: Full=Glucose kinase {ECO:0000255|HAMAP-Rule:MF_00524}; GN Name=glk {ECO:0000255|HAMAP-Rule:MF_00524}; OrderedLocusNames=NMB1390; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + D-glucose = ADP + D-glucose 6-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00524}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00524}. CC -!- SIMILARITY: Belongs to the bacterial glucokinase family. CC {ECO:0000255|HAMAP-Rule:MF_00524}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41754.1; -; Genomic_DNA. DR PIR; E81089; E81089. DR RefSeq; NP_274404.1; NC_003112.2. DR RefSeq; WP_002216974.1; NC_003112.2. DR ProteinModelPortal; P64254; -. DR STRING; 122586.NMB1390; -. DR PaxDb; P64254; -. DR EnsemblBacteria; AAF41754; AAF41754; NMB1390. DR GeneID; 903812; -. DR KEGG; nme:NMB1390; -. DR PATRIC; 20358463; VBINeiMen85645_1743. DR eggNOG; ENOG4105CHC; Bacteria. DR eggNOG; COG0837; LUCA. DR HOGENOM; HOG000274469; -. DR KO; K00845; -. DR OMA; GHADFAP; -. DR OrthoDB; EOG64BQ47; -. DR BioCyc; NMEN122586:GHGG-1428-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00524; Glucokinase; 1. DR InterPro; IPR003836; Glucokinase. DR Pfam; PF02685; Glucokinase; 1. DR TIGRFAMs; TIGR00749; glk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 328 Glucokinase. FT /FTId=PRO_0000215131. FT NP_BIND 16 21 ATP. {ECO:0000255|HAMAP-Rule:MF_00524}. SQ SEQUENCE 328 AA; 34951 MW; A7B4AA6BD6C92F0C CRC64; MSSTPNKQAG YPRLVADIGG TNARFALETA PRVIEKAAVL PCKDYDTVTD AVRAYLNQSG ATAVRHAAFA IANPILGDWV QMTNHHWAFS IETTRQTLGL DTLILLNDFT AQALAVTQTS SKDLMQVGGQ KPVEFAPKAV IGPGTGLGVS GLVHSHAGWV ALAGEGGHTS FPPFDDMEVL IWQYAKNKYG HVSAERFLSG AGLSLVYEAL AAKQKAKPAK LMPSEITEKA LSGASPLCRQ TLDIFCAMLG TVASNLALTL GARGGVYLCG GIIPRVLEYF KTSPFRSRFE NKGRFEAYLA AIPVYVVLSE FPGISGAAAA LDNHLRNV // ID GLMU_NEIMB Reviewed; 456 AA. AC Q9K1P3; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631}; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631}; GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; GN OrderedLocusNames=NMB0038; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de CC novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- CC GlcNAc). The C-terminal domain catalyzes the transfer of acetyl CC group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) CC to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is CC converted into UDP-GlcNAc by the transfer of uridine 5- CC monophosphate (from uridine 5-triphosphate), a reaction catalyzed CC by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01631}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40509.1; -; Genomic_DNA. DR PIR; H81244; H81244. DR RefSeq; NP_273104.1; NC_003112.2. DR RefSeq; WP_002225769.1; NC_003112.2. DR ProteinModelPortal; Q9K1P3; -. DR SMR; Q9K1P3; 5-450. DR STRING; 122586.NMB0038; -. DR PaxDb; Q9K1P3; -. DR EnsemblBacteria; AAF40509; AAF40509; NMB0038. DR GeneID; 902141; -. DR KEGG; nme:NMB0038; -. DR PATRIC; 20355033; VBINeiMen85645_0053. DR eggNOG; ENOG4105CAJ; Bacteria. DR eggNOG; COG1207; LUCA. DR HOGENOM; HOG000283476; -. DR KO; K04042; -. DR OMA; SITANYD; -. DR OrthoDB; EOG6Z6FQZ; -. DR BioCyc; NMEN122586:GHGG-39-MONOMER; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01173; glmU; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. FT CHAIN 1 456 Bifunctional protein GlmU. FT /FTId=PRO_0000233805. FT REGION 1 228 Pyrophosphorylase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 11 14 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 80 81 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 102 104 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 229 249 Linker. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 250 456 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 385 386 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 362 362 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 104 104 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 226 226 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 25 25 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 75 75 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 138 138 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 153 153 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 168 168 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 226 226 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 332 332 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 350 350 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 365 365 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 376 376 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 379 379 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 404 404 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 422 422 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 439 439 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. SQ SEQUENCE 456 AA; 49013 MW; 718E769288882828 CRC64; MPQNTLNIVI LAAGKGTRMY SKMPKVLHRI GGKPMVGRVI DTAAALNPQN ICVVIGHGKE QVLDTVKRDV VWVEQTEQLG TGHAVKTALP HLSAEGRTLV LYGDVPLIDV ETLETLLEAA GNEVGLLTDV PNDPTGLGRI IRDSNGSVTA IVEEKDADAV QKAVKEINTG ILVLPNAKLE NWLNSLSSNN AQGEYYLTDL IAKAVADGIK VHPVQVRASH LAAGVNNKLQ LTELERIFQT EQAQELLKAG VTLRDPARFD LRGRLKHGQD VVIDVNCIFE GDIELGDNVE IGANCVIKNA KIGANSKIAP FSHLESCEVG ENNRIGPYAR LRPQARLADD VHVGNFVEIK NAAIGKGTKA NHLTYIGDAE VGCKTNFGAG TIIANYDGVH KHKTVIGDEV RIGSNCVLVA PVTLGNKVTT GAGSTITRNV EDNKLALARA RQTVIEGWVR PEKDKQ // ID GLND_NEIMB Reviewed; 852 AA. AC Q9JZB4; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277}; DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277}; DE Includes: DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277}; DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277}; DE Includes: DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277}; GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; GN OrderedLocusNames=NMB1203; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII CC regulatory proteins (GlnB and homologs), in response to the CC nitrogen status of the cell that GlnD senses through the glutamine CC level. Under low glutamine levels, catalyzes the conversion of the CC PII proteins and UTP to PII-UMP and PPi, while under higher CC glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP CC (deuridylylation). Thus, controls uridylylation state and activity CC of the PII proteins, and plays an important role in the regulation CC of nitrogen assimilation and metabolism. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl- CC [protein-PII]. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- CATALYTIC ACTIVITY: Uridylyl-[protein-PII] + H(2)O = UMP + CC [protein-PII]. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277}; CC -!- ENZYME REGULATION: Uridylyltransferase (UTase) activity is CC inhibited by glutamine, while glutamine activates uridylyl- CC removing (UR) activity. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- DOMAIN: Has four distinct domains: an N-terminal CC nucleotidyltransferase (NT) domain responsible for UTase activity, CC a central HD domain that encodes UR activity, and two C-terminal CC ACT domains that seem to have a role in glutamine sensing. CC {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- SIMILARITY: Contains 2 ACT domains. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41585.1; -; Genomic_DNA. DR PIR; B81110; B81110. DR RefSeq; NP_274228.1; NC_003112.2. DR RefSeq; WP_002225207.1; NC_003112.2. DR ProteinModelPortal; Q9JZB4; -. DR STRING; 122586.NMB1203; -. DR PaxDb; Q9JZB4; -. DR EnsemblBacteria; AAF41585; AAF41585; NMB1203. DR GeneID; 903625; -. DR KEGG; nme:NMB1203; -. DR PATRIC; 20357995; VBINeiMen85645_1510. DR eggNOG; ENOG4105E1P; Bacteria. DR eggNOG; COG2844; LUCA. DR HOGENOM; HOG000261778; -. DR KO; K00990; -. DR OMA; HTLFWIA; -. DR OrthoDB; EOG6CCH44; -. DR BioCyc; NMEN122586:GHGG-1240-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR HAMAP; MF_00277; PII_uridylyl_transf; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR InterPro; IPR010043; UTase/UR. DR Pfam; PF08335; GlnD_UR_UTase; 1. DR Pfam; PF01966; HD; 1. DR PIRSF; PIRSF006288; PII_uridyltransf; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR01693; UTase_glnD; 1. DR PROSITE; PS51671; ACT; 2. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Multifunctional enzyme; KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1 852 Bifunctional FT uridylyltransferase/uridylyl-removing FT enzyme. FT /FTId=PRO_0000192748. FT DOMAIN 437 539 HD. {ECO:0000255|HAMAP-Rule:MF_00277}. FT DOMAIN 673 757 ACT 1. {ECO:0000255|HAMAP-Rule:MF_00277}. FT DOMAIN 785 852 ACT 2. {ECO:0000255|HAMAP-Rule:MF_00277}. FT REGION 1 318 Uridylyltransferase. FT REGION 319 672 Uridylyl-removing. SQ SEQUENCE 852 AA; 97008 MW; 1F377E3C95355F1B CRC64; MPANLSSALE TFKQQRDAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE YFQNSALCLM AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT LWDCKLMPSV KSGSVDELCE SVRNDITGDT AFLEARFLFG NRQTVDKLAE KMNAQRNVAA FVEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL LWIAKAQGLA TDLPDLLKQR ILTRAEAGML SHGYRRLAHI RIHLHLNAKR AEDRLLFDLQ PQVAESMGYE GLNLRRQSEE LMRVFYRAIK TVKQLGGILT PMLQSRVSST PLRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNPENRRRFA GFFRNGNGLT QTLRFLNLYG VLGRYLPAWE KIIGLLQHDL FHIYPVDDHI LTVVRNVRRL ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAIQGIADA RQFAADHFLT GEESDLLAWL VENHLLMSAV AQKEDIQDPS VLDAFCKRVQ THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLTGNGGNP HTLFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA NLVHDFETPI VRSRILPKSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA ETQSRSRRIS RRSRYMPIAP SITITPEEDY PDWYSVEITA VNRPFLLADM AEVFFAHNVS LRYAKISTLD ERAEDSFTVF SPDLKNPKIQ SSLKQTLLEQ LS // ID GLUQ_NEIMB Reviewed; 295 AA. AC Q9K141; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000255|HAMAP-Rule:MF_01428}; DE Short=Glu-Q-RSs {ECO:0000255|HAMAP-Rule:MF_01428}; DE EC=6.1.1.- {ECO:0000255|HAMAP-Rule:MF_01428}; GN Name=gluQ {ECO:0000255|HAMAP-Rule:MF_01428}; GN OrderedLocusNames=NMB0349; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate CC in presence of ATP and the subsequent transfer of glutamate onto a CC tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- CC dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the CC wobble position of the QUC anticodon. {ECO:0000255|HAMAP- CC Rule:MF_01428}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01428}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01428}; CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. GluQ subfamily. {ECO:0000255|HAMAP-Rule:MF_01428}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40792.1; -; Genomic_DNA. DR PIR; C81210; C81210. DR RefSeq; NP_273398.1; NC_003112.2. DR RefSeq; WP_002221978.1; NC_003112.2. DR ProteinModelPortal; Q9K141; -. DR STRING; 122586.NMB0349; -. DR PaxDb; Q9K141; -. DR EnsemblBacteria; AAF40792; AAF40792; NMB0349. DR GeneID; 902464; -. DR KEGG; nme:NMB0349; -. DR PATRIC; 20355845; VBINeiMen85645_0441. DR eggNOG; ENOG4106F3G; Bacteria. DR eggNOG; COG0008; LUCA. DR HOGENOM; HOG000252723; -. DR KO; K01894; -. DR OMA; WQGVTDI; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NMEN122586:GHGG-370-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_01428; Glu_Q_tRNA_synth; 1. DR InterPro; IPR022380; Glu-Q_TRNA(Asp)_Synthase. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR TIGRFAMs; TIGR03838; queuosine_YadB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1 295 Glutamyl-Q tRNA(Asp) synthetase. FT /FTId=PRO_0000208308. FT REGION 5 9 Glutamate binding. {ECO:0000255|HAMAP- FT Rule:MF_01428}. FT MOTIF 8 18 "HIGH" region. FT MOTIF 234 238 "KMSKS" region. FT METAL 97 97 Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}. FT METAL 99 99 Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}. FT METAL 117 117 Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}. FT METAL 121 121 Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}. FT BINDING 41 41 Glutamate. {ECO:0000255|HAMAP- FT Rule:MF_01428}. FT BINDING 178 178 Glutamate. {ECO:0000255|HAMAP- FT Rule:MF_01428}. FT BINDING 196 196 Glutamate. {ECO:0000255|HAMAP- FT Rule:MF_01428}. FT BINDING 237 237 ATP. {ECO:0000255|HAMAP-Rule:MF_01428}. SQ SEQUENCE 295 AA; 33121 MW; 8923A84FD0237F63 CRC64; MYTGRFAPSP TGLLHIGSLL TAVASYADAR AHGGKWLIRM EDLDPPREMP GAASHILHTL EAFGFEWDGE VAYQSRRYAL YEETLCRLKT AGLVYPCHCS RKDWQAGARR GADGFVYNGR CRHPGQRPAL QGKQPAWRIR VPDRIIGFSD GIVGGYAQNL ARDIGDFVLL RADGYWAYQL AVVADDAEQG VTHIVRGQDL LVSTPRQIYL QQCLDVPTPQ YAHLPLLTNA QGQKWSKQTL APALDLNRRE QLLRQVFRYL KLPEAPETDR PAELLDWAVA HWDMDKVPKH AVTAP // ID GLYA_NEIMB Reviewed; 416 AA. AC P56990; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051}; DE EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; GN OrderedLocusNames=NMB1055; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with tetrahydrofolate (THF) serving as the one-carbon CC carrier. This reaction serves as the major source of one-carbon CC groups required for the biosynthesis of purines, thymidylate, CC methionine, and other important biomolecules. Also exhibits THF- CC independent aldolase activity toward beta-hydroxyamino acids, CC producing glycine and aldehydes, via a retro-aldol mechanism. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP- CC Rule:MF_00051}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP- CC Rule:MF_00051}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41452.1; -; Genomic_DNA. DR PIR; B81126; B81126. DR RefSeq; NP_274089.1; NC_003112.2. DR RefSeq; WP_002225269.1; NC_003112.2. DR ProteinModelPortal; P56990; -. DR SMR; P56990; 1-415. DR STRING; 122586.NMB1055; -. DR PaxDb; P56990; -. DR EnsemblBacteria; AAF41452; AAF41452; NMB1055. DR GeneID; 903374; -. DR KEGG; nme:NMB1055; -. DR PATRIC; 20357651; VBINeiMen85645_1342. DR eggNOG; ENOG4105C65; Bacteria. DR eggNOG; COG0112; LUCA. DR HOGENOM; HOG000239404; -. DR KO; K00600; -. DR OMA; VSFTTHK; -. DR OrthoDB; EOG6Z0QB2; -. DR BioCyc; NMEN122586:GHGG-1092-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR PANTHER; PTHR11680; PTHR11680; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00096; SHMT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW One-carbon metabolism; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 416 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113623. FT REGION 125 127 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 35 35 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 57 57 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 64 64 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 65 65 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 99 99 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 121 121 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 175 175 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 203 203 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 228 228 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 235 235 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 261 261 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 361 361 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 229 229 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00051}. SQ SEQUENCE 416 AA; 44916 MW; 393E4BBF7825921C CRC64; MFSKSVTLAQ YDPDLAAAIA QEDQRQQDHV ELIASENYVS CAVMDAQGSQ LTNKYAEGYP GKRYYGGCEY VDIVEQLAID RVKELFGAAY ANVQPHSGSQ ANQAVYASVL KPGDTILGMS LAHGGHLTHG ASVNISGKLY NAVTYGLDEN EVLDYAEVER LALEHKPKMI VAGASAYALQ IDWAKFREIA DKVGAYLFVD MAHYAGLVAG GEYPNPVPFC DFVTTTTHKT LRGPRGGVIL CRDNTHEKAL NSSIFPSLQG GPLMHVIAAK AVAFKEALQP EFKQYAKQVK INAAAMAEEL VKRGLRIVSG RTESHVFLVD LQPMKITGKA AEAALGKAHI TVNKNAIPND PEKPFVTSGI RIGSAAMTTR GFNEADARVL ANLVADVLSN PEDEANLAKV RKQVTALCNK YPVYGA // ID GPDA_NEIMB Reviewed; 329 AA. AC Q9JXG6; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 103. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; GN OrderedLocusNames=NMB2060; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) = CC glycerone phosphate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62339.1; -; Genomic_DNA. DR RefSeq; NP_275050.1; NC_003112.2. DR RefSeq; WP_002215013.1; NC_003112.2. DR ProteinModelPortal; Q9JXG6; -. DR STRING; 122586.NMB2060; -. DR PaxDb; Q9JXG6; -. DR EnsemblBacteria; AAF62339; AAF62339; NMB2060. DR GeneID; 904020; -. DR KEGG; nme:NMB2060; -. DR PATRIC; 20360276; VBINeiMen85645_2638. DR eggNOG; ENOG4105CSF; Bacteria. DR eggNOG; COG0240; LUCA. DR HOGENOM; HOG000246853; -. DR KO; K00057; -. DR OMA; VVIMHAS; -. DR OrthoDB; EOG6JDWF4; -. DR BioCyc; NMEN122586:GHGG-2123-MONOMER; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC. DR GO; GO:0036439; F:glycerol-3-phosphate dehydrogenase [NADP+] activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW NAD; Oxidoreductase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome. FT CHAIN 1 329 Glycerol-3-phosphate dehydrogenase FT [NAD(P)+]. FT /FTId=PRO_0000137999. FT NP_BIND 7 12 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. FT REGION 253 254 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT ACT_SITE 189 189 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT BINDING 105 105 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 105 105 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT BINDING 138 138 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 253 253 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 279 279 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. SQ SEQUENCE 329 AA; 35338 MW; 5D6705ED43EAECD2 CRC64; MKITVIGAGS WGTALALHFS QHGNRVSLWT RNADQVRQMQ EARENKRGLP GFSFPETLEV CADLADALKD SGLVLIVTSV AGLRSSAELL KQYGAGHLPV LAACKGFEQD TGLLTFQVLK EVLPDNKKIG VLSGPSFAQE LAKQLPCAVV LASENQEWIE ELVPQLNTTV MRLYGSTDVI GVAVGGAVKN VMAIATGLSD GLEYGLNARA ALVTRGLAEI TRLASAMGAQ PKTMMGLAGI GDLILTCTGA LSRNRRVGLG LAEGKELHQV LVEIGHVSEG VSTIEEVFNT ACKYQIDMPI TQTLLQLIRK EMTPQQVVER LMERSARFE // ID GPMA_NEIMB Reviewed; 227 AA. AC Q9JYF7; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 97. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039}; DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039}; GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; GN OrderedLocusNames=NMB1604; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01039}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41956.1; -; Genomic_DNA. DR PIR; F81064; F81064. DR RefSeq; NP_274610.1; NC_003112.2. DR RefSeq; WP_002225017.1; NC_003112.2. DR ProteinModelPortal; Q9JYF7; -. DR SMR; Q9JYF7; 2-227. DR STRING; 122586.NMB1604; -. DR PaxDb; Q9JYF7; -. DR PRIDE; Q9JYF7; -. DR EnsemblBacteria; AAF41956; AAF41956; NMB1604. DR GeneID; 904297; -. DR KEGG; nme:NMB1604; -. DR PATRIC; 20359088; VBINeiMen85645_2056. DR eggNOG; ENOG4105DKJ; Bacteria. DR eggNOG; COG0588; LUCA. DR HOGENOM; HOG000221682; -. DR OMA; VKNQGKK; -. DR OrthoDB; EOG6C8N1H; -. DR BioCyc; NMEN122586:GHGG-1652-MONOMER; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1240; -; 1. DR HAMAP; MF_01039; PGAM_GpmA; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR005952; Phosphogly_mut1. DR PANTHER; PTHR11931; PTHR11931; 1. DR Pfam; PF00300; His_Phos_1; 2. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR TIGRFAMs; TIGR01258; pgm_1; 1. PE 3: Inferred from homology; KW Complete proteome; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 227 2,3-bisphosphoglycerate-dependent FT phosphoglycerate mutase. FT /FTId=PRO_0000179896. FT REGION 7 14 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 20 21 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 86 89 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 113 114 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 182 183 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT ACT_SITE 8 8 Tele-phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT ACT_SITE 86 86 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT BINDING 59 59 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT BINDING 97 97 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT SITE 181 181 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01039}. SQ SEQUENCE 227 AA; 25959 MW; BE59CA3654ACAAD3 CRC64; MELVFIRHGQ SEWNAKNLFT GWRDVKLSEQ GLAEAAAAGK KLKENGYEFD IAFTSVLTRA IKTCNIVLEE SDQLFVPQIK TWRLNERHYG QLQGLDKKQT AEQYGDEQVR IWRRSYDTLP PLLDKDDEFS AHKDRRYAHL PADVVPDGEN LKVTLERVLP FWEDQIAPAI LSGKRVLVAA HGNSLRALAK HIEGISDEDI MGLEIPTGQP LVYKLDDNLK VIEKFYL // ID GREA_NEIMB Reviewed; 158 AA. AC Q9JYU3; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Transcription elongation factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; DE AltName: Full=Transcript cleavage factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; GN Name=greA {ECO:0000255|HAMAP-Rule:MF_00105}; GN OrderedLocusNames=NMB1430; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription CC elongation past template-encoded arresting sites. The arresting CC sites in DNA have the property of trapping a certain fraction of CC elongating RNA polymerases that pass through, resulting in locked CC ternary complexes. Cleavage of the nascent transcript by cleavage CC factors such as GreA or GreB allows the resumption of elongation CC from the new 3'terminus. GreA releases sequences of 2 to 3 CC nucleotides. {ECO:0000255|HAMAP-Rule:MF_00105}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000255|HAMAP- CC Rule:MF_00105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41791.1; -; Genomic_DNA. DR PIR; G81084; G81084. DR RefSeq; NP_274442.1; NC_003112.2. DR RefSeq; WP_002225115.1; NC_003112.2. DR ProteinModelPortal; Q9JYU3; -. DR SMR; Q9JYU3; 2-137. DR STRING; 122586.NMB1430; -. DR PaxDb; Q9JYU3; -. DR EnsemblBacteria; AAF41791; AAF41791; NMB1430. DR GeneID; 903852; -. DR KEGG; nme:NMB1430; -. DR PATRIC; 20358573; VBINeiMen85645_1798. DR eggNOG; ENOG4108UKH; Bacteria. DR eggNOG; COG0782; LUCA. DR HOGENOM; HOG000241145; -. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; NMEN122586:GHGG-1468-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.180; -; 1. DR Gene3D; 3.10.50.30; -; 1. DR HAMAP; MF_00105; GreA_GreB; 1. DR InterPro; IPR018151; TF_GreA/GreB_CS. DR InterPro; IPR006359; Tscrpt_elong_fac_GreA. DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B. DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C. DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam. DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N. DR Pfam; PF01272; GreA_GreB; 1. DR Pfam; PF03449; GreA_GreB_N; 1. DR PIRSF; PIRSF006092; GreA_GreB; 1. DR SUPFAM; SSF46557; SSF46557; 1. DR TIGRFAMs; TIGR01462; greA; 1. DR PROSITE; PS00829; GREAB_1; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 158 Transcription elongation factor GreA. FT /FTId=PRO_0000176947. FT COILED 46 66 {ECO:0000255|HAMAP-Rule:MF_00105}. SQ SEQUENCE 158 AA; 17515 MW; 45F4017ACE39B459 CRC64; MQKIPLTVRG AELLKQELQQ LKSVARPEVI EAIAEARSHG DLSENAEYEA AKERQGFIEG RISELEHKLS VAHIINPTEI HAEGKIVFGT TVTLEDLETE EHVIYQIVGE DEADIKQGKI YVGSPIARAL IGKEEGDTAE VQAPGGVREY DIIEVRYI // ID GLRX_NEIMB Reviewed; 85 AA. AC Q9JY15; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Glutaredoxin; GN Name=grx; OrderedLocusNames=NMB1790; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in CC the presence of NADPH and glutathione reductase. Reduces low CC molecular weight disulfides and proteins (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42129.1; -; Genomic_DNA. DR PIR; E81041; E81041. DR RefSeq; NP_274789.1; NC_003112.2. DR RefSeq; WP_002221441.1; NC_003112.2. DR ProteinModelPortal; Q9JY15; -. DR STRING; 122586.NMB1790; -. DR PaxDb; Q9JY15; -. DR EnsemblBacteria; AAF42129; AAF42129; NMB1790. DR GeneID; 903309; -. DR KEGG; nme:NMB1790; -. DR PATRIC; 20359545; VBINeiMen85645_2278. DR eggNOG; ENOG4105VW4; Bacteria. DR eggNOG; COG0695; LUCA. DR HOGENOM; HOG000095203; -. DR KO; K03676; -. DR OMA; MARVVMY; -. DR OrthoDB; EOG6Z3KS6; -. DR BioCyc; NMEN122586:GHGG-1845-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014025; Glutaredoxin_subgr. DR InterPro; IPR011900; GRX_bact. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02181; GRX_bact; 1. DR PROSITE; PS00195; GLUTAREDOXIN_1; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; Electron transport; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1 85 Glutaredoxin. FT /FTId=PRO_0000141593. FT DOMAIN 1 85 Glutaredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT DISULFID 12 15 Redox-active. {ECO:0000250}. SQ SEQUENCE 85 AA; 9283 MW; C198FF550450C168 CRC64; MQTVTMYTGP FCPYCAMAKR LLHAAGVGHI DEIRVDASPE AFAEMQQLSG QRSVPQIFIG ETHVGGFTDL YRLQQEGGLD GLLNP // ID GREB_NEIMB Reviewed; 163 AA. AC Q9K0C5; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Transcription elongation factor GreB {ECO:0000255|HAMAP-Rule:MF_00930}; DE AltName: Full=Transcript cleavage factor GreB {ECO:0000255|HAMAP-Rule:MF_00930}; GN Name=greB {ECO:0000255|HAMAP-Rule:MF_00930}; GN OrderedLocusNames=NMB0689; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription CC elongation past template-encoded arresting sites. The arresting CC sites in DNA have the property of trapping a certain fraction of CC elongating RNA polymerases that pass through, resulting in locked CC ternary complexes. Cleavage of the nascent transcript by cleavage CC factors such as GreA or GreB allows the resumption of elongation CC from the new 3'terminus. GreB releases sequences of up to 9 CC nucleotides in length. {ECO:0000255|HAMAP-Rule:MF_00930}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. GreB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00930}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41107.1; -; Genomic_DNA. DR PIR; H81169; H81169. DR RefSeq; NP_273731.1; NC_003112.2. DR RefSeq; WP_002225493.1; NC_003112.2. DR ProteinModelPortal; Q9K0C5; -. DR STRING; 122586.NMB0689; -. DR PaxDb; Q9K0C5; -. DR EnsemblBacteria; AAF41107; AAF41107; NMB0689. DR GeneID; 902801; -. DR KEGG; nme:NMB0689; -. DR PATRIC; 20356705; VBINeiMen85645_0874. DR eggNOG; ENOG4108RRZ; Bacteria. DR eggNOG; COG0782; LUCA. DR HOGENOM; HOG000241145; -. DR KO; K04760; -. DR OMA; DQIFFGA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; NMEN122586:GHGG-717-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.180; -; 1. DR Gene3D; 3.10.50.30; -; 1. DR HAMAP; MF_00105; GreA_GreB; 1. DR HAMAP; MF_00930; GreB; 1. DR InterPro; IPR018151; TF_GreA/GreB_CS. DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B. DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C. DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam. DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N. DR InterPro; IPR006358; Tscrpt_elong_fac_GreB. DR Pfam; PF01272; GreA_GreB; 1. DR Pfam; PF03449; GreA_GreB_N; 1. DR PIRSF; PIRSF006092; GreA_GreB; 1. DR SUPFAM; SSF46557; SSF46557; 1. DR TIGRFAMs; TIGR01461; greB; 1. DR PROSITE; PS00829; GREAB_1; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 163 Transcription elongation factor GreB. FT /FTId=PRO_0000176948. FT COILED 54 76 {ECO:0000255|HAMAP-Rule:MF_00930}. SQ SEQUENCE 163 AA; 18666 MW; E10073949DCC2F65 CRC64; MSTETKNYIT PAGWQALKDE LYQLVNKERP EIVQIVNWAA GNGDRSENGD YLYGKRRMRE IDRRIRFLTK RLEAAVVVDP ELREATDQVF FGATVGLLRD DGREQTVKIV GIDEIDTAQN KISWISPLAR CLIKAREGDE VVLNTPEGRE EIEILSVEYI KID // ID GRPE_NEIMB Reviewed; 192 AA. AC Q7DDM9; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151}; DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151}; GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; GN OrderedLocusNames=NMB0561; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates actively in the response to hyperosmotic CC and heat shock by preventing the aggregation of stress-denatured CC proteins, in association with DnaK and GrpE. It is the nucleotide CC exchange factor for DnaK and may function as a thermosensor. CC Unfolded proteins bind initially to DnaJ; upon interaction with CC the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting CC in the formation of a stable complex. GrpE releases ADP from DnaK; CC ATP binding to DnaK triggers the release of the substrate protein, CC thus completing the reaction cycle. Several rounds of ATP- CC dependent interactions between DnaJ, DnaK and GrpE are required CC for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP- CC Rule:MF_01151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40989.1; -; Genomic_DNA. DR RefSeq; NP_273605.1; NC_003112.2. DR RefSeq; WP_002214370.1; NC_003112.2. DR ProteinModelPortal; Q7DDM9; -. DR STRING; 122586.NMB0561; -. DR PaxDb; Q7DDM9; -. DR EnsemblBacteria; AAF40989; AAF40989; NMB0561. DR GeneID; 902676; -. DR KEGG; nme:NMB0561; -. DR PATRIC; 20356399; VBINeiMen85645_0719. DR eggNOG; ENOG4105K90; Bacteria. DR eggNOG; COG0576; LUCA. DR HOGENOM; HOG000252084; -. DR KO; K03687; -. DR OMA; HERHDGA; -. DR OrthoDB; EOG6FJNJ9; -. DR BioCyc; NMEN122586:GHGG-587-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.30.22.10; -; 1. DR Gene3D; 3.90.20.20; -; 1. DR HAMAP; MF_01151; GrpE; 1. DR InterPro; IPR000740; GrpE. DR InterPro; IPR013805; GrpE_coiled_coil. DR InterPro; IPR009012; GrpE_head. DR PANTHER; PTHR21237; PTHR21237; 1. DR Pfam; PF01025; GrpE; 1. DR PRINTS; PR00773; GRPEPROTEIN. DR SUPFAM; SSF51064; SSF51064; 1. DR PROSITE; PS01071; GRPE; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Stress response. FT CHAIN 1 192 Protein GrpE. FT /FTId=PRO_0000113826. SQ SEQUENCE 192 AA; 21322 MW; 8BCC7428F9BC338C CRC64; MSEQTQQQNS EEAVENVEAV ETVETVGNAD GVQEQAAAEP AYEDLQARIA ELEAQLKDEQ LRALANEQNL RRRHQQEIAD THKFAGQKFA VEMLPVKDYL EMALLDQSGN FDALKMGVQM TLNELQKAFD ATQIKEINPK AGDKLDPNIH QAMQAVASEQ EPNTVVGVMK KGYTLSDRVL RPAMVTVAQK EA // ID GUAA_NEIMB Reviewed; 521 AA. AC Q9JXR2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=GMP synthase [glutamine-hydrolyzing]; DE EC=6.3.5.2; DE AltName: Full=GMP synthetase; DE AltName: Full=Glutamine amidotransferase; GN Name=guaA; OrderedLocusNames=NMB1920; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42250.1; -; Genomic_DNA. DR PIR; D81026; D81026. DR RefSeq; NP_274914.1; NC_003112.2. DR RefSeq; WP_002223072.1; NC_003112.2. DR ProteinModelPortal; Q9JXR2; -. DR SMR; Q9JXR2; 3-521. DR STRING; 122586.NMB1920; -. DR MEROPS; C26.957; -. DR PaxDb; Q9JXR2; -. DR EnsemblBacteria; AAF42250; AAF42250; NMB1920. DR GeneID; 904234; -. DR KEGG; nme:NMB1920; -. DR PATRIC; 20359887; VBINeiMen85645_2448. DR eggNOG; ENOG4105CM0; Bacteria. DR eggNOG; COG0518; LUCA. DR eggNOG; COG0519; LUCA. DR HOGENOM; HOG000223964; -. DR KO; K01951; -. DR OMA; MSHGDSV; -. DR OrthoDB; EOG6JHRJV; -. DR BioCyc; NMEN122586:GHGG-1977-MONOMER; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00344; GMP_synthase; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR022955; GMP_synthase. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 521 GMP synthase [glutamine-hydrolyzing]. FT /FTId=PRO_0000140152. FT DOMAIN 5 197 Glutamine amidotransferase type-1. FT DOMAIN 198 390 GMPS ATP-PPase. FT NP_BIND 225 231 ATP. {ECO:0000250}. FT ACT_SITE 81 81 Nucleophile. {ECO:0000250}. FT ACT_SITE 171 171 {ECO:0000250}. FT ACT_SITE 173 173 {ECO:0000250}. SQ SEQUENCE 521 AA; 57685 MW; FFC9DFB27FD1FA57 CRC64; MTQDKILILD FGSQVTQLIA RRVREAHVYC ELHSFDMPLD EIKAFNPKGI ILSGGPNSVY ESDYQADTGI FDLGIPVLGI CYGMQFMAHH LGGEVQPGNQ REFGYAQVKT IDSELTRGIQ DGEPNTLDVW MSHGDKVSKL PDGFAVIGNT PSCPIAMMEN AEKQFYGIQF HPEVTHTKQG RALLNRFVLD ICGAQPGWTM PNYIEEAVAK IREQVGSDEV ILGLSGGVDS SVAAALIHRA IGDQLTCVFV DHGLLRLNES KMVMDMFARN LGVKVIHVDA EGQFMAKLAG VTDPEKKRKI IGAEFIEVFD AEEKKLTNAK WLAQGTIYPD VIESAGAKTK KAHAIKSHHN VGGLPENMKL KLLEPLRDLF KDEVRELGVA LGLPREMVYR HPFPGPGLGV RILGEVKKEY ADLLRQADDI FIQELRNTTD ENGTSWYDLT SQAFAVFLPV KSVGVMGDGR TYDYVIALRA VITSDFMTAH WAELPYSLLG KVSNRIINEV KGINRVVYDV SGKPPATIEW E // ID GMHBB_NEIMB Reviewed; 187 AA. AC Q9JXI5; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase; DE EC=3.1.3.82; DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase; DE Short=HBP phosphatase; GN Name=gmhB; Synonyms=gmhX; OrderedLocusNames=NMB2033; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP ROLE IN HEPTOSE ASSEMBLY. RC STRAIN=NMB / Serogroup B; RX PubMed=11496013; RA Shih G.C., Kahler C.M., Carlson R.W., Rahman M.M., Stephens D.S.; RT "gmhX, a novel gene required for the incorporation of L-glycero-D- RT manno-heptose into lipooligosaccharide in Neisseria meningitidis."; RL Microbiology 147:2367-2377(2001). RN [3] RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. RX PubMed=12101286; RA Valvano M.A., Messner P., Kosma P.; RT "Novel pathways for biosynthesis of nucleotide-activated glycero- RT manno-heptose precursors of bacterial glycoproteins and cell surface RT polysaccharides."; RL Microbiology 148:1979-1989(2002). CC -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7- CC bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1- CC phosphate by removing the phosphate group at the C-7 position. CC {ECO:0000305|PubMed:11496013}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1,7- CC bisphosphate + H(2)O = D-glycero-beta-D-manno-heptose 1-phosphate CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42354.1; -; Genomic_DNA. DR PIR; F81013; F81013. DR RefSeq; NP_275024.1; NC_003112.2. DR RefSeq; WP_002224688.1; NC_003112.2. DR ProteinModelPortal; Q9JXI5; -. DR STRING; 122586.NMB2033; -. DR PaxDb; Q9JXI5; -. DR EnsemblBacteria; AAF42354; AAF42354; NMB2033. DR GeneID; 904065; -. DR KEGG; nme:NMB2033; -. DR PATRIC; 20360186; VBINeiMen85645_2592. DR eggNOG; ENOG4108ZI0; Bacteria. DR eggNOG; COG0241; LUCA. DR HOGENOM; HOG000016503; -. DR KO; K03273; -. DR OMA; DEWVALP; -. DR OrthoDB; EOG68SVXZ; -. DR BioCyc; NMEN122586:GHGG-2095-MONOMER; -. DR UniPathway; UPA00356; UER00438. DR UniPathway; UPA00976; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016311; P:dephosphorylation; ISS:GOC. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:CACAO. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR004446; Heptose_bisP_phosphatase. DR InterPro; IPR006543; Histidinol-phos. DR PIRSF; PIRSF004682; GmhB; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 187 D-glycero-beta-D-manno-heptose-1,7- FT bisphosphate 7-phosphatase. FT /FTId=PRO_0000209399. FT REGION 7 9 Substrate binding. {ECO:0000250}. FT REGION 15 19 Substrate binding. {ECO:0000250}. FT REGION 50 53 Substrate binding. {ECO:0000250}. FT REGION 100 101 Substrate binding. {ECO:0000250}. FT ACT_SITE 7 7 Nucleophile. {ECO:0000250}. FT ACT_SITE 9 9 Proton donor. {ECO:0000250}. FT METAL 7 7 Magnesium. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 9 9 Magnesium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 89 89 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 91 91 Zinc; via pros nitrogen. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 97 97 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 99 99 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 126 126 Magnesium. FT {ECO:0000250|UniProtKB:Q7WG29}. FT SITE 50 50 Stabilizes the phosphoryl group. FT {ECO:0000250}. FT SITE 100 100 Contributes to substrate recognition. FT {ECO:0000250}. FT SITE 101 101 Stabilizes the phosphoryl group. FT {ECO:0000250}. SQ SEQUENCE 187 AA; 20713 MW; 0E4D689BEC2017AF CRC64; MKLIILDRDG VINQDRDDFV KSVDEWIPVE GSMDAVAFLT QAGYTVAVAT NQSGIGRKYF TVQNLTEMHA KMHRLVRQAG GEINGIWFCP HTDADNCNCR KPKPGMIEDI IGRFNAQASE TWLVGDSLRD LQAIDAVGGK PALVLTGKGK KTLSQHGHEL PEHTQVFDTL LDFSQYIMQE NTAPQAD // ID GPXA_NEIMB Reviewed; 177 AA. AC P0A0T5; P52036; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Glutathione peroxidase homolog; GN Name=gpxA; Synonyms=gph; OrderedLocusNames=NMB1621; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Important in the cellular metabolism or defense CC processes particular to this pathogen. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41973.1; -; Genomic_DNA. DR PIR; C81062; C81062. DR RefSeq; NP_274627.1; NC_003112.2. DR RefSeq; WP_002218952.1; NC_003112.2. DR ProteinModelPortal; P0A0T5; -. DR STRING; 122586.NMB1621; -. DR PaxDb; P0A0T5; -. DR EnsemblBacteria; AAF41973; AAF41973; NMB1621. DR GeneID; 904057; -. DR KEGG; nme:NMB1621; -. DR PATRIC; 20359142; VBINeiMen85645_2082. DR eggNOG; ENOG4108V06; Bacteria. DR eggNOG; COG0386; LUCA. DR HOGENOM; HOG000277054; -. DR KO; K00432; -. DR OMA; GARIEWN; -. DR OrthoDB; EOG66QM2H; -. DR BioCyc; NMEN122586:GHGG-1670-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR029759; GPX_AS. DR InterPro; IPR029760; GPX_CS. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 2. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Peroxidase; Reference proteome. FT CHAIN 1 177 Glutathione peroxidase homolog. FT /FTId=PRO_0000066659. FT ACT_SITE 35 35 {ECO:0000250}. SQ SEQUENCE 177 AA; 19929 MW; 89E50641FCAED5B5 CRC64; MGIYDFQMKD AEGNAVDLSG YRGKVLLIVN TATRCGLTPQ YEALQKLYAQ YTAEGLEILD FPCNQFREQA PESSGEIAQV CMMKFGTKFK IFDKIEVNGA NTAPLYAYLK SVKPQDKGNH LFKDFVLKLA ALGEKRDEGD IKWNFTKFLV NRDGEVVERF APSVTPEEIE ADIRALL // ID GSA_NEIMB Reviewed; 427 AA. AC Q9JXW0; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375}; DE Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375}; DE EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375}; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375}; DE Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375}; GN Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375}; GN OrderedLocusNames=NMB1864; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5- CC aminolevulinate. {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00375}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 2/2. {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00375}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42198.1; -; Genomic_DNA. DR PIR; A81034; A81034. DR RefSeq; NP_274860.1; NC_003112.2. DR RefSeq; WP_002223025.1; NC_003112.2. DR ProteinModelPortal; Q9JXW0; -. DR SMR; Q9JXW0; 3-420. DR STRING; 122586.NMB1864; -. DR PaxDb; Q9JXW0; -. DR PRIDE; Q9JXW0; -. DR EnsemblBacteria; AAF42198; AAF42198; NMB1864. DR GeneID; 904324; -. DR KEGG; nme:NMB1864; -. DR PATRIC; 20359755; VBINeiMen85645_2383. DR eggNOG; ENOG4105CDM; Bacteria. DR eggNOG; COG0001; LUCA. DR HOGENOM; HOG000020210; -. DR KO; K01845; -. DR OMA; CGHAHPE; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NMEN122586:GHGG-1920-MONOMER; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00375; HemL_aminotrans_3; 1. DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00713; hemL; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1 427 Glutamate-1-semialdehyde 2,1-aminomutase. FT /FTId=PRO_0000120428. FT MOD_RES 265 265 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00375}. SQ SEQUENCE 427 AA; 45315 MW; 2ECC6C2E76A1B558 CRC64; MNRNEILFDR AKAIIPGGVN SPVRAFGSVG GVPRFIKKAE GAYVWDENGT RYTDYVGSWG PAIVGHAHPE VVETVCEAAL GGLSFGAPTE GEIVIAEEIA KIMPSVERLR LVSSGTEATM TAIRLARGFT GRDKIIKFEG CYHGHSDSLL VKAGSGLLTF GNPSSAGVPA DFTKHTLVLE YNNIAQLEEA FAQSGNEIAC VIVEPFVGNM NLVRPTEAFV KALRGLTEKY GAVLIYDEVM TGFRVALGGA QSLHGITPDL TTMGKVIGGG MPLAAFGGRK DIMECISPLG GVYQAGTLSG NPIAVAAGLK TLEIIQREGF YENLTARTEQ LVQGFRTAAD AAGIEFTADS VGGMFGLYFA AHAPRNYADM ARSNIEGFKQ FFHGMLDRNV AFGPSAYEAG FVSAAHTPEL IDETVAVAVE VFKAMAE // ID H8_NEIMB Reviewed; 183 AA. AC P57026; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Outer membrane protein H.8; DE Flags: Precursor; GN OrderedLocusNames=NMB1533; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 plastocyanin-like domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41888.1; -; Genomic_DNA. DR PIR; A81072; A81072. DR RefSeq; NP_274540.1; NC_003112.2. DR RefSeq; WP_002225055.1; NC_003112.2. DR ProteinModelPortal; P57026; -. DR SMR; P57026; 58-181. DR STRING; 122586.NMB1533; -. DR PaxDb; P57026; -. DR EnsemblBacteria; AAF41888; AAF41888; NMB1533. DR GeneID; 904058; -. DR KEGG; nme:NMB1533; -. DR PATRIC; 20358872; VBINeiMen85645_1945. DR eggNOG; ENOG41090JD; Bacteria. DR eggNOG; COG3241; LUCA. DR HOGENOM; HOG000280572; -. DR OMA; KSCKTFT; -. DR BioCyc; NMEN122586:GHGG-1574-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR014068; Azurin_proteobac. DR InterPro; IPR000923; BlueCu_1. DR InterPro; IPR028871; BlueCu_1_BS. DR InterPro; IPR008972; Cupredoxin. DR Pfam; PF00127; Copper-bind; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR TIGRFAMs; TIGR02695; azurin; 1. DR PROSITE; PS00196; COPPER_BLUE; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Copper; Electron transport; KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome; KW Signal; Transport. FT SIGNAL 1 17 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 18 183 Outer membrane protein H.8. FT /FTId=PRO_0000002855. FT DOMAIN 57 183 Plastocyanin-like. FT METAL 102 102 Copper. {ECO:0000250}. FT METAL 166 166 Copper. {ECO:0000250}. FT METAL 171 171 Copper. {ECO:0000250}. FT METAL 175 175 Copper. {ECO:0000250}. FT LIPID 18 18 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 18 18 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 183 AA; 18544 MW; 7E2ECD90F7CC728C CRC64; MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAAEAPASEA PAAEAAPADA AEAPAAGNCA ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKASM GHNLVIAKAE DMDGVFKDGV GAADTDYVKP DDARVVAHTK LIGGGEEASL TLDPAKLADG EYKFACTFPG HGALMNGKVT LVD // ID GSHB_NEIMB Reviewed; 319 AA. AC Q9JYJ3; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162}; DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162}; DE AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162}; DE Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162}; DE Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162}; DE AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162}; GN Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162}; GN OrderedLocusNames=NMB1559; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine = CC ADP + phosphate + glutathione. {ECO:0000255|HAMAP-Rule:MF_00162}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_00162}. CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00162}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00162}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41913.1; -; Genomic_DNA. DR PIR; D81069; D81069. DR RefSeq; NP_274566.1; NC_003112.2. DR RefSeq; WP_002225038.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ3; -. DR STRING; 122586.NMB1559; -. DR PaxDb; Q9JYJ3; -. DR EnsemblBacteria; AAF41913; AAF41913; NMB1559. DR GeneID; 904122; -. DR KEGG; nme:NMB1559; -. DR PATRIC; 20358974; VBINeiMen85645_2006. DR eggNOG; ENOG4105D7Z; Bacteria. DR eggNOG; COG0189; LUCA. DR HOGENOM; HOG000265022; -. DR KO; K01920; -. DR OMA; MKPLHGH; -. DR OrthoDB; EOG6WMHWB; -. DR BioCyc; NMEN122586:GHGG-1600-MONOMER; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00162; GSH_S; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR006284; Glut_synth_pro. DR InterPro; IPR004218; GSHS_ATP-bd. DR InterPro; IPR004215; GSHS_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF02955; GSH-S_ATP; 1. DR Pfam; PF02951; GSH-S_N; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01380; glut_syn; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 319 Glutathione synthetase. FT /FTId=PRO_0000197470. FT DOMAIN 129 314 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00162}. FT NP_BIND 155 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00162}. FT METAL 285 285 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00162}. FT METAL 287 287 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00162}. SQ SEQUENCE 319 AA; 35146 MW; 327C0F342F09C2F0 CRC64; MMKVLFIADP MASFKTYKDT TYAMMREMAK RGWRLFHTLS GELSVNGGLV TAQASAFEFL GAKNDDDHAW FKSADKVQTA LEAFDAVIMR TDPPFDMQYL YATQLLTLAE QQGAKVFNSG QAMRDFNEKL AILNFSRFIA PTLVTTRSAD VRTFLKEHGD IIIKPLDGMG GMGIFRLTEK DPNIGSILET LMQLDSRTIM AQRYIPEIVH GDKRILIIGG EVVPYALARI PQNGETRGNL AAGGRGVAQE LGGRDREIAE TLAPELKRRG ILLAGLDVIG SNLTEVNVTS PTGFQEIMKQ KGFDVAAMFA DAVAAWSVR // ID HEMH_NEIMB Reviewed; 336 AA. AC Q9K097; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 11-MAY-2016, entry version 96. DE RecName: Full=Ferrochelatase; DE EC=4.99.1.1; DE AltName: Full=Heme synthase; DE AltName: Full=Protoheme ferro-lyase; GN Name=hemH; OrderedLocusNames=NMB0718; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+). CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ferrochelatase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41131.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41131.1; ALT_INIT; Genomic_DNA. DR PIR; C81167; C81167. DR RefSeq; NP_273760.1; NC_003112.2. DR ProteinModelPortal; Q9K097; -. DR STRING; 122586.NMB0718; -. DR PaxDb; Q9K097; -. DR DNASU; 902830; -. DR EnsemblBacteria; AAF41131; AAF41131; NMB0718. DR GeneID; 902830; -. DR KEGG; nme:NMB0718; -. DR PATRIC; 20356789; VBINeiMen85645_0916. DR eggNOG; ENOG4105CFX; Bacteria. DR eggNOG; COG0276; LUCA. DR HOGENOM; HOG000060730; -. DR KO; K01772; -. DR OMA; LPIQNKL; -. DR OrthoDB; EOG6XHC5H; -. DR BioCyc; NMEN122586:GHGG-746-MONOMER; -. DR UniPathway; UPA00252; UER00325. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004325; F:ferrochelatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00323; Ferrochelatase; 1. DR InterPro; IPR001015; Ferrochelatase. DR InterPro; IPR019772; Ferrochelatase_AS. DR PANTHER; PTHR11108; PTHR11108; 1. DR Pfam; PF00762; Ferrochelatase; 1. DR TIGRFAMs; TIGR00109; hemH; 1. DR PROSITE; PS00534; FERROCHELATASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Heme biosynthesis; Iron; Lyase; KW Metal-binding; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 336 Ferrochelatase. FT /FTId=PRO_0000175170. FT METAL 206 206 Iron. {ECO:0000250}. FT METAL 287 287 Iron. {ECO:0000250}. SQ SEQUENCE 336 AA; 38040 MW; 3E924490A7BE52BD CRC64; MLPFFPEPSL SYTQQNRTAV LLLNLGTPDA PTAQAVRPYL KSFLTDRRVV ELPKWLWYPI LHGLVLTLRP KKSAHAYEKI WFKEGSPLEV YTARQAAALA KRMPDLIVRH AMTYGNPSVA DVLSELKAQG AGRLLVIPMY PQYAASSSGA AVDKVCEQLL LQRNQMSVRT VSRFYDDTGY IDAMKNHILR YWAEHGRGKK LMLSFHGVPQ KHHDLGDPYP DECRHTAKLL AEALELTEDQ YVVSFQSQFG RAKWVTPSTQ DLFGKLPKQG VTELDVFCPG FLADCLETME EIALMGREQF YEAGGKSYRY IPCLNDNPDW IDALVALAEE NLGSWR // ID HIS1_NEIMB Reviewed; 217 AA. AC P64347; Q9JQS2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=ATP phosphoribosyltransferase; DE Short=ATP-PRT; DE Short=ATP-PRTase; DE EC=2.4.2.17; GN Name=hisG; OrderedLocusNames=NMB1579; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a CC crucial role in the pathway because the rate of histidine CC biosynthesis seems to be controlled primarily by regulation of CC HisG enzymatic activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced CC by HisZ. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. CC Short subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41932.1; -; Genomic_DNA. DR PIR; C81067; C81067. DR RefSeq; NP_274585.1; NC_003112.2. DR RefSeq; WP_002261539.1; NC_003112.2. DR ProteinModelPortal; P64347; -. DR STRING; 122586.NMB1579; -. DR PaxDb; P64347; -. DR EnsemblBacteria; AAF41932; AAF41932; NMB1579. DR GeneID; 904212; -. DR KEGG; nme:NMB1579; -. DR PATRIC; 20359024; VBINeiMen85645_2030. DR eggNOG; ENOG4105E21; Bacteria. DR eggNOG; COG0040; LUCA. DR HOGENOM; HOG000223248; -. DR KO; K00765; -. DR OMA; VATKFPR; -. DR OrthoDB; EOG66MQT3; -. DR BioCyc; NMEN122586:GHGG-1621-MONOMER; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01018; HisG_Short; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short. DR PANTHER; PTHR21403; PTHR21403; 1. DR Pfam; PF01634; HisG; 1. DR TIGRFAMs; TIGR00070; hisG; 1. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 217 ATP phosphoribosyltransferase. FT /FTId=PRO_0000151919. SQ SEQUENCE 217 AA; 23263 MW; D7492BCF038E54B2 CRC64; MQDNALTIAL SKGRIFEETL PLLAAAGIVP TEEPEKSRKL IIGTNHENIR LVIVRATDVP TYVRYGAADF GIAGKDVLIE HGGTGLYRPL DLEIAKCRMM VAVRKGFDYE AASQPGCRLK IATKYPEIAA SHFAGKGVHV DIIKLYGSME LAPLVGLSDA IVDLVSTGNT LKANGLEAVE HIVDISSRLV VNKAALKTKY ALLEPIIQAF GGAVKAK // ID HFQ_NEIMB Reviewed; 97 AA. AC P64345; Q9JQW6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436}; GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=NMB0748; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) CC and mRNAs to facilitate mRNA translational regulation in response CC to envelope stress, environmental stress and changes in metabolite CC concentrations. Also binds with high specificity to tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP- CC Rule:MF_00436}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41161.1; -; Genomic_DNA. DR PIR; C81163; C81163. DR RefSeq; NP_273790.1; NC_003112.2. DR RefSeq; WP_002214042.1; NC_003112.2. DR ProteinModelPortal; P64345; -. DR SMR; P64345; 5-71. DR STRING; 122586.NMB0748; -. DR PaxDb; P64345; -. DR EnsemblBacteria; AAF41161; AAF41161; NMB0748. DR GeneID; 902863; -. DR KEGG; nme:NMB0748; -. DR PATRIC; 20356867; VBINeiMen85645_0952. DR eggNOG; ENOG4105KW8; Bacteria. DR eggNOG; COG1923; LUCA. DR HOGENOM; HOG000004931; -. DR KO; K03666; -. DR OMA; RRDGHAQ; -. DR OrthoDB; EOG68SW3W; -. DR BioCyc; NMEN122586:GHGG-779-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR HAMAP; MF_00436; Hfq; 1. DR InterPro; IPR005001; Hfq. DR InterPro; IPR010920; LSM_dom. DR SUPFAM; SSF50182; SSF50182; 1. DR TIGRFAMs; TIGR02383; Hfq; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding; Stress response. FT CHAIN 1 97 RNA-binding protein Hfq. FT /FTId=PRO_0000095652. SQ SEQUENCE 97 AA; 10841 MW; AC50A6BD58C11EA0 CRC64; MTAKGQMLQD PFLNALRKEH VPVSIYLVNG IKLQGQVESF DQYVVLLRNT SVTQMVYKHA ISTIVPARSV NLQHENRPQA APTSTLVQVE TVQQPAE // ID HIS2_NEIMB Reviewed; 107 AA. AC Q9K0J4; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisE; OrderedLocusNames=NMB0603; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-AMP + diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41030.1; -; Genomic_DNA. DR PIR; D81178; D81178. DR RefSeq; NP_273647.1; NC_003112.2. DR RefSeq; WP_002222845.1; NC_003112.2. DR ProteinModelPortal; Q9K0J4; -. DR SMR; Q9K0J4; 5-94. DR STRING; 122586.NMB0603; -. DR PaxDb; Q9K0J4; -. DR EnsemblBacteria; AAF41030; AAF41030; NMB0603. DR GeneID; 902717; -. DR KEGG; nme:NMB0603; -. DR PATRIC; 20356491; VBINeiMen85645_0765. DR eggNOG; ENOG4105KPZ; Bacteria. DR eggNOG; COG0140; LUCA. DR HOGENOM; HOG000220965; -. DR KO; K01523; -. DR OMA; EQSWTAK; -. DR OrthoDB; EOG6CGCMH; -. DR BioCyc; NMEN122586:GHGG-629-MONOMER; -. DR UniPathway; UPA00031; UER00007. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01020; HisE; 1. DR InterPro; IPR008179; PRib-ATP_PPHydrolase. DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like. DR Pfam; PF01503; PRA-PH; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 107 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_0000136374. SQ SEQUENCE 107 AA; 11924 MW; C0080C03D8C66EEF CRC64; MGDSVLSAIQ QTITQRKSAN PSESYVAQLL HKGEDKILKK VIEEAGEVLM ASKDKNPSHL VYEVADLWFH TMILLTHHDL KAEDVLDELA RRQGLSGLVE KAARTES // ID HISX_NEIMB Reviewed; 429 AA. AC Q9JYH8; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; GN OrderedLocusNames=NMB1581; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine CC + 2 NADH. {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01024}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41934.1; -; Genomic_DNA. DR PIR; E81067; E81067. DR RefSeq; NP_274587.1; NC_003112.2. DR RefSeq; WP_002220532.1; NC_003112.2. DR ProteinModelPortal; Q9JYH8; -. DR STRING; 122586.NMB1581; -. DR PaxDb; Q9JYH8; -. DR EnsemblBacteria; AAF41934; AAF41934; NMB1581. DR GeneID; 904220; -. DR KEGG; nme:NMB1581; -. DR PATRIC; 20359028; VBINeiMen85645_2032. DR eggNOG; ENOG4105CEK; Bacteria. DR eggNOG; COG0141; LUCA. DR HOGENOM; HOG000243914; -. DR KO; K00013; -. DR OMA; TEIYRVG; -. DR OrthoDB; EOG6CVVCR; -. DR BioCyc; NMEN122586:GHGG-1623-MONOMER; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01024; HisD; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 429 Histidinol dehydrogenase. FT /FTId=PRO_0000135802. FT ACT_SITE 327 327 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT ACT_SITE 328 328 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT METAL 259 259 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 262 262 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 361 361 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 420 420 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT BINDING 130 130 NAD. {ECO:0000255|HAMAP-Rule:MF_01024}. FT BINDING 191 191 NAD. {ECO:0000255|HAMAP-Rule:MF_01024}. FT BINDING 214 214 NAD. {ECO:0000255|HAMAP-Rule:MF_01024}. FT BINDING 237 237 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 259 259 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 262 262 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 328 328 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 361 361 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 415 415 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 420 420 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. SQ SEQUENCE 429 AA; 46324 MW; 1A6597DF1E685847 CRC64; MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE YTNKFDQTNA KSIDDLILTQ ADLNAAFERI PNDVQTALQT AARRVESYHQ RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAVAALAYGT ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA SLGNRGAMIL AKDLDEACEI ANYISPEHLE LSVENPQEWA KKIRHAGAIF MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG AQKLGETASV LAHGESLTAH ARAAEFRMK // ID HEM1_NEIMB Reviewed; 415 AA. AC P56994; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 09-DEC-2015, entry version 106. DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087}; DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087}; DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087}; GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; GN OrderedLocusNames=NMB0576; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl- CC tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) + CC tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 1/2. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure CC with each monomer consisting of three distinct domains arranged CC along a curved 'spinal' alpha-helix. The N-terminal catalytic CC domain specifically recognizes the glutamate moiety of the CC substrate. The second domain is the NADPH-binding domain, and the CC third C-terminal domain is responsible for dimerization. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a CC nucleophile attacking the alpha-carbonyl group of tRNA-bound CC glutamate with the formation of a thioester intermediate between CC enzyme and glutamate, and the concomitant release of tRNA(Glu). CC The thioester intermediate is finally reduced by direct hydride CC transfer from NADPH, to form the product GSA. {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41004.1; -; Genomic_DNA. DR PIR; C81183; C81183. DR RefSeq; NP_273620.1; NC_003112.2. DR RefSeq; WP_002225559.1; NC_003112.2. DR ProteinModelPortal; P56994; -. DR STRING; 122586.NMB0576; -. DR PaxDb; P56994; -. DR EnsemblBacteria; AAF41004; AAF41004; NMB0576. DR GeneID; 902691; -. DR KEGG; nme:NMB0576; -. DR PATRIC; 20356433; VBINeiMen85645_0736. DR eggNOG; ENOG4105C7E; Bacteria. DR eggNOG; COG0373; LUCA. DR HOGENOM; HOG000109650; -. DR KO; K02492; -. DR OMA; NHCPNIK; -. DR OrthoDB; EOG6MWNBM; -. DR BioCyc; NMEN122586:GHGG-602-MONOMER; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00087; Glu_tRNA_reductase; 1. DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase. DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer. DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N. DR InterPro; IPR018214; GluRdtase_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF00745; GlutR_dimer; 1. DR Pfam; PF05201; GlutR_N; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69075; SSF69075; 1. DR SUPFAM; SSF69742; SSF69742; 1. DR TIGRFAMs; TIGR01035; hemA; 1. DR PROSITE; PS00747; GLUTR; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis; KW Reference proteome. FT CHAIN 1 415 Glutamyl-tRNA reductase. FT /FTId=PRO_0000114046. FT NP_BIND 184 189 NADP. {ECO:0000255|HAMAP-Rule:MF_00087}. FT REGION 49 52 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT REGION 109 111 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT ACT_SITE 50 50 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT BINDING 104 104 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT BINDING 115 115 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT SITE 94 94 Important for activity. FT {ECO:0000255|HAMAP-Rule:MF_00087}. SQ SEQUENCE 415 AA; 45480 MW; 6C5DD4A0D6B03894 CRC64; MQLTAVGLNH QTAPLSIREK LAFAAAALPK AVRNLARSNA ATEAVILSTC NRTELYCVGD SEEIIRWLAD YHSLPIEEIR PYLYALDMQE TVRHAFRVAC GLDSMVLGEP QILGQIKDAV RVAQEQESMG KKLNALFQKT FSVAKEVRTD TAVGENSVSM ASASVKLAEQ IFPDIGDLNV LFIGAGEMIE LVATYFAAKS PRLMTVANRT LARAQELCDK LGVNAEPCLL SDLPAILHDY DVVVSSTASQ LPIVGKGMVE RALKQRQSMP LFMLDLAVPR DIEAEVGDLN DAYLYTVDDM VNIVQSGKEA RQKAAAAAET LVSEKVAEFV RQQQGRQSVP LIKALRDEGE KARKQVLENA MKQLAKGATA EEVLERLSVQ LTNKLLHSPT QTLNKAGEED KDLVHAVAQI YHLDK // ID HIS7_NEIMB Reviewed; 305 AA. AC P64371; Q9JRJ7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076}; DE Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076}; DE EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076}; GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; GN OrderedLocusNames=NMB1583; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase CC family. {ECO:0000255|HAMAP-Rule:MF_00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41936.1; -; Genomic_DNA. DR PIR; G81067; G81067. DR RefSeq; NP_274589.2; NC_003112.2. DR ProteinModelPortal; P64371; -. DR SMR; P64371; 110-291. DR STRING; 122586.NMB1583; -. DR PaxDb; P64371; -. DR EnsemblBacteria; AAF41936; AAF41936; NMB1583. DR GeneID; 904235; -. DR KEGG; nme:NMB1583; -. DR PATRIC; 20359032; VBINeiMen85645_2034. DR eggNOG; ENOG4105ECC; Bacteria. DR eggNOG; COG0131; LUCA. DR HOGENOM; HOG000228064; -. DR KO; K01693; -. DR OMA; HHIAESC; -. DR OrthoDB; EOG60PHGP; -. DR BioCyc; NMEN122586:GHGG-1625-MONOMER; -. DR UniPathway; UPA00031; UER00011. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00076; HisB; 1. DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase. DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 1. DR Pfam; PF00475; IGPD; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1. DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 305 Imidazoleglycerol-phosphate dehydratase. FT /FTId=PRO_0000158148. SQ SEQUENCE 305 AA; 33739 MW; 03C6BA9EB5DCE1A7 CRC64; MNLTKTQRQL HNFLTLAQEA GSLSKLAKLC GYRTPVALYK LKQRLEKQAE DPDARGIRPS LMAKLEKHTG KPKGWLDRKH RERTVPETAA ESTGTAETQI AETASAAGCR SVTVNRNTCE TQITVSINLD GSGKSRLDTG VPFLEHMIDQ IARHGMIDID ISCKGDLHID DHHTAEDIGI TLGQAIRQAL GDKKGIRRYG HSYVPLDEAL SRVVIDLSGR PGLVYNIEFT RALIGRFDVD LFEEFFHGIV NHSMMTLHID NLSGKNAHHQ AETVFKAFGR ALRMAVEHDP RMAGQTPSTK GTLTA // ID HEM3_NEIMB Reviewed; 311 AA. AC Q9K0P6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Porphobilinogen deaminase; DE Short=PBG; DE EC=2.5.1.61; DE AltName: Full=Hydroxymethylbilane synthase; DE Short=HMBS; DE AltName: Full=Pre-uroporphyrinogen synthase; GN Name=hemC; OrderedLocusNames=NMB0539; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the CC hydroxymethylbilane pre-uroporphyrinogen in several discrete CC steps. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 porphobilinogen + H(2)O = CC hydroxymethylbilane + 4 NH(3). CC -!- COFACTOR: CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; CC Evidence={ECO:0000250}; CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 2/4. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the CC dipyrromethane group. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40968.1; -; Genomic_DNA. DR PIR; B81188; B81188. DR RefSeq; NP_273584.1; NC_003112.2. DR RefSeq; WP_002217854.1; NC_003112.2. DR ProteinModelPortal; Q9K0P6; -. DR SMR; Q9K0P6; 4-308. DR STRING; 122586.NMB0539; -. DR PaxDb; Q9K0P6; -. DR EnsemblBacteria; AAF40968; AAF40968; NMB0539. DR GeneID; 902654; -. DR KEGG; nme:NMB0539; -. DR PATRIC; 20356335; VBINeiMen85645_0686. DR eggNOG; ENOG4105D6W; Bacteria. DR eggNOG; COG0181; LUCA. DR HOGENOM; HOG000228587; -. DR KO; K01749; -. DR OMA; GIECRTD; -. DR OrthoDB; EOG6HB9Z6; -. DR BioCyc; NMEN122586:GHGG-565-MONOMER; -. DR UniPathway; UPA00251; UER00319. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.160.40; -; 1. DR HAMAP; MF_00260; Porphobil_deam; 1. DR InterPro; IPR000860; HemC. DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS. DR InterPro; IPR022417; Porphobilin_deaminase_N. DR InterPro; IPR022418; Porphobilinogen_deaminase_C. DR PANTHER; PTHR11557; PTHR11557; 1. DR Pfam; PF01379; Porphobil_deam; 1. DR Pfam; PF03900; Porphobil_deamC; 1. DR PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1. DR PRINTS; PR00151; PORPHBDMNASE. DR SUPFAM; SSF54782; SSF54782; 1. DR TIGRFAMs; TIGR00212; hemC; 1. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1. PE 3: Inferred from homology; KW Complete proteome; Porphyrin biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 311 Porphobilinogen deaminase. FT /FTId=PRO_0000142962. FT MOD_RES 242 242 S-(dipyrrolylmethanemethyl)cysteine. FT {ECO:0000250}. SQ SEQUENCE 311 AA; 33478 MW; 8446DBED7BF0577F CRC64; MNPKKLVIAS RESLLAMWQA KHIQGRLKAL YPDCEVEILG MTTRGDQILD KTLSKVGGKG LFVKELEQAL YDGRADLAVH SIKDVPMDLP EGFALAAIGE RANPFDAFVS NQYTRLEEMP EGAVVGTSSL RREAQLRARY PHLLIKPLRG NVQTRLSKLD NGEYDAIILA AAGLQRLKLD GRIRMILSES DSLPAAGQGA LGIEIAAHRE DLYEVLKPLN HGVTNACVTA ERALARALGG SCQVPLAAYC TEENGLLTLR GLVGHPDGSV VLRADAQAPA EYADALGRAV AKKLADDGAR ELIGAVLNTE N // ID HIS6_NEIMB Reviewed; 255 AA. AC Q9K0H4; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF; DE EC=4.1.3.-; DE AltName: Full=IGP synthase cyclase subunit; DE AltName: Full=IGP synthase subunit HisF; DE AltName: Full=ImGP synthase subunit HisF; DE Short=IGPS subunit HisF; GN Name=hisF; OrderedLocusNames=NMB0628; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisF subunit catalyzes the CC cyclization activity that produces IGP and AICAR from PRFAR using CC the ammonia provided by the HisH subunit (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41053.1; -; Genomic_DNA. DR PIR; H81176; H81176. DR RefSeq; NP_273671.1; NC_003112.2. DR RefSeq; WP_002222827.1; NC_003112.2. DR ProteinModelPortal; Q9K0H4; -. DR SMR; Q9K0H4; 2-255. DR STRING; 122586.NMB0628; -. DR PaxDb; Q9K0H4; -. DR EnsemblBacteria; AAF41053; AAF41053; NMB0628. DR GeneID; 902741; -. DR KEGG; nme:NMB0628; -. DR PATRIC; 20356553; VBINeiMen85645_0796. DR eggNOG; ENOG4105C0S; Bacteria. DR eggNOG; COG0107; LUCA. DR HOGENOM; HOG000224612; -. DR KO; K02500; -. DR OMA; KGTNFVN; -. DR OrthoDB; EOG6H1Q3W; -. DR BioCyc; NMEN122586:GHGG-654-MONOMER; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01013; HisF; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004651; HisF. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00735; hisF; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 255 Imidazole glycerol phosphate synthase FT subunit HisF. FT /FTId=PRO_0000142188. FT ACT_SITE 12 12 {ECO:0000255}. FT ACT_SITE 131 131 {ECO:0000255}. SQ SEQUENCE 255 AA; 27001 MW; EAABB234BF30E23C CRC64; MALAKRIIPC LDVKDGRVVK GVNFIGLRDA GDPVEAAKRY NGEGADELTF LDITASSDNR DTILHIIEEV AGQVFIPLTV GGGVRTVADI RRLLNAGADK VSINTAAVTR PDLIDEAAGF FGSQAIVAAV DAKAANPENT RWEIFTHGGR NPTGLDAVEW AVEMQKRGAG EILLTGMDRD GTKQGFNLPL TRAVAEAVDI PVIASGGVGN VRHLIEGITE GKADAVLAAG IFHFGEIAIR EAKRAMREAG IEVRL // ID HIS8_NEIMB Reviewed; 365 AA. AC Q9JYH7; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023}; DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023}; DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023}; GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; GN OrderedLocusNames=NMB1582; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3- CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01023}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. CC {ECO:0000255|HAMAP-Rule:MF_01023}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41935.1; -; Genomic_DNA. DR PIR; F81067; F81067. DR RefSeq; NP_274588.1; NC_003112.2. DR RefSeq; WP_002225029.1; NC_003112.2. DR ProteinModelPortal; Q9JYH7; -. DR STRING; 122586.NMB1582; -. DR PaxDb; Q9JYH7; -. DR EnsemblBacteria; AAF41935; AAF41935; NMB1582. DR GeneID; 904223; -. DR KEGG; nme:NMB1582; -. DR PATRIC; 20359030; VBINeiMen85645_2033. DR eggNOG; ENOG4105CIH; Bacteria. DR eggNOG; COG0079; LUCA. DR HOGENOM; HOG000288510; -. DR KO; K00817; -. DR OMA; YPSEANY; -. DR OrthoDB; EOG6P5ZBR; -. DR BioCyc; NMEN122586:GHGG-1624-MONOMER; -. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01023; HisC_aminotrans_2; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR005861; HisP_aminotrans. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01141; hisC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 365 Histidinol-phosphate aminotransferase. FT /FTId=PRO_0000153400. FT MOD_RES 220 220 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01023}. SQ SEQUENCE 365 AA; 39931 MW; C00C46FF70268F10 CRC64; MKSVRSFIRD DIQAMSAYQI ADVPPGFAKL DSMESPVHPF AGHETLLQEW QARLAAAPIH LYPNPSGSGL QEALRSAFDI PDCADIALGN GSDELIQFIT MLTAKPGAAM LAAEPSFVMY RHNAALYGMD YVGVPLNGDF TLNLPAVLEA VRKHRPALTF IAYPNNPTGV CFTRAEIEAV IEASDGIVVV DEAYGAFNGD SFLPQAGRIP NLIVLRTLSK IGFAGLRIGY AAGCPEVIGE LQKILPPYNM NQLSLTTAKL ALRHYGIISA NIDSLKNERE RMFAELGKIC RLNTFSSQAN FITIRVPDAD LLFDTLKQNR ILVKKLHGAH PLLEHCLRIT VGSPAQNDAV LNIIRQLYCQ PTDFL // ID HSCB_NEIMB Reviewed; 166 AA. AC Q9JYX6; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Co-chaperone protein HscB homolog {ECO:0000255|HAMAP-Rule:MF_00682}; GN Name=hscB {ECO:0000255|HAMAP-Rule:MF_00682}; GN OrderedLocusNames=NMB1383; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Co-chaperone involved in the maturation of iron-sulfur CC cluster-containing proteins. Seems to help targeting proteins to CC be folded toward HscA. {ECO:0000255|HAMAP-Rule:MF_00682}. CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity. CC {ECO:0000255|HAMAP-Rule:MF_00682}. CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000255|HAMAP- CC Rule:MF_00682}. CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|HAMAP- CC Rule:MF_00682}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62332.1; -; Genomic_DNA. DR RefSeq; NP_274399.1; NC_003112.2. DR RefSeq; WP_002219110.1; NC_003112.2. DR ProteinModelPortal; Q9JYX6; -. DR STRING; 122586.NMB1383; -. DR PaxDb; Q9JYX6; -. DR EnsemblBacteria; AAF62332; AAF62332; NMB1383. DR GeneID; 903805; -. DR KEGG; nme:NMB1383; -. DR PATRIC; 20358445; VBINeiMen85645_1734. DR eggNOG; ENOG4108SWN; Bacteria. DR eggNOG; COG1076; LUCA. DR HOGENOM; HOG000262077; -. DR KO; K04082; -. DR OMA; FNPFQIF; -. DR OrthoDB; EOG66F07J; -. DR BioCyc; NMEN122586:GHGG-1421-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0051259; P:protein oligomerization; IEA:InterPro. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 1.20.1280.20; -; 1. DR HAMAP; MF_00682; HscB; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR004640; HscB. DR InterPro; IPR009073; HscB_oligo_C. DR PANTHER; PTHR14021; PTHR14021; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF07743; HSCB_C; 1. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF47144; SSF47144; 1. DR TIGRFAMs; TIGR00714; hscB; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 166 Co-chaperone protein HscB homolog. FT /FTId=PRO_0000070975. FT DOMAIN 3 75 J. {ECO:0000255|HAMAP-Rule:MF_00682}. SQ SEQUENCE 166 AA; 19131 MW; BBCBE95D2070DC20 CRC64; MSQYFTLFRI EPAFDIDTEN LEQTYRALAA RFHPDKFASA SAFEQKQAVM MSSTINDAYR TLKNPIDRAA YLLKTSGIDA DAPEHTAFAP EFLMQQMEWR ETLMEARAGN DLESLKNLDN EIRDEQEKLF CGLKQSFARQ DYDTAAQQVR QGRFLDKLRN EISSAL // ID HIS4_NEIMB Reviewed; 245 AA. AC Q9K0H3; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=NMB0629; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho- CC beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5- CC ((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41054.1; -; Genomic_DNA. DR PIR; A81177; A81177. DR RefSeq; NP_273672.1; NC_003112.2. DR RefSeq; WP_010980820.1; NC_003112.2. DR ProteinModelPortal; Q9K0H3; -. DR STRING; 122586.NMB0629; -. DR PaxDb; Q9K0H3; -. DR EnsemblBacteria; AAF41054; AAF41054; NMB0629. DR GeneID; 902742; -. DR KEGG; nme:NMB0629; -. DR PATRIC; 20356555; VBINeiMen85645_0797. DR eggNOG; ENOG4105CJV; Bacteria. DR eggNOG; COG0106; LUCA. DR HOGENOM; HOG000224614; -. DR KO; K01814; -. DR OMA; EWLHLVD; -. DR OrthoDB; EOG6H1Q3W; -. DR BioCyc; NMEN122586:GHGG-655-MONOMER; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA. DR InterPro; IPR023016; Isoase_HisA. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00007; TIGR00007; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Isomerase; Reference proteome. FT CHAIN 1 245 1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] FT imidazole-4-carboxamide isomerase. FT /FTId=PRO_0000142026. FT ACT_SITE 8 8 Proton acceptor. {ECO:0000250}. FT ACT_SITE 131 131 Proton donor. {ECO:0000250}. SQ SEQUENCE 245 AA; 25924 MW; B343E19DAE512967 CRC64; MLLIPAIDLK EGRCVRLKQG LMEEATVFSD SPAETALHWF KQGARRLHLV DLNGAFAGVP QNLPAIKDIL AAVAKDIPVQ LGGGIRDLKT IGQYLDLGLN DVIIGTAAVK NPDFVREACK AFPGRIIVGL DAKDGMAAID GWATVTGHHV IDLAKRFEDD GVNSIIYTDI GRDGMMSGVN IDATVKLAQT VRIPVISSGG LTGLDDIRAL CAAEKHGVAG AITGRAIYEG SIDFAQAQQL ADSLD // ID HISZ_NEIMB Reviewed; 383 AA. AC Q9K013; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit; GN Name=hisZ; OrderedLocusNames=NMB0814; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the first step of histidine biosynthesis. CC May allow the feedback regulation of ATP phosphoribosyltransferase CC activity by histidine (By similarity). {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: This function is generally fulfilled by the C- CC terminal part of HisG, which is missing in some bacteria such as CC this one. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. HisZ subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41227.1; -; Genomic_DNA. DR PIR; E81156; E81156. DR RefSeq; NP_273856.1; NC_003112.2. DR RefSeq; WP_002213944.1; NC_003112.2. DR ProteinModelPortal; Q9K013; -. DR STRING; 122586.NMB0814; -. DR PaxDb; Q9K013; -. DR EnsemblBacteria; AAF41227; AAF41227; NMB0814. DR GeneID; 902929; -. DR KEGG; nme:NMB0814; -. DR PATRIC; 20357015; VBINeiMen85645_1026. DR eggNOG; ENOG4105C49; Bacteria. DR eggNOG; COG3705; LUCA. DR HOGENOM; HOG000018074; -. DR KO; K02502; -. DR OMA; RADMTTQ; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; NMEN122586:GHGG-845-MONOMER; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00125; HisZ; 1. DR InterPro; IPR004516; HisRS/HisZ. DR InterPro; IPR004517; HisZ. DR PANTHER; PTHR11476; PTHR11476; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Reference proteome. FT CHAIN 1 383 ATP phosphoribosyltransferase regulatory FT subunit. FT /FTId=PRO_0000171046. SQ SEQUENCE 383 AA; 41746 MW; 8D8A3F07B94193F2 CRC64; MQTWQLPEHI ADVLPTNARQ LESAREQLLA LFRVHGYELV QPPLMEYAHS LLTHIDAGLS LKTILVTDRL SGRQLGIRAD ITPQVARIDA HLLSANQGIN RLCYAGPVLH AQPDGLLNMR EPLQAGAEMY GFADIRGDIE LIDLMLKSMK IADMGKVLLS LGHIGIFRAL SDAAHLDAGQ SATLLALMQD KDTGAVEAQV KAWKLDGMWA KAFSLLPRLY GGREVLSDAR GRLPDLSAVG GALGELQAVC DAFPDCEIHI DLSELRVDNY HTGLLYAAYA ADFHDAVARG GRYDGLGGYF GRARPATGFS FDLRSFIGRL PAIERQPAVL VDAEDAEAAH EAVEALREQG QCVVIDYGIG HNVSEELAGR LKKTDGVWQV VKR // ID HSLO_NEIMB Reviewed; 302 AA. AC Q9JXK1; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117}; DE AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117}; DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117}; GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; GN OrderedLocusNames=NMB2000; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both CC thermally unfolding and oxidatively damaged proteins from CC irreversible aggregation. Plays an important role in the bacterial CC defense system toward oxidative stress. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed CC involving the reactive cysteines. Under reducing conditions zinc CC is bound to the reactive cysteines and the protein is inactive. CC {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42327.1; -; Genomic_DNA. DR PIR; F81016; F81016. DR RefSeq; NP_274992.1; NC_003112.2. DR RefSeq; WP_010981020.1; NC_003112.2. DR ProteinModelPortal; Q9JXK1; -. DR STRING; 122586.NMB2000; -. DR PaxDb; Q9JXK1; -. DR EnsemblBacteria; AAF42327; AAF42327; NMB2000. DR GeneID; 904125; -. DR KEGG; nme:NMB2000; -. DR PATRIC; 20360099; VBINeiMen85645_2554. DR eggNOG; ENOG4105F4C; Bacteria. DR eggNOG; COG1281; LUCA. DR HOGENOM; HOG000261998; -. DR KO; K04083; -. DR OMA; DMQCECC; -. DR OrthoDB; EOG651SSJ; -. DR BioCyc; NMEN122586:GHGG-2057-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.10.287.480; -; 1. DR Gene3D; 3.55.30.10; -; 1. DR Gene3D; 3.90.1280.10; -; 1. DR HAMAP; MF_00117; HslO; 1. DR InterPro; IPR000397; Heat_shock_Hsp33. DR InterPro; IPR016154; Heat_shock_Hsp33_C. DR InterPro; IPR016153; Heat_shock_Hsp33_N. DR InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom. DR Pfam; PF01430; HSP33; 1. DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1. DR SUPFAM; SSF118352; SSF118352; 1. DR SUPFAM; SSF64397; SSF64397; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Disulfide bond; KW Redox-active center; Reference proteome; Zinc. FT CHAIN 1 302 33 kDa chaperonin. FT /FTId=PRO_0000192187. FT DISULFID 234 236 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. FT DISULFID 267 270 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. SQ SEQUENCE 302 AA; 33205 MW; 2C1CF800E1D0DC26 CRC64; MNQTAINRAD VRTRFIFDDM PVRGLHVRLE NVWQHIVKQK NYPAAIRRAL GELLAAGVLL SGNLKNEGTL IVQVQGRGRL KMLVAEAASD RTVRATARWD ETAEIADDES LGDLLGEGGV FVLTLQPKDG EPWQGVVPLE GGGIAQMLVN YMKRSEQLDT HIVLSASDEA AGGLLVQRLP EEVLDEEAWE HVSTLARTLT AEELAGLDAQ HVLYRLFHET PPRVFEPETF EFSCTCSRGK VSDMLLMLGG EEVGGVVVEQ GSIEVDCDFC HSKYVFDETD VNALFGEDVV GVAKGLPRHT VQ // ID HIS5_NEIMB Reviewed; 212 AA. AC Q9K0H2; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=2.4.2.-; DE AltName: Full=IGP synthase glutamine amidotransferase subunit; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; GN Name=hisH; OrderedLocusNames=NMB0630; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisH subunit provides the glutamine CC amidotransferase activity that produces the ammonia necessary to CC HisF for the synthesis of IGP and AICAR (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41055.1; -; Genomic_DNA. DR PIR; B81177; B81177. DR RefSeq; NP_273673.1; NC_003112.2. DR RefSeq; WP_002225527.1; NC_003112.2. DR ProteinModelPortal; Q9K0H2; -. DR STRING; 122586.NMB0630; -. DR PaxDb; Q9K0H2; -. DR EnsemblBacteria; AAF41055; AAF41055; NMB0630. DR GeneID; 902743; -. DR KEGG; nme:NMB0630; -. DR PATRIC; 20356557; VBINeiMen85645_0798. DR eggNOG; ENOG4108UJE; Bacteria. DR eggNOG; COG0118; LUCA. DR HOGENOM; HOG000025030; -. DR KO; K02501; -. DR OMA; GMQMLLT; -. DR OrthoDB; EOG69KV05; -. DR BioCyc; NMEN122586:GHGG-656-MONOMER; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00278; HisH; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Histidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 212 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152398. FT DOMAIN 2 212 Glutamine amidotransferase type-1. FT ACT_SITE 85 85 Nucleophile. {ECO:0000250}. FT ACT_SITE 194 194 {ECO:0000250}. FT ACT_SITE 196 196 {ECO:0000250}. SQ SEQUENCE 212 AA; 23773 MW; 959B2F21BB5DF77B CRC64; MQTAIIDYGM GNLHSVLKSV RTAGQLAGKN TEIFLSGDPD RVSRADKVIF PGQGAMPDCM AALKRDGLDE AVKDALKNKP FFGICVGAQL LFDHSEEGNT DGLGWFGGKV RRFERDLRDP QGCRLKVPHM GWNTVRQTQN HPLFKDIPQD TRFYFVHSYY FAPENPETIL GESDYPSPFA CIVGKDNVFA TQFHTEKSHD AGLTMLKNFL NW // ID HLDD_NEIMB Reviewed; 334 AA. AC Q9K002; DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE EC=5.1.3.20 {ECO:0000255|HAMAP-Rule:MF_01601}; DE AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=ADP-hep 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=AGME {ECO:0000255|HAMAP-Rule:MF_01601}; GN Name=hldD {ECO:0000255|HAMAP-Rule:MF_01601}; GN OrderedLocusNames=NMB0828; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero- CC beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an CC epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP- CC Rule:MF_01601}. CC -!- CATALYTIC ACTIVITY: ADP-D-glycero-D-manno-heptose = ADP-L-glycero- CC D-manno-heptose. {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- COFACTOR: CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01601}; CC Note=Binds 1 NADP(+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01601}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a CC smaller C-terminal substrate-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01601}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. HldD subfamily. {ECO:0000255|HAMAP-Rule:MF_01601}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41240.1; -; Genomic_DNA. DR PIR; E81152; E81152. DR RefSeq; NP_273870.1; NC_003112.2. DR RefSeq; WP_002225405.1; NC_003112.2. DR ProteinModelPortal; Q9K002; -. DR STRING; 122586.NMB0828; -. DR PaxDb; Q9K002; -. DR EnsemblBacteria; AAF41240; AAF41240; NMB0828. DR GeneID; 902942; -. DR KEGG; nme:NMB0828; -. DR PATRIC; 20357043; VBINeiMen85645_1040. DR eggNOG; ENOG4105CUI; Bacteria. DR eggNOG; COG0451; LUCA. DR HOGENOM; HOG000167987; -. DR KO; K03274; -. DR OMA; KGRYQSF; -. DR OrthoDB; EOG6384GP; -. DR BioCyc; NMEN122586:GHGG-859-MONOMER; -. DR UniPathway; UPA00356; UER00440. DR UniPathway; UPA00976; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01601; Heptose_epimerase; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR011912; Heptose_epim. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR02197; heptose_epim; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; NADP; KW Reference proteome. FT CHAIN 1 334 ADP-L-glycero-D-manno-heptose-6- FT epimerase. FT /FTId=PRO_0000205802. FT NP_BIND 11 12 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT NP_BIND 32 33 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT NP_BIND 77 81 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT REGION 203 206 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT ACT_SITE 141 141 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT ACT_SITE 180 180 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 39 39 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 54 54 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 94 94 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 145 145 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 171 171 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 172 172 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 180 180 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 182 182 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 189 189 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 216 216 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 295 295 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. SQ SEQUENCE 334 AA; 38436 MW; 7CFDE2FF1666BE48 CRC64; MTIIVTGAAG FIGSNIVKAL NQRGITDIVA VDNLSKGEKF KNLAECEIAH YLDKHEFIRQ VREHILPYQN IEAVFHQGAC SDTMNHDGLY MMDNNYQYTL DLLDWCQDER IPFLYASSAA VYGKGEIFRE ERELEKPLNV YGYSKFLFDQ VLRRRMKEGL TAQVVGFRYF NVYGQHEQHK GRMASVAFHH FHQYREHGYV NLFGSNDGYG NGEQTRDFVS VEDVAKVNLY FFDHPELSGI YNLGTGRSQQ FNELAAATVN ACRAAEGKPE MSLKELVEEE LIRYIPFPDA LKGKYQSFTQ ADITKLREAG YKEEFFDVKS GVDRYVKWML ENLA // ID HPRK_NEIMB Reviewed; 320 AA. AC Q9K081; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=HPr kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249}; DE Short=HPrK/P {ECO:0000255|HAMAP-Rule:MF_01249}; DE EC=2.7.11.- {ECO:0000255|HAMAP-Rule:MF_01249}; DE EC=2.7.4.- {ECO:0000255|HAMAP-Rule:MF_01249}; DE AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249}; GN Name=hprK {ECO:0000255|HAMAP-Rule:MF_01249}; GN OrderedLocusNames=NMB0737; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate- CC dependent phosphorylation of a specific serine residue in HPr, a CC phosphocarrier protein of the phosphoenolpyruvate-dependent sugar CC phosphotransferase system (PTS). HprK/P also catalyzes the CC pyrophosphate-producing, inorganic phosphate-dependent CC dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P- CC Ser-HPr). {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr. CC {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01249}; CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi. CC {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried CC out by the same active site and suggest a common mechanism for CC both reactions. {ECO:0000255|HAMAP-Rule:MF_01249}. CC -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000255|HAMAP- CC Rule:MF_01249}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41150.1; -; Genomic_DNA. DR PIR; A81165; A81165. DR RefSeq; NP_273779.1; NC_003112.2. DR RefSeq; WP_002225452.1; NC_003112.2. DR ProteinModelPortal; Q9K081; -. DR STRING; 122586.NMB0737; -. DR PaxDb; Q9K081; -. DR EnsemblBacteria; AAF41150; AAF41150; NMB0737. DR GeneID; 902850; -. DR KEGG; nme:NMB0737; -. DR PATRIC; 20356833; VBINeiMen85645_0937. DR eggNOG; ENOG4105D1C; Bacteria. DR eggNOG; COG1493; LUCA. DR HOGENOM; HOG000099173; -. DR KO; K06023; -. DR OMA; AVRRKMR; -. DR OrthoDB; EOG6F55HT; -. DR BioCyc; NMEN122586:GHGG-766-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1390.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01249; HPr_kinase; 1. DR InterPro; IPR003755; HPr(Ser)_kin/Pase. DR InterPro; IPR011104; Hpr_kin/Pase_C. DR InterPro; IPR011126; Hpr_kin/Pase_Hpr_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR Pfam; PF07475; Hpr_kinase_C; 1. DR Pfam; PF02603; Hpr_kinase_N; 1. DR SUPFAM; SSF75138; SSF75138; 1. DR TIGRFAMs; TIGR00679; hpr-ser; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 320 HPr kinase/phosphorylase. FT /FTId=PRO_0000058976. FT NP_BIND 156 163 ATP. {ECO:0000255|HAMAP-Rule:MF_01249}. FT REGION 204 213 Important for the catalytic mechanism of FT both phosphorylation and FT dephosphorylation. {ECO:0000255|HAMAP- FT Rule:MF_01249}. FT REGION 269 274 Important for the catalytic mechanism of FT dephosphorylation. {ECO:0000255|HAMAP- FT Rule:MF_01249}. FT ACT_SITE 141 141 {ECO:0000255|HAMAP-Rule:MF_01249}. FT ACT_SITE 162 162 {ECO:0000255|HAMAP-Rule:MF_01249}. FT ACT_SITE 180 180 Proton acceptor; for phosphorylation FT activity. Proton donor; for FT dephosphorylation activity. FT {ECO:0000255|HAMAP-Rule:MF_01249}. FT ACT_SITE 248 248 {ECO:0000255|HAMAP-Rule:MF_01249}. FT METAL 163 163 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01249}. FT METAL 205 205 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01249}. SQ SEQUENCE 320 AA; 35800 MW; F57DED8C8DD02A13 CRC64; MPSISVRRLF DDNQYKLQLA WAAGNSGADN RIGVEADKPV LALVGHLNFI HPNQIQVVGL AESEYLNRLE SGETGYQFGD LFDISMSLVI VANGLPVSPG LRDYCHKNDI PLLTSKLESP YLMDVLRIYL QRTLAASSVK HGVFLDVFEI GVLITGHSGL GKSELALELI SRGHSLIADD AVELFRIGPE TLEGRCSPML RDFLEVRGLG ILNIRHIFGE TSIRPKKILQ LIINLVEADD EYMKQLDRLS IRTETESILN VNVRSVTLPV AVGRNLAVLV EAAVRNYILQ LRGKDSTREF LERHQTQLKE NEQHNEDRPD // ID HSCA_NEIMB Reviewed; 620 AA. AC Q9JS04; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679}; GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; GN OrderedLocusNames=NMB1169; GN and GN OrderedLocusNames=NMB1131; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur CC cluster-containing proteins. Has a low intrinsic ATPase activity CC which is markedly stimulated by HscB. {ECO:0000255|HAMAP- CC Rule:MF_00679}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000255|HAMAP-Rule:MF_00679}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41554.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41519.1; -; Genomic_DNA. DR PIR; B81118; B81118. DR RefSeq; NP_274160.1; NC_003112.2. DR RefSeq; NP_274196.1; NC_003112.2. DR RefSeq; WP_002244129.1; NC_003112.2. DR ProteinModelPortal; Q9JS04; -. DR SMR; Q9JS04; 393-619. DR STRING; 122586.NMB1169; -. DR PaxDb; Q9JS04; -. DR EnsemblBacteria; AAF41519; AAF41519; NMB1131. DR EnsemblBacteria; AAF41554; AAF41554; NMB1169. DR GeneID; 903552; -. DR GeneID; 903589; -. DR KEGG; nme:NMB1131; -. DR KEGG; nme:NMB1169; -. DR PATRIC; 20357837; VBINeiMen85645_1434. DR eggNOG; ENOG4105C9I; Bacteria. DR eggNOG; COG0443; LUCA. DR HOGENOM; HOG000228136; -. DR KO; K04044; -. DR OMA; LRGIPAM; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; NMEN122586:GHGG-1167-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1204-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 2.60.34.10; -; 1. DR HAMAP; MF_00679; HscA; 1. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C. DR InterPro; IPR029047; HSP70_peptide-bd. DR InterPro; IPR013126; Hsp_70_fam. DR InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. DR SUPFAM; SSF100934; SSF100934; 1. DR TIGRFAMs; TIGR01991; HscA; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 620 Chaperone protein HscA homolog. FT /FTId=PRO_0000078635. SQ SEQUENCE 620 AA; 66166 MW; 7B4C06AD48AA4E8F CRC64; MALLQISEPG MSAAPHRHRL AAGIDLGTTN SLVATVRSGS AACLPDAEGR VTLPSVVRYL ENGGIEVGKT ALSAQKTDPL NTVSSAKRLI GRTLADLHQN THYLPYRFGD NQRVIELHTR QGVKTPVEVS AEILKTLKSR AEETLGGDLV GVVITVPAYF DDAQRQATKD AARLAGLNVL RLLNEPTAAA IAYGLDNASE GTFVVYDLGG GTFDVSVLQL TKGLFEVKAT GGNSALGGDD FDHRLFCRLL EQNGLSQLNE QDSQLLLSLV RAAKEQLTTQ TEARIQATLS DGMAIDTSIS RAEFHNLTQH LVMKTLEPVT QALKDAGVGK NEVKGVIMVG GSTRMLHVQQ AVATFFGQTP LNNLNPDEVV ALGAAIQANV LAGNKTDGEW LLLDVTPLSL GLETYGGLAE KIIPRNSTIP TARAQDFTTF KDGQTAMTIH VVQGERELVA DCRSLAKFTL RGIPPMAAGA ARIRVTFQID ADGLLSVSAQ EQSTGVQAQI EVKPSYGLDD DTITQMLKDS MSNAAEDMAA RARAEAVVEA ESLTDAVNAA LELDSDLLDA EELQQIRQGI ADLQGRLKDG KAEDIRAAAA KLGSITDNFA AKRMNRNIQR ALTGQSVDNI // ID HIS3_NEIMB Reviewed; 131 AA. AC Q9K0H5; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021}; GN OrderedLocusNames=NMB0627; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- CC ribosylamino)methylideneamino)imidazole-4-carboxamide. CC {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP- CC Rule:MF_01021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41052.1; -; Genomic_DNA. DR PIR; G81176; G81176. DR RefSeq; NP_273670.1; NC_003112.2. DR RefSeq; WP_002225530.1; NC_003112.2. DR ProteinModelPortal; Q9K0H5; -. DR STRING; 122586.NMB0627; -. DR PaxDb; Q9K0H5; -. DR DNASU; 902740; -. DR EnsemblBacteria; AAF41052; AAF41052; NMB0627. DR GeneID; 902740; -. DR KEGG; nme:NMB0627; -. DR PATRIC; 20356551; VBINeiMen85645_0795. DR eggNOG; ENOG4105K8F; Bacteria. DR eggNOG; COG0139; LUCA. DR HOGENOM; HOG000277504; -. DR KO; K01496; -. DR OMA; DDRGLIT; -. DR OrthoDB; EOG6PGKB6; -. DR BioCyc; NMEN122586:GHGG-653-MONOMER; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01021; HisI; 1. DR InterPro; IPR026660; PRA-CH. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR Pfam; PF01502; PRA-CH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 131 Phosphoribosyl-AMP cyclohydrolase. FT /FTId=PRO_0000136489. FT METAL 78 78 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 79 79 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 80 80 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 82 82 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 96 96 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 103 103 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. SQ SEQUENCE 131 AA; 14787 MW; 67803D28AFC625B2 CRC64; MDKNLLEAVK FDEKGLVCAI AQDAETKRIL MVAWMNAEAL QKTVETGFAH YYSRSRQKQW MKGEESGHTQ KVRALRLDCD GDAIVMLIAQ NGGIACHTGR ESCFYKVWRG SAWETADAVL KDEKEIYGST H // ID IF2_NEIMB Reviewed; 962 AA. AC Q9JYD2; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100}; GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; GN OrderedLocusNames=NMB1643; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Protects formylmethionyl-tRNA from spontaneous CC hydrolysis and promotes its binding to the 30S ribosomal subunits. CC Also involved in the hydrolysis of GTP during the formation of the CC 70S ribosomal complex. {ECO:0000255|HAMAP-Rule:MF_00100}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00100}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41992.1; -; Genomic_DNA. DR PIR; C81060; C81060. DR RefSeq; NP_274648.1; NC_003112.2. DR RefSeq; WP_002225000.1; NC_003112.2. DR ProteinModelPortal; Q9JYD2; -. DR STRING; 122586.NMB1643; -. DR PaxDb; Q9JYD2; -. DR PRIDE; Q9JYD2; -. DR EnsemblBacteria; AAF41992; AAF41992; NMB1643. DR GeneID; 903928; -. DR KEGG; nme:NMB1643; -. DR PATRIC; 20359206; VBINeiMen85645_2115. DR eggNOG; ENOG4107QHU; Bacteria. DR eggNOG; COG0532; LUCA. DR HOGENOM; HOG000076907; -. DR KO; K02519; -. DR OMA; KFAVVES; -. DR OrthoDB; EOG67HJSV; -. DR BioCyc; NMEN122586:GHGG-1692-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.10050; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00100_B; IF_2_B; 1. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR000178; TF_IF2_bacterial-like. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF04760; IF2_N; 2. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50447; SSF50447; 2. DR SUPFAM; SSF52156; SSF52156; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00487; IF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. DR PROSITE; PS01176; IF2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Initiation factor; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 962 Translation initiation factor IF-2. FT /FTId=PRO_0000137227. FT DOMAIN 462 631 tr-type G. FT NP_BIND 471 478 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT NP_BIND 517 521 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT NP_BIND 571 574 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT REGION 471 478 G1. {ECO:0000250}. FT REGION 496 500 G2. {ECO:0000250}. FT REGION 517 520 G3. {ECO:0000250}. FT REGION 571 574 G4. {ECO:0000250}. FT REGION 607 609 G5. {ECO:0000250}. SQ SEQUENCE 962 AA; 103143 MW; D7DDBC7A45F89AAC CRC64; MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KNSGSDSLTL DDKQLLNAYL TKKNGSNSST ISIRRTKTEV STVDGVKVET RKRGRTVKIP SAEELAAQVK AAQTQAAPVR PEQTAEDAAK ARAEAAARAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEESKA EKAQADKMPS EKPAEPKEKA AKPKHERNGK GKDAKKPAKP AAPAVPQPVV SAEEQAQRDE EARRAAALRA HQEALLKEKQ ERQARREAMK QQAEQQAKAA QEAKTGRQRP AKPAEKPQAA APAVENKPVN PAKAKKEDRR NRDDEGQGRN AKGKGGKGGR DRNNARNGDD ERVRGGKKGK KLKLEPNQHA FQAPTEPVVH EVLVPETITV ADLAHKMAVK GVEVVKALMK MGMMVTINQS IDQDTALIVV EELGHIGKPA AADDPEAFLD EGAEAVEAEA LPRPPVVTVM GHVDHGKTSL LDYIRRTKVV QGEAGGITQH IGAYHVETPR GVITFLDTPG HEAFTAMRAR GAKATDIVIL VVAADDGVMP QTIEAIAHAK AAGVPMVVAV NKIDKEAANP ERIRQELTAH EVVPDEWGGD VQFIDVSAKK GLNIDALLEA VLLEAEVLEL TAPVDAPAKG IIVEARLDKG RGAVATLLVQ SGTLKKGDML LAGTAFGKIR AMVDENGKSI TEAGPSIPVE ILGLSDVPNA GEDAMVLADE KKAREIALFR QGKYRDVRLA KQQAAKLENM FNNMGETQAQ SLSVIIKADV QGSYEALAGS LKKLSTDEVK VNVLHSGVGG ITESDVNLAI ASGAFIIGFN VRADASSRKL AENENVEIRY YNIIYDAIND VKAAMSGMLS PEEKEQVTGT VEIRQVISVS KVGNIAGCMV TDGVVKRDSH VRLIRNNVVI HTGELASLKR YKDDVKEVRM GFECGLMLKG YNEIMEGDQL ECFDIVEVAR SL // ID IF3_NEIMB Reviewed; 173 AA. AC P65138; Q9JVA2; Q9K094; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080}; GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; GN OrderedLocusNames=NMB0721; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the CC equilibrum between 70S ribosomes and their 50S and 30S subunits in CC favor of the free subunits, thus enhancing the availability of 30S CC subunits on which protein synthesis initiation begins. CC {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP- CC Rule:MF_00080}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41134.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41134.1; ALT_INIT; Genomic_DNA. DR PIR; F81167; F81167. DR RefSeq; NP_273763.1; NC_003112.2. DR ProteinModelPortal; P65138; -. DR SMR; P65138; 6-81, 86-173. DR STRING; 122586.NMB0721; -. DR PaxDb; P65138; -. DR EnsemblBacteria; AAF41134; AAF41134; NMB0721. DR GeneID; 902834; -. DR KEGG; nme:NMB0721; -. DR PATRIC; 20356797; VBINeiMen85645_0919. DR eggNOG; ENOG4108UUX; Bacteria. DR eggNOG; COG0290; LUCA. DR HOGENOM; HOG000035157; -. DR KO; K02520; -. DR OMA; HDFNVKV; -. DR OrthoDB; EOG63JRGJ; -. DR BioCyc; NMEN122586:GHGG-750-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.80; -; 1. DR Gene3D; 3.30.110.10; -; 1. DR HAMAP; MF_00080; IF_3; 1. DR InterPro; IPR019813; Translation_initiation_fac3_CS. DR InterPro; IPR001288; Translation_initiation_fac_3. DR InterPro; IPR019815; Translation_initiation_fac_3_C. DR InterPro; IPR019814; Translation_initiation_fac_3_N. DR PANTHER; PTHR10938; PTHR10938; 1. DR Pfam; PF00707; IF3_C; 1. DR Pfam; PF05198; IF3_N; 1. DR SUPFAM; SSF54364; SSF54364; 1. DR SUPFAM; SSF55200; SSF55200; 1. DR TIGRFAMs; TIGR00168; infC; 1. DR PROSITE; PS00938; IF3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 173 Translation initiation factor IF-3. FT /FTId=PRO_0000177549. SQ SEQUENCE 173 AA; 19779 MW; 201427899834382E CRC64; MIAQEREARI NGEITAKEVR LISESGEQLG VVSVREALAM AEGQDVDLVE ISPTAKPPVC KLMDYGKYKY QQAKKRDEAK KNQKQVQIKE IKFRPGTDEG DYQIKMRNIN RFLADGDKVK VTLRFRGREM AHQQLGAQLL ERVKEDLAEV AQIESFPKME GRQMVMMIAP KKK // ID IHFA_NEIMB Reviewed; 100 AA. AC P64393; Q9JR90; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Integration host factor subunit alpha; DE Short=IHF-alpha; GN Name=ihfA; Synonyms=himA; OrderedLocusNames=NMB0729; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein is one of the two subunits of integration CC host factor, a specific DNA-binding protein that functions in CC genetic recombination as well as in transcriptional and CC translational control. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41142.1; -; Genomic_DNA. DR PIR; D81166; D81166. DR RefSeq; NP_273771.1; NC_003112.2. DR RefSeq; WP_002214080.1; NC_003112.2. DR ProteinModelPortal; P64393; -. DR SMR; P64393; 3-94. DR STRING; 122586.NMB0729; -. DR PaxDb; P64393; -. DR EnsemblBacteria; AAF41142; AAF41142; NMB0729. DR GeneID; 902842; -. DR KEGG; nme:NMB0729; -. DR PATRIC; 20356813; VBINeiMen85645_0927. DR eggNOG; ENOG4108ZUF; Bacteria. DR eggNOG; COG0776; LUCA. DR HOGENOM; HOG000043829; -. DR KO; K04764; -. DR OMA; FDLRDKK; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NMEN122586:GHGG-758-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 4.10.520.10; -; 1. DR HAMAP; MF_00380; IHF_alpha; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR InterPro; IPR005684; IHF_alpha. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR TIGRFAMs; TIGR00987; himA; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transcription; Transcription regulation; Translation regulation. FT CHAIN 1 100 Integration host factor subunit alpha. FT /FTId=PRO_0000105014. SQ SEQUENCE 100 AA; 11422 MW; 4ADE0C995A1CF982 CRC64; MTLTKAELAD ILVDKVSNVT KNDAKEIVEL FFEEIRSTLA SGEEIKISGF GNFQLRDKPQ RPGRNPKTGE EVPITARRVV TFHASQKLKS MVEHYYDKQR // ID HTPX_NEIMB Reviewed; 279 AA. AC Q9K006; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 13-APR-2016, entry version 98. DE RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188}; GN Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; GN OrderedLocusNames=NMB0822; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00188}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00188}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00188}. CC -!- SIMILARITY: Belongs to the peptidase M48B family. CC {ECO:0000255|HAMAP-Rule:MF_00188}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41235.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41235.1; ALT_INIT; Genomic_DNA. DR PIR; E81154; E81154. DR RefSeq; NP_273864.1; NC_003112.2. DR ProteinModelPortal; Q9K006; -. DR SMR; Q9K006; 58-158. DR STRING; 122586.NMB0822; -. DR MEROPS; M48.002; -. DR PaxDb; Q9K006; -. DR EnsemblBacteria; AAF41235; AAF41235; NMB0822. DR GeneID; 902937; -. DR KEGG; nme:NMB0822; -. DR PATRIC; 20357029; VBINeiMen85645_1033. DR eggNOG; ENOG4105D0M; Bacteria. DR eggNOG; COG0501; LUCA. DR HOGENOM; HOG000227302; -. DR KO; K03799; -. DR OMA; QHNSMAG; -. DR OrthoDB; EOG6F55J5; -. DR BioCyc; NMEN122586:GHGG-853-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00188; Pept_M48_protease_HtpX; 1. DR InterPro; IPR022919; Pept_M48_protease_HtpX. DR InterPro; IPR001915; Peptidase_M48. DR Pfam; PF01435; Peptidase_M48; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 279 Protease HtpX homolog. FT /FTId=PRO_0000138878. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 34 54 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 155 175 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 189 209 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT ACT_SITE 141 141 {ECO:0000255|HAMAP-Rule:MF_00188}. FT METAL 140 140 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 144 144 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 215 215 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. SQ SEQUENCE 279 AA; 30202 MW; 71348DCD6CADD15E CRC64; MKRIFLFLAT NIAVLVVINI VLAVLGINSR GGTGSLLAYS AVVGFTGSII SLLMSKFIAK QSVGAEVIDT PRTEEEAWLL NTVEAQARQW NLKTPEVAIY HSPEPNAFAT GASRNSSLIA VSTGLLDHMT RDEVEAVLAH EMAHVGNGDM VTLTLIQGVV NTFVVFLSRI IANLIARNND GSQSQGTYFL VSMVFQILFG FLASLIVMWF SRQREYRADA GAAKLVGAPK MISALQRLKG NPVDLPEEMN AMGIAGDTRD SLLSTHPSLD NRIARLKSL // ID ILVC_NEIMB Reviewed; 337 AA. AC Q9JYI2; Q9X5I7; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase; GN Name=ilvC; OrderedLocusNames=NMB1574; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CDC 8201085 / NMB / Serogroup B; RA Kahler C.M., Stephens D.S.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF125563; AAD32178.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41927.1; -; Genomic_DNA. DR PIR; F81066; F81066. DR RefSeq; NP_274580.1; NC_003112.2. DR RefSeq; WP_002218988.1; NC_003112.2. DR ProteinModelPortal; Q9JYI2; -. DR SMR; Q9JYI2; 1-326. DR STRING; 122586.NMB1574; -. DR PaxDb; Q9JYI2; -. DR EnsemblBacteria; AAF41927; AAF41927; NMB1574. DR GeneID; 904172; -. DR KEGG; nme:NMB1574; -. DR PATRIC; 20359012; VBINeiMen85645_2025. DR eggNOG; ENOG4105C6M; Bacteria. DR eggNOG; COG0059; LUCA. DR HOGENOM; HOG000016230; -. DR KO; K00053; -. DR OMA; EPNIKQG; -. DR OrthoDB; EOG625K07; -. DR BioCyc; NMEN122586:GHGG-1615-MONOMER; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 337 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151332. FT ACT_SITE 106 106 {ECO:0000255}. FT CONFLICT 294 294 N -> G (in Ref. 1; AAD32178). FT {ECO:0000305}. SQ SEQUENCE 337 AA; 36438 MW; D10814C7CCCB83A3 CRC64; MQVYYDKDAD LSLIKGKTVA IIGYGSQGHA HAANLKDSGV NVVIGLRQGS SWKKAEAAGH VVKTVAEATK EADVVMLLLP DETMPAVYHA EVTANLKEGA TLAFAHGFNV HYNQIVPRAD LDVIMVAPKG PGHTVRSEYK RGGGVPSLIA VYQDNSGKAK DIALSYAAAN GGTKGGVIET TFREETETDL FGEQAVLCGG VVELIKAGFE TLTEAGYAPE MAYFECLHEM KLIVDLIFEG GIANMNYSIS NNAEYGEYVT GPEVVNASSK EAMRNALKRI QTGEYAKMFI QEGNVNYASM TARRRLNADH QVEKVGAQLR AMMPWITANK LVDQDKN // ID IHFB_NEIMB Reviewed; 104 AA. AC P0A0U2; Q9JRH3; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Integration host factor subunit beta; DE Short=IHF-beta; GN Name=ihfB; Synonyms=himD, hip; OrderedLocusNames=NMB1302; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein is one of the two subunits of integration CC host factor, a specific DNA-binding protein that functions in CC genetic recombination as well as in transcriptional and CC translational control. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41677.1; -; Genomic_DNA. DR PIR; H81099; H81099. DR RefSeq; NP_274321.1; NC_003112.2. DR RefSeq; WP_002213349.1; NC_003112.2. DR ProteinModelPortal; P0A0U2; -. DR SMR; P0A0U2; 45-97. DR STRING; 122586.NMB1302; -. DR PaxDb; P0A0U2; -. DR EnsemblBacteria; AAF41677; AAF41677; NMB1302. DR GeneID; 903724; -. DR KEGG; nme:NMB1302; -. DR PATRIC; 20358245; VBINeiMen85645_1634. DR eggNOG; ENOG41080YA; Bacteria. DR eggNOG; COG0776; LUCA. DR HOGENOM; HOG000043828; -. DR KO; K05788; -. DR OMA; RDRVNIY; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NMEN122586:GHGG-1340-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 4.10.520.10; -; 1. DR HAMAP; MF_00381; IHF_beta; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR InterPro; IPR005685; IHF_beta. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR TIGRFAMs; TIGR00988; hip; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transcription; Transcription regulation; Translation regulation. FT CHAIN 1 104 Integration host factor subunit beta. FT /FTId=PRO_0000105056. SQ SEQUENCE 104 AA; 11804 MW; 12DFA7350CDCBD8D CRC64; MTKSELMVRL AEVFAAKNGT HLLAKDVEYS VKVLVDTMTR SLARGQRIEI RGFGSFDLNH RPARIGRNPK TGERVEVPEK HVPHFKPGKE LRERVDLALK ENAN // ID IF1_NEIMB Reviewed; 72 AA. AC P65113; Q9JR12; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; GN OrderedLocusNames=NMB0163; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the CC 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently CC binds. Helps modulate mRNA selection, yielding the 30S pre- CC initiation complex (PIC). Upon addition of the 50S ribosomal CC subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S CC translation initation complex. {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation CC complex which assembles on the 30S ribosome in the order IF-2 and CC IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can CC occur at any time during PIC assembly. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SIMILARITY: Contains 1 S1-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40621.1; -; Genomic_DNA. DR PIR; E81233; E81233. DR RefSeq; NP_273221.1; NC_003112.2. DR RefSeq; WP_002215452.1; NC_003112.2. DR ProteinModelPortal; P65113; -. DR SMR; P65113; 2-72. DR STRING; 122586.NMB0163; -. DR PaxDb; P65113; -. DR EnsemblBacteria; AAF40621; AAF40621; NMB0163. DR GeneID; 23781882; -. DR GeneID; 902270; -. DR KEGG; nme:NMB0163; -. DR PATRIC; 20355349; VBINeiMen85645_0204. DR eggNOG; ENOG4105K9U; Bacteria. DR eggNOG; COG0361; LUCA. DR HOGENOM; HOG000221323; -. DR KO; K02518; -. DR OMA; HHITILR; -. DR OrthoDB; EOG6384SC; -. DR BioCyc; NMEN122586:GHGG-173-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00075; IF_1; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006196; RNA-binding_domain_S1_IF1. DR InterPro; IPR004368; TIF_IF1. DR Pfam; PF01176; eIF-1a; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00008; infA; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1 72 Translation initiation factor IF-1. FT /FTId=PRO_0000095833. FT DOMAIN 1 72 S1-like. {ECO:0000255|HAMAP- FT Rule:MF_00075}. SQ SEQUENCE 72 AA; 8295 MW; 7FA8CE16D8309FA7 CRC64; MAKEDTIQMQ GEILETLPNA TFKVKLENDH IVLGHISGKM RMHYIRISPG DKVTVELTPY DLTRARIVFR AR // ID ISCS_NEIMB Reviewed; 404 AA. AC Q9JYY0; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331}; DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331}; GN Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331}; GN OrderedLocusNames=NMB1379; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Master enzyme that delivers sulfur to a number of CC partners involved in Fe-S cluster assembly, tRNA modification or CC cofactor biosynthesis. Catalyzes the removal of elemental sulfur CC atoms from cysteine to produce alanine. Functions as a sulfur CC delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S CC scaffold assembly protein, as well as other S acceptor proteins. CC {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S- CC sulfanyl-acceptor. {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00331}; CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, interacts CC with other sulfur acceptors. {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00331}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62329.1; -; Genomic_DNA. DR RefSeq; NP_274395.1; NC_003112.2. DR RefSeq; WP_010980928.1; NC_003112.2. DR ProteinModelPortal; Q9JYY0; -. DR SMR; Q9JYY0; 4-391. DR STRING; 122586.NMB1379; -. DR PaxDb; Q9JYY0; -. DR PRIDE; Q9JYY0; -. DR EnsemblBacteria; AAF62329; AAF62329; NMB1379. DR GeneID; 903801; -. DR KEGG; nme:NMB1379; -. DR PATRIC; 20358435; VBINeiMen85645_1729. DR eggNOG; ENOG4105C3J; Bacteria. DR eggNOG; COG1104; LUCA. DR HOGENOM; HOG000017510; -. DR KO; K04487; -. DR OMA; EPIQSGG; -. DR OrthoDB; EOG62RSBK; -. DR BioCyc; NMEN122586:GHGG-1417-MONOMER; -. DR UniPathway; UPA00266; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00331; Cys_desulf_IscS; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR010240; Cys_deSase_IscS. DR InterPro; IPR016454; Cysteine_dSase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF005572; NifS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR02006; IscS; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 404 Cysteine desulfurase IscS. FT /FTId=PRO_0000150272. FT REGION 75 76 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT REGION 203 205 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT ACT_SITE 328 328 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT METAL 328 328 Iron-sulfur (2Fe-2S); via persulfide FT group; shared with IscU. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT BINDING 155 155 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT BINDING 183 183 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT BINDING 243 243 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT MOD_RES 206 206 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00331}. SQ SEQUENCE 404 AA; 44647 MW; E8C4360B91FBFE68 CRC64; MTVKTPVYLD YAATPPVDKR VAEKMIPYLT ETFGNPASNS HSFGWEAEEA VEKARADIAA LINADSKEIV FTSGATESNN LAIKGAAHFY KSKGNHLITV KTEHKAVLDT MRELERQGYE VTYLDVQENG LVDLDVLKAA IREDTILVSV MWVNNEIGVV QDIPAIGEIC RERKIIFHVD AAQACGKVPV DVEAAKVDLL SMSGHKVYGP KGIGALYVRR KPRVRLEAQM HGGGHERGFR SGTLPTHQIV GMGEAFRIAK EELAQDTAHY LKLRDIFLKG IEGIEEVYIN GDLEHRVPNN LNVSFNFVEG ESLIMAVKEL AVSSGSACTS ASLEPSYVLR ALGRNDELAH SSLRITFGRM TTEEEVQFAA ELIKSKIGKL RELSPLWEMF KDGIDLNSIE WAAH // ID ISPF_NEIMB Reviewed; 160 AA. AC Q9JYM5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPS {ECO:0000255|HAMAP-Rule:MF_00107}; DE EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_00107}; GN Name=ispF {ECO:0000255|HAMAP-Rule:MF_00107}; GN OrderedLocusNames=NMB1512; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate CC (IPP) and dimethylallyl diphosphate (DMAPP), two major building CC blocks of isoprenoid compounds. Catalyzes the conversion of 4- CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to CC 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a CC corresponding release of cytidine 5-monophosphate (CMP). CC {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C- CC methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate CC + CMP. {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00107}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00107}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000255|HAMAP- CC Rule:MF_00107}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000255|HAMAP- CC Rule:MF_00107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41868.1; -; Genomic_DNA. DR PIR; G81073; G81073. DR RefSeq; NP_274520.1; NC_003112.2. DR RefSeq; WP_002218386.1; NC_003112.2. DR ProteinModelPortal; Q9JYM5; -. DR SMR; Q9JYM5; 3-159. DR STRING; 122586.NMB1512; -. DR PaxDb; Q9JYM5; -. DR EnsemblBacteria; AAF41868; AAF41868; NMB1512. DR GeneID; 903980; -. DR KEGG; nme:NMB1512; -. DR PATRIC; 20358812; VBINeiMen85645_1916. DR eggNOG; ENOG4108UH8; Bacteria. DR eggNOG; COG0245; LUCA. DR HOGENOM; HOG000239175; -. DR KO; K01770; -. DR OMA; IRIGNGY; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NMEN122586:GHGG-1552-MONOMER; -. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.50; -; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. DR TIGRFAMs; TIGR00151; ispF; 1. DR PROSITE; PS01350; ISPF; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 160 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT /FTId=PRO_0000189487. FT REGION 11 13 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 37 38 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 41 49 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 59 61 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT METAL 11 11 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT METAL 13 13 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT METAL 45 45 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT BINDING 145 145 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT SITE 37 37 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT SITE 136 136 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00107}. SQ SEQUENCE 160 AA; 17020 MW; 9C223BCED4D9BF3D CRC64; MTNIRIGQGY DVHQLTEGRK LILGGVEIPF EKGLLGHSDA DALLHAVTDA LLGAAGLGDI GSHFPDTAAE FKDADSRVLL RAAYQSVQAQ GWQAVNVDTT VIAQKPKLAP HIPQMRANIA ADLGIDISCV NIKGKTNEKL GYLGRMEGIE AQAAVLLVRI // ID ILVD_NEIMB Reviewed; 619 AA. AC Q9JS61; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD1 {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=NMB1150; GN and GN Name=ilvD2 {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=NMB1188; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- CC oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41537.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41572.1; -; Genomic_DNA. DR PIR; E81117; E81117. DR RefSeq; NP_274178.1; NC_003112.2. DR RefSeq; NP_274214.1; NC_003112.2. DR RefSeq; WP_002244135.1; NC_003112.2. DR STRING; 122586.NMB1188; -. DR PaxDb; Q9JS61; -. DR PRIDE; Q9JS61; -. DR EnsemblBacteria; AAF41537; AAF41537; NMB1150. DR EnsemblBacteria; AAF41572; AAF41572; NMB1188. DR GeneID; 903571; -. DR GeneID; 903608; -. DR KEGG; nme:NMB1150; -. DR KEGG; nme:NMB1188; -. DR PATRIC; 20357879; VBINeiMen85645_1455. DR eggNOG; ENOG4105C01; Bacteria. DR eggNOG; COG0129; LUCA. DR HOGENOM; HOG000173155; -. DR KO; K01687; -. DR OMA; QGRNMAG; -. DR OrthoDB; EOG6MSS24; -. DR BioCyc; NMEN122586:GHGG-1186-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1223-MONOMER; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR004404; DihydroxyA_deHydtase. DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR PANTHER; PTHR21000; PTHR21000; 2. DR Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00110; ilvD; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Lyase; Metal-binding; Reference proteome. FT CHAIN 1 619 Dihydroxy-acid dehydratase. FT /FTId=PRO_0000103484. FT METAL 122 122 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. FT METAL 198 198 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. SQ SEQUENCE 619 AA; 66786 MW; 1346AE03A24DD58F CRC64; MPEYRSKTST HGRNMAGARA LWRATGVMET DFGKPIIAVA NSFTQFVPGH VHLHNMGQLV AREIEKAGAI AKEFNTIAID DGIAMGHSGM LYSLPSRDLI ADSIEYMVNA HCADALVCIS NCDKITPGML IAAMRLNIPT IFVSGGPMEA GKVIGVANIQ PERRLDLIDA MIESADDNVS NRQVEEVEQN ACPTCGSCSG MFTANSMNCL TEALGLSLPG NGSYLATHAG RKELFLEAGR MIVEITKRYY EQNDETVLPR SIATKKAFEN AMTMDIAMGG STNTILHLLA VANEAGVDFK MADIDRLSRV VPCICKTAPN NHDYYMEDVH RAGGIFAILK ELDKAGKLHT DVHTIHAPTL KDAIEQWDVT NPENTRAIER FKAAPGGVRT TQAFSQNRMW KTLDLDREKG CIRDVAHAYS QDGGLAVLFG NIAERGCVVK TAGVDESILK FTGRARVFES QEDAVEGILG NQIVAGDIVI IRYEGPKGGP GMQEMLYPTS YLKSKGLGKA CALLTDGRFS GGTSGLSIGH ASPEAAEGGA IGLVHEGDTV EIDIPNRSIH LAISDEELAA RRAEMEARGS KAWKPKNRDR YVSAALRAYG AMATSADKGA VRDVAQIER // ID IPYR_NEIMB Reviewed; 177 AA. AC Q9K0G4; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209}; DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209}; DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209}; DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209}; GN Name=ppa {ECO:0000255|HAMAP-Rule:MF_00209}; OrderedLocusNames=NMB0641; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00209}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209}; CC Note=Binds 4 Mg(2+) ions per subunit. Other metal ions can support CC activity, but at a lower rate. Two Mg(2+) ions are required for CC the activation of the enzyme and are present before substrate CC binds, two additional Mg(2+) ions form complexes with substrate CC and product. {ECO:0000255|HAMAP-Rule:MF_00209}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}. CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP- CC Rule:MF_00209}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41064.1; -; Genomic_DNA. DR PIR; F81175; F81175. DR RefSeq; NP_273684.1; NC_003112.2. DR RefSeq; WP_002219633.1; NC_003112.2. DR ProteinModelPortal; Q9K0G4; -. DR STRING; 122586.NMB0641; -. DR PaxDb; Q9K0G4; -. DR EnsemblBacteria; AAF41064; AAF41064; NMB0641. DR GeneID; 902752; -. DR KEGG; nme:NMB0641; -. DR PATRIC; 20356581; VBINeiMen85645_0810. DR eggNOG; ENOG4105F0N; Bacteria. DR eggNOG; COG0221; LUCA. DR HOGENOM; HOG000236472; -. DR KO; K01507; -. DR OMA; SEVEYFF; -. DR OrthoDB; EOG6NKR4X; -. DR BioCyc; NMEN122586:GHGG-667-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.90.80.10; -; 1. DR HAMAP; MF_00209; Inorganic_PPase; 1. DR InterPro; IPR008162; Pyrophosphatase. DR PANTHER; PTHR10286; PTHR10286; 1. DR Pfam; PF00719; Pyrophosphatase; 1. DR SUPFAM; SSF50324; SSF50324; 1. DR PROSITE; PS00387; PPASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 177 Inorganic pyrophosphatase. FT /FTId=PRO_0000137515. FT METAL 67 67 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00209}. FT METAL 72 72 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00209}. FT METAL 72 72 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00209}. FT METAL 104 104 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00209}. SQ SEQUENCE 177 AA; 19811 MW; 6017182C446A8567 CRC64; MADFNQILTP GDVDGGIINV VNEIPAGSNH KIEWNRKLAA FQLDRVEPAI FAKPTNYGFI PQTLDEDGDE LDVLLVTEQP LATGVFLEAR VIGVMKFVDD GEVDDKIVCV PADDRNNGNA YKTLSDLPQQ LIKQIEFHFN HYKDLKKAGT TKVESWGDAE EAKKVIKESI ERWNKQA // ID ISPD_NEIMB Reviewed; 229 AA. AC Q9JYM4; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108}; DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108}; DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108}; DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108}; DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108}; GN Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; GN OrderedLocusNames=NMB1513; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C- CC methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4- CC phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}. CC -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate = CC diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. CC {ECO:0000255|HAMAP-Rule:MF_00108}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000255|HAMAP- CC Rule:MF_00108}. CC -!- SIMILARITY: Belongs to the IspD family. {ECO:0000255|HAMAP- CC Rule:MF_00108}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41869.1; -; Genomic_DNA. DR PIR; H81073; H81073. DR RefSeq; NP_274521.1; NC_003112.2. DR RefSeq; WP_002225068.1; NC_003112.2. DR ProteinModelPortal; Q9JYM4; -. DR SMR; Q9JYM4; 1-227. DR STRING; 122586.NMB1513; -. DR PaxDb; Q9JYM4; -. DR EnsemblBacteria; AAF41869; AAF41869; NMB1513. DR GeneID; 903982; -. DR KEGG; nme:NMB1513; -. DR PATRIC; 20358814; VBINeiMen85645_1917. DR eggNOG; ENOG4105CE5; Bacteria. DR eggNOG; COG1211; LUCA. DR HOGENOM; HOG000218564; -. DR KO; K00991; -. DR OMA; QAYTPQM; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NMEN122586:GHGG-1553-MONOMER; -. DR UniPathway; UPA00056; UER00093. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00108; IspD; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR018294; ISPD_synthase_CS. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00453; ispD; 1. DR PROSITE; PS01295; ISPD; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 229 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. FT /FTId=PRO_0000075594. FT SITE 17 17 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00108}. FT SITE 24 24 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00108}. FT SITE 158 158 Positions MEP for the nucleophilic FT attack. {ECO:0000255|HAMAP- FT Rule:MF_00108}. FT SITE 212 212 Positions MEP for the nucleophilic FT attack. {ECO:0000255|HAMAP- FT Rule:MF_00108}. SQ SEQUENCE 229 AA; 24561 MW; 3569A7721486AB33 CRC64; MKRKNIALIP AAGIGARFGA DKPKQYVEIG SKTVLEHTIG IFERHEAVDL TVVVVSPEDT FADKVQTAFP QVRVWKNGGQ TRAETVRNGV AKLLETGLAA ETDNILVHDA ARCCLPSEAL TRLIEQAGNA AEGGILAIPI ADTLKCADGG NISATVERTS LWQAQTPQLF RAGLLHRALA AENLDGITDE ASAVEKLGVR PLLIQGDVRN LKLTQPQDAY IVRLLLDAV // ID ISPH_NEIMB Reviewed; 322 AA. AC P65192; Q9JR39; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; Synonyms=lytB; GN OrderedLocusNames=NMB1831; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate CC (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00191}; CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3- CC methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42166.1; -; Genomic_DNA. DR PIR; D81038; D81038. DR RefSeq; NP_274828.1; NC_003112.2. DR RefSeq; WP_002221497.1; NC_003112.2. DR STRING; 122586.NMB1831; -. DR PaxDb; P65192; -. DR EnsemblBacteria; AAF42166; AAF42166; NMB1831. DR GeneID; 903269; -. DR KEGG; nme:NMB1831; -. DR PATRIC; 20359651; VBINeiMen85645_2331. DR eggNOG; ENOG4105C48; Bacteria. DR eggNOG; COG0761; LUCA. DR HOGENOM; HOG000220192; -. DR KO; K03527; -. DR OMA; DDLTFMT; -. DR OrthoDB; EOG6HF624; -. DR BioCyc; NMEN122586:GHGG-1886-MONOMER; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 3Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 322 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase. FT /FTId=PRO_0000128845. FT REGION 226 228 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 15 15 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 99 99 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 198 198 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 44 44 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 127 127 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 168 168 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 270 270 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. SQ SEQUENCE 322 AA; 35322 MW; 6E92762C0653D78F CRC64; MNEKTIILAN PRGFCAGVDR AISIVERALE EFGAPIYVRH EVVHNKFVVD NLREKGAVFI EDLAEVPPGA TLVYSAHGVS KAVRQEAAER GFRVFDATCP LVTKVHKEVA RLDAQDCEII MIGHKGHVEV EGTMGQLAPG KMLLVETVGD VAKLEVRNPD KLAYVSQTTL SVDETKDIIA ALNARFPNIR NPHKEDICYA TTNRQTAVKE LAEQCDIVIV VGSPNSSNSN RLREVAASRG IDAYMVDNAG YLQRAWFEGK NKVGVTAGAS APEVLVREVL ATIRGWGHET VREGEGAEES IVFVLPKELR REGETKPDLC KR // ID ISPT_NEIMB Reviewed; 248 AA. AC Q9K1G6; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Isoprenyl transferase {ECO:0000255|HAMAP-Rule:MF_01139}; DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139}; GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; GN OrderedLocusNames=NMB0186; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate CC (IPP) with allylic pyrophosphates generating different type of CC terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01139}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- SIMILARITY: Belongs to the UPP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01139}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40643.1; -; Genomic_DNA. DR PIR; C81229; C81229. DR RefSeq; NP_273244.1; NC_003112.2. DR RefSeq; WP_002218592.1; NC_003112.2. DR ProteinModelPortal; Q9K1G6; -. DR STRING; 122586.NMB0186; -. DR PaxDb; Q9K1G6; -. DR EnsemblBacteria; AAF40643; AAF40643; NMB0186. DR GeneID; 902293; -. DR KEGG; nme:NMB0186; -. DR PATRIC; 20355397; VBINeiMen85645_0228. DR eggNOG; ENOG4105CR3; Bacteria. DR eggNOG; COG0020; LUCA. DR HOGENOM; HOG000006054; -. DR KO; K00806; -. DR OMA; WNRPKLE; -. DR OrthoDB; EOG68H89T; -. DR BioCyc; NMEN122586:GHGG-196-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1180.10; -; 1. DR HAMAP; MF_01139; ISPT; 1. DR InterPro; IPR001441; UPP_synth-like. DR InterPro; IPR018520; UPP_synth-like_CS. DR PANTHER; PTHR10291; PTHR10291; 1. DR Pfam; PF01255; Prenyltransf; 1. DR SUPFAM; SSF64005; SSF64005; 1. DR TIGRFAMs; TIGR00055; uppS; 1. DR PROSITE; PS01066; UPP_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1 248 Isoprenyl transferase. FT /FTId=PRO_0000123644. FT REGION 24 27 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 68 70 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 191 193 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT ACT_SITE 23 23 {ECO:0000255|HAMAP-Rule:MF_01139}. FT ACT_SITE 71 71 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 23 23 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 204 204 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 28 28 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 36 36 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 40 40 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 72 72 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 74 74 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 185 185 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. SQ SEQUENCE 248 AA; 28344 MW; 74818515BD2A32C8 CRC64; MKSSTQAVLE HTAIPKHIAV IMDGNGRWAK KRFLPRIMGH KRGLDALENM VKHCAKLGVQ YLTVFAFSTE NWRRPEDEVS FLMGLFLQAL QKQVRRLHEN NMRLKILGSR ERFNRQILQG IEEAEALTAN NTGLTLSIAA DYGGRWDILQ AANKLIAEGV SEITEDTLAK HLMLGDAPEP DLFIRTGGET RISNFLLWQM AYAELYFTDI LWPDFDGKAL DDAVASFQKR ERRFGRTSEQ LPIEQQRN // ID KCY_NEIMB Reviewed; 218 AA. AC P57065; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00238}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238}; GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=NMB1300; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00238}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41675.1; -; Genomic_DNA. DR PIR; F81099; F81099. DR RefSeq; NP_274319.1; NC_003112.2. DR RefSeq; WP_002224491.1; NC_003112.2. DR ProteinModelPortal; P57065; -. DR STRING; 122586.NMB1300; -. DR PaxDb; P57065; -. DR EnsemblBacteria; AAF41675; AAF41675; NMB1300. DR GeneID; 903722; -. DR KEGG; nme:NMB1300; -. DR PATRIC; 20358241; VBINeiMen85645_1632. DR eggNOG; ENOG4105CAT; Bacteria. DR eggNOG; COG0283; LUCA. DR HOGENOM; HOG000242849; -. DR KO; K00945; -. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NMEN122586:GHGG-1338-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kinase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02224; Cytidylate_kin; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00017; cmk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 218 Cytidylate kinase. FT /FTId=PRO_0000131945. FT NP_BIND 11 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 218 AA; 23762 MW; 3BC860899CD36845 CRC64; MNRQKVIAID GPGASGKGTV AARVAAALGY DYLDTGALYR LTALYAQKQG VGWHDEENVS ELAKKLPAVF SGSRILLGGE DVSDGIRTEA IGMGASAVAQ LPKVRAALLQ RQRDFLTEKG LVADGRDTGS VVFPQAELKI FLTAESKIRA ERRAKQIGIP CEGLAFERIL SDIEARDEAD RNRKVAPLKQ QPDALLLDTS RLTIEETVKK VLDWYREV // ID ISPE_NEIMB Reviewed; 281 AA. AC Q9JZW4; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061}; DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061}; DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; GN OrderedLocusNames=NMB0874; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy CC group of 4-diphosphocytidyl-2C-methyl-D-erythritol. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D- CC erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl- CC D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000255|HAMAP- CC Rule:MF_00061}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41285.1; -; Genomic_DNA. DR PIR; B81149; B81149. DR RefSeq; NP_273915.1; NC_003112.2. DR RefSeq; WP_002222667.1; NC_003112.2. DR ProteinModelPortal; Q9JZW4; -. DR STRING; 122586.NMB0874; -. DR PaxDb; Q9JZW4; -. DR EnsemblBacteria; AAF41285; AAF41285; NMB0874. DR GeneID; 902990; -. DR KEGG; nme:NMB0874; -. DR PATRIC; 20357147; VBINeiMen85645_1090. DR eggNOG; ENOG4105CTR; Bacteria. DR eggNOG; COG1947; LUCA. DR HOGENOM; HOG000019601; -. DR KO; K00919; -. DR OMA; RWPSPAK; -. DR OrthoDB; EOG62VNQ2; -. DR BioCyc; NMEN122586:GHGG-907-MONOMER; -. DR UniPathway; UPA00056; UER00094. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00061; IspE; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR004424; IspE. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR20861:SF2; PTHR20861:SF2; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF010376; IspE; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00154; ispE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 281 4-diphosphocytidyl-2-C-methyl-D- FT erythritol kinase. FT /FTId=PRO_0000189238. FT NP_BIND 98 108 ATP. {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 15 15 {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 140 140 {ECO:0000255|HAMAP-Rule:MF_00061}. SQ SEQUENCE 281 AA; 31316 MW; FBFA5216CC2B7703 CRC64; MNIADGRQAF SAPAKLNLDL RITGRREDGY HNIESIFCLI DLQDTVYLKP RDDGKIILHN PVDGMPQEVD LSYRAASLLQ KYARNPAGVE IWLDKKIPTG AGLGGGSSDA ATVLLVLNRW WQCGLTQRQL IDSGAALGAD VPFFIFGKNA FARGIGDRLD EMDIPKQWYV IVKPPVHVST AKIFTHESLT RNSASSIMPT FQNLQPFRND MQAVVFKEYP EVWKAYSELS RYGFALMTGS GACVFTACQD RNSAYNIYRQ VSDLYEAYLA EGLSKHPLLS V // ID ISPG_NEIMB Reviewed; 421 AA. AC Q9JZ40; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000255|HAMAP-Rule:MF_00159}; DE EC=1.17.7.3 {ECO:0000255|HAMAP-Rule:MF_00159}; DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00159}; GN Name=ispG {ECO:0000255|HAMAP-Rule:MF_00159}; GN OrderedLocusNames=NMB1310; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- CATALYTIC ACTIVITY: (E)-4-hydroxy-3-methylbut-2-en-1-yl CC diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D- CC erythritol 2,4-cyclodiphosphate + reduced flavodoxin. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 5/6. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41685.1; -; Genomic_DNA. DR PIR; D81098; D81098. DR RefSeq; NP_274329.1; NC_003112.2. DR RefSeq; WP_002227267.1; NC_003112.2. DR ProteinModelPortal; Q9JZ40; -. DR STRING; 122586.NMB1310; -. DR PaxDb; Q9JZ40; -. DR EnsemblBacteria; AAF41685; AAF41685; NMB1310. DR GeneID; 903732; -. DR KEGG; nme:NMB1310; -. DR PATRIC; 20358265; VBINeiMen85645_1644. DR eggNOG; ENOG4105C4E; Bacteria. DR eggNOG; COG0821; LUCA. DR HOGENOM; HOG000261017; -. DR KO; K03526; -. DR OMA; HNGMKIA; -. DR OrthoDB; EOG67Q96Z; -. DR BioCyc; NMEN122586:GHGG-1348-MONOMER; -. DR UniPathway; UPA00056; UER00096. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00159; IspG; 1. DR InterPro; IPR016425; IspG_bac. DR InterPro; IPR004588; IspG_bac-typ. DR Pfam; PF04551; GcpE; 1. DR PIRSF; PIRSF004640; IspG; 1. DR TIGRFAMs; TIGR00612; ispG_gcpE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 421 4-hydroxy-3-methylbut-2-en-1-yl FT diphosphate synthase (flavodoxin). FT /FTId=PRO_0000190605. FT METAL 298 298 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 301 301 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 344 344 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 351 351 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. SQ SEQUENCE 421 AA; 45360 MW; C366F8C28FCD10BD CRC64; MNTLQRRKTH QVRIDHITVG SEAPVVIQSM TNTDTADAKA TALQIKELSD AGSEMVRITV NSPEAASKVA EIRRRLDDMG YATPLIGDFH FNGERLLAEF PECGKALSKY RINPGNVGKG VKGDEKFAFM IRTAAENDKA VRIGVNWGSL DQSLAKRMMD ANLASSAPKP PEEVTKEALI VSALESAEKA VLLGLPEDKI ILSCKVSAVQ DLIQVYRELG SRCAYPLHLG LTEAGMGSKG IVASTAALSV LLQEGIGDTI RISLTPEPGS PRTQEVVVGQ EILQTMGLRS FTPMVTACPG CGRTTSTVFQ ELAQDVQNYL RQKMSIWRTL YPGVESLNVA VMGCVVNGPG ESKLADIGIS LPGTGETPVA PVYVDGERKV TLKGDNIATE FLAIVEEYVK TNYGENGLKR HQGKVIPIHS L // ID KGUA_NEIMB Reviewed; 205 AA. AC Q9JYB5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=NMB1661; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42010.1; -; Genomic_DNA. DR PIR; G81055; G81055. DR RefSeq; NP_274666.1; NC_003112.2. DR RefSeq; WP_002222146.1; NC_003112.2. DR ProteinModelPortal; Q9JYB5; -. DR STRING; 122586.NMB1661; -. DR PaxDb; Q9JYB5; -. DR EnsemblBacteria; AAF42010; AAF42010; NMB1661. DR GeneID; 903450; -. DR KEGG; nme:NMB1661; -. DR PATRIC; 20359260; VBINeiMen85645_2138. DR eggNOG; ENOG4108UHA; Bacteria. DR eggNOG; COG0194; LUCA. DR HOGENOM; HOG000037638; -. DR KO; K00942; -. DR OMA; MEGVKQI; -. DR OrthoDB; EOG6CP410; -. DR BioCyc; NMEN122586:GHGG-1715-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03263; guanyl_kin; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 205 Guanylate kinase. FT /FTId=PRO_0000170573. FT DOMAIN 7 185 Guanylate kinase-like. FT NP_BIND 14 21 ATP. {ECO:0000250}. SQ SEQUENCE 205 AA; 22500 MW; 54EE07E545189008 CRC64; MSAYRKGNIF IISAASGTGK TTLVSRLLAN HNGLRVSVSH TTRPPREGEA NGVHYHFVSK EEFESLIAQE AFLEYADVFG NYYGTGAEGV NALAAAGYDV ILEIDVQGAA QVRDALPEAV GIFILPPSFD VLAARLNGRG TDSREVIQRR LSKARHEIEQ SVLFDFVVVN DDLARAEEDL RHIVNACRLK RSRQLGFIAD LLENS // ID KAD_NEIMB Reviewed; 215 AA. AC P0A0U7; P49980; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=NMB0823; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate group between ATP and AMP. Plays an important role in CC cellular energy homeostasis and in adenine nucleotide metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP- CC Rule:MF_00235}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and CC two small peripheral domains, NMPbind and LID, which undergo CC movements during catalysis. The LID domain closes over the site of CC phosphoryl transfer upon ATP binding. Assembling and dissambling CC the active center during each catalytic cycle provides an CC effective means to prevent ATP hydrolysis. {ECO:0000255|HAMAP- CC Rule:MF_00235}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00235}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41236.1; -; Genomic_DNA. DR PIR; F81154; F81154. DR RefSeq; NP_273865.1; NC_003112.2. DR RefSeq; WP_002222696.1; NC_003112.2. DR ProteinModelPortal; P0A0U7; -. DR SMR; P0A0U7; 1-214. DR STRING; 122586.NMB0823; -. DR PaxDb; P0A0U7; -. DR EnsemblBacteria; AAF41236; AAF41236; NMB0823. DR GeneID; 902938; -. DR KEGG; nme:NMB0823; -. DR PATRIC; 20357031; VBINeiMen85645_1034. DR eggNOG; ENOG4105CC8; Bacteria. DR eggNOG; COG0563; LUCA. DR HOGENOM; HOG000238772; -. DR KO; K00939; -. DR OMA; PKCSHIP; -. DR OrthoDB; EOG679TH4; -. DR BioCyc; NMEN122586:GHGG-854-MONOMER; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23359; PTHR23359; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01351; adk; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 215 Adenylate kinase. FT /FTId=PRO_0000158813. FT NP_BIND 10 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 57 59 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 85 88 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 132 133 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT REGION 30 59 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT REGION 122 159 LID. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 31 31 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 36 36 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 92 92 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 123 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 156 156 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 167 167 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 200 200 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00235}. SQ SEQUENCE 215 AA; 23190 MW; 845DA8C390469836 CRC64; MKALLLGAPG AGKGTQAQFI TAAFGIPQIS TGDMLRAAIK AGTPLGLEAK KIIDEGGLVR DDIIIGMVKE RIAQDDCKNG FLFDGFPRTL AQAEAMVEAG VDLDAVVEID VPDSVIVDRM SGRRVHLASG RTYHVTYNPP KVEGKDDVTG EDLIQRDDDK EETVKKRLAV YHEQTEVLVD FYSKLEGEHA PKYIKVDGTQ AVEAVKAEVL GALGK // ID KDSB_NEIMB Reviewed; 253 AA. AC Q9K0D6; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00057}; DE EC=2.7.7.38 {ECO:0000255|HAMAP-Rule:MF_00057}; DE AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00057}; DE Short=CKS {ECO:0000255|HAMAP-Rule:MF_00057}; DE Short=CMP-KDO synthase {ECO:0000255|HAMAP-Rule:MF_00057}; GN Name=kdsB {ECO:0000255|HAMAP-Rule:MF_00057}; GN OrderedLocusNames=NMB0675; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for CC incorporation into bacterial lipopolysaccharide in Gram-negative CC bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}. CC -!- CATALYTIC ACTIVITY: CTP + 3-deoxy-D-manno-octulosonate = CC diphosphate + CMP-3-deoxy-D-manno-octulosonate. CC {ECO:0000255|HAMAP-Rule:MF_00057}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno- CC octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from CC 3-deoxy-D-manno-octulosonate and CTP: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00057}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00057}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00057}. CC -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000255|HAMAP- CC Rule:MF_00057}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41093.1; -; Genomic_DNA. DR PIR; A81171; A81171. DR RefSeq; NP_273717.1; NC_003112.2. DR RefSeq; WP_002225504.1; NC_003112.2. DR ProteinModelPortal; Q9K0D6; -. DR SMR; Q9K0D6; 3-249. DR STRING; 122586.NMB0675; -. DR PaxDb; Q9K0D6; -. DR EnsemblBacteria; AAF41093; AAF41093; NMB0675. DR GeneID; 902786; -. DR KEGG; nme:NMB0675; -. DR PATRIC; 20356653; VBINeiMen85645_0845. DR eggNOG; ENOG4105CET; Bacteria. DR eggNOG; COG1212; LUCA. DR HOGENOM; HOG000007602; -. DR KO; K00979; -. DR OMA; NSGTERC; -. DR OrthoDB; EOG6KT2SK; -. DR BioCyc; NMEN122586:GHGG-702-MONOMER; -. DR BRENDA; 2.7.7.38; 3593. DR UniPathway; UPA00030; -. DR UniPathway; UPA00358; UER00476. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00057; CMP_KDO_synth; 1. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR004528; KdsB. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR21485:SF4; PTHR21485:SF4; 1. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00466; kdsB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipopolysaccharide biosynthesis; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 253 3-deoxy-manno-octulosonate FT cytidylyltransferase. FT /FTId=PRO_0000370104. SQ SEQUENCE 253 AA; 27834 MW; 9DB371766C3B1264 CRC64; MTEFVVLIPA RLDSSRLPGK ALADIHGKPM VVRVAEQAAK SKAARVVVAT DHPDIQTACQ AHGIEVVMTS NRHESGTTRL AEASVALKLP PHLIVVNVQG DEPLIAPELI DRTAEVLVEN NVQMATAAHE LHDFDELMNP NAVKVVLDKN RNAIYFSRAP IPYPRDAIRA GKREMPSETA VLRHIGIYAY RAGFLQRYAE MSVSPLETIE SLEQLRVLWH GYPIAVETAK EAPAAGVDTQ EDLDRVRAVF QTV // ID KTHY_NEIMB Reviewed; 206 AA. AC Q9K0D9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=NMB0670; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41088.1; -; Genomic_DNA. DR PIR; B81173; B81173. DR RefSeq; NP_273712.1; NC_003112.2. DR RefSeq; WP_002225507.1; NC_003112.2. DR ProteinModelPortal; Q9K0D9; -. DR STRING; 122586.NMB0670; -. DR PaxDb; Q9K0D9; -. DR EnsemblBacteria; AAF41088; AAF41088; NMB0670. DR GeneID; 902781; -. DR KEGG; nme:NMB0670; -. DR PATRIC; 20356641; VBINeiMen85645_0839. DR eggNOG; ENOG4108ZMD; Bacteria. DR eggNOG; COG0125; LUCA. DR HOGENOM; HOG000229078; -. DR KO; K00943; -. DR OMA; GGIDIAE; -. DR OrthoDB; EOG64JFSH; -. DR BioCyc; NMEN122586:GHGG-697-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018094; Thymidylate_kinase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 206 Thymidylate kinase. FT /FTId=PRO_0000155312. FT NP_BIND 10 17 ATP. {ECO:0000255}. SQ SEQUENCE 206 AA; 22986 MW; 2D356EFE373E8F5E CRC64; MKPQFITLDG IDGAGKSTNL AVIKAWFERR GLPVLFTREP GGTPVGEALR EILLNPETKA GLRAETLMMF AARMQHIEEV ILPALSDGIH VVSDRFTDAT FAYQGGGRGM PSEDIEILEH WVQGGLKPDL TLLLDVPLEV SMARIGQTRE KDRFEQEQAD FFMRVRGVYL DRAAACPERY AVIDSNRNLD EVRNSIEKVL DGHFGC // ID KHSE_NEIMB Reviewed; 305 AA. AC Q4W557; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00301}; DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00301}; DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00301}; DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00301}; GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00301}; GN OrderedLocusNames=NMB2029; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00301}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00301}. CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family. CC {ECO:0000255|HAMAP-Rule:MF_00301}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52153.1; -; Genomic_DNA. DR RefSeq; NP_275021.1; NC_003112.2. DR RefSeq; WP_002218156.1; NC_003112.2. DR ProteinModelPortal; Q4W557; -. DR STRING; 122586.NMB2029; -. DR PaxDb; Q4W557; -. DR EnsemblBacteria; AAY52153; AAY52153; NMB2029. DR GeneID; 903113; -. DR KEGG; nme:NMB2029; -. DR PATRIC; 20360173; VBINeiMen85645_2586. DR eggNOG; ENOG4105CUV; Bacteria. DR eggNOG; COG2334; LUCA. DR HOGENOM; HOG000004810; -. DR KO; K02204; -. DR OMA; AGALRFW; -. DR OrthoDB; EOG6BW4W1; -. DR BioCyc; NMEN122586:GHGG-2091-MONOMER; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00301; Homoser_kinase_2; 1. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR005280; Homoserine_kinase_ThrB. DR InterPro; IPR011009; Kinase-like_dom. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR00938; thrB_alt; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Threonine biosynthesis; KW Transferase. FT CHAIN 1 305 Homoserine kinase. FT /FTId=PRO_0000172193. SQ SEQUENCE 305 AA; 33619 MW; 9F1C764520D09EE5 CRC64; MSVYTSVSDD EMRGFLSGYD LGEFVSLQGI AQGITNSNYF LTTTSGRYVL TVFEVLKQEE LPFFLELNRH LSMKGVAVAA PVARKDGRLD SVLAGKPACL VACLKGSDTA LPTAEQCFHT GAMLAKMHLA AADFPLEMEN PRYNAWWTEA CARLLPVLSQ DDAALLCSEI DALKDNLGNH LPSGIIHADL FKDNVLLDGG QVSGFIDFYY ACRGNFMYDL AIAVNDWART ADNKLDEALK KAFIGGYEGV RPLSAEEKAY FPTAQRAGCI RFWVSRLLDF HFPQAGEMTF IKDPNAFRNL LLSLG // ID KDSA_NEIMB Reviewed; 280 AA. AC Q9JZ55; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056}; DE EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056}; DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056}; DE AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056}; DE Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056}; DE Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056}; DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056}; GN Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056}; GN OrderedLocusNames=NMB1283; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + D-arabinose 5-phosphate CC + H(2)O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00056}. CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5- CC phosphate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00056}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056}. CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP- CC Rule:MF_00056}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41659.1; -; Genomic_DNA. DR PIR; B81100; B81100. DR RefSeq; NP_274303.1; NC_003112.2. DR RefSeq; WP_002222386.1; NC_003112.2. DR PDB; 2QKF; X-ray; 1.75 A; A/B/C/D=1-280. DR PDB; 3FYO; X-ray; 1.90 A; A/B/C/D=1-280. DR PDB; 3FYP; X-ray; 1.85 A; A/B/C/D=1-280. DR PDB; 3QPY; X-ray; 1.95 A; A/B/C/D=1-280. DR PDB; 3QPZ; X-ray; 1.75 A; A/B/C/D=1-280. DR PDB; 3QQ0; X-ray; 1.90 A; A/B/C/D=1-280. DR PDB; 3QQ1; X-ray; 2.70 A; A/B/C/D=1-280. DR PDB; 3STC; X-ray; 1.91 A; A/B/C/D=1-280. DR PDB; 3STE; X-ray; 2.05 A; A/B/C/D=1-280. DR PDB; 3STF; X-ray; 1.90 A; A/B/C/D=1-280. DR PDB; 3STG; X-ray; 2.20 A; A/B/C/D=1-280. DR PDB; 4JTE; X-ray; 1.90 A; A/B/C/D=1-280. DR PDB; 4JTF; X-ray; 1.80 A; A/B/C/D=1-280. DR PDB; 4JTG; X-ray; 1.85 A; A/B/C/D=1-280. DR PDB; 4JTH; X-ray; 2.00 A; A/B/C/D=1-280. DR PDB; 4JTI; X-ray; 1.75 A; A/B/C/D=1-280. DR PDB; 4JTJ; X-ray; 1.75 A; A/B/C/D=1-280. DR PDB; 4JTK; X-ray; 1.86 A; A/B/C/D=1-280. DR PDB; 4JTL; X-ray; 2.10 A; A/B/C/D=1-280. DR PDBsum; 2QKF; -. DR PDBsum; 3FYO; -. DR PDBsum; 3FYP; -. DR PDBsum; 3QPY; -. DR PDBsum; 3QPZ; -. DR PDBsum; 3QQ0; -. DR PDBsum; 3QQ1; -. DR PDBsum; 3STC; -. DR PDBsum; 3STE; -. DR PDBsum; 3STF; -. DR PDBsum; 3STG; -. DR PDBsum; 4JTE; -. DR PDBsum; 4JTF; -. DR PDBsum; 4JTG; -. DR PDBsum; 4JTH; -. DR PDBsum; 4JTI; -. DR PDBsum; 4JTJ; -. DR PDBsum; 4JTK; -. DR PDBsum; 4JTL; -. DR ProteinModelPortal; Q9JZ55; -. DR SMR; Q9JZ55; 1-277. DR STRING; 122586.NMB1283; -. DR BindingDB; Q9JZ55; -. DR ChEMBL; CHEMBL1938218; -. DR PaxDb; Q9JZ55; -. DR EnsemblBacteria; AAF41659; AAF41659; NMB1283. DR GeneID; 903705; -. DR KEGG; nme:NMB1283; -. DR PATRIC; 20358193; VBINeiMen85645_1608. DR eggNOG; ENOG4105CXR; Bacteria. DR eggNOG; COG2877; LUCA. DR HOGENOM; HOG000023021; -. DR KO; K01627; -. DR OMA; PIATDIH; -. DR OrthoDB; EOG680X4R; -. DR BioCyc; NMEN122586:GHGG-1321-MONOMER; -. DR BRENDA; 2.5.1.55; 3593. DR UniPathway; UPA00030; -. DR UniPathway; UPA00357; UER00474. DR EvolutionaryTrace; Q9JZ55; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00056; KDO8P_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR InterPro; IPR006269; KDO8P_synthase. DR Pfam; PF00793; DAHP_synth_1; 1. DR TIGRFAMs; TIGR01362; KDO8P_synth; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 280 2-dehydro-3-deoxyphosphooctonate FT aldolase. FT /FTId=PRO_0000187143. FT STRAND 3 5 {ECO:0000244|PDB:2QKF}. FT STRAND 8 11 {ECO:0000244|PDB:2QKF}. FT STRAND 17 24 {ECO:0000244|PDB:2QKF}. FT HELIX 28 45 {ECO:0000244|PDB:2QKF}. FT STRAND 49 55 {ECO:0000244|PDB:2QKF}. FT STRAND 61 65 {ECO:0000244|PDB:2QKF}. FT HELIX 71 85 {ECO:0000244|PDB:2QKF}. FT STRAND 89 92 {ECO:0000244|PDB:2QKF}. FT HELIX 96 98 {ECO:0000244|PDB:2QKF}. FT HELIX 99 105 {ECO:0000244|PDB:2QKF}. FT STRAND 107 111 {ECO:0000244|PDB:2QKF}. FT HELIX 113 115 {ECO:0000244|PDB:2QKF}. FT HELIX 119 127 {ECO:0000244|PDB:2QKF}. FT STRAND 131 135 {ECO:0000244|PDB:2QKF}. FT HELIX 142 144 {ECO:0000244|PDB:2QKF}. FT HELIX 145 154 {ECO:0000244|PDB:2QKF}. FT STRAND 160 164 {ECO:0000244|PDB:2QKF}. FT STRAND 170 172 {ECO:0000244|PDB:4JTI}. FT HELIX 180 187 {ECO:0000244|PDB:2QKF}. FT TURN 188 190 {ECO:0000244|PDB:2QKF}. FT STRAND 193 196 {ECO:0000244|PDB:2QKF}. FT HELIX 197 200 {ECO:0000244|PDB:2QKF}. FT TURN 201 203 {ECO:0000244|PDB:4JTI}. FT TURN 204 206 {ECO:0000244|PDB:4JTF}. FT HELIX 208 211 {ECO:0000244|PDB:4JTF}. FT HELIX 214 226 {ECO:0000244|PDB:2QKF}. FT STRAND 231 236 {ECO:0000244|PDB:2QKF}. FT TURN 243 246 {ECO:0000244|PDB:3STG}. FT STRAND 251 253 {ECO:0000244|PDB:3STG}. FT HELIX 256 273 {ECO:0000244|PDB:2QKF}. SQ SEQUENCE 280 AA; 30483 MW; 7183B4CC6E3FEE28 CRC64; MDIKINDITL GNNSPFVLFG GINVLESLDS TLQTCAHYVE VTRKLGIPYI FKASFDKANR SSIHSYRGVG LEEGLKIFEK VKAEFGIPVI TDVHEPHQCQ PVAEVCDVIQ LPAFLARQTD LVVAMAKTGN VVNIKKPQFL SPSQMKNIVE KFHEAGNGKL ILCERGSSFG YDNLVVDMLG FGVMKQTCGN LPVIFDVTHS LQTRDAGSAA SGGRRAQALD LALAGMATRL AGLFLESHPD PKLAKCDGPS ALPLHLLEDF LIRIKALDDL IKSQPILTIE // ID LEU1_NEIMB Reviewed; 517 AA. AC Q9JZG1; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025}; DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025}; DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025}; DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025}; GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; GN OrderedLocusNames=NMB1070; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). CC {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = CC (2S)-2-isopropylmalate + CoA. {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 1/4. CC {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41465.1; -; Genomic_DNA. DR PIR; G81125; G81125. DR RefSeq; NP_274103.1; NC_003112.2. DR RefSeq; WP_010980887.1; NC_003112.2. DR PDB; 3RMJ; X-ray; 1.95 A; A/B=1-364. DR PDBsum; 3RMJ; -. DR ProteinModelPortal; Q9JZG1; -. DR STRING; 122586.NMB1070; -. DR PaxDb; Q9JZG1; -. DR EnsemblBacteria; AAF41465; AAF41465; NMB1070. DR GeneID; 903489; -. DR KEGG; nme:NMB1070; -. DR PATRIC; 20357689; VBINeiMen85645_1361. DR eggNOG; ENOG4105CYQ; Bacteria. DR eggNOG; COG0119; LUCA. DR HOGENOM; HOG000046859; -. DR KO; K01649; -. DR OMA; MAIKTRQ; -. DR OrthoDB; EOG6CGCF3; -. DR BioCyc; NMEN122586:GHGG-1107-MONOMER; -. DR BRENDA; 2.3.3.13; 3593. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01025; LeuA_type1; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005671; LeuA_bact_synth. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR00973; leuA_bact; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; KW Leucine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 517 2-isopropylmalate synthase. FT /FTId=PRO_0000140364. FT STRAND 8 11 {ECO:0000244|PDB:3RMJ}. FT HELIX 13 17 {ECO:0000244|PDB:3RMJ}. FT HELIX 27 40 {ECO:0000244|PDB:3RMJ}. FT STRAND 43 49 {ECO:0000244|PDB:3RMJ}. FT HELIX 50 52 {ECO:0000244|PDB:3RMJ}. FT HELIX 54 64 {ECO:0000244|PDB:3RMJ}. FT STRAND 68 79 {ECO:0000244|PDB:3RMJ}. FT HELIX 80 90 {ECO:0000244|PDB:3RMJ}. FT STRAND 93 103 {ECO:0000244|PDB:3RMJ}. FT HELIX 106 111 {ECO:0000244|PDB:3RMJ}. FT HELIX 117 131 {ECO:0000244|PDB:3RMJ}. FT TURN 132 134 {ECO:0000244|PDB:3RMJ}. FT STRAND 138 143 {ECO:0000244|PDB:3RMJ}. FT HELIX 145 147 {ECO:0000244|PDB:3RMJ}. FT HELIX 150 163 {ECO:0000244|PDB:3RMJ}. FT STRAND 167 171 {ECO:0000244|PDB:3RMJ}. FT STRAND 173 175 {ECO:0000244|PDB:3RMJ}. FT HELIX 179 192 {ECO:0000244|PDB:3RMJ}. FT HELIX 196 198 {ECO:0000244|PDB:3RMJ}. FT STRAND 199 204 {ECO:0000244|PDB:3RMJ}. FT HELIX 212 221 {ECO:0000244|PDB:3RMJ}. FT STRAND 226 230 {ECO:0000244|PDB:3RMJ}. FT HELIX 231 233 {ECO:0000244|PDB:3RMJ}. FT HELIX 243 252 {ECO:0000244|PDB:3RMJ}. FT HELIX 254 257 {ECO:0000244|PDB:3RMJ}. FT HELIX 265 267 {ECO:0000244|PDB:3RMJ}. FT HELIX 268 279 {ECO:0000244|PDB:3RMJ}. FT TURN 288 290 {ECO:0000244|PDB:3RMJ}. FT TURN 292 295 {ECO:0000244|PDB:3RMJ}. FT HELIX 319 321 {ECO:0000244|PDB:3RMJ}. SQ SEQUENCE 517 AA; 55397 MW; 6D9EF77D2F6FCD6A CRC64; MTQTNRVIIF DTTLRDGEQS PGAAMTKEEK IRVARQLEKL GVDIIEAGFA AASPGDFEAV NAIAKTITKS TVCSLSRAIE RDIRQAGEAV APAPKKRIHT FIATSPIHME YKLKMKPKQV IEAAVKAVKI AREYTDDVEF SCEDALRSEI DFLAEICGAV IEAGATTINI PDTVGYSIPY KTEEFFRELI AKTPNGGKVV WSAHCHNDLG LAVANSLAAL KGGARQVECT VNGLGERAGN ASVEEIVMAL KVRHDLFGLE TGIDTTQIVP SSKLVSTITG YPVQPNKAIV GANAFSHESG IHQDGVLKHR ETYEIMSAES VGWATNRLSL GKLSGRNAFK TKLADLGIEL ESEEALNAAF ARFKELADKK REIFDEDLHA LVSDEMGSMN AESYKFISQK ISTETGEEPR ADIVFSIKGE EKRASATGSG PVDAIFKAIE SVAQSGAALQ IYSVNAVTQG TESQGETSVR LARGNRVVNG QGADTDVLVA TAKAYLSALS KLEFSAAKPK AQGSGTI // ID KPRS_NEIMB Reviewed; 327 AA. AC P65235; Q9JQV4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; Synonyms=prsA; GN OrderedLocusNames=NMB0875; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00583}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route I): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000255|HAMAP-Rule:MF_00583}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41286.1; -; Genomic_DNA. DR PIR; F81146; F81146. DR RefSeq; NP_273916.1; NC_003112.2. DR RefSeq; WP_002213870.1; NC_003112.2. DR ProteinModelPortal; P65235; -. DR SMR; P65235; 7-311. DR STRING; 122586.NMB0875; -. DR PaxDb; P65235; -. DR PRIDE; P65235; -. DR EnsemblBacteria; AAF41286; AAF41286; NMB0875. DR GeneID; 902994; -. DR KEGG; nme:NMB0875; -. DR PATRIC; 20357155; VBINeiMen85645_1091. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR HOGENOM; HOG000210449; -. DR KO; K00948; -. DR OMA; HENVRGQ; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; NMEN122586:GHGG-911-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.2020; -; 2. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 327 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141167. FT NP_BIND 40 42 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 99 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 196 198 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 223 230 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 310 312 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 132 132 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 134 134 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 143 143 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 147 147 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 108 108 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 134 134 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 139 139 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 173 173 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 327 AA; 35598 MW; B92FF8F029589B92 CRC64; MAAYDSLMVF TGNANPELAQ RVVRHLDISL GNASVSKFSD GEVAVELLEN VRGRDVFILQ PTCAPTNDNL MEILTMADAL KRASAGRITT AIPYFGYARQ DRRPRSVRVP ISAKLVANML YSAGIDRVLT VDLHADQIQG FFDIPVDNIY ATPILLNDIK QQRIENLTVV SPDIGGVVRA RAVAKSLNAD LAIIDKRRPK ANVAEVMNII GDIQGRTCLI VDDMIDTANT LCKAAVALKE RGAERVLAYA SHAVFSGEAV SRIASSEIDQ VVVTDTIPLS EAAKNCDRIR QVTIAGLLAE TVRRISNEES VSYLFNEEVM TGSMLLP // ID LEPA_NEIMB Reviewed; 597 AA. AC Q9K055; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071}; DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN OrderedLocusNames=NMB0766; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for accurate and efficient protein synthesis CC under certain stress conditions. May act as a fidelity factor of CC the translation reaction, by catalyzing a one-codon backward CC translocation of tRNAs on improperly translocated ribosomes. Back- CC translocation proceeds from a post-translocation (POST) complex to CC a pre-translocation (PRE) complex, thus giving elongation factor G CC a second chance to translocate the tRNAs correctly. Binds to CC ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00071}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41179.1; -; Genomic_DNA. DR PIR; C81162; C81162. DR RefSeq; NP_273808.1; NC_003112.2. DR RefSeq; WP_002225433.1; NC_003112.2. DR ProteinModelPortal; Q9K055; -. DR SMR; Q9K055; 1-555. DR STRING; 122586.NMB0766; -. DR PaxDb; Q9K055; -. DR EnsemblBacteria; AAF41179; AAF41179; NMB0766. DR GeneID; 902881; -. DR KEGG; nme:NMB0766; -. DR PATRIC; 20356905; VBINeiMen85645_0971. DR eggNOG; ENOG4105C4S; Bacteria. DR eggNOG; COG0481; LUCA. DR HOGENOM; HOG000020624; -. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR BioCyc; NMEN122586:GHGG-797-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR013842; LepA_GTP-bd_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR01393; lepA; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; GTP-binding; KW Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 597 Elongation factor 4. FT /FTId=PRO_0000176309. FT DOMAIN 2 184 tr-type G. FT NP_BIND 14 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT NP_BIND 131 134 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. SQ SEQUENCE 597 AA; 66016 MW; B2DDBA3F0F8C448C CRC64; MKNIRNFSII AHIDHGKSTL ADRFIQYCGG LDLREMSTQV LDSMDIEKER GITIKAQTAA LNYKARDGQV YQLNLIDTPG HVDFSYEVSR SLSACEGALL VVDASQGVEA QTVANCYTAI DLGVEVVPVL NKIDLPAADP ERVEQEIEDI IGIDAVGAVQ CSAKSGIGVE DVLEEIVAKI PAPTGDENAP LQAVIVDSWF DNYVGVVMLI RVKNGTIKLK DKVRFMSTKA ETQVEQLGVF TPKSVQKQEL KAGEVGFLIT GVKELGQAKV GDTVTLVANP ATEPLPGFQE VQSQVFAGLY PVESHDYEAL RDALEKLQLN DASLKFEPEV SQALGFGFRC GFLGLLHLEI VQERLEREFD MDLITTAPTV IYEVVLKSGE KIEVENPSKL PDIGSIETIL EPIITATILV PQEYVGNVMT LCNQKRGVQV NMQYMGRQVM LTYDLPMNEV VMDFFDKLKS TSRGYASLDY HFKEFQPSDL IKLDIMVNGE KVDALSLIVH RQSAVHRGRE LASKMRELIP RQMFDIAVQA AIGSQIIARE NVKALRKNVL AKCYGGDITR KKKLLEKQKA GKRRMKQVGN VEIPQSAFLA ILQVSDK // ID LFTR_NEIMB Reviewed; 241 AA. AC Q9K1E9; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Leucyl/phenylalanyl-tRNA--protein transferase {ECO:0000255|HAMAP-Rule:MF_00688}; DE EC=2.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00688}; DE AltName: Full=L/F-transferase {ECO:0000255|HAMAP-Rule:MF_00688}; DE AltName: Full=Leucyltransferase {ECO:0000255|HAMAP-Rule:MF_00688}; DE AltName: Full=Phenyalanyltransferase {ECO:0000255|HAMAP-Rule:MF_00688}; GN Name=aat {ECO:0000255|HAMAP-Rule:MF_00688}; OrderedLocusNames=NMB0206; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Functions in the N-end rule pathway of protein CC degradation where it conjugates Leu, Phe and, less efficiently, CC Met from aminoacyl-tRNAs to the N-termini of proteins containing CC an N-terminal arginine or lysine. {ECO:0000255|HAMAP- CC Rule:MF_00688}. CC -!- CATALYTIC ACTIVITY: L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + CC L-leucyl-[protein]. {ECO:0000255|HAMAP-Rule:MF_00688}. CC -!- CATALYTIC ACTIVITY: L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + CC L-phenylalanyl-[protein]. {ECO:0000255|HAMAP-Rule:MF_00688}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00688}. CC -!- SIMILARITY: Belongs to the L/F-transferase family. CC {ECO:0000255|HAMAP-Rule:MF_00688}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40663.1; -; Genomic_DNA. DR PIR; H81226; H81226. DR RefSeq; NP_273264.1; NC_003112.2. DR RefSeq; WP_002236619.1; NC_003112.2. DR ProteinModelPortal; Q9K1E9; -. DR STRING; 122586.NMB0206; -. DR PaxDb; Q9K1E9; -. DR EnsemblBacteria; AAF40663; AAF40663; NMB0206. DR GeneID; 902314; -. DR KEGG; nme:NMB0206; -. DR PATRIC; 20355453; VBINeiMen85645_0255. DR eggNOG; ENOG4108R4Z; Bacteria. DR eggNOG; COG2360; LUCA. DR HOGENOM; HOG000102325; -. DR KO; K00684; -. DR OMA; YRQGIFP; -. DR OrthoDB; EOG6WX4R3; -. DR BioCyc; NMEN122586:GHGG-217-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008914; F:leucyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00688; Leu_Phe_trans; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR004616; Leu/Phe-tRNA_Trfase. DR Pfam; PF03588; Leu_Phe_trans; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR00667; aat; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 241 Leucyl/phenylalanyl-tRNA--protein FT transferase. FT /FTId=PRO_0000207230. SQ SEQUENCE 241 AA; 26836 MW; 7DD1C8E340E5CF42 CRC64; MRIPLLAPDN YAFPDPAYAL ARCDGLVGVS GDLDAGRLLE AYRNGVFPWF SRDGWFFWYA VGPRAVVFPD RLHIPRSLAK TLRNGSYRVA VNGCFAEVVA HCAAAARPNQ DGTWIAPEFQ TAYLKLHEMG YAHSFECHYP DESGETRLAG GFYGVQIGRV FYGESMFALQ PDASKIAFAC AVPFLADLGV ELIDCQQDTE HMRRFGSELL PFADFAERLR MLNAVPLKEE IGRREVACKG L // ID LIPM_NEIMB Reviewed; 704 AA. AC Q05013; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Capsule polysaccharide modification protein LipA; GN Name=lipA; OrderedLocusNames=NMB0082; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 184-704. RC STRAIN=B1940 / Serogroup B; RX PubMed=8326861; DOI=10.1111/j.1365-2958.1993.tb01592.x; RA Frosch M., Mueller A.; RT "Phospholipid substitution of capsular polysaccharides and mechanisms RT of capsule formation in Neisseria meningitidis."; RL Mol. Microbiol. 8:483-493(1993). CC -!- FUNCTION: Involved in the phospholipid modification of the CC capsular polysaccharide, a strong requirement for its CC translocation to the cell surface. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=Z13995; Type=Frameshift; Positions=566; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40546.1; -; Genomic_DNA. DR EMBL; Z13995; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; D81240; D81240. DR PIR; S32879; S32879. DR RefSeq; NP_273145.1; NC_003112.2. DR RefSeq; WP_002224756.1; NC_003112.2. DR STRING; 122586.NMB0082; -. DR PaxDb; Q05013; -. DR EnsemblBacteria; AAF40546; AAF40546; NMB0082. DR GeneID; 902186; -. DR KEGG; nme:NMB0082; -. DR PATRIC; 20355167; VBINeiMen85645_0117. DR eggNOG; ENOG4105E12; Bacteria. DR eggNOG; COG3563; LUCA. DR HOGENOM; HOG000256563; -. DR KO; K07266; -. DR OMA; IYIKIHP; -. DR OrthoDB; EOG6QK4NH; -. DR BioCyc; NMEN122586:GHGG-88-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW. DR InterPro; IPR007833; Capsule_polysaccharide_synth. DR Pfam; PF05159; Capsule_synth; 3. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Polysaccharide transport; Reference proteome; Sugar transport; KW Transport. FT CHAIN 1 704 Capsule polysaccharide modification FT protein LipA. FT /FTId=PRO_0000084439. FT CONFLICT 238 238 H -> N (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 253 253 V -> I (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 294 297 EINR -> KIDS (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 306 306 T -> P (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 316 316 A -> R (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 331 331 A -> R (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 390 390 R -> G (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 449 449 S -> G (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 456 456 T -> A (in Ref. 2; Z13995). FT {ECO:0000305}. FT CONFLICT 462 462 Y -> H (in Ref. 2; Z13995). FT {ECO:0000305}. SQ SEQUENCE 704 AA; 79606 MW; 2909C40642CD326A CRC64; MFLFSDGLQS INNNNRRKRI VKNAYIPSRG IRKIPHLSTL LPEFHICKDG KEAEAVVGWG LRPTTHKARA FAAEHQLPFI ALEDGFLRSL GLGVAGYPPY SIVYDDIGIY YDTTRPSRLE QLILAADTMP SETLAQAQQA MDFILQHHLS KYNHAPELSD DHPLRSPSKP ETVLIIDQTF GDMAIQYGGA DASTFELMFQ TALNENPQAD IWVKTHPDVL CGKKQGYLTQ LAQQHRVHLL AEDINPISLL QNVDKVYCVT SQMGFEALLC GKPLTTFGLP WYAGWGVSDD RHPEINRLVQ TQRRATRNLL QLFAAAYLQY SRYLNPNTGE AGSLFDVIDY LATVKRKNDK LRGELYCVGM SLWKRAVAKP FFNVPSCRLK FISSTQKLAR VKLSDDARIL AWGNGKEAIV RFAEQHHIPL LRMEDGFIRS VGLGSNLVPP LSLVTDDMSI YFNAETPSRL EYILQNQNFD DQDFQTALKL QKMLTENHIS KYNVGSSDFT APSTDKTVIL VPGQVEDDAS IRYGSPQIYR NLDLLRTVRE RNPNAYIIYK PHPDVVSGNR IGHISPEDAA RYADQTAEQA DILTCLQYAD EIHTMTSLTG FEALLRGKKV SCYGLPFYAG WGLTQDLLPI PRRSRRLELW QLIAGTLIHY PDYIHPETHQ AINAETAAQI LIRQKNMQKN NNGLHRGCFA KKLGKIKQLY RSFK // ID LBPA_NEIMB Reviewed; 943 AA. AC Q06379; Q9JYK5; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 11-NOV-2015, entry version 106. DE RecName: Full=Lactoferrin-binding protein A; DE AltName: Full=Iron-regulated outer membrane protein A; DE Flags: Precursor; GN Name=lbpA; Synonyms=iroA; OrderedLocusNames=NMB1540; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BNCV / Serogroup B; RX PubMed=8406871; RA Pettersson A., van der Ley P., Poolman J.T., Tommassen J.; RT "Molecular characterization of the 98-kilodalton iron-regulated outer RT membrane protein of Neisseria meningitidis."; RL Infect. Immun. 61:4724-4733(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Unknown. May be an iron-siderophore receptor. CC -!- SUBCELLULAR LOCATION: Cell outer membrane. CC -!- INDUCTION: By iron starvation. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X69214; CAA49148.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41895.1; -; Genomic_DNA. DR PIR; G81070; G81070. DR RefSeq; NP_274547.1; NC_003112.2. DR RefSeq; WP_002247545.1; NC_003112.2. DR ProteinModelPortal; Q06379; -. DR STRING; 122586.NMB1540; -. DR PaxDb; Q06379; -. DR EnsemblBacteria; AAF41895; AAF41895; NMB1540. DR GeneID; 904077; -. DR KEGG; nme:NMB1540; -. DR PATRIC; 20358906; VBINeiMen85645_1967. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000219090; -. DR KO; K16087; -. DR OMA; FPAYAAQ; -. DR OrthoDB; EOG6HB9KP; -. DR BioCyc; NMEN122586:GHGG-1581-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010948; TonB_lacto/transferrin_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR TIGRFAMs; TIGR01776; TonB-tbp-lbp; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 2: Evidence at transcript level; KW Cell outer membrane; Complete proteome; Ion transport; Iron; KW Iron transport; Membrane; Receptor; Reference proteome; Signal; KW TonB box; Transmembrane; Transmembrane beta strand; Transport. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 943 Lactoferrin-binding protein A. FT /FTId=PRO_0000034766. FT MOTIF 926 943 TonB C-terminal box. FT CONFLICT 8 8 P -> Q (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 16 18 IAT -> VAA (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 22 22 A -> S (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 26 31 QAGGAT -> NPETAA (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 43 43 I -> V (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 64 64 V -> A (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 233 233 R -> H (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 243 243 E -> A (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 247 247 D -> N (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 257 269 DIKRKTREPFFSV -> GIKKPSEGGEYFLA (in Ref. FT 1). {ECO:0000305}. FT CONFLICT 273 275 RES -> SEL (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 281 281 L -> V (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 284 286 YGK -> NGN (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 313 313 Q -> M (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 389 389 E -> K (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 420 423 KNLV -> QKLI (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 455 455 A -> K (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 546 546 K -> N (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 564 572 STGFDENNQ -> YSDYTDKG (in Ref. 1; FT CAA49148). {ECO:0000305}. FT CONFLICT 658 658 L -> V (in Ref. 1; CAA49148). FT {ECO:0000305}. FT CONFLICT 667 667 V -> L (in Ref. 1; CAA49148). FT {ECO:0000305}. SQ SEQUENCE 943 AA; 105681 MW; BD569ECACFC01A84 CRC64; MNKKHGFPLT LTALAIATAF PAYAAQAGGA TPDAAQTQSL KEITVRAAKV GRRSKEATGL GKIVKTSETL NKEQVLGIRD LTRYDPGVAV VEQGNGASGG YSIRGVDKNR VAVSVDGVAQ IQAFTVQGSL SGYGGRGGSG AINEIEYENI STVEIDKGAG SSDHGSGALG GAVAFRTKEA ADLISDGKSW GIQAKTAYGS KNRQFMKSLG AGFSKDGWEG LLIRTERQGR ETRPHGDIAD GVEYGIDRLD AFRQTYDIKR KTREPFFSVE GERESKPVAK LAGYGKYLNN QLNRWVKERI EQNQPLSAEE EAQVREAQAR HENLSAQAYT GGGRILPDPM DYRSGSWLAK LGYRFGGRHY VGGVFEDTKQ RYDIRDMTEK QYYGTDEAEK FRDKSGVYDG DDFRDGLYFV PNIEEWKGDK NLVRGIGLKY SRTKFIDEHH RRRRMGLLYR YENEAYSDNW ADKAVLSFDK QGVATDNNTL KLNCAVYPAV DKSCRASADK PYSYDSSDRF HYREQHNVLN ASFEKSLKNK WTKHHLTLGF GYDASKAISR PEQLSHNAAR ISESTGFDEN NQDKYLLGKP EVVEGSVCGY IETLRSRKCV PRKINGSNIH ISLNDRFSIG KYFDFSLGGR YDRKNFTTSE ELVRSGRYVD RSWNSGILFK PNRHFSVSYR ASSGFRTPSF QELFGIDIYH DYPKGWQRPA LKSEKAANRE IGLQWKGDFG FLEISSFRNR YTDMIAVADH KTKLPNQAGQ LTEIDIRDYY NAQNMSLQGV NILGKIDWNG VYGKLPEGLY TTLAYNRIKP KSVSNRPGLS LRSYALDAVQ PSRYVLGFGY DQPEGKWGAN IMLTYSKGKN PDELAYLAGD QKRYSTKRAS SSWSTADVSA YLNLKKRLTL RAAIYNIGNY RYVTWESLRQ TAESTANRHG GDSNYGRYAA PGRNFSLALE MKF // ID LOLC_NEIMB Reviewed; 415 AA. AC P57062; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Lipoprotein-releasing system transmembrane protein LolC; GN Name=lolC; OrderedLocusNames=NMB1235; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of an ATP-dependent transport system responsible CC for the release of lipoproteins targeted to the outer membrane CC from the inner membrane. Such a release is dependent of the CC sorting-signal (absence of an Asp at position 2 of the mature CC lipoprotein) and of LolA (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC LolC/E subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41616.1; -; Genomic_DNA. DR PIR; D81107; D81107. DR RefSeq; NP_274259.1; NC_003112.2. DR RefSeq; WP_002225196.1; NC_003112.2. DR STRING; 122586.NMB1235; -. DR PaxDb; P57062; -. DR EnsemblBacteria; AAF41616; AAF41616; NMB1235. DR GeneID; 903657; -. DR KEGG; nme:NMB1235; -. DR PATRIC; 20358065; VBINeiMen85645_1545. DR eggNOG; ENOG4105D60; Bacteria. DR eggNOG; COG4591; LUCA. DR HOGENOM; HOG000218040; -. DR KO; K09808; -. DR OMA; FEKKLFV; -. DR OrthoDB; EOG68SVTW; -. DR BioCyc; NMEN122586:GHGG-1272-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042954; F:lipoprotein transporter activity; IEA:InterPro. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR011925; LolCE_TM. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. DR TIGRFAMs; TIGR02212; lolCE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 415 Lipoprotein-releasing system FT transmembrane protein LolC. FT /FTId=PRO_0000201815. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 324 344 Helical. {ECO:0000255}. FT TRANSMEM 378 398 Helical. {ECO:0000255}. SQ SEQUENCE 415 AA; 45293 MW; 48D172B2D9605B6E CRC64; MFSLEAWIGL RYLRAKKRNG FMSFITMVSI AGIALGVTAL IVVLSVMNGF QKEIRGQLLN VAPHAEIGYI DNTDTDWRNL LRFTENRKGI LAAAPYVSNQ ALLANAGEIR GVQMRGILPS EERKVVEYGD KMPAGKFEDL IPGEFDIILG VGLAEALGAE VGNKVTVITP EGNVTPAGVV PRLKQFTVVG LVKTGVYEVD NSLAMTHIQD ARVLYRLDKE VAGLRLKLAD PQNAPALTAT LIPEAQRDAV WVRDWTYSNR SYFEAVELEK RMMFIILTLI IAVAAFNLVS SLVMAVTEKQ ADIAILRTLG LSPAGVMKIF MVQGAFSGFF GTLAGVVCGV LLGWNVGRVV AFFENLLGVH LINSQVYFID YLPSDVDMGD VALIACISLG LSFVATLYPS RRASKTQPAE ALRYE // ID LGTB_NEIMB Reviewed; 275 AA. AC Q51116; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=Lacto-N-neotetraose biosynthesis glycosyltransferase LgtB; DE EC=2.-.-.-; GN Name=lgtB; OrderedLocusNames=NMB1928; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=8817494; DOI=10.1111/j.1365-2958.1995.mmi_18040729.x; RA Jennings M.P., Hood D., Peak I.R.A., Virji M., Moxon E.R.; RT "Molecular analysis of a locus for the biosynthesis and phase-variable RT expression of the lacto-N-neotetraose terminal lipopolysaccharide RT structure in Neisseria meningitidis."; RL Mol. Microbiol. 18:729-740(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Adds the second galactose to the lacto-N-tetraose chain CC in lipooligosaccharide (LOS). CC -!- PATHWAY: Glycan metabolism; lacto-N-neotetraose biosynthesis. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide CC biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U25839; AAC44085.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42257.1; -; Genomic_DNA. DR PIR; C81027; C81027. DR PIR; S70814; S70814. DR RefSeq; NP_274922.1; NC_003112.2. DR RefSeq; WP_002225824.1; NC_003112.2. DR STRING; 122586.NMB1928; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR PaxDb; Q51116; -. DR EnsemblBacteria; AAF42257; AAF42257; NMB1928. DR GeneID; 904227; -. DR KEGG; nme:NMB1928; -. DR PATRIC; 20359903; VBINeiMen85645_2456. DR eggNOG; ENOG4105W1T; Bacteria. DR eggNOG; COG3306; LUCA. DR HOGENOM; HOG000218751; -. DR KO; K07270; -. DR OMA; AQFKRVE; -. DR OrthoDB; EOG6R5C54; -. DR BioCyc; NMEN122586:GHGG-1985-MONOMER; -. DR UniPathway; UPA00501; -. DR UniPathway; UPA00820; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 275 Lacto-N-neotetraose biosynthesis FT glycosyltransferase LgtB. FT /FTId=PRO_0000216237. FT CONFLICT 97 97 A -> E (in Ref. 1; AAC44085). FT {ECO:0000305}. SQ SEQUENCE 275 AA; 31578 MW; E871305E2F6CF70F CRC64; MQNHVISLAS AAERRAHIAD TFGRHGIPFQ FFDALMPSER LEQAMAELVP GLSAHPYLSG VEKACFMSHA VLWKQALDEG LPYITVFEDD VLLGEGAEKF LAEDAWLQER FDPDTAFIVR LETMFMHVLT SPSGVADYCG RAFPLLESEH WGTAGYIISR KAMRFFLDRF AALPPEGLHP VDLMMFSDFF DREGMPVCQL NPALCAQELH YAKFHDQNSA LGSLIEHDRL LNRKQQRRDS PANTFKHRLI RALTKISRER EKRRQRREQF IVPFQ // ID LIPA_NEIMB Reviewed; 327 AA. AC Q9JZA5; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000255|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN OrderedLocusNames=NMB1216; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur CC atoms into the C-6 and C-8 positions of the octanoyl moiety bound CC to the lipoyl domains of lipoate-dependent enzymes, thereby CC converting the octanoylated domains into lipoylated derivatives. CC {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur- CC (sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] CC ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 CC L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] CC ferredoxin. {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00206}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000255|HAMAP-Rule:MF_00206}; CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl CC synthase family. {ECO:0000255|HAMAP-Rule:MF_00206}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41598.1; -; Genomic_DNA. DR PIR; D81109; D81109. DR RefSeq; NP_274241.1; NC_003112.2. DR RefSeq; WP_002217175.1; NC_003112.2. DR ProteinModelPortal; Q9JZA5; -. DR STRING; 122586.NMB1216; -. DR PaxDb; Q9JZA5; -. DR EnsemblBacteria; AAF41598; AAF41598; NMB1216. DR GeneID; 903638; -. DR KEGG; nme:NMB1216; -. DR PATRIC; 20358013; VBINeiMen85645_1519. DR eggNOG; ENOG4105C0G; Bacteria. DR eggNOG; COG0320; LUCA. DR HOGENOM; HOG000235997; -. DR KO; K03644; -. DR OMA; NVCTRSC; -. DR OrthoDB; EOG6038ZS; -. DR BioCyc; NMEN122586:GHGG-1253-MONOMER; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00206; Lipoyl_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR031691; LIAS_N. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR10949; PTHR10949; 1. DR Pfam; PF16881; LIAS_N; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF005963; Lipoyl_synth; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00510; lipA; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 327 Lipoyl synthase. FT /FTId=PRO_0000102329. FT METAL 66 66 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 71 71 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 77 77 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 92 92 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 96 96 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 99 99 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. SQ SEQUENCE 327 AA; 37061 MW; 0D20E8B6FAD90143 CRC64; MSEIKTDDPK RGIKLRGADK TARIPIKVVP LQEKLKKPEW IRAKLPSRKF FEIKDILREQ KMHTVCEEAS CPNIGECFSK GTATFMIMGD ICTRRCPFCD VGHGRPNMLD PDEPRNLAES VKAMNLRYVV ITSVDRDDLR DGGAQHFADC IKAIRETSPN TKIEILVPDF RGRLDIALKI LAETPPDVMN HNLETHPSLY RKARPGANYQ HSLDLLKRYK EMMPHIPTKS GIMVGLGETD EDVREIMRDM RAHNIEMITI GQYLQPSDGH LPVLRYVTPE QFKIFEKEAY ELGFSNAAIG AMVRSSYHAD EQAAEALRES HGGCGHH // ID LOLA_NEIMB Reviewed; 207 AA. AC P57068; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Outer-membrane lipoprotein carrier protein; DE Flags: Precursor; GN Name=lolA; OrderedLocusNames=NMB0622; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates in the translocation of lipoproteins from CC the inner membrane to the outer membrane. Only forms a complex CC with a lipoprotein if the residue after the N-terminal Cys is not CC an aspartate (The Asp acts as a targeting signal to indicate that CC the lipoprotein should stay in the inner membrane) (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LolA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41048.1; -; Genomic_DNA. DR PIR; C81178; C81178. DR RefSeq; NP_273666.1; NC_003112.2. DR RefSeq; WP_002222831.1; NC_003112.2. DR ProteinModelPortal; P57068; -. DR STRING; 122586.NMB0622; -. DR PaxDb; P57068; -. DR EnsemblBacteria; AAF41048; AAF41048; NMB0622. DR GeneID; 902735; -. DR KEGG; nme:NMB0622; -. DR PATRIC; 20356535; VBINeiMen85645_0787. DR eggNOG; ENOG4107Y7W; Bacteria. DR eggNOG; COG2834; LUCA. DR HOGENOM; HOG000257500; -. DR KO; K03634; -. DR OMA; YDADLNQ; -. DR OrthoDB; EOG6677VP; -. DR BioCyc; NMEN122586:GHGG-648-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0042954; F:lipoprotein transporter activity; IEA:InterPro. DR HAMAP; MF_00240; LolA; 1. DR InterPro; IPR029046; LolA/LolB/LppX. DR InterPro; IPR004564; OM_lipoprot_carrier_LolA-like. DR InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac. DR Pfam; PF03548; LolA; 1. DR SUPFAM; SSF89392; SSF89392; 1. DR TIGRFAMs; TIGR00547; lolA; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Periplasm; Protein transport; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 207 Outer-membrane lipoprotein carrier FT protein. FT /FTId=PRO_0000018265. SQ SEQUENCE 207 AA; 22284 MW; 849827D2CB0D86CA CRC64; MMKPHNLFQF LAVCSLTVAV ASAQAGAVDA LKQFNNDADG ISGSFTQTVQ SKKKTQTAHG TFKILRPGLF KWEYTKPYRQ TIVGDGQTVW LYDVDLAQVT KSSQDQAIGG SPAAILSNKT ALESSYTLKE DGSSNGIDYV LATPKRNNAG YQYIRIGFKG GNLAAMQLKD SFGNQTSISF GGLNTNPQLS RGAFKFTPPK GVDVLSN // ID LEU3_NEIMB Reviewed; 356 AA. AC Q9JZI9; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; DE EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033}; DE AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033}; DE AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033}; DE Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033}; GN Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033}; GN OrderedLocusNames=NMB1031; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- CC oxopentanoate. The product decarboxylates to 4-methyl-2 CC oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01033}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01033}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01033}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41430.1; -; Genomic_DNA. DR PIR; E81130; E81130. DR RefSeq; NP_274065.1; NC_003112.2. DR RefSeq; WP_002213431.1; NC_003112.2. DR ProteinModelPortal; Q9JZI9; -. DR SMR; Q9JZI9; 3-356. DR STRING; 122586.NMB1031; -. DR PaxDb; Q9JZI9; -. DR PRIDE; Q9JZI9; -. DR EnsemblBacteria; AAF41430; AAF41430; NMB1031. DR GeneID; 903168; -. DR KEGG; nme:NMB1031; -. DR PATRIC; 20357597; VBINeiMen85645_1315. DR eggNOG; ENOG4105C0C; Bacteria. DR eggNOG; COG0473; LUCA. DR HOGENOM; HOG000021112; -. DR KO; K00052; -. DR OMA; HCGPEVV; -. DR OrthoDB; EOG65N1BN; -. DR BioCyc; NMEN122586:GHGG-1068-MONOMER; -. DR UniPathway; UPA00048; UER00072. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_01033; LeuB_type1; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR004429; Isopropylmalate_DH. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR00169; leuB; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; KW Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 356 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000083712. FT NP_BIND 281 293 NAD. {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 223 223 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 247 247 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT METAL 251 251 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT BINDING 95 95 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 105 105 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 133 133 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT BINDING 223 223 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01033}. FT SITE 140 140 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01033}. FT SITE 191 191 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01033}. SQ SEQUENCE 356 AA; 38983 MW; 25FC63BB238A82BD CRC64; MTKHIAILRG DGIGPEIVAE TVRVLDKLIA QGLDAGYEYA PLGGEAYDEY GHPYPEFTQN LCRKADAVLL GAVGSPQYDN LDRPLRPERG LLAIRKDLNL FANLRPAVLY PELANASTLK PEIVAGLDIL IVRELTGDIY FGEPRGIRVL ENGEREGYNT MKYSESEIRR IAHVAFQSAQ KRSKKVCSVG KANVLETTEL WREIFEEIGK EYPDVELSHM YVDNAAMQLV RAPKQFDVIA TGNIFGDILS DEASMLTGSI GMLPSASLDE NGKGLYEPSH GSAPDIAGQN KANPLATILS LAMLLRYSLN DEARAQQVEN AVQKVLQQGL RTSDIYEEGT KLVSCSEMGD AVLAAL // ID LEUD_NEIMB Reviewed; 213 AA. AC Q9JZI6; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000255|HAMAP-Rule:MF_01031}; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01031}; DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01031}; DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01031}; DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01031}; GN Name=leuD {ECO:0000255|HAMAP-Rule:MF_01031}; GN OrderedLocusNames=NMB1034; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000255|HAMAP-Rule:MF_01031}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01031}. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01031}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP- CC Rule:MF_01031}. CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01031}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41433.1; -; Genomic_DNA. DR PIR; E81128; E81128. DR RefSeq; NP_274068.1; NC_003112.2. DR RefSeq; WP_002222556.1; NC_003112.2. DR ProteinModelPortal; Q9JZI6; -. DR STRING; 122586.NMB1034; -. DR PaxDb; Q9JZI6; -. DR PRIDE; Q9JZI6; -. DR EnsemblBacteria; AAF41433; AAF41433; NMB1034. DR GeneID; 903171; -. DR KEGG; nme:NMB1034; -. DR PATRIC; 20357603; VBINeiMen85645_1318. DR eggNOG; ENOG4105MQS; Bacteria. DR eggNOG; COG0066; LUCA. DR HOGENOM; HOG000222939; -. DR KO; K01704; -. DR OMA; AFTTHTG; -. DR OrthoDB; EOG661HCP; -. DR BioCyc; NMEN122586:GHGG-1071-MONOMER; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01031; LeuD_type1; 1. DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00171; leuD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 213 3-isopropylmalate dehydratase small FT subunit. FT /FTId=PRO_0000141845. SQ SEQUENCE 213 AA; 24264 MW; 871B2A849D610A0B CRC64; MKAFTKITAI VAPLDRSNVD TDAIIPKQFL KSIKRSGFGP NAFDEWRYLD HGEPGMDNSK RPLNPDFSLN QPRYQGAQIL LTRKNFGCGS SREHAPWALD DYGFRAVIAP SFADIFFNNC YKNGLLPIVL TEERVDRLFK EVEANEGYQL SIDLAEQTLT TPSGETFTFD ITEHRKHCLL NGLDEIGLTL QHADEIHAFE EKRRQSQPWL FNG // ID LEUC_NEIMB Reviewed; 469 AA. AC Q9JZI5; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026}; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026}; DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026}; DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026}; DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026}; GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; GN OrderedLocusNames=NMB1036; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01026}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP- CC Rule:MF_01026}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41435.1; -; Genomic_DNA. DR PIR; G81128; G81128. DR RefSeq; NP_274070.1; NC_003112.2. DR RefSeq; WP_002219221.1; NC_003112.2. DR ProteinModelPortal; Q9JZI5; -. DR STRING; 122586.NMB1036; -. DR PaxDb; Q9JZI5; -. DR EnsemblBacteria; AAF41435; AAF41435; NMB1036. DR GeneID; 903173; -. DR KEGG; nme:NMB1036; -. DR PATRIC; 20357607; VBINeiMen85645_1320. DR eggNOG; ENOG4105CQI; Bacteria. DR eggNOG; COG0065; LUCA. DR HOGENOM; HOG000226972; -. DR KO; K01703; -. DR OMA; CNMSIEM; -. DR OrthoDB; EOG600DP5; -. DR BioCyc; NMEN122586:GHGG-1073-MONOMER; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 3. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01026; LeuC_type1; 1. DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR PANTHER; PTHR11670; PTHR11670; 2. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR00170; leuC; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 469 3-isopropylmalate dehydratase large FT subunit. FT /FTId=PRO_0000076769. FT METAL 349 349 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. FT METAL 410 410 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. FT METAL 413 413 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. SQ SEQUENCE 469 AA; 50844 MW; D538C334E590E4E0 CRC64; MTAQTLYDKL WNSHVVREEE DGTVLLYIDR HLVHEVTSPQ AFEGLKMAGR KLWRIDSVVS TADHNTPTGD WDKGIQDPIS KLQVDTLDKN IKEFGALAYF PFMDKGQGIV HVMGPEQGAT LPGMTVVCGD SHTSTHGAFG ALAHGIGTSE VEHTMATQCI TAKKSKSMLI SVDGKLKAGV TAKDVALYII GQIGTAGGTG YAIEFGGEAI RSLSMESRMT LCNMAIEAGA RSGMVAVDQT TIDYVKDKPF APEGEAWDKA VEYWRTLVSD EGAVFDKEYR FNAEDIEPQV TWGTSPEMVL DISSKVPNPA EETDPVKRSG MERALEYMGL EAGTPLNEIP VDIVFIGSCT NSRIEDLREA AAIAKDRKKA ANVQRVLIVP GSGLVKEQAE KEGLDKIFIE AGFEWREPGC SMCLAMNADR LTPGQRCAST SNRNFEGRQG NGGRTHLVSP AMAAAAAVTG RFTDIRMMA // ID LGTE_NEIMB Reviewed; 280 AA. AC Q51117; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Lacto-N-neotetraose biosynthesis glycosyltransferase LgtE; DE EC=2.-.-.-; GN Name=lgtE; OrderedLocusNames=NMB1926; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=8817494; DOI=10.1111/j.1365-2958.1995.mmi_18040729.x; RA Jennings M.P., Hood D., Peak I.R.A., Virji M., Moxon E.R.; RT "Molecular analysis of a locus for the biosynthesis and phase-variable RT expression of the lacto-N-neotetraose terminal lipopolysaccharide RT structure in Neisseria meningitidis."; RL Mol. Microbiol. 18:729-740(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Adds the first galactose to the lacto-N-tetraose chain CC in lipooligosaccharide (LOS). CC -!- PATHWAY: Glycan metabolism; lacto-N-neotetraose biosynthesis. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide CC biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U25839; AAC44086.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42255.1; -; Genomic_DNA. DR PIR; A81027; A81027. DR PIR; S70815; S70815. DR RefSeq; NP_274920.1; NC_003112.2. DR RefSeq; WP_002225823.1; NC_003112.2. DR STRING; 122586.NMB1926; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR PaxDb; Q51117; -. DR EnsemblBacteria; AAF42255; AAF42255; NMB1926. DR GeneID; 904229; -. DR KEGG; nme:NMB1926; -. DR PATRIC; 20359901; VBINeiMen85645_2455. DR eggNOG; ENOG4107J0A; Bacteria. DR eggNOG; COG3306; LUCA. DR HOGENOM; HOG000218751; -. DR KO; K07270; -. DR OMA; KDREQGR; -. DR OrthoDB; EOG6R5C54; -. DR BioCyc; NMEN122586:GHGG-1983-MONOMER; -. DR UniPathway; UPA00501; -. DR UniPathway; UPA00820; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 280 Lacto-N-neotetraose biosynthesis FT glycosyltransferase LgtE. FT /FTId=PRO_0000216239. FT CONFLICT 16 16 A -> G (in Ref. 1; AAC44086). FT {ECO:0000305}. FT CONFLICT 89 92 Missing (in Ref. 1; AAC44086). FT {ECO:0000305}. FT CONFLICT 176 178 EWI -> RVD (in Ref. 1; AAC44086). FT {ECO:0000305}. SQ SEQUENCE 280 AA; 32790 MW; 826827E942BA5842 CRC64; MQNHVISLAS AAERRAHIAA TFGVRGIPFQ FFDALMPSEE LNRMMAELVP GLAKQHLLSE VEKACFMSHA VLWKQALDEG LPYVAVFEDD VLLGKDAEKF LAEDTWLEER FDKDSAFIVR LETMFAKVIV RPDKVLNYEN RSFPLLESEH WGTAGYIISR EAMRFFLERF AVLPAEWIKA VDWMMFTYFF DKEGMPVYQV NPALCTQELH YAKFLSKNSM LGSDLEKDRE QERRHRRSLK VMFDLKRALG KFGREKKKRM ERQRQAELEK AYGRRVISFK // ID LGUL_NEIMB Reviewed; 138 AA. AC P0A0T3; O33393; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Lactoylglutathione lyase; DE EC=4.4.1.5; DE AltName: Full=Aldoketomutase; DE AltName: Full=Glyoxalase I; DE Short=Glx I; DE AltName: Full=Ketone-aldehyde mutase; DE AltName: Full=Methylglyoxalase; DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase; GN Name=gloA; OrderedLocusNames=NMB0340; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SD / Serogroup B / Serotype 15 / Subtype 16; RX PubMed=10882093; RA Kizil G., Wilks K., Wells D., Ala'Aldeen D.A.A.; RT "Detection and characterisation of the genes encoding glyoxalase I and RT II from Neisseria meningitidis."; RL J. Med. Microbiol. 49:669-673(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from CC methylglyoxal and glutathione, to S-lactoylglutathione. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione + CC methylglyoxal. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; CC Note=Binds 1 nickel ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal CC degradation; (R)-lactate from methylglyoxal: step 1/2. CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y14298; CAA74673.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40783.1; -; Genomic_DNA. DR PIR; G81211; G81211. DR RefSeq; NP_273389.1; NC_003112.2. DR RefSeq; WP_002216418.1; NC_003112.2. DR ProteinModelPortal; P0A0T3; -. DR SMR; P0A0T3; 1-126. DR STRING; 122586.NMB0340; -. DR PaxDb; P0A0T3; -. DR EnsemblBacteria; AAF40783; AAF40783; NMB0340. DR GeneID; 902455; -. DR KEGG; nme:NMB0340; -. DR PATRIC; 20355825; VBINeiMen85645_0431. DR eggNOG; ENOG4108UYE; Bacteria. DR eggNOG; COG0346; LUCA. DR HOGENOM; HOG000232011; -. DR KO; K01759; -. DR OMA; THNWDTP; -. DR OrthoDB; EOG6DVJXX; -. DR BioCyc; NMEN122586:GHGG-361-MONOMER; -. DR BRENDA; 4.4.1.5; 3593. DR UniPathway; UPA00619; UER00675. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.180.10; -; 1. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR InterPro; IPR004361; Glyoxalase_1. DR InterPro; IPR018146; Glyoxalase_1_CS. DR Pfam; PF00903; Glyoxalase; 1. DR SUPFAM; SSF54593; SSF54593; 1. DR TIGRFAMs; TIGR00068; glyox_I; 1. DR PROSITE; PS00934; GLYOXALASE_I_1; 1. DR PROSITE; PS00935; GLYOXALASE_I_2; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Nickel; Reference proteome. FT CHAIN 1 138 Lactoylglutathione lyase. FT /FTId=PRO_0000168095. FT ACT_SITE 122 122 Proton donor/acceptor. {ECO:0000250}. FT METAL 5 5 Nickel; via tele nitrogen. {ECO:0000250}. FT METAL 56 56 Nickel. {ECO:0000250}. FT METAL 74 74 Nickel; via tele nitrogen. {ECO:0000250}. FT METAL 122 122 Nickel. {ECO:0000250}. FT BINDING 9 9 Substrate. {ECO:0000250}. FT BINDING 60 60 Substrate. {ECO:0000250}. FT BINDING 74 74 Substrate. {ECO:0000250}. SQ SEQUENCE 138 AA; 15669 MW; 3C3EFEA4FACAAFD3 CRC64; MRLLHTMLRV GNLEKSLDFY QNVLGMKLLR RKDYPEGRFT LAFVGYGDET DSTVLELTHN WDTERYDLGN AYGHIAVEVD DAYEACERVK RQGGNVVREA GPMKHGTTVI AFVEDPDGYK IEFIQKKSGD DSVAYQTA // ID LIPB_NEIMB Reviewed; 207 AA. AC Q9JZA4; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013}; DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013}; GN Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; GN OrderedLocusNames=NMB1217; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate CC although octanoyl-ACP is likely to be the physiological substrate. CC {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. CC {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of CC octanoic acid is attached via an amide linkage to the epsilon- CC amino group of a specific lysine residue of lipoyl domains of CC lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP- CC Rule:MF_00013}. CC -!- SIMILARITY: Contains 1 BPL/LPL catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41599.2; -; Genomic_DNA. DR PIR; E81109; E81109. DR RefSeq; NP_274242.2; NC_003112.2. DR RefSeq; WP_002217173.1; NC_003112.2. DR ProteinModelPortal; Q9JZA4; -. DR STRING; 122586.NMB1217; -. DR PaxDb; Q9JZA4; -. DR EnsemblBacteria; AAF41599; AAF41599; NMB1217. DR GeneID; 903639; -. DR KEGG; nme:NMB1217; -. DR PATRIC; 20358015; VBINeiMen85645_1520. DR eggNOG; ENOG4108BDP; Bacteria. DR eggNOG; COG0321; LUCA. DR HOGENOM; HOG000194321; -. DR KO; K03801; -. DR OMA; QLGRQPY; -. DR OrthoDB; EOG6XM7G6; -. DR BioCyc; NMEN122586:GHGG-1254-MONOMER; -. DR UniPathway; UPA00538; UER00592. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC. DR GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro. DR HAMAP; MF_00013; LipB; 1. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR000544; Octanoyltransferase. DR InterPro; IPR020605; Octanoyltransferase_CS. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR PIRSF; PIRSF016262; LPLase; 1. DR TIGRFAMs; TIGR00214; lipB; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. DR PROSITE; PS01313; LIPB; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 207 Octanoyltransferase. FT /FTId=PRO_0000062854. FT DOMAIN 27 203 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT REGION 66 73 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT REGION 133 135 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT REGION 146 148 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT ACT_SITE 164 164 Acyl-thioester intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00013}. FT SITE 130 130 Lowers pKa of active site Cys. FT {ECO:0000255|HAMAP-Rule:MF_00013}. SQ SEQUENCE 207 AA; 22841 MW; A2F6149B153D535C CRC64; MKIIHKGLVE YLPTFEAMKT FNAGRNADTE DELWVVEHPP VFTQGLAGKP EHLLIRDDIP VVQIDRGGQI TYHGPGQLVV YTMIDFKRRK TSVRNIVSAL ENSIIATLAE YGIEAAADPK RPGVYVGERK IASLGLRIKN GSVYHGLALN VNMDLSPFTH INPCGYAGME MTQIADFVQP CPTPDEVAAK LTAHLETQFT PKADNNE // ID LOLB_NEIMB Reviewed; 193 AA. AC P57024; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Outer-membrane lipoprotein LolB; DE Flags: Precursor; GN Name=lolB; OrderedLocusNames=NMB0873; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Plays a critical role in the incorporation of CC lipoproteins in the outer membrane after they are released by the CC LolA protein. {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LolB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41284.1; -; Genomic_DNA. DR PIR; A81149; A81149. DR RefSeq; NP_273914.1; NC_003112.2. DR RefSeq; WP_002219458.1; NC_003112.2. DR ProteinModelPortal; P57024; -. DR STRING; 122586.NMB0873; -. DR PaxDb; P57024; -. DR EnsemblBacteria; AAF41284; AAF41284; NMB0873. DR GeneID; 902989; -. DR KEGG; nme:NMB0873; -. DR PATRIC; 20357145; VBINeiMen85645_1089. DR eggNOG; COG3017; LUCA. DR HOGENOM; HOG000220712; -. DR KO; K02494; -. DR OMA; EILMKHT; -. DR OrthoDB; EOG6R5C6M; -. DR BioCyc; NMEN122586:GHGG-906-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008565; F:protein transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00233; LolB; 1. DR InterPro; IPR029046; LolA/LolB/LppX. DR InterPro; IPR004565; OM_lipoprot_LolB. DR Pfam; PF03550; LolB; 1. DR SUPFAM; SSF89392; SSF89392; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Chaperone; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Protein transport; Reference proteome; Signal; KW Transport. FT SIGNAL 1 15 {ECO:0000255}. FT CHAIN 16 193 Outer-membrane lipoprotein LolB. FT /FTId=PRO_0000018302. FT LIPID 16 16 N-palmitoyl cysteine. {ECO:0000255}. FT LIPID 16 16 S-diacylglycerol cysteine. {ECO:0000255}. SQ SEQUENCE 193 AA; 21141 MW; 4C2E97734BB2C41E CRC64; MKHTVSASVI LLLTACAQLP QNNENLWQPS EHISSFAAEG RLAVKAEGKG SYANFDWTYQ PPVETININT PLGSTLGQLC QDRDGALAVD GKGNVYQAES AEELSRQLVG FKLPIQYLHI WADGRRVAGA PYRILPDGIL EQYGWTVGRT ADSGGQVRTL QLNNGNLNIR LVFTEIGMPS ETETPERCAA RTR // ID LPB1_NEIMB Reviewed; 419 AA. AC Q05014; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 80. DE RecName: Full=Capsule polysaccharide modification protein LipB; GN Name=lipB; OrderedLocusNames=NMB0083; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=8326861; DOI=10.1111/j.1365-2958.1993.tb01592.x; RA Frosch M., Mueller A.; RT "Phospholipid substitution of capsular polysaccharides and mechanisms RT of capsule formation in Neisseria meningitidis."; RL Mol. Microbiol. 8:483-493(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the phospholipid modification of the CC capsular polysaccharide, a strong requirement for its CC translocation to the cell surface. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z13995; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AE002098; AAF40547.1; -; Genomic_DNA. DR PIR; E81240; E81240. DR RefSeq; NP_273146.1; NC_003112.2. DR RefSeq; WP_002223278.1; NC_003112.2. DR STRING; 122586.NMB0083; -. DR PaxDb; Q05014; -. DR EnsemblBacteria; AAF40547; AAF40547; NMB0083. DR GeneID; 902187; -. DR KEGG; nme:NMB0083; -. DR PATRIC; 20355169; VBINeiMen85645_0118. DR eggNOG; ENOG41084CK; Bacteria. DR eggNOG; COG3562; LUCA. DR HOGENOM; HOG000256629; -. DR KO; K07265; -. DR OMA; EHPLDNG; -. DR OrthoDB; EOG6W71WC; -. DR BioCyc; NMEN122586:GHGG-89-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW. DR InterPro; IPR007833; Capsule_polysaccharide_synth. DR Pfam; PF05159; Capsule_synth; 1. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Polysaccharide transport; Reference proteome; Sugar transport; KW Transport. FT CHAIN 1 419 Capsule polysaccharide modification FT protein LipB. FT /FTId=PRO_0000084464. FT CONFLICT 410 410 K -> N (in Ref. 1). {ECO:0000305}. FT CONFLICT 413 413 N -> D (in Ref. 1). {ECO:0000305}. FT CONFLICT 418 419 VI -> TT (in Ref. 1). {ECO:0000305}. SQ SEQUENCE 419 AA; 48702 MW; 096A5E05CB5D8283 CRC64; MKQTVLKNNL QNLLESAENI LLLQGPVGDF FLRLADWLTA NGKTVHKFNF NAGDDYFYPP TQAHTVVFND NYDAFPEFLQ EYITQHHIQA VVCFGDTRPY HVIAKRIANE NQASFWAFEE GYFRPYYITL EKDGVNAFSP LPRRADFFLE QFPKLAQQEY KAPTPVHGGF TPMAKNAIRY YIELFRNPRK YPDYIHHRAP NAGHYLKPWS LSILKRLNYY IEDIQIAKRV EAGKYGKFFI VPLQVFNDSQ VRIHCDFPSV RSFLLHVLSS FAEHAPADTN IIIKHHPMDR GFIDYWRDIK RFIKEHPELK GRVIYVHDVP LPVFLRHGLG MVTINSTSGL SGLIHNMPVK VLGRAYYDIP GITDQNTLAE FWNHPTPPDK ELFHAYRMYH LNVTQINGNF YSQVFFPNKK TSNSSTPVI // ID LGT_NEIMB Reviewed; 283 AA. AC Q9JZF9; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147}; DE EC=2.4.99.- {ECO:0000255|HAMAP-Rule:MF_01147}; GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147}; OrderedLocusNames=NMB1072; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers the N-acyl diglyceride group on what will CC become the N-terminal cysteine of membrane lipoproteins. CC {ECO:0000255|HAMAP-Rule:MF_01147}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis CC (diacylglyceryl transfer). {ECO:0000255|HAMAP-Rule:MF_01147}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01147}. CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP- CC Rule:MF_01147}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41467.1; -; Genomic_DNA. DR PIR; C81124; C81124. DR RefSeq; NP_274105.1; NC_003112.2. DR RefSeq; WP_002244115.1; NC_003112.2. DR STRING; 122586.NMB1072; -. DR PaxDb; Q9JZF9; -. DR EnsemblBacteria; AAF41467; AAF41467; NMB1072. DR GeneID; 903491; -. DR KEGG; nme:NMB1072; -. DR PATRIC; 20357693; VBINeiMen85645_1363. DR eggNOG; ENOG4105C3B; Bacteria. DR eggNOG; COG0682; LUCA. DR HOGENOM; HOG000098666; -. DR KO; K13292; -. DR OMA; YFAHPLD; -. DR OrthoDB; EOG6MH5CQ; -. DR BioCyc; NMEN122586:GHGG-1109-MONOMER; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro. DR HAMAP; MF_01147; Lgt; 1. DR InterPro; IPR001640; Prolipoprot_diAcglycer_Trfase. DR Pfam; PF01790; LGT; 1. DR TIGRFAMs; TIGR00544; lgt; 1. DR PROSITE; PS01311; LGT; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 283 Prolipoprotein diacylglyceryl FT transferase. FT /FTId=PRO_0000172641. FT TRANSMEM 15 37 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 57 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 91 113 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 224 241 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 256 278 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. SQ SEQUENCE 283 AA; 31821 MW; 82DCDA889788B9B9 CRC64; MITHPQFDPV LISIGPLAVR WYALSYILGF ILFTFLGRRR IAQGLSVFTK ESLDDFLTWG ILGVILGGRL GYVLFYKFSD YLAHPLDIFK VWEGGMSFHG GFLGVVIAIR LFGRKHGIGF LKLMDTVAPL VPLGLASGRI GNFINGELWG RVTDINAFWA MGFPQARYED AEAAAHNPLW AEWLQQYGML PRHPSQLYQF ALEGICLFTV IWLFSKKQRS TGQVASLFLG GYGIFRFIAE FARQPDDYLG LLTLGLSMGQ WLSVPMIVLG IVGFVRFGMK KQH // ID LPXH_NEIMB Reviewed; 240 AA. AC Q9K0P2; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000255|HAMAP-Rule:MF_00575}; DE EC=3.6.1.54 {ECO:0000255|HAMAP-Rule:MF_00575}; DE AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000255|HAMAP-Rule:MF_00575}; GN Name=lpxH {ECO:0000255|HAMAP-Rule:MF_00575}; GN OrderedLocusNames=NMB0544; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of the pyrophosphate bond of CC UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1- CC phosphate (lipid X) and UMP. {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- CATALYTIC ACTIVITY: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosamine + H(2)O = 2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + UMP. CC {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 4/6. {ECO:0000255|HAMAP- CC Rule:MF_00575}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000255|HAMAP- CC Rule:MF_00575}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40973.1; -; Genomic_DNA. DR PIR; F81186; F81186. DR RefSeq; NP_273589.1; NC_003112.2. DR RefSeq; WP_002225581.1; NC_003112.2. DR ProteinModelPortal; Q9K0P2; -. DR STRING; 122586.NMB0544; -. DR PaxDb; Q9K0P2; -. DR EnsemblBacteria; AAF40973; AAF40973; NMB0544. DR GeneID; 902659; -. DR KEGG; nme:NMB0544; -. DR PATRIC; 20356347; VBINeiMen85645_0692. DR eggNOG; ENOG4105F10; Bacteria. DR eggNOG; COG2908; LUCA. DR HOGENOM; HOG000261930; -. DR KO; K03269; -. DR OMA; FMHGNRD; -. DR OrthoDB; EOG6FNHR2; -. DR BioCyc; NMEN122586:GHGG-570-MONOMER; -. DR UniPathway; UPA00359; UER00480. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 2. DR HAMAP; MF_00575; LpxH; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR01854; lipid_A_lpxH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome. FT CHAIN 1 240 UDP-2,3-diacylglucosamine hydrolase. FT /FTId=PRO_0000214114. SQ SEQUENCE 240 AA; 27661 MW; 281B15453A2A078F CRC64; MKPAYFISDL HLSEKQPELT ALLLRFLRSS AAGQARAIYI LGDLFDFWVG DDEVSELNTS VAREIRKLSD KGVAVFFVRG NRDFLIGQDF CRQAGMTLLP DYSVLDLFGC KTLICHGDTL CTDDRAYQRF RKIVHRKRLQ KLFLMLPLKW RTRLATKIRR VSKMEKQVKP ADIMDVNAAF TARQVRAFGA ERLIHGHTHR EHIHHENGFT RIVLGDWHND YASILRVDGD GAVFVPLEKY // ID LPXK_NEIMB Reviewed; 344 AA. AC Q9K0D7; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409}; DE EC=2.7.1.130 {ECO:0000255|HAMAP-Rule:MF_00409}; DE AltName: Full=Lipid A 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409}; GN Name=lpxK {ECO:0000255|HAMAP-Rule:MF_00409}; GN OrderedLocusNames=NMB0672; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position CC of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1- CC P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). CC {ECO:0000255|HAMAP-Rule:MF_00409}. CC -!- CATALYTIC ACTIVITY: ATP + (2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl)-(1->6)-(2-N,3-O- CC bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl phosphate) = CC ADP + (2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-4-O-phospho-beta- CC D-glucosaminyl)-(1->6)-(2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosaminyl phosphate). {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41090.1; -; Genomic_DNA. DR PIR; F81170; F81170. DR RefSeq; NP_273714.1; NC_003112.2. DR RefSeq; WP_002217704.1; NC_003112.2. DR STRING; 122586.NMB0672; -. DR PaxDb; Q9K0D7; -. DR EnsemblBacteria; AAF41090; AAF41090; NMB0672. DR GeneID; 902783; -. DR KEGG; nme:NMB0672; -. DR PATRIC; 20356647; VBINeiMen85645_0842. DR eggNOG; ENOG4105CHD; Bacteria. DR eggNOG; COG1663; LUCA. DR HOGENOM; HOG000004953; -. DR KO; K00912; -. DR OMA; PTVIYLI; -. DR OrthoDB; EOG60GRWT; -. DR BioCyc; NMEN122586:GHGG-699-MONOMER; -. DR UniPathway; UPA00359; UER00482. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00409; LpxK; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003758; Tetraacyldisaccharide_4-kinase. DR Pfam; PF02606; LpxK; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00682; lpxK; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 344 Tetraacyldisaccharide 4'-kinase. FT /FTId=PRO_0000190933. FT NP_BIND 65 72 ATP. {ECO:0000255|HAMAP-Rule:MF_00409}. SQ SEQUENCE 344 AA; 37008 MW; 82A46DBCDE4AE3DD CRC64; MPNCFKFHTV IERHWQKPYP VLSFLLKPLS GLFAKIAAKR RTDFLSGKRQ SEKLPVPVVV VGNIHAGGTG KTPIVAALVS GLQEKGVKVG IISRGYGRKS KAVHVLNAES RAEDAGDEPL LLFRKTGAPT AVGSSRAEAG RALLAAHPDI GLIVADDGLQ HYALRRDVEI AVFPAADTGR TDLDLLPNGS LREPLLRLDS VDAVVVSGGK ADALFRPSEN MFHSRIEAGR IYRLNNPSEI LDTGRLKNQT VVAVAGIAKP ARFFDSLRNM GITVKRTVAL PDHADISAAD LPDADAVIIT EKDAVKFSDG ICTDNVWVLP VCAIIEPDLA AFVLERLEDV PKAV // ID LNT_NEIMB Reviewed; 512 AA. AC Q9K0A2; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 2. DT 13-APR-2016, entry version 84. DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148}; DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148}; DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01148}; GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=NMB0713; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins. CC {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01148}. CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- SIMILARITY: Contains 1 CN hydrolase domain. {ECO:0000255|HAMAP- CC Rule:MF_01148}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41128.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41128.1; ALT_INIT; Genomic_DNA. DR PIR; H81166; H81166. DR RefSeq; NP_273755.1; NC_003112.2. DR ProteinModelPortal; Q9K0A2; -. DR STRING; 122586.NMB0713; -. DR PaxDb; Q9K0A2; -. DR DNASU; 902825; -. DR EnsemblBacteria; AAF41128; AAF41128; NMB0713. DR GeneID; 902825; -. DR KEGG; nme:NMB0713; -. DR PATRIC; 20356775; VBINeiMen85645_0909. DR eggNOG; ENOG4105CE8; Bacteria. DR eggNOG; COG0815; LUCA. DR HOGENOM; HOG000264279; -. DR KO; K03820; -. DR OMA; IPQSMKW; -. DR OrthoDB; EOG6VTJXM; -. DR BioCyc; NMEN122586:GHGG-741-MONOMER; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; -; 1. DR HAMAP; MF_01148; Lnt; 1. DR InterPro; IPR004563; Apolipo_AcylTrfase. DR InterPro; IPR003010; C-N_Hydrolase. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR TIGRFAMs; TIGR00546; lnt; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 512 Apolipoprotein N-acyltransferase. FT /FTId=PRO_0000178077. FT TRANSMEM 15 37 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 58 80 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 90 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 124 143 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 163 185 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 198 215 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 488 507 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT DOMAIN 228 512 CN hydrolase. {ECO:0000255|HAMAP- FT Rule:MF_01148}. SQ SEQUENCE 512 AA; 57062 MW; 5FE83A4794DB64B0 CRC64; MVSKLDKYWQ HPALYWPLLI LFAAATPFTF APYYHFWLMP LIFGAFVRLI ELRPRFAVSS AYLFGLTAYT TQFYWIHTAL HDVSGLPDLY AVPLTFLLPA YLALYPALCF WLWKKFTLPR GIKIGLVLPI LWTLTEFARE RFLTGFGWGA IGYSQITPDS PLAGFAPLGG IHMVTLATAF LGVWLVLASN NTARSGKRLL PIILIAALLA AGYTARQTDF TRPDGSRSTV ALLQGNIDQT LKWREDQVIP TIQKYYEQVG KTTADIVILP ETAIPVMRQN LPENILAKFA EQAQNNGSAL AVGISQYTSD GNGYENAVIN LTGYQENNQD GIPYYAKNHL VPFGEYKPLP FLTTPLYKMM DMPLSDFRKG GGKQSALLMK NQKIAFNICY EDGFGDELIA AAKDATLLAN ASNMAWYGKS NAMYQHLQQS QARAMELGRY MVRATNTGAT AIISPKGNII AQAQPDTETV LEGHIKGYVG ETPYMKTGSS WWLMGILALA ALILFIFRNK EH // ID LOLD_NEIMB Reviewed; 231 AA. AC P57031; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Lipoprotein-releasing system ATP-binding protein LolD {ECO:0000255|HAMAP-Rule:MF_01708}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01708}; GN Name=lolD {ECO:0000255|HAMAP-Rule:MF_01708}; Synonyms=lolB; GN OrderedLocusNames=NMB1234; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter complex LolCDE involved in CC the translocation of mature outer membrane-directed lipoproteins, CC from the inner membrane to the periplasmic chaperone, LolA. CC Responsible for the formation of the LolA-lipoprotein complex in CC an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01708}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (LolD) and two transmembrane proteins (LolC and LolE). CC {ECO:0000255|HAMAP-Rule:MF_01708}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01708}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Lipoprotein translocase (TC 3.A.1.125) family. {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41615.1; -; Genomic_DNA. DR PIR; C81107; C81107. DR RefSeq; NP_274258.1; NC_003112.2. DR RefSeq; WP_002225197.1; NC_003112.2. DR ProteinModelPortal; P57031; -. DR STRING; 122586.NMB1234; -. DR PaxDb; P57031; -. DR EnsemblBacteria; AAF41615; AAF41615; NMB1234. DR GeneID; 903656; -. DR KEGG; nme:NMB1234; -. DR PATRIC; 20358063; VBINeiMen85645_1544. DR eggNOG; ENOG4105CQU; Bacteria. DR eggNOG; COG1136; LUCA. DR KO; K09810; -. DR OMA; SSGRYWL; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-1271-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0042954; F:lipoprotein transporter activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015854; ABC_transpr_LolD. DR InterPro; IPR011924; LolD_lipo_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02211; LolD_lipo_ex; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51244; LOLD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 231 Lipoprotein-releasing system ATP-binding FT protein LolD. FT /FTId=PRO_0000092443. FT DOMAIN 6 231 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01708}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_01708}. SQ SEQUENCE 231 AA; 25216 MW; 703FFB44BF8732B8 CRC64; MSELILKCEG VGKRYRDGGL DVRVLHGLDL EIHAGESTGI IGSSGSGKST LLHILGGLDM PSEGRVLLMG EDLRTLNQRR LGDLRNRHLG FVYQFHHLLP EFSALENVMM PLLIGKKSRE EAAEAAMAML EKVGLKHRST HRAGELSGGE RQRAAIARAL VTQPKCLLAD EPTGNLDRAN ARNVLDMMLE LKTELGTGLV VVTHDDELAG RFERVMVMKD GSLHPKQGAN A // ID LPXB_NEIMB Reviewed; 384 AA. AC Q9K1F5; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-MAY-2016, entry version 82. DE RecName: Full=Lipid-A-disaccharide synthase; DE EC=2.4.1.182; GN Name=lpxB; OrderedLocusNames=NMB0199; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a CC precursor of lipid A, a phosphorylated glycolipid that anchors the CC lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosamine + 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosaminyl 1-phosphate = UDP + 2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis((3R)- CC 3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 5/6. CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40656.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40656.1; ALT_INIT; Genomic_DNA. DR PIR; A81226; A81226. DR RefSeq; NP_273257.1; NC_003112.2. DR RefSeq; WP_010980760.1; NC_003112.2. DR ProteinModelPortal; Q9K1F5; -. DR STRING; 122586.NMB0199; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR PaxDb; Q9K1F5; -. DR EnsemblBacteria; AAF40656; AAF40656; NMB0199. DR GeneID; 902307; -. DR KEGG; nme:NMB0199; -. DR PATRIC; 20355441; VBINeiMen85645_0249. DR eggNOG; ENOG4105D0V; Bacteria. DR eggNOG; COG0763; LUCA. DR HOGENOM; HOG000018003; -. DR KO; K00748; -. DR OMA; YIAPQEW; -. DR OrthoDB; EOG6FBWZR; -. DR BioCyc; NMEN122586:GHGG-210-MONOMER; -. DR UniPathway; UPA00359; UER00481. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00392; LpxB; 1. DR InterPro; IPR003835; Glyco_trans_19. DR Pfam; PF02684; LpxB; 1. DR TIGRFAMs; TIGR00215; lpxB; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1 384 Lipid-A-disaccharide synthase. FT /FTId=PRO_0000190172. SQ SEQUENCE 384 AA; 42420 MW; 0951D9F9BE00821D CRC64; MADKKSPLIA VSVGEASGDL LGAHLIRAIR KRCPQARFTG IGGELMKAEG FESLYDQERL AVRGFVEVVR RLPEILRIRR GLVRDLLSLK PDVFVGIDAP DFNLGVAEKL KRSGIPTVHY VSPSVWAWRR ERVGKIVHQV NRVLCLFPME PQLYLDAGGR AEFVGHPMAQ LMPLEDDRET ARQTLGVDAG IPVFALLPGS RVSEIDYMAP VFFQTALLLL ERYPAARFLL PAATEATKRR LAEVLQRPEF AGLPLTVIDR QSETVCRAAD AVLVTSGTAT LEVALCKRPM VISYKISPLT YAYVKRKIKV PHVGLPNILL GKEAVPELLQ SEAKPEKLAA ALADWYEHPD KVAALQQDFR ALHLLLKKDT ADLAARAVLE EAGC // ID LPTD_NEIMB Reviewed; 802 AA. AC Q9K187; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 2. DT 16-MAR-2016, entry version 80. DE RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411}; DE Flags: Precursor; GN Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA; GN OrderedLocusNames=NMB0280; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Together with LptE, is involved in the assembly of CC lipopolysaccharide (LPS) at the surface of the outer membrane. CC {ECO:0000255|HAMAP-Rule:MF_01411}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. Interacts with LptE and LptA. CC {ECO:0000255|HAMAP-Rule:MF_01411}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01411}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP- CC Rule:MF_01411}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40734.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40734.1; ALT_INIT; Genomic_DNA. DR PIR; E81217; E81217. DR RefSeq; NP_273336.1; NC_003112.2. DR RefSeq; WP_010980769.1; NC_003112.2. DR STRING; 122586.NMB0280; -. DR TCDB; 1.B.42.1.1; the outer membrane lipopolysaccharide export porin (lps-ep) family. DR PaxDb; Q9K187; -. DR EnsemblBacteria; AAF40734; AAF40734; NMB0280. DR GeneID; 902391; -. DR KEGG; nme:NMB0280; -. DR PATRIC; 20355650; VBINeiMen85645_0349. DR eggNOG; ENOG4105E7H; Bacteria. DR eggNOG; COG1452; LUCA. DR HOGENOM; HOG000220687; -. DR KO; K04744; -. DR OMA; DYSHLDW; -. DR OrthoDB; EOG6SZ1CP; -. DR BioCyc; NMEN122586:GHGG-295-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro. DR GO; GO:0010033; P:response to organic substance; IEA:InterPro. DR HAMAP; MF_01411; LPS_assembly_LptD; 1. DR InterPro; IPR020889; LipoPS_assembly_LptD. DR InterPro; IPR007543; OstA_C. DR Pfam; PF04453; OstA_C; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal. FT SIGNAL 1 25 {ECO:0000255|HAMAP-Rule:MF_01411}. FT CHAIN 26 802 LPS-assembly protein LptD. FT /FTId=PRO_0000281620. SQ SEQUENCE 802 AA; 88693 MW; 3960E1F1C804B3AF CRC64; MARLFSLKPL VLALGLCFGT HCAAADAVAA EETDNPTAGE SVRSVSEPIQ PTSLSLGSTC LFCSNESGSP ERTEAAVQGS GEASIPEDYT RIVADRMEGQ SQVQVRAEGN VVVERNRTTL NTDWADYDQS GDTVTAGDRF ALQQDGTLIR GETLTYNLEQ QTGEAHNVRM EIEQGGRRLQ SVSRTAEMLG EGHYKLTETQ FNTCSAGDAG WYVKAASVEA DREKGIGVAK HAAFVFGGVP IFYTPWADFP LDGNRKSGLL VPSLSAGSDG VSLSVPYYFN LAPNLDATFA PSVIGERGAV FDGQVRYLRP DYAGQSDLTW LPHDKKSGRN NRYQAKWQHR HDISDTLQAG VDFNQVSDSG YYRDFYGNKE IAGNVNLNRR VWLDYGGRAA GGSLNAGLSV LKYQTLANQS GYKDKPYALM PRLSVEWRKN TGRAQIGVSA QFTRFSHDSR QDGSRLVVYP DIKWDFSNSW GYVRPKLGLH ATYYSLNRFG SQEARRVSRT LPIVNIDSGA TFERNTRMFG GEVLQTLEPR LFYNYIPAKS QNDLPNFDSS ESSFGYGQLF RENLYYGNDR INTANSLSAA VQSRILDGAT GEERFRAGIG QKFYFKDDAV MLDGSVGKKP RNRSDWVAFA SGSIGSRFIL DSSIHYNQND KRAENYAVGA SYRPAQGKVL NARYKYGRNE KIYLKSDGSY FYDKLSQLDL SAQWPLTRNL SAVVRYNYGF EAKKPIEVLA GAEYKSSCGC WGAGVYAQRY VTGENTYKNA VFFSLQLKDL SSVGRNPADR MDVAVPGYIT AHSLSAGRNK RP // ID LUXS_NEIMB Reviewed; 168 AA. AC Q9JXL8; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=S-ribosylhomocysteine lyase {ECO:0000255|HAMAP-Rule:MF_00091}; DE EC=4.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00091}; DE AltName: Full=AI-2 synthesis protein {ECO:0000255|HAMAP-Rule:MF_00091}; DE AltName: Full=Autoinducer-2 production protein LuxS {ECO:0000255|HAMAP-Rule:MF_00091}; GN Name=luxS {ECO:0000255|HAMAP-Rule:MF_00091}; GN OrderedLocusNames=NMB1981; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which CC is secreted by bacteria and is used to communicate both the cell CC density and the metabolic potential of the environment. The CC regulation of gene expression in response to changes in cell CC density is called quorum sensing. Catalyzes the transformation of CC S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5- CC dihydroxy-2,3-pentadione (DPD). {ECO:0000255|HAMAP-Rule:MF_00091}. CC -!- CATALYTIC ACTIVITY: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L- CC homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. CC {ECO:0000255|HAMAP-Rule:MF_00091}. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00091}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00091}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00091}. CC -!- SIMILARITY: Belongs to the LuxS family. {ECO:0000255|HAMAP- CC Rule:MF_00091}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42309.1; -; Genomic_DNA. DR PIR; F81020; F81020. DR RefSeq; NP_274974.1; NC_003112.2. DR RefSeq; WP_002225854.1; NC_003112.2. DR ProteinModelPortal; Q9JXL8; -. DR SMR; Q9JXL8; 3-162. DR STRING; 122586.NMB1981; -. DR PaxDb; Q9JXL8; -. DR EnsemblBacteria; AAF42309; AAF42309; NMB1981. DR GeneID; 904156; -. DR KEGG; nme:NMB1981; -. DR PATRIC; 20360037; VBINeiMen85645_2523. DR eggNOG; ENOG4106762; Bacteria. DR eggNOG; COG1854; LUCA. DR HOGENOM; HOG000040371; -. DR KO; K07173; -. DR OMA; AGFMREH; -. DR OrthoDB; EOG68WRBM; -. DR BioCyc; NMEN122586:GHGG-2038-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.80; -; 1. DR HAMAP; MF_00091; LuxS; 1. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR003815; S-ribosylhomocysteinase. DR Pfam; PF02664; LuxS; 1. DR PIRSF; PIRSF006160; AI2; 1. DR PRINTS; PR01487; LUXSPROTEIN. DR ProDom; PD013172; S-ribosylhomocysteinase; 1. DR SUPFAM; SSF63411; SSF63411; 1. PE 3: Inferred from homology; KW Autoinducer synthesis; Complete proteome; Iron; Lyase; Metal-binding; KW Quorum sensing; Reference proteome. FT CHAIN 1 168 S-ribosylhomocysteine lyase. FT /FTId=PRO_0000172240. FT METAL 54 54 Iron. {ECO:0000255|HAMAP-Rule:MF_00091}. FT METAL 58 58 Iron. {ECO:0000255|HAMAP-Rule:MF_00091}. FT METAL 128 128 Iron. {ECO:0000255|HAMAP-Rule:MF_00091}. SQ SEQUENCE 168 AA; 18653 MW; D4D3D9E4C6888953 CRC64; MPLLDSFKVD HTRMHAPAVR VAKTMTTPKG DTITVFDLRF CVPNKEILPG KGIHTLEHLF AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWLASMQD VLNVKDQSKI PELNEYQCGT YQMHSLAEAQ QIAQNVLARK VAVNKNEELT LDEGLLNA // ID LPXA_NEIMB Reviewed; 258 AA. AC P95379; Q9K1H3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-NOV-2015, entry version 106. DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387}; GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387}; GN OrderedLocusNames=NMB0178; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=9197543; DOI=10.1016/S0378-1119(97)00005-X; RA Steeghs L., Jennings M.P., Poolman J.T., Der Ley P.; RT "Isolation and characterization of the Neisseria meningitidis lpxD- RT fabZ-lpxA gene cluster involved in lipid A biosynthesis."; RL Gene 190:263-270(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a CC phosphorylated glycolipid that anchors the lipopolysaccharide to CC the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxytetradecanoyl-[acyl-carrier- CC protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier- CC protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D- CC glucosamine. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00387}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC LpxA subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U79481; AAC45424.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40635.1; -; Genomic_DNA. DR PIR; C81228; C81228. DR RefSeq; NP_273236.1; NC_003112.2. DR RefSeq; WP_002243945.1; NC_003112.2. DR ProteinModelPortal; P95379; -. DR STRING; 122586.NMB0178; -. DR PaxDb; P95379; -. DR EnsemblBacteria; AAF40635; AAF40635; NMB0178. DR GeneID; 902285; -. DR KEGG; nme:NMB0178; -. DR PATRIC; 20355381; VBINeiMen85645_0220. DR eggNOG; ENOG4105DAF; Bacteria. DR eggNOG; COG1043; LUCA. DR HOGENOM; HOG000294326; -. DR KO; K00677; -. DR OMA; VQDRSET; -. DR OrthoDB; EOG6F81P1; -. DR BioCyc; NMEN122586:GHGG-188-MONOMER; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1180.10; -; 1. DR HAMAP; MF_00387; LpxA; 1. DR InterPro; IPR029098; Acetyltransf_C. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR010137; Lipid_A_LpxA. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF13720; Acetyltransf_11; 1. DR Pfam; PF00132; Hexapep; 2. DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat; KW Transferase. FT CHAIN 1 258 Acyl-[acyl-carrier-protein]--UDP-N- FT acetylglucosamine O-acyltransferase. FT /FTId=PRO_0000188055. FT CONFLICT 64 64 L -> F (in Ref. 1; AAC45424). FT {ECO:0000305}. SQ SEQUENCE 258 AA; 28155 MW; EED23DB49DD62C8D CRC64; MTLIHPTAVI DPKAELDSGV KVGAYTVIGP NVQIGANTEI GPHAVINGHT SIGENNRIFQ FASLGEIPQD KKYRDEPTKL IIGNGNTIRE FTTFNLGTVT GIGETRIGDD NWIMAYCHLA HDCVIGNHTI FANNASLAGH VTIGDYVVLG GYTLVFQFCR IGDYAMTAFA AGVHKDVPPY FMASGYRAEP AGLNSEGMRR NGFTAEQISA VKDVYKTLYH RGIPFEEAKA DILRRAETQA ELAVFRDFFA QSARGIIR // ID LPXC_NEIMB Reviewed; 307 AA. AC Q9K1Q3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; DE EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388}; DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; GN Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388}; GN OrderedLocusNames=NMB0017; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and CC acetate, the committed step in lipid A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00388}. CC -!- CATALYTIC ACTIVITY: UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N- CC acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3- CC hydroxytetradecanoyl)-alpha-D-glucosamine + acetate. CC {ECO:0000255|HAMAP-Rule:MF_00388}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388}; CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP- CC Rule:MF_00388}. CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP- CC Rule:MF_00388}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40496.1; -; Genomic_DNA. DR PIR; E81246; E81246. DR RefSeq; NP_273083.1; NC_003112.2. DR RefSeq; WP_002216134.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q3; -. DR SMR; Q9K1Q3; 1-295. DR STRING; 122586.NMB0017; -. DR PaxDb; Q9K1Q3; -. DR EnsemblBacteria; AAF40496; AAF40496; NMB0017. DR GeneID; 902120; -. DR KEGG; nme:NMB0017; -. DR PATRIC; 20354969; VBINeiMen85645_0021. DR eggNOG; ENOG4105C7C; Bacteria. DR eggNOG; COG0774; LUCA. DR HOGENOM; HOG000256663; -. DR KO; K02535; -. DR OMA; NSMLVKA; -. DR OrthoDB; EOG6PGK74; -. DR BioCyc; NMEN122586:GHGG-18-MONOMER; -. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1700.10; -; 1. DR Gene3D; 3.30.230.20; -; 1. DR HAMAP; MF_00388; LpxC; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR004463; UDP-acyl_GlcNac_deAcase. DR InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C. DR InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N. DR Pfam; PF03331; LpxC; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR TIGRFAMs; TIGR00325; lpxC; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 307 UDP-3-O-acyl-N-acetylglucosamine FT deacetylase. FT /FTId=PRO_0000191941. FT ACT_SITE 266 266 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00388}. FT METAL 80 80 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00388}. FT METAL 239 239 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00388}. FT METAL 243 243 Zinc. {ECO:0000255|HAMAP-Rule:MF_00388}. SQ SEQUENCE 307 AA; 33987 MW; 2DD0122D744D3E1D CRC64; MLQRTLAKSI SVTGVGLHSG ERVALTLHPA PENSGISFRR TDLDGEMGEQ IKLTPYLIND TRLSSTIVTD KGVRVGTIEH IMSALSAYGI DNALIELNAP EIPIMDGSSL PFIYLLQDAG VVDQKAQKRF LKILKPVEIK EAGKWVRFTP YDGFKVTLTI EFDHPVFNRS SPTFEIDFAG KSYIDEIARA RTFGFMHEVE MMRAHNLGLG GNLNNAIVID DTDVLNPEGL RYPDEFVRHK ILDAIGDLYI VGHPIVGAFE GYKSGHAINN ALLRAVLADE TAYDRVEFAD SDDLPDAFHE LNIRTCG // ID LPXD_NEIMB Reviewed; 348 AA. AC P95377; Q9K1H2; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 11-NOV-2015, entry version 97. DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523}; DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00523}; GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; GN OrderedLocusNames=NMB0180; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=9197543; DOI=10.1016/S0378-1119(97)00005-X; RA Steeghs L., Jennings M.P., Poolman J.T., Der Ley P.; RT "Isolation and characterization of the Neisseria meningitidis lpxD- RT fabZ-lpxA gene cluster involved in lipid A biosynthesis."; RL Gene 190:263-270(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine CC using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the CC biosynthesis of lipid A, a phosphorylated glycolipid that anchors CC the lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + CC UDP-3-O-acyl-alpha-D-glucosamine = UDP-2,3-diacyl-alpha-D- CC glucosamine + [acyl-carrier-protein]. {ECO:0000255|HAMAP- CC Rule:MF_00523}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC LpxD subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U79481; AAC45422.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40637.1; -; Genomic_DNA. DR PIR; E81228; E81228. DR RefSeq; NP_273238.1; NC_003112.2. DR RefSeq; WP_002243946.1; NC_003112.2. DR ProteinModelPortal; P95377; -. DR STRING; 122586.NMB0180; -. DR PaxDb; P95377; -. DR EnsemblBacteria; AAF40637; AAF40637; NMB0180. DR GeneID; 902287; -. DR KEGG; nme:NMB0180; -. DR PATRIC; 20355385; VBINeiMen85645_0222. DR eggNOG; ENOG4105D7M; Bacteria. DR eggNOG; COG1044; LUCA. DR HOGENOM; HOG000294339; -. DR KO; K02536; -. DR OMA; WANVTLY; -. DR OrthoDB; EOG6JB11D; -. DR BioCyc; NMEN122586:GHGG-190-MONOMER; -. DR BRENDA; 2.3.1.191; 3593. DR UniPathway; UPA00973; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00523; LpxD; 1. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR007691; LpxD. DR InterPro; IPR011004; Trimer_LpxA-like. DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep. DR Pfam; PF00132; Hexapep; 2. DR Pfam; PF04613; LpxD; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat; KW Transferase. FT CHAIN 1 348 UDP-3-O-acylglucosamine N- FT acyltransferase. FT /FTId=PRO_0000059684. FT ACT_SITE 241 241 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00523}. FT CONFLICT 1 3 MIP -> VAV (in Ref. 2; AAC45422). FT {ECO:0000305}. SQ SEQUENCE 348 AA; 36449 MW; F555038EEAE229A8 CRC64; MIPATYTLSQ ITARLGGEWR GEDISVTAVR PLADAQAEHI SFLANPKYKA EVHDSSAGAV IVSAKAADGF EGRNLIVADD PYLYFAKVAR LFSPVVKARG GIHPTAVVEP GATVPTSCEI GANVYIGANT VLGEGCRILA NAVVQHDCKL GDEVVLHPNA VVYYGCTLGR RVEIHSGAVI GADGFGLAFA DDSWFKIPQT GAVTLGDDVE IGSNTNIDRG AMSDTTVGNG TKIDNQVQIG HNCKIGSHTV IAAKTGISGS VTIGSYCIIG GGVGTVGHIE IADKTTIGGG TSVTHSITES GKHLAGIFPM STHKEWARNA VYIHRLSEMN KRLKTLEQQL SDAGQDSK // ID MAFA_NEIMB Reviewed; 313 AA. AC Q9JS44; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=Adhesin MafA; DE Flags: Precursor; GN Name=mafA1; OrderedLocusNames=NMB0375; GN and GN Name=mafA2; OrderedLocusNames=NMB0652; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP INDUCTION. RC STRAIN=MC58; RX PubMed=12172557; DOI=10.1038/nbt728; RA Grifantini R., Bartolini E., Muzzi A., Draghi M., Frigimelica E., RA Berger J., Ratti G., Petracca R., Galli G., Agnusdei M., RA Giuliani M.M., Santini L., Brunelli B., Tettelin H., Rappuoli R., RA Randazzo F., Grandi G.; RT "Previously unrecognized vaccine candidates against group B RT meningococcus identified by DNA microarrays."; RL Nat. Biotechnol. 20:914-921(2002). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. CC -!- INDUCTION: Induced during interaction with human epithelial cells. CC {ECO:0000269|PubMed:12172557}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the MafA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41073.1; -; Genomic_DNA. DR EMBL; AE002098; AAF62309.1; -; Genomic_DNA. DR PIR; G81173; G81173. DR RefSeq; NP_273424.1; NC_003112.2. DR RefSeq; NP_273694.1; NC_003112.2. DR RefSeq; WP_002222000.1; NC_003112.2. DR STRING; 122586.NMB0652; -. DR PaxDb; Q9JS44; -. DR EnsemblBacteria; AAF41073; AAF41073; NMB0652. DR EnsemblBacteria; AAF62309; AAF62309; NMB0375. DR GeneID; 902490; -. DR GeneID; 902764; -. DR KEGG; nme:NMB0375; -. DR KEGG; nme:NMB0652; -. DR PATRIC; 20355909; VBINeiMen85645_0472. DR HOGENOM; HOG000071263; -. DR OMA; LTKNNGR; -. DR OrthoDB; EOG6VMTH8; -. DR BioCyc; NMEN122586:GHGG-397-MONOMER; -. DR BioCyc; NMEN122586:GHGG-679-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell adhesion; Cell outer membrane; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Reference proteome; Signal; Virulence. FT SIGNAL 1 14 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 15 313 Adhesin MafA. FT /FTId=PRO_0000344487. FT LIPID 15 15 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 15 15 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 313 AA; 34000 MW; 360676272DAD60C1 CRC64; MKTLLLLIPL VLTACGTLTG IPAHGGGKRF AVEQELVAAS SRAAVKEMDL SALKGRKAAL YVSVMGDQGS GNISGGRYSI DALIRGGYHN NPESATQYSY PAYDTTATTK SDALSSVTTS TSLLNAPAAA LTKNSGRKGE RSAGLSVNGT GDYRNETLLA NPRDVSFLTN LIQTVFYLRG IEVVPPEYAD TDVFVTVDVF GTVRSRTELH LYNAETLKAQ TKLEYFAVDR DSRKLLITPK TAAYESQYQE QYALWTGPYK VSKTVKASDR LMVDFSDITP YGDTTAQNRP DFKQNNGKKP DVGNEVIRRR KGG // ID LSPA_NEIMB Reviewed; 165 AA. AC P65265; Q9JVY3; Q9JXY8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161}; DE EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161}; DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161}; DE AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161}; DE Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161}; GN Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161}; Synonyms=lsp; GN OrderedLocusNames=NMB1832; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000255|HAMAP- CC Rule:MF_00161}. CC -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial CC membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|- CC (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably CC Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, CC neutral side chains. {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00161}. CC -!- SIMILARITY: Belongs to the peptidase A8 family. CC {ECO:0000255|HAMAP-Rule:MF_00161}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42167.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42167.1; ALT_INIT; Genomic_DNA. DR PIR; E81038; E81038. DR RefSeq; NP_274829.1; NC_003112.2. DR STRING; 122586.NMB1832; -. DR MEROPS; A08.001; -. DR PaxDb; P65265; -. DR EnsemblBacteria; AAF42167; AAF42167; NMB1832. DR GeneID; 903268; -. DR KEGG; nme:NMB1832; -. DR PATRIC; 20359653; VBINeiMen85645_2332. DR eggNOG; ENOG4105M02; Bacteria. DR eggNOG; COG0597; LUCA. DR HOGENOM; HOG000096993; -. DR KO; K03101; -. DR OMA; DCAITVG; -. DR OrthoDB; EOG6PGKBM; -. DR BioCyc; NMEN122586:GHGG-1887-MONOMER; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00161; LspA; 1. DR InterPro; IPR001872; Peptidase_A8. DR PANTHER; PTHR33695:SF1; PTHR33695:SF1; 1. DR Pfam; PF01252; Peptidase_A8; 1. DR PRINTS; PR00781; LIPOSIGPTASE. DR TIGRFAMs; TIGR00077; lspA; 1. DR PROSITE; PS00855; SPASE_II; 1. PE 3: Inferred from homology; KW Aspartyl protease; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Protease; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 165 Lipoprotein signal peptidase. FT /FTId=PRO_0000178800. FT TRANSMEM 39 61 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 71 88 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 95 117 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 130 152 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT ACT_SITE 113 113 {ECO:0000255|HAMAP-Rule:MF_00161}. FT ACT_SITE 140 140 {ECO:0000255|HAMAP-Rule:MF_00161}. SQ SEQUENCE 165 AA; 18600 MW; 0A72DAB8B4973963 CRC64; MSSSVSSKTR YWVLALAAIV LDQWSKWAVL SSFQYRERVN VIPSFFDLTL VYNPGAAFSF LADQGGWQKY FFLVLAVAVS AYLVRAILRD EFATLGKTGA AMIIGGALGN VIDRLIHGHV VDFLLFYWQN WFYPAFNIAD SFICVGAVLA VLDNIVHRKT QEEKY // ID MACB_NEIMB Reviewed; 644 AA. AC Q9K0N7; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000255|HAMAP-Rule:MF_01720}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01720}; GN Name=macB {ECO:0000255|HAMAP-Rule:MF_01720}; GN OrderedLocusNames=NMB0549; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Non-canonical ABC transporter that contains CC transmembrane domains (TMD), which form a pore in the inner CC membrane, and an ATP-binding domain (NBD), which is responsible CC for energy generation. Confers resistance against macrolides. CC {ECO:0000255|HAMAP-Rule:MF_01720}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01720}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01720}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide CC exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01720}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40978.1; -; Genomic_DNA. DR PIR; C81187; C81187. DR RefSeq; NP_273594.1; NC_003112.2. DR RefSeq; WP_002247530.1; NC_003112.2. DR ProteinModelPortal; Q9K0N7; -. DR STRING; 122586.NMB0549; -. DR PaxDb; Q9K0N7; -. DR EnsemblBacteria; AAF40978; AAF40978; NMB0549. DR GeneID; 902664; -. DR KEGG; nme:NMB0549; -. DR PATRIC; 20356361; VBINeiMen85645_0699. DR eggNOG; ENOG4105D6C; Bacteria. DR eggNOG; COG0577; LUCA. DR eggNOG; COG1136; LUCA. DR HOGENOM; HOG000208217; -. DR KO; K05685; -. DR OMA; LNTDDIR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-575-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0042895; F:antibiotic transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0016820; F:hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR017911; ABC_transptr_macrolide_ATP-bd. DR InterPro; IPR025857; MacB_PCD. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51267; MACB; 1. PE 3: Inferred from homology; KW Antibiotic resistance; ATP-binding; Cell inner membrane; KW Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 644 Macrolide export ATP-binding/permease FT protein MacB. FT /FTId=PRO_0000269950. FT TRANSMEM 270 290 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01720}. FT TRANSMEM 524 544 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01720}. FT TRANSMEM 574 594 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01720}. FT TRANSMEM 607 627 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01720}. FT DOMAIN 4 242 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01720}. FT NP_BIND 40 47 ATP. {ECO:0000255|HAMAP-Rule:MF_01720}. SQ SEQUENCE 644 AA; 69439 MW; 4256DC41D64D3A9D CRC64; MSLIECKNIN RYFGSGENRV HILKDISLSI EKGDFVAIIG QSGSGKSTLM NILGCLDTAG SGSYRIDGIE TAKMQPDELA ALRRERFGFI FQRYNLLSSL TARDNVALPA VYMGAGGKER SARADKLLQD LGLASKEGNK PGELSGGQQQ RVSIARALMN GGEIIFADEP TGALDTASGK NVMEIIRRLH EAGHTVIMVT HDPDIAANAN RVIEIRDGEI ISDTSKNPEI PASNVGRIRE KASWSFYYDQ FVEAFRMSVQ AVLAHKMRSL LTMLGIIIGI ASVVSVVALG NGSQKKILED ISSIGTNTIS IFPGRGFGDR RSGRIKTLTI DDAKIIAKQS YVASATPMTS SGGTLTYRNT DLTASLYGVG EQYFDVRGLK LETGRLFDEN DVKEDAQVVV IDQNVKDKLF ADSDPLGKTI LFRKRPLTVI GVMKKDENAF GNSDVLMLWS PYTTVMHQIT GESHTNSITV KIKDNANTQV AEKGLTDLLK ARHGTEDFFM NNSDSIRQIV ESTTGTMKLL ISSIALISLV VGGIGVMNIM LVSVTERTKE IGIRMAIGAR RGNILQQFLI EAVLICVIGG LVGVGLSAAV SLVFNHFVTD FPMDISAMSV IGAVACSTGI GIAFGFMPAN KAAKLNPIDA LAQD // ID LST_NEIMB Reviewed; 371 AA. AC P72097; P72099; P72100; P72101; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase; DE Short=Alpha 2,3-ST; DE Short=Beta-galactoside alpha-2,3-sialyltransferase; DE EC=2.4.99.-; DE AltName: Full=Lipooligosaccharide sialyltransferase; GN Name=lst; OrderedLocusNames=NMB0922; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=406Y / NRCC 4030, M982B / NRCC 4725, and MC58 / NRCC 4728; RX PubMed=8910446; DOI=10.1074/jbc.271.45.28271; RA Gilbert M., Watson D.C., Cunningham A.-M., Jennings M.P., Young N.M., RA Wakarchuk W.W.; RT "Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from RT the bacterial pathogens Neisseria meningitidis and Neisseria RT gonorrhoeae."; RL J. Biol. Chem. 271:28271-28276(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=126E / NRCC 4010; RA Gilbert M., Michniewicz J.J., Watson D.C., Wakarchuk W.W.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Transfers sialic acid from the substrate CMP-sialic acid CC donor to the terminal beta-D-galactosyl-1,4-acetyl-beta-D- CC glucosamine on the lacto-N-neotetraose branch of the CC lipooligosaccharide. CC -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl- CC 1,4-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl- CC 2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U60660; AAC44541.1; -; Genomic_DNA. DR EMBL; U60661; AAC44543.1; -; Genomic_DNA. DR EMBL; U60662; AAC44544.2; -; Genomic_DNA. DR EMBL; U60663; AAC44545.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41330.1; -; Genomic_DNA. DR PIR; D81143; D81143. DR RefSeq; NP_273962.1; NC_003112.2. DR RefSeq; WP_002244089.1; NC_003112.2. DR PDB; 2YK4; X-ray; 1.94 A; A=49-370. DR PDB; 2YK5; X-ray; 2.32 A; A=49-370. DR PDB; 2YK6; X-ray; 2.83 A; A=49-370. DR PDB; 2YK7; X-ray; 2.18 A; A=49-370. DR PDBsum; 2YK4; -. DR PDBsum; 2YK5; -. DR PDBsum; 2YK6; -. DR PDBsum; 2YK7; -. DR STRING; 122586.NMB0922; -. DR CAZy; GT52; Glycosyltransferase Family 52. DR PaxDb; P72097; -. DR EnsemblBacteria; AAF41330; AAF41330; NMB0922. DR GeneID; 903043; -. DR KEGG; nme:NMB0922; -. DR PATRIC; 20357291; VBINeiMen85645_1159. DR eggNOG; ENOG4105P7J; Bacteria. DR eggNOG; ENOG4111XG2; LUCA. DR HOGENOM; HOG000220741; -. DR KO; K00785; -. DR OMA; CCTPLQV; -. DR OrthoDB; EOG6MD922; -. DR BioCyc; NMEN122586:GHGG-960-MONOMER; -. DR UniPathway; UPA00030; -. DR EvolutionaryTrace; P72097; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012477; Glyco_transf_52. DR Pfam; PF07922; Glyco_transf_52; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 371 CMP-N-acetylneuraminate-beta- FT galactosamide-alpha-2,3- FT sialyltransferase. FT /FTId=PRO_0000080574. FT VARIANT 2 2 G -> S (in strain: M982B / NRCC 4725). FT VARIANT 29 29 Q -> H (in strain: 406Y / NRCC 4030 and FT NRCC 4725). FT VARIANT 40 40 E -> D (in strain: 406Y / NRCC 4030, FT M982B / NRCC 4725 and 126E / NRCC 4010). FT VARIANT 94 94 N -> K (in strain: 406Y / NRCC 4030 and FT M982B / NRCC 4725). FT VARIANT 102 102 R -> W (in strain: 126E / NRCC 4010). FT VARIANT 129 129 S -> A (in strain: 126E / NRCC 4010). FT VARIANT 168 168 G -> I (in strain: 126E / NRCC 4010). FT VARIANT 242 242 T -> A (in strain: 406Y / NRCC 4030 and FT 126E / NRCC 4010). FT VARIANT 273 273 K -> N (in strain: 406Y / NRCC 4030 and FT 126E / NRCC 4010). FT STRAND 50 55 {ECO:0000244|PDB:2YK4}. FT HELIX 58 70 {ECO:0000244|PDB:2YK4}. FT STRAND 74 83 {ECO:0000244|PDB:2YK4}. FT HELIX 87 99 {ECO:0000244|PDB:2YK4}. FT STRAND 100 107 {ECO:0000244|PDB:2YK4}. FT HELIX 122 131 {ECO:0000244|PDB:2YK4}. FT STRAND 136 141 {ECO:0000244|PDB:2YK4}. FT HELIX 144 147 {ECO:0000244|PDB:2YK4}. FT HELIX 149 153 {ECO:0000244|PDB:2YK4}. FT STRAND 158 163 {ECO:0000244|PDB:2YK4}. FT HELIX 167 170 {ECO:0000244|PDB:2YK4}. FT HELIX 173 177 {ECO:0000244|PDB:2YK4}. FT HELIX 179 181 {ECO:0000244|PDB:2YK4}. FT STRAND 183 186 {ECO:0000244|PDB:2YK6}. FT HELIX 187 204 {ECO:0000244|PDB:2YK4}. FT STRAND 210 214 {ECO:0000244|PDB:2YK4}. FT STRAND 224 231 {ECO:0000244|PDB:2YK4}. FT HELIX 237 240 {ECO:0000244|PDB:2YK7}. FT STRAND 249 254 {ECO:0000244|PDB:2YK4}. FT HELIX 259 261 {ECO:0000244|PDB:2YK4}. FT HELIX 262 272 {ECO:0000244|PDB:2YK4}. FT STRAND 276 278 {ECO:0000244|PDB:2YK4}. FT STRAND 290 292 {ECO:0000244|PDB:2YK4}. FT HELIX 299 309 {ECO:0000244|PDB:2YK4}. FT STRAND 314 321 {ECO:0000244|PDB:2YK4}. FT HELIX 324 328 {ECO:0000244|PDB:2YK4}. FT STRAND 334 341 {ECO:0000244|PDB:2YK4}. FT HELIX 346 348 {ECO:0000244|PDB:2YK4}. FT HELIX 351 359 {ECO:0000244|PDB:2YK4}. FT STRAND 364 367 {ECO:0000244|PDB:2YK4}. SQ SEQUENCE 371 AA; 42611 MW; 1C0E51DA3DAACD15 CRC64; MGLKKACLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKE KLFNEEGEPV NLIFCYTILQ MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFHLPY GLNKSFNFIP TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTGNL IQSSSYLGDE FSVNGTIKRN FARMMIGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL KTGDETGGTV RILLGSPDKE MKEISEKAAK NFKIQYVAPH PRQTYGLSGV TTLNSPYVIE DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFTQS GIPILTFDDK N // ID METE_NEIMB Reviewed; 758 AA. AC Q9JZQ2; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; DE EC=2.1.1.14; DE AltName: Full=Cobalamin-independent methionine synthase; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme; GN Name=metE; OrderedLocusNames=NMB0944; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L- CC homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetE route): step CC 1/1. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine CC synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41350.1; -; Genomic_DNA. DR PIR; E81140; E81140. DR RefSeq; NP_273982.1; NC_003112.2. DR RefSeq; WP_002223856.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ2; -. DR STRING; 122586.NMB0944; -. DR PaxDb; Q9JZQ2; -. DR PRIDE; Q9JZQ2; -. DR EnsemblBacteria; AAF41350; AAF41350; NMB0944. DR GeneID; 903064; -. DR KEGG; nme:NMB0944; -. DR PATRIC; 20357369; VBINeiMen85645_1199. DR eggNOG; ENOG4105DSS; Bacteria. DR eggNOG; COG0620; LUCA. DR HOGENOM; HOG000246221; -. DR KO; K00549; -. DR OMA; RFGWVQS; -. DR OrthoDB; EOG6FFS3G; -. DR BioCyc; NMEN122586:GHGG-981-MONOMER; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00172; Meth_synth; 1. DR InterPro; IPR013215; Cbl-indep_Met_Synth_N. DR InterPro; IPR006276; Cobalamin-indep_Met_synthase. DR InterPro; IPR002629; Met_Synth_C/arc. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW Repeat; Transferase; Zinc. FT CHAIN 1 758 5-methyltetrahydropteroyltriglutamate-- FT homocysteine methyltransferase. FT /FTId=PRO_0000098644. FT METAL 643 643 Zinc. {ECO:0000250}. FT METAL 645 645 Zinc. {ECO:0000250}. FT METAL 728 728 Zinc. {ECO:0000250}. SQ SEQUENCE 758 AA; 85077 MW; B0EAE33B7ECDEE7D CRC64; MTTLHFSGFP RVGAFRELKF AQEKYWRKEI SEQELLAVAK DLREKNWKHQ VAANADFVAV GDFTFYDHIL DLQVATGAIP ARFGFDSQNL SLEQFFQLAR GNKDQFAIEM TKWFDTNYHY LVPEFHADTE FKANAKHYVQ QLQEAQALGL KAKPTVVGPL TFLWVGKEKG AVEFDRLSLL PKLLPVYVEI LTALVEAGAE WIQIDEPALA VDLPKEWVEA YKDVYATLSK VSAKILLSTY FGSVAEHAAL LKALPVDGLH IDLVRAPEQL DAFADYDKVL SAGVIDGRNI WRANLNKVLE TVEPLQAKLG DRLWISSSCS LLHTPFDLSV EEKLKANKPD LYSWLAFTLQ KTQELRVLKA ALNEGRDSVA EELAASQAAA DSRANSSEIH RADVAKRLAD LPANADQRKS PFADRIKAQQ AWLNLPLLPT TNIGSFPQTT EIRQARSAFK KGELSAADYE AAMKKEIALV VEEQEKLDLD VLVHGEAERN DMVEYFGELL SGFAFTQYGW VQSYGSRCVK PPIIFGDVSR PEAMTVAWST YAQSLTKRPM KGMLTGPVTI LQWSFVRNDI PRSTVCKQIA LALNDEVLDL EKAGIKVIQI DEPAIREGLP LKRADWDAYL NWAGESFRLS SAGCEDSTQI HTHMCYSEFN DILPAIAAMD ADVITIETSR SDMELLTAFG EFQYPNDIGP GVYDIHSPRV PTEAEVEHLL RKAIEVVPVE RLWVNPDCGL KTRGWKETLE QLQVMMNVTR KLRAELAK // ID METK_NEIMB Reviewed; 389 AA. AC Q9JY09; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00086}; DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00086}; DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00086}; DE AltName: Full=MAT {ECO:0000255|HAMAP-Rule:MF_00086}; DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00086}; GN Name=metK {ECO:0000255|HAMAP-Rule:MF_00086}; GN OrderedLocusNames=NMB1799; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. The overall synthetic reaction is composed of CC two sequential steps, AdoMet formation and the subsequent CC tripolyphosphate hydrolysis which occurs prior to release of CC AdoMet from the enzyme. {ECO:0000255|HAMAP-Rule:MF_00086}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. {ECO:0000255|HAMAP- CC Rule:MF_00086}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086}; CC Note=Binds 2 divalent ions per subunit. Magnesium or cobalt. CC {ECO:0000255|HAMAP-Rule:MF_00086}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00086}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00086}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00086}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00086}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42136.1; -; Genomic_DNA. DR PIR; D81042; D81042. DR RefSeq; NP_274796.1; NC_003112.2. DR RefSeq; WP_002225644.1; NC_003112.2. DR ProteinModelPortal; Q9JY09; -. DR SMR; Q9JY09; 2-389. DR STRING; 122586.NMB1799; -. DR PaxDb; Q9JY09; -. DR EnsemblBacteria; AAF42136; AAF42136; NMB1799. DR GeneID; 903300; -. DR KEGG; nme:NMB1799; -. DR PATRIC; 20359567; VBINeiMen85645_2289. DR eggNOG; ENOG4105CPH; Bacteria. DR eggNOG; COG0192; LUCA. DR HOGENOM; HOG000245710; -. DR KO; K00789; -. DR OMA; DNFLAFD; -. DR OrthoDB; EOG68WR6M; -. DR BioCyc; NMEN122586:GHGG-1854-MONOMER; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00086; S_AdoMet_synth1; 1. DR InterPro; IPR022631; ADOMET_SYNTHASE_CS. DR InterPro; IPR022630; S-AdoMet_synt_C. DR InterPro; IPR022629; S-AdoMet_synt_central. DR InterPro; IPR022628; S-AdoMet_synt_N. DR InterPro; IPR002133; S-AdoMet_synthetase. DR InterPro; IPR022636; S-AdoMet_synthetase_sfam. DR PANTHER; PTHR11964; PTHR11964; 1. DR Pfam; PF02773; S-AdoMet_synt_C; 1. DR Pfam; PF02772; S-AdoMet_synt_M; 1. DR Pfam; PF00438; S-AdoMet_synt_N; 1. DR PIRSF; PIRSF000497; MAT; 1. DR SUPFAM; SSF55973; SSF55973; 3. DR TIGRFAMs; TIGR01034; metK; 1. DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cobalt; Complete proteome; Cytoplasm; Magnesium; KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 389 S-adenosylmethionine synthase. FT /FTId=PRO_0000174560. FT NP_BIND 264 271 ATP. {ECO:0000255|HAMAP-Rule:MF_00086}. FT METAL 17 17 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00086}. FT METAL 43 43 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00086}. FT METAL 268 268 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00086}. FT METAL 276 276 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00086}. SQ SEQUENCE 389 AA; 42099 MW; 18F4E98E56084FA7 CRC64; MSEYLFTSES VSEGHPDKVA DQVSDAILDA ILAQDPKARV AAETLVNTGL CVLAGEITTT AQVDYIKVAR ETIKRIGYNS SELGFDANGC AVGVYYDQQS PDIAQGVNEG EGIDLNQGAG DQGLMFGYAC DETPTLMPFA IYYSHRLMQR QSELRKDGRL PWLRPDAKAQ LTVVYDSETG KVKRIDTVVL STQHDPSIAY EELKNAVIEH IIKPVLPSEL LTDETKYLIN PTGRFVIGGP QGDCGLTGRK IIVDTYGGAA PHGGGAFSGK DPSKVDRSAA YACRYVAKNI VAAGLATQCQ IQVSYAIGVA EPTSISIDTF GTGKISEEKL IALVREHFDL RPKGIVQMLD LLRPIYSKSA AYGHFGREEP EFTWERTDKA AALRAAAGL // ID METF_NEIMB Reviewed; 292 AA. AC Q9JZQ3; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=5,10-methylenetetrahydrofolate reductase; DE EC=1.5.1.20; GN Name=metF; OrderedLocusNames=NMB0943; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41349.1; -; Genomic_DNA. DR PIR; D81140; D81140. DR RefSeq; NP_273981.1; NC_003112.2. DR RefSeq; WP_002223857.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ3; -. DR SMR; Q9JZQ3; 3-292. DR STRING; 122586.NMB0943; -. DR PaxDb; Q9JZQ3; -. DR PRIDE; Q9JZQ3; -. DR EnsemblBacteria; AAF41349; AAF41349; NMB0943. DR GeneID; 903063; -. DR KEGG; nme:NMB0943; -. DR PATRIC; 20357367; VBINeiMen85645_1198. DR eggNOG; ENOG4105SYT; Bacteria. DR eggNOG; COG0685; LUCA. DR HOGENOM; HOG000246232; -. DR KO; K00297; -. DR OMA; EMHPQAR; -. DR OrthoDB; EOG6D2KVW; -. DR BioCyc; NMEN122586:GHGG-980-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR004620; MTHF_reductase_bac. DR Pfam; PF02219; MTHFR; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR TIGRFAMs; TIGR00676; fadh2; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; KW Methionine biosynthesis; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 292 5,10-methylenetetrahydrofolate reductase. FT /FTId=PRO_0000320271. FT NP_BIND 26 31 NAD. {ECO:0000250}. FT NP_BIND 57 60 FAD. {ECO:0000250}. FT NP_BIND 57 58 NAD. {ECO:0000250}. FT NP_BIND 116 118 FAD. {ECO:0000250}. FT NP_BIND 129 130 FAD. {ECO:0000250}. FT NP_BIND 154 157 FAD. {ECO:0000250}. FT NP_BIND 163 170 FAD. {ECO:0000250}. FT ACT_SITE 26 26 Proton donor/acceptor. {ECO:0000250}. FT BINDING 86 86 FAD. {ECO:0000250}. FT BINDING 118 118 Substrate. {ECO:0000250}. FT BINDING 150 150 FAD. {ECO:0000250}. FT BINDING 181 181 Substrate. {ECO:0000250}. FT BINDING 217 217 Substrate. {ECO:0000250}. FT BINDING 273 273 Substrate. {ECO:0000250}. FT BINDING 277 277 Substrate. {ECO:0000250}. SQ SEQUENCE 292 AA; 33056 MW; 32B22282A681CB1F CRC64; MNYAKEINAL NNSLSDLKGD INVSFEFFPP KNEQMETMLW DSIHRLQTLH PKFVSVTYGA NSGERDRTHG IVKRIKQETG LEAAPHLTGI DASPDELRQI AKDYWDSGIR RIVALRGDEP AGYEKKPFYA EDLVKLLRSV ADFDISVAAY PEVHPEAKSA QADLINLKRK IDAGANHVIT QFFFDVERYL RFRDRCVMLG IDVEIVPGIL PVTNFKQLGK MAQVTNVKIP SWLSQMYEGL DDDQGTRNLV AASIAIDMVK VLSREGVKDF HFYTLNRSEL TYAICHILGV RP // ID METX_NEIMB Reviewed; 379 AA. AC Q9JZQ5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296}; DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296}; DE AltName: Full=Homoserine O-trans-acetylase {ECO:0000255|HAMAP-Rule:MF_00296}; DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296}; DE Short=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296}; GN Name=metX {ECO:0000255|HAMAP-Rule:MF_00296}; GN OrderedLocusNames=NMB0940; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the methionine biosynthesis. Catalyzes the CC transfer of the acetyl group from acetyl-CoA to the hydroxyl group CC of L-homoserine to yield O-acetyl-L-homoserine. CC {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-homoserine = CoA + O-acetyl-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. HTA family. CC {ECO:0000255|HAMAP-Rule:MF_00296}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41346.1; -; Genomic_DNA. DR PIR; A81140; A81140. DR RefSeq; NP_273978.1; NC_003112.2. DR RefSeq; WP_002225323.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ5; -. DR STRING; 122586.NMB0940; -. DR ESTHER; neima-metx; Homoserine_transacetylase. DR PaxDb; Q9JZQ5; -. DR EnsemblBacteria; AAF41346; AAF41346; NMB0940. DR GeneID; 903060; -. DR KEGG; nme:NMB0940; -. DR PATRIC; 20357355; VBINeiMen85645_1192. DR eggNOG; ENOG4105DWV; Bacteria. DR eggNOG; COG2021; LUCA. DR HOGENOM; HOG000246301; -. DR KO; K00641; -. DR OMA; GSVGGMN; -. DR OrthoDB; EOG67T5J4; -. DR BioCyc; NMEN122586:GHGG-977-MONOMER; -. DR UniPathway; UPA00051; UER00074. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1820; -; 2. DR HAMAP; MF_00296; Homoser_O_acetyltr; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR008220; Homoserine_AcTrfase. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Complete proteome; KW Cytoplasm; Methionine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 379 Homoserine O-acetyltransferase. FT /FTId=PRO_0000155733. FT ACT_SITE 154 154 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00296}. FT ACT_SITE 319 319 {ECO:0000255|HAMAP-Rule:MF_00296}. FT ACT_SITE 352 352 {ECO:0000255|HAMAP-Rule:MF_00296}. SQ SEQUENCE 379 AA; 42174 MW; D56AC364101EE8EE CRC64; MSQNASVGIV MPQKIPFEMP LVLENGKTLP RFDLMIETYG ELNAEKNNAV LICHALSGNH HVAGRHSAED KYTGWWDNMV GPGKPIDTER FFVVGLNNLG GCDGSSGPLS INPETGREYG ADFPVVTVKD WVKSQAALAD YLGIEQWAAI VGGSLGGMQA LQWTISYPER VRHALVIASA PKLSTQNIAF NDVARQAILT DPDFNEGHYR SHNTVPARGL RIARMMGHIT YLAEDGLGKK FGRDLRSNGY QYGFGVEFEV ESYLRYQGDK FVGRFDANTY LLMTKALDYF DPAADFGDSL TRALQNVKAK FFVASFSTDW RFAPERSHEL VKALIAAQKS VQYIEVKSAH GHDAFLMEDE AYMRAVAAYM NNVYKECQQ // ID MIAA_NEIMB Reviewed; 313 AA. AC Q9JZR0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; GN OrderedLocusNames=NMB0935; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the CC adenine at position 37 in tRNAs that read codons beginning with CC uridine, leading to the formation of N6-(dimethylallyl)adenosine CC (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + adenine(37) in CC tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41341.1; -; Genomic_DNA. DR PIR; A81142; A81142. DR RefSeq; NP_273973.1; NC_003112.2. DR RefSeq; WP_002225331.1; NC_003112.2. DR ProteinModelPortal; Q9JZR0; -. DR STRING; 122586.NMB0935; -. DR PaxDb; Q9JZR0; -. DR EnsemblBacteria; AAF41341; AAF41341; NMB0935. DR GeneID; 903055; -. DR KEGG; nme:NMB0935; -. DR PATRIC; 20357337; VBINeiMen85645_1183. DR eggNOG; ENOG4105DKX; Bacteria. DR eggNOG; COG0324; LUCA. DR HOGENOM; HOG000039996; -. DR KO; K00791; -. DR OMA; TWFRNQT; -. DR OrthoDB; EOG661HB3; -. DR BioCyc; NMEN122586:GHGG-972-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR018022; IPP_trans. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 313 tRNA dimethylallyltransferase. FT /FTId=PRO_0000163944. FT NP_BIND 11 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 13 18 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00185}. FT REGION 36 39 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 160 164 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 243 248 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 102 102 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 124 124 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. SQ SEQUENCE 313 AA; 34870 MW; 05967C4917E99A4C CRC64; MPTPKAFALL GPTAGGKTAL ALKIAETLPV EIISLDSALV YRDMDIGTAK PSASERAFVP HHLIDIIPPT ESYSAARFVE DCTRLVGEIS SRGRFALIVG GTMMYFRALT QGLNDLPEAD ACLRADLDEQ KQMYGLDFLY RTLQKVDPET ACRLKPNDSQ RIGRALEVYY LTGKPMSTHL GSLTSHTLPF DLHTAALIPE NRARLHENIA LRFHLMLEQG FIGEVENLRR RYPGLTAYSP AIRCVGYRQA WKYLDGKTDF PAFVEKGIAA TRQLAKRQLT WLRKTPLDCV ADPFSDCTSC TRLIEAAKRF FGA // ID MIND_NEIMB Reviewed; 271 AA. AC Q7DDS7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Septum site-determining protein MinD; DE AltName: Full=Cell division inhibitor MinD; GN Name=minD; OrderedLocusNames=NMB0171; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: ATPase required for the correct placement of the CC division site. Cell division inhibitors MinC and MinD act in CC concert to form an inhibitor capable of blocking formation of the CC polar Z ring septums. Rapidly oscillates between the poles of the CC cell to destabilize FtsZ filaments that have formed before they CC mature into polar Z rings (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40628.1; -; Genomic_DNA. DR PIR; C81230; C81230. DR RefSeq; NP_273229.1; NC_003112.2. DR RefSeq; WP_002215463.1; NC_003112.2. DR ProteinModelPortal; Q7DDS7; -. DR STRING; 122586.NMB0171; -. DR PaxDb; Q7DDS7; -. DR PRIDE; Q7DDS7; -. DR EnsemblBacteria; AAF40628; AAF40628; NMB0171. DR GeneID; 902278; -. DR KEGG; nme:NMB0171; -. DR PATRIC; 20355365; VBINeiMen85645_0212. DR eggNOG; ENOG4107QMS; Bacteria. DR eggNOG; COG2894; LUCA. DR HOGENOM; HOG000019419; -. DR KO; K03609; -. DR OMA; VNRIRNH; -. DR OrthoDB; EOG6NPMB6; -. DR BioCyc; NMEN122586:GHGG-181-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0000918; P:barrier septum site selection; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR025501; MinD. DR InterPro; IPR010223; MinD_bac-type. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF003092; MinD; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01968; minD_bact; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; KW Cell membrane; Complete proteome; Membrane; Nucleotide-binding; KW Reference proteome; Septation. FT CHAIN 1 271 Septum site-determining protein MinD. FT /FTId=PRO_0000320272. FT NP_BIND 10 17 ATP. {ECO:0000255}. SQ SEQUENCE 271 AA; 29559 MW; 9ACDB52A03BD6170 CRC64; MAKIIVVTSG KGGVGKTTTS ASIATGLALR GYKTAVIDFD VGLRNLDLIM GCERRVVYDL INVIQGEATL NQALIKDKNC ENLFILPASQ TRDKDALTRE GVEKVMQELS GKKMGFEYII CDSPAGIEQG ALMALYFADE AIVTTNPEVS SVRDSDRILG ILQSKSHKAE QGGSVKEHLL ITRYSPERVA KGEMLSVQDI CDILHIPLLG VIPESQNVLQ ASNSGEPVIH QDSVAASEAY KDVIARLLGE NREMRFLEAE KKSFFKRLFG G // ID MINE_NEIMB Reviewed; 87 AA. AC Q9K1H9; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Cell division topological specificity factor; GN Name=minE; OrderedLocusNames=NMB0172; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Prevents the cell division inhibition by proteins MinC CC and MinD at internal division sites while permitting inhibition at CC polar sites. This ensures cell division at the proper site by CC restricting the formation of a division septum at the midpoint of CC the long axis of the cell (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MinE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40629.1; -; Genomic_DNA. DR PIR; D81230; D81230. DR RefSeq; NP_273230.1; NC_003112.2. DR RefSeq; WP_002215465.1; NC_003112.2. DR ProteinModelPortal; Q9K1H9; -. DR STRING; 122586.NMB0172; -. DR PaxDb; Q9K1H9; -. DR EnsemblBacteria; AAF40629; AAF40629; NMB0172. DR GeneID; 902279; -. DR KEGG; nme:NMB0172; -. DR PATRIC; 20355367; VBINeiMen85645_0213. DR eggNOG; ENOG4105VJP; Bacteria. DR eggNOG; COG0851; LUCA. DR HOGENOM; HOG000218362; -. DR KO; K03608; -. DR OMA; HERTGHS; -. DR OrthoDB; EOG6HMXJM; -. DR BioCyc; NMEN122586:GHGG-182-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032955; P:regulation of barrier septum assembly; IEA:InterPro. DR Gene3D; 3.30.1070.10; -; 1. DR HAMAP; MF_00262; MinE; 1. DR InterPro; IPR005527; MinE. DR Pfam; PF03776; MinE; 1. DR SUPFAM; SSF55229; SSF55229; 1. DR TIGRFAMs; TIGR01215; minE; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Reference proteome. FT CHAIN 1 87 Cell division topological specificity FT factor. FT /FTId=PRO_0000205881. SQ SEQUENCE 87 AA; 10045 MW; AF57460A9C3FF013 CRC64; MSLIEFLFGR KQKTATVARD RLQIIIAQER AQEGQAPDYL PTLRKELMEV LSKYVNVSLD NIRISQEKQD GMDVLELNIT LPEQKKV // ID MIAB_NEIMB Reviewed; 442 AA. AC Q9JXV8; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864}; DE EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864}; GN Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864}; GN OrderedLocusNames=NMB1866; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC (dimethylallyl)adenosine (i(6)A), leading to the formation of 2- CC methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 CC in tRNAs that read codons beginning with uridine. CC {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA + CC sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced CC electron acceptor = 2-methylthio-N(6)-dimethylallyladenine(37) in CC tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine CC + 5'-deoxyadenosine + electron acceptor. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01864}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01864}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42200.1; -; Genomic_DNA. DR PIR; C81034; C81034. DR RefSeq; NP_274862.1; NC_003112.2. DR RefSeq; WP_002214640.1; NC_003112.2. DR ProteinModelPortal; Q9JXV8; -. DR STRING; 122586.NMB1866; -. DR PaxDb; Q9JXV8; -. DR EnsemblBacteria; AAF42200; AAF42200; NMB1866. DR GeneID; 904322; -. DR KEGG; nme:NMB1866; -. DR PATRIC; 20359761; VBINeiMen85645_2386. DR eggNOG; ENOG4105CIW; Bacteria. DR eggNOG; COG0621; LUCA. DR HOGENOM; HOG000224767; -. DR KO; K06168; -. DR OMA; IPMDLIL; -. DR OrthoDB; EOG6P5ZD8; -. DR BioCyc; NMEN122586:GHGG-1922-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR006463; MiaB_methiolase. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 442 tRNA-2-methylthio-N(6)- FT dimethylallyladenosine synthase. FT /FTId=PRO_0000374403. FT DOMAIN 2 120 MTTase N-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT DOMAIN 378 441 TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 11 11 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 49 49 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 161 161 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 164 164 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. SQ SEQUENCE 442 AA; 49566 MW; 9BA772C3DFCC1454 CRC64; MKKVFIRTFG CQMNEYDSDK MLAVLAEEHG GIEQVTQADE ADIILFNTCS VREKAQEKVF SDLGRVRPLK EKNPGLIIGV AGCVASQEGE NIIKRAPYVD VVFGPQTLHR LPKMIVDKET SGLSQVDISF PEIEKFDHLP PARVEGGAAF VSIMEGCSKY CSFCVVPYTR GEEFSRPLND VLTEIANLAQ QGVKEINLLG QNVNAYRGEM DDGEICDFAT LLRIVHEIPG IERMRFTTSH PREFTDSIIE CYRDLPKLVS HLHLPIQSGS DRVLSAMKRG YTALEYKSII RKLRAIRPDL CLSSDFIVGF PGETEREFEQ TLKLVKDIAF DLSFVFIYSP RPGTPAANLP DDTPHEEKVR RLEALNEVIE AETARINQTM VGTVQRCLVE GISKKDPDQL QARTANNRVV NFTGTPDMIN QMIDLEITEA YTFSLRGKVV EA // ID MNMG_NEIMB Reviewed; 628 AA. AC Q9K1G0; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 20-JAN-2016, entry version 86. DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129}; DE AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129}; GN Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129}; GN Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129}; GN OrderedLocusNames=NMB0193; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NAD-binding protein involved in the addition of a CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34) CC of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP- CC Rule:MF_00129}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00129}; CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG CC subunits. {ECO:0000255|HAMAP-Rule:MF_00129}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}. CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP- CC Rule:MF_00129}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40650.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40650.1; ALT_INIT; Genomic_DNA. DR PIR; F81227; F81227. DR RefSeq; NP_273251.1; NC_003112.2. DR ProteinModelPortal; Q9K1G0; -. DR SMR; Q9K1G0; 1-554. DR STRING; 122586.NMB0193; -. DR PaxDb; Q9K1G0; -. DR EnsemblBacteria; AAF40650; AAF40650; NMB0193. DR GeneID; 902301; -. DR KEGG; nme:NMB0193; -. DR PATRIC; 20355419; VBINeiMen85645_0238. DR eggNOG; ENOG4107RE5; Bacteria. DR eggNOG; COG0445; LUCA. DR HOGENOM; HOG000201059; -. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR BioCyc; NMEN122586:GHGG-204-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00129; MnmG_GidA; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR026904; GidA-assoc_3. DR InterPro; IPR004416; MnmG. DR InterPro; IPR002218; MnmG-rel. DR InterPro; IPR020595; MnmG-rel_CS. DR Pfam; PF01134; GIDA; 1. DR Pfam; PF13932; GIDA_assoc; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR00136; gidA; 1. DR PROSITE; PS01280; GIDA_1; 1. DR PROSITE; PS01281; GIDA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; KW Reference proteome; tRNA processing. FT CHAIN 1 628 tRNA uridine 5-carboxymethylaminomethyl FT modification enzyme MnmG. FT /FTId=PRO_0000117141. FT NP_BIND 13 18 FAD. {ECO:0000255|HAMAP-Rule:MF_00129}. FT NP_BIND 273 287 NAD. {ECO:0000255|HAMAP-Rule:MF_00129}. SQ SEQUENCE 628 AA; 69438 MW; 0265B68714660D6E CRC64; MIYPKTYDVI VVGGGHAGTE AALAAARMGA QTLLLSHNIE TLGQMSCNPS IGGIGKGHLV RELDALGGAM ALATDKSGIQ FRRLNASKGA AVRATRAQAD RILYKAAIRE MLENQENLDL FQQAVEDVTL DGERISGVIT AMGVEFKARA VVLTAGTFLS GKIHIGLENY EGGRAGDPAA KSLGGRLREL KLPQGRLKTG TPPRIDGRTI DFSQLTEQPG DTPVPVMSVR GNADMHPRQV SCWITHTNTQ THDIIRSGFD RSPMFTGKIE GVGPRYCPSI EDKINRFADK DSHQIFLEPE GLTTHEYYPN GISTSLPFDI QIALVRSMKG LENAHILRPG YAIEYDYFDP RNLKASLETK TIAGLFFAGQ INGTTGYEEA AAQGLLAGAN AVQYVRGQDP LLLRREQAYL GVLVDDLITK GVNEPYRMFT SRAEYRLQLR EDNADMRLTE DGYKIGLVSE AQWRMFNEKR EAVEREIQRL KTTWYTPQKL AEGEQIRVFG QKLSREANLH DLLRRPNLDY AALMTLEGAM PSENLSAEVI EQVEIQVKYQ GYIDRQNEEI DSRRDIETLK LPDGIDYGKV KGLSAEVQQK LNQHKPETVG QASRISGVTP AAVALLMVHL KRGFKDAK // ID MNTP_NEIMB Reviewed; 188 AA. AC Q9K1E1; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Putative manganese efflux pump MntP {ECO:0000255|HAMAP-Rule:MF_01521}; GN Name=mntP {ECO:0000255|HAMAP-Rule:MF_01521}; GN OrderedLocusNames=NMB0215; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Probably functions as a manganese efflux pump. CC {ECO:0000255|HAMAP-Rule:MF_01521}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01521}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01521}. CC -!- SIMILARITY: Belongs to the MntP (TC 9.B.29) family. CC {ECO:0000255|HAMAP-Rule:MF_01521}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40671.1; -; Genomic_DNA. DR PIR; C81224; C81224. DR RefSeq; NP_273272.1; NC_003112.2. DR RefSeq; WP_002221883.1; NC_003112.2. DR STRING; 122586.NMB0215; -. DR PaxDb; Q9K1E1; -. DR EnsemblBacteria; AAF40671; AAF40671; NMB0215. DR GeneID; 902327; -. DR KEGG; nme:NMB0215; -. DR PATRIC; 20355494; VBINeiMen85645_0271. DR eggNOG; ENOG4108UI1; Bacteria. DR eggNOG; COG1971; LUCA. DR HOGENOM; HOG000238852; -. DR OMA; FIGGKMI; -. DR OrthoDB; EOG676Z87; -. DR BioCyc; NMEN122586:GHGG-230-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01521; MntP_pump; 1. DR InterPro; IPR003810; Mntp/YtaF. DR InterPro; IPR022929; Put_MntP. DR Pfam; PF02659; Mntp; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Manganese; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 188 Putative manganese efflux pump MntP. FT /FTId=PRO_0000155658. FT TRANSMEM 3 23 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. FT TRANSMEM 35 55 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. FT TRANSMEM 63 83 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. FT TRANSMEM 104 126 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. FT TRANSMEM 140 160 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. FT TRANSMEM 167 187 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01521}. SQ SEQUENCE 188 AA; 19700 MW; F3B0226487BA5B79 CRC64; MGFYALLLIA LGMSMDAFAV ALAKGAAVRM PPRKIAATAL VFGTVEALTP LAGWVGGFYA KPFISEWDHW VAFVLLGGLG LKMMREGLSG EAEDVRESKR ESLWMTVLTA FGTSIDSMIV GVGLAFMEVN IAFAAAIIGM ATTVMVAVGL TAGRALGVLF GRCAEFAGGL VLIAIGTWTL LSHLGLIQ // ID MINC_NEIMB Reviewed; 237 AA. AC Q9K1I0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Probable septum site-determining protein MinC; GN Name=minC; OrderedLocusNames=NMB0170; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell division inhibitor that blocks the formation of CC polar Z ring septums. Rapidly oscillates between the poles of the CC cell to destabilize FtsZ filaments that have formed before they CC mature into polar Z rings. Prevents FtsZ polymerization (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40627.1; -; Genomic_DNA. DR PIR; B81230; B81230. DR RefSeq; NP_273228.1; NC_003112.2. DR RefSeq; WP_002224775.1; NC_003112.2. DR ProteinModelPortal; Q9K1I0; -. DR STRING; 122586.NMB0170; -. DR PaxDb; Q9K1I0; -. DR EnsemblBacteria; AAF40627; AAF40627; NMB0170. DR GeneID; 902277; -. DR KEGG; nme:NMB0170; -. DR PATRIC; 20355363; VBINeiMen85645_0211. DR eggNOG; ENOG4105K7U; Bacteria. DR eggNOG; COG0850; LUCA. DR HOGENOM; HOG000062060; -. DR KO; K03610; -. DR OMA; WAAVAMK; -. DR OrthoDB; EOG606588; -. DR BioCyc; NMEN122586:GHGG-180-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR GO; GO:0051726; P:regulation of cell cycle; IEA:UniProtKB-HAMAP. DR GO; GO:0051302; P:regulation of cell division; IEA:InterPro. DR Gene3D; 2.160.20.70; -; 1. DR HAMAP; MF_00267; MinC; 1. DR InterPro; IPR016098; CAP/MinC_C. DR InterPro; IPR013033; MinC. DR InterPro; IPR007874; MinC_N. DR InterPro; IPR005526; Septum_form_inhib_MinC_C. DR Pfam; PF03775; MinC_C; 1. DR Pfam; PF05209; MinC_N; 1. DR SUPFAM; SSF63848; SSF63848; 1. DR TIGRFAMs; TIGR01222; minC; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Reference proteome; KW Septation. FT CHAIN 1 237 Probable septum site-determining protein FT MinC. FT /FTId=PRO_0000189046. SQ SEQUENCE 237 AA; 26221 MW; E42BD0C1B9C16853 CRC64; MMVYIMNAFD IKSTKMDVLS ISLHTSDLFD LEDVLVKLGK KFQESGVVPF VLDVQEFDYP ESLDLAALVS LFSRHGMQIL GLKHSNERWA AAAMKYHLLF CLSHSENVKE LGQVEVQKTE DGQKARKTVL ITSPVRTGQQ VYAEDGDLIV TGAVSQGAEL IADGNIHIYA PMRGRALAGA KGDTSARIFI HSMQAELVSV AGIYRNFEQD LPNHLHKQPV QILLQDNRLV ISAIGSE // ID MNME_NEIMB Reviewed; 448 AA. AC Q9JXL4; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379}; DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379}; GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN Synonyms=thdF {ECO:0000255|HAMAP-Rule:MF_00379}, GN trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=NMB1987; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate. CC Involved in the addition of a carboxymethylaminomethyl (cmnm) CC group at the wobble position (U34) of certain tRNAs, forming tRNA- CC cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00379}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00379}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00379}; CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG CC subunits. {ECO:0000255|HAMAP-Rule:MF_00379}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00379}. CC -!- SIMILARITY: Contains 1 TrmE-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42314.1; -; Genomic_DNA. DR PIR; F81019; F81019. DR RefSeq; NP_274979.1; NC_003112.2. DR RefSeq; WP_002225859.1; NC_003112.2. DR ProteinModelPortal; Q9JXL4; -. DR STRING; 122586.NMB1987; -. DR PaxDb; Q9JXL4; -. DR EnsemblBacteria; AAF42314; AAF42314; NMB1987. DR GeneID; 904145; -. DR KEGG; nme:NMB1987; -. DR PATRIC; 20360067; VBINeiMen85645_2538. DR eggNOG; ENOG4105C1H; Bacteria. DR eggNOG; COG0486; LUCA. DR HOGENOM; HOG000200714; -. DR KO; K03650; -. DR OMA; FTPRYAY; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; NMEN122586:GHGG-2044-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.430; -; 3. DR Gene3D; 3.30.1360.120; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00379; GTPase_MnmE; 1. DR InterPro; IPR031168; G_TrmE. DR InterPro; IPR018948; GTP-bd_TrmE_N. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR004520; GTPase_MnmE. DR InterPro; IPR027368; MnmE_dom2. DR InterPro; IPR025867; MnmE_helical. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF12631; MnmE_helical; 1. DR Pfam; PF10396; TrmE_N; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51709; G_TRME; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome; KW tRNA processing. FT CHAIN 1 448 tRNA modification GTPase MnmE. FT /FTId=PRO_0000188895. FT DOMAIN 216 373 TrmE-type G. FT NP_BIND 226 231 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 245 251 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 270 273 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 226 226 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 230 230 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 245 245 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 247 247 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 250 250 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 251 251 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT BINDING 24 24 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 81 81 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 120 120 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 448 448 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. SQ SEQUENCE 448 AA; 47562 MW; E3F6ECF225BB22D8 CRC64; MSDNVPTIAA VATAPGRGGV GVIRISGKNL LPMAQALCGK TPKPRTATYA DFTDTDGQAI DSGLLLFFAA PASFTGEDVI ELQGHGGPVV MDMLLNRCLE LGARLAEPGE FTKRAFLNDK LDLAQAEGVA DLIDASSRSA ARLALRSLKG DFSRRIHGLV EDLITLRMLV EATLDFPEED IDFLEAADAR GKLDGLRRAV DDVLANAQQG AILREGLNVV LVGAPNVGKS SLLNALAGDE VAIVTDIAGT TRDAVRERIL IDGVPVHIVD TAGLRETDDV VERIGIERSR KAVSEADVAL VLVDPREGLN EKTRAILDAL PPELKRIEIH SKSDLHAHAA GGFGTGAETV IALSAKTGDG LDALKRTLLR EAGWQGESEG LFLARTRHVN ALKAAQEELS LAALCGNHQI ELFAEHLRLA QVACGEITGE FTADDLLGVI FSRFCIGK // ID MRAY_NEIMB Reviewed; 360 AA. AC Q9K0Y6; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038}; DE EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038}; DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038}; GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; GN OrderedLocusNames=NMB0418; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: First step of the lipid cycle reactions in the CC biosynthesis of the cell wall peptidoglycan. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala- CC D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00038}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40856.1; -; Genomic_DNA. DR PIR; E81200; E81200. DR RefSeq; NP_273466.1; NC_003112.2. DR RefSeq; WP_002224924.1; NC_003112.2. DR STRING; 122586.NMB0418; -. DR PaxDb; Q9K0Y6; -. DR EnsemblBacteria; AAF40856; AAF40856; NMB0418. DR GeneID; 902534; -. DR KEGG; nme:NMB0418; -. DR PATRIC; 20356030; VBINeiMen85645_0530. DR eggNOG; ENOG4105CPY; Bacteria. DR eggNOG; COG0472; LUCA. DR HOGENOM; HOG000275122; -. DR KO; K01000; -. DR OMA; HQNKKDT; -. DR OrthoDB; EOG69GZPZ; -. DR BioCyc; NMEN122586:GHGG-442-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00038; MraY; 1. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase. DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR TIGRFAMs; TIGR00445; mraY; 1. DR PROSITE; PS01347; MRAY_1; 1. DR PROSITE; PS01348; MRAY_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 360 Phospho-N-acetylmuramoyl-pentapeptide- FT transferase. FT /FTId=PRO_0000108858. FT TRANSMEM 24 44 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 69 89 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 133 153 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 158 178 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 239 259 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 263 283 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 288 308 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 337 357 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. SQ SEQUENCE 360 AA; 39328 MW; D07D16876DF5FA22 CRC64; MFLWLAHFSN WLTGLNIFQY TTFRAVMAAL TALAFSLMFG PWTIRRLTAL KCGQAVRTDG PQTHLVKNGT PTMGGSLILT AITVSTLLWG NWANPYIWIL LGVLLATGAL GFYDDWRKVV YKDPNGVSAK FKMVWQSSVA IIASLALFYL AANSANNILI VPFFKQIALP LGVVGFLVLS YLTIVGTSNA VNLTDGLDGL ATFPVVLVAA GLAIFAYASG HSQFAQYLQL PYVAGANEVV IFCTAMCGAC LGFLWFNAYP AQVFMGDVGA LALGAALGTV AVIVRQEFVL VIMGGLFVVE AVSVMLQVGW YKKTKKRIFL MAPIHHHYEQ KGWKETQVVV RFWIITIVLV LIGLSTLKIR // ID MNMA_NEIMB Reviewed; 367 AA. AC Q9JYJ6; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144}; DE EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144}; GN Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144}; Synonyms=trmU; GN OrderedLocusNames=NMB1556; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble CC position (U34) of tRNA, leading to the formation of s(2)U34. CC {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- CATALYTIC ACTIVITY: A [protein]-S-sulfanyl-L-cysteine + CC uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L- CC cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + CC acceptor. {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP- CC Rule:MF_00144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41910.1; -; Genomic_DNA. DR PIR; A81069; A81069. DR RefSeq; NP_274563.1; NC_003112.2. DR RefSeq; WP_002232768.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ6; -. DR SMR; Q9JYJ6; 8-360. DR STRING; 122586.NMB1556; -. DR PaxDb; Q9JYJ6; -. DR EnsemblBacteria; AAF41910; AAF41910; NMB1556. DR GeneID; 904116; -. DR KEGG; nme:NMB1556; -. DR PATRIC; 20358966; VBINeiMen85645_2002. DR eggNOG; ENOG4105CCJ; Bacteria. DR eggNOG; COG0482; LUCA. DR HOGENOM; HOG000218046; -. DR KO; K00566; -. DR OMA; LHKINFA; -. DR OrthoDB; EOG6RZB5H; -. DR BioCyc; NMEN122586:GHGG-1597-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.280; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1. DR InterPro; IPR023382; Adenine_a_hdrlase_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; tRNA-specific_2-thiouridylase. DR PANTHER; PTHR11933; PTHR11933; 1. DR TIGRFAMs; TIGR00420; trmU; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1 367 tRNA-specific 2-thiouridylase MnmA. FT /FTId=PRO_0000121659. FT NP_BIND 13 20 ATP. {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 99 101 Interaction with target base in tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 150 152 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 307 308 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT ACT_SITE 104 104 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT ACT_SITE 200 200 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT BINDING 39 39 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT BINDING 128 128 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 129 129 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 340 340 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT DISULFID 104 200 Alternate. {ECO:0000255|HAMAP- FT Rule:MF_00144}. SQ SEQUENCE 367 AA; 40900 MW; 0A279F58FF042AEA CRC64; MNTTANPSNI IVGLSGGVDS SVTAALLKQQ GYQVRGVFMQ NWEDDDNDEY CSIKQDSFDA IAVADIIGID IDIVNFAAQY KDKVFAYFLQ EYSAGRTPNP DVLCNAEIKF KCFLDYAVGQ GADTIATGHY ARKEVRNGVH YLLKGLDRNK DQSYFLYRLK PFQLERAIFP LGGLEKPEVR RLAAEFKLPT AAKKDSTGIC FIGERPFREF LQKYLPTDNG KMVTPEGKTV GEHVGLMFYT LGQRKGLGIG GAGEPWFVAA KDLTKNELIV VQGHDHPLLY TRSLVMNDLS FTLPERPKAG RYTCKTRYRM ADAPCELRYL DDETAELVFD EPQWAVTPGQ SAVLYDGDIC LGGGIIQTTD KPVIITR // ID MQO_NEIMB Reviewed; 488 AA. AC Q9JXD7; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00212}; DE EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212}; DE AltName: Full=MQO {ECO:0000255|HAMAP-Rule:MF_00212}; DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00212}; GN Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=NMB2096; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (S)-malate + a quinone = oxaloacetate + CC reduced quinone. {ECO:0000255|HAMAP-Rule:MF_00212}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00212}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC oxaloacetate from (S)-malate (quinone route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00212}. CC -!- SIMILARITY: Belongs to the MQO family. {ECO:0000255|HAMAP- CC Rule:MF_00212}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42413.1; -; Genomic_DNA. DR PIR; A81006; A81006. DR RefSeq; NP_275084.1; NC_003112.2. DR RefSeq; WP_002219978.1; NC_003112.2. DR ProteinModelPortal; Q9JXD7; -. DR STRING; 122586.NMB2096; -. DR PaxDb; Q9JXD7; -. DR PRIDE; Q9JXD7; -. DR EnsemblBacteria; AAF42413; AAF42413; NMB2096. DR GeneID; 903948; -. DR KEGG; nme:NMB2096; -. DR PATRIC; 20360364; VBINeiMen85645_2679. DR eggNOG; ENOG4105DWT; Bacteria. DR eggNOG; COG0579; LUCA. DR HOGENOM; HOG000109379; -. DR KO; K00116; -. DR OMA; EPIAATK; -. DR OrthoDB; EOG6X6R8Z; -. DR BioCyc; NMEN122586:GHGG-2161-MONOMER; -. DR UniPathway; UPA00223; UER01008. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 2. DR HAMAP; MF_00212; MQO; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR006231; MQO. DR Pfam; PF06039; Mqo; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR01320; mal_quin_oxido; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 488 Probable malate:quinone oxidoreductase. FT /FTId=PRO_0000128724. SQ SEQUENCE 488 AA; 53968 MW; B24FDEC06C63243A CRC64; MAEATDVVLV GGGIMSATLG VLLKELEPSW EITLIERLED VALESSNAWN NAGTGHSALC ELNYAPLGAN GIIDPARALN IAEQFHVSRQ FWATLVAEGK LEDNSFINAV PHMSLVMNED HCSYLQKRYD AFKTQKLFEN MEFSTDRNKI SDWAPLMMRG RDENQPVAAN YSAEGTDVDF GRLTRQMVKY LQGKGVKTEF NRHVEDIKRE SDGAWVLKTA DTRNPDGQLT LRTRFLFLGA GGGALTLLQK SGIPEGKGYG GFPVSGLFFR NSNPETAEQH NAKVYGQASV GAPPMSVPHL DTRNVDGKRH LMFGPYAGFR SNFLKQGSLM DLPLSIHMDN LYPMLCAGWA NMPLTKYLLG ELRKTKEERF ASLLEYYPEA NPDDWELITA GQRVQIIKKD SEKGGVLQFG TEIVAHADGS LAALLGASPG ASTAVPLMIR LMHQCFPERA PSWEDRLKEL VPGYGIKLNE NPERADEIIA YTAKVLDI // ID MSBA_NEIMB Reviewed; 621 AA. AC Q9JXR3; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000255|HAMAP-Rule:MF_01703}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01703}; GN Name=msbA {ECO:0000255|HAMAP-Rule:MF_01703}; GN OrderedLocusNames=NMB1919; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in lipid A export and possibly also in CC glycerophospholipid export and for biogenesis of the outer CC membrane. Transmembrane domains (TMD) form a pore in the inner CC membrane and the ATP-binding domain (NBD) is responsible for CC energy generation. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01703}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01703}. CC -!- DOMAIN: In MsbA the ATP-binding domain (NBD) and the transmembrane CC domain (TMD) are fused. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid CC exporter (TC 3.A.1.106) family. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42249.1; -; Genomic_DNA. DR PIR; C81026; C81026. DR RefSeq; NP_274913.1; NC_003112.2. DR RefSeq; WP_002238384.1; NC_003112.2. DR ProteinModelPortal; Q9JXR3; -. DR STRING; 122586.NMB1919; -. DR PaxDb; Q9JXR3; -. DR EnsemblBacteria; AAF42249; AAF42249; NMB1919. DR GeneID; 904243; -. DR KEGG; nme:NMB1919; -. DR PATRIC; 20359885; VBINeiMen85645_2447. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K11085; -. DR OMA; HMLKILP; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-1976-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR011917; ABC_transpr_lipidA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 2. DR TIGRFAMs; TIGR02203; MsbA_lipidA; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51239; MSBA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Lipid transport; Membrane; Nucleotide-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 621 Lipid A export ATP-binding/permease FT protein MsbA. FT /FTId=PRO_0000092590. FT TRANSMEM 32 52 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 91 111 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 192 212 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 286 306 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 312 332 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT DOMAIN 32 344 ABC transmembrane type-1. FT {ECO:0000255|HAMAP-Rule:MF_01703}. FT DOMAIN 378 611 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT NP_BIND 410 417 ATP. {ECO:0000255|HAMAP-Rule:MF_01703}. SQ SEQUENCE 621 AA; 68903 MW; 708DA9DBD97C5456 CRC64; MIEKLTFGLF KKEDARSFMR LMAYVRPYKI RIVAALIAIF GVAATESYLA AFIAPLINHG FSAPAAPPEL SAAAGIISTL QNWREQFTYM VWGTENKIWT VPLFLIILVV IRGICRFTST YLMTWVSVMT ISKIRKDMFA KMLTLSSRYH QETPSGTVLM NMLNLTEQSV SNASDIFTVL TRDTMIVTGL TIVLLYLNWQ LSLIVVLMFP LLSLLSRYYR DRLKHVISDS QKSIGTMNNV IAETHQGHRV VKLFNGQAQA ANRFDAVNRT IVRLSKKITQ ATAAHSPFSE LIASIALAVV IFIALWQSQN GYTTIGEFMA FIVAMLQMYA PIKSLANISI PMQTMFLAAD GVCAFLDTPP EQDKGTLAPQ RVEGRISFRN VDVEYRSDGI KALDNFNLDI RQGERVALVG RSGSGKSTVV NLLPRFVEPS AGNICIDGID IADIKLDCLR AQFALVSQDV FLFDDTLFEN VRYSRPDAGE AEVLFALQTA NLQSLIDSSP LGLHQPIGSN GSNLSGGQRQ RVAIARAILK DAPILLLDEA TSALDNESER LVQQALERLM ENRTGIIVAH RLTTIEGADR IIVMDDGKII EQGTHEQLMS QNGYYTMLRN ISNKDAAVRT A // ID MOBA_NEIMB Reviewed; 192 AA. AC P58747; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Putative molybdenum cofactor guanylyltransferase; DE Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316}; DE Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316}; GN Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316}; GN OrderedLocusNames=NMB1248; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo- CC MPT) cofactor (Moco or molybdenum cofactor) to form Mo- CC molybdopterin guanine dinucleotide (Mo-MGD) cofactor. CC {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate + CC guanylyl molybdenum cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00316}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition CC and specific binding, while the C-terminal domain determines the CC specific binding to the target protein. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AE002098; Type=Frameshift; Positions=28; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P58747; -. DR OMA; RTSAMKT; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00316; MobA; 1. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR013482; Molybde_CF_guanTrfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 5: Uncertain; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Molybdenum cofactor biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 192 Putative molybdenum cofactor FT guanylyltransferase. FT /FTId=PRO_0000134897. FT NP_BIND 8 10 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT METAL 101 101 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00316}. FT BINDING 21 21 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 67 67 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 101 101 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. SQ SEQUENCE 192 AA; 21727 MW; A18E989E7D6B88B6 CRC64; MKTFALILAG GQASRMGGED KGLALLGGKA LIDHVIDRVR PQVSHIAIST NRNLEEYARR SPHIFPDARQ WQHFGPLSAL CTAANDLQLA AADWLLVVPC DMPYLPDDLV ARFETVSKRT PLCNAYYVET PITMHYNIMY IRPQILQSAI PYLFSGMKTL RSWLQQQRAR PVRFEFDGHF ADLNTQIDLQ EG // ID MRAZ_NEIMB Reviewed; 151 AA. AC Q9K0Z1; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Transcriptional regulator MraZ; GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; GN OrderedLocusNames=NMB0410; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Forms oligomers. {ECO:0000255|HAMAP-Rule:MF_01008}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01008}. CC -!- SIMILARITY: Belongs to the MraZ family. {ECO:0000255|HAMAP- CC Rule:MF_01008}. CC -!- SIMILARITY: Contains 2 SpoVT-AbrB domains. {ECO:0000255|PROSITE- CC ProRule:PRU01076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40849.1; -; Genomic_DNA. DR PIR; G81201; G81201. DR RefSeq; NP_273459.1; NC_003112.2. DR RefSeq; WP_002224918.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z1; -. DR STRING; 122586.NMB0410; -. DR PaxDb; Q9K0Z1; -. DR EnsemblBacteria; AAF40849; AAF40849; NMB0410. DR GeneID; 902526; -. DR KEGG; nme:NMB0410; -. DR PATRIC; 20356009; VBINeiMen85645_0520. DR eggNOG; ENOG4108V6E; Bacteria. DR eggNOG; COG2001; LUCA. DR HOGENOM; HOG000283907; -. DR KO; K03925; -. DR OMA; SNRVEIW; -. DR OrthoDB; EOG6G4W1C; -. DR BioCyc; NMEN122586:GHGG-434-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_01008; MraZ; 1. DR InterPro; IPR003444; MraZ. DR InterPro; IPR020603; MraZ_dom. DR InterPro; IPR007159; SpoVT-AbrB_dom. DR Pfam; PF02381; MraZ; 2. DR ProDom; PD006745; MraZ; 1. DR TIGRFAMs; TIGR00242; TIGR00242; 1. DR PROSITE; PS51740; SPOVT_ABRB; 2. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1 151 Transcriptional regulator MraZ. FT /FTId=PRO_0000108514. FT DOMAIN 5 51 SpoVT-AbrB 1. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT DOMAIN 81 124 SpoVT-AbrB 2. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. SQ SEQUENCE 151 AA; 17204 MW; D7A1F311F1FE73B0 CRC64; MFGGAHELSI DSKGRLAVPA KFRDILSRLY TPAVVVTLES KHKLLMYPVA EWEKVAAQLL NLKVADNPVL RRFQNLLLHN AEILEWDSAG RVLVSAGLRK RVDFDREVVL VGRANRLELW GREQWEAEMV QALDDDPDEL AFQLSQTDLQ L // ID MSRAB_NEIMB Reviewed; 522 AA. AC Q9K1N8; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; DE Includes: DE RecName: Full=Thioredoxin; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrAB; Synonyms=pilB; OrderedLocusNames=NMB0044; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA CC and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B CC exhibits a thioredoxin dependent methionine sulfoxide reductase CC activity; the Cys-495 is probably involved in the reduction of CC MetSO and in formation of the sulfenic acid derivative. The CC regeneration of Cys-495 is probably done via formation of a CC disulfide bond with Cys-440 followed by its reduction by CC thioredoxin. CC -!- SIMILARITY: In the N-terminal section; belongs to the thioredoxin CC family. {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the MsrA Met CC sulfoxide reductase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met CC sulfoxide reductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MsrB (methionine-R-sulfoxide reductase) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01126}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40515.1; -; Genomic_DNA. DR PIR; G81243; G81243. DR RefSeq; NP_273110.1; NC_003112.2. DR RefSeq; WP_010980745.1; NC_003112.2. DR ProteinModelPortal; Q9K1N8; -. DR SMR; Q9K1N8; 32-182, 196-364, 375-521. DR STRING; 122586.NMB0044; -. DR PaxDb; Q9K1N8; -. DR EnsemblBacteria; AAF40515; AAF40515; NMB0044. DR GeneID; 902147; -. DR KEGG; nme:NMB0044; -. DR PATRIC; 20355045; VBINeiMen85645_0059. DR eggNOG; ENOG4105E0X; Bacteria. DR eggNOG; COG0225; LUCA. DR eggNOG; COG0229; LUCA. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000243423; -. DR KO; K12267; -. DR OMA; WIDEKNG; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; NMEN122586:GHGG-45-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR Gene3D; 3.30.1060.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_01400; MsrB; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR10173; PTHR10173; 2. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF08534; Redoxin; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Electron transport; KW Multifunctional enzyme; Oxidoreductase; Redox-active center; KW Reference proteome; Transport. FT CHAIN 1 522 Peptide methionine sulfoxide reductase FT MsrA/MsrB. FT /FTId=PRO_0000138510. FT DOMAIN 17 174 Thioredoxin. FT DOMAIN 383 506 MsrB. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT REGION 199 354 Peptide methionine sulfoxide reductase A. FT ACT_SITE 207 207 {ECO:0000250}. FT ACT_SITE 495 495 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT DISULFID 68 71 Redox-active. {ECO:0000250}. FT DISULFID 440 495 {ECO:0000250}. SQ SEQUENCE 522 AA; 58015 MW; 535A823EDB76BFD1 CRC64; MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK LPVVTDNGGT IAQSLNISVY PSWALIGKDS DVQRIVKGSI NEAQALALIR DPNADLGSLK HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGK VK // ID MTGA_NEIMB Reviewed; 233 AA. AC P0A0Z4; O52423; O52424; O52425; O52426; O52427; O52428; O52429; AC O52430; O52431; O52432; O54548; O54634; O54659; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; DE Short=Monofunctional TGase {ECO:0000255|HAMAP-Rule:MF_00766}; DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_00766}; GN Name=mtgA {ECO:0000255|HAMAP-Rule:MF_00766}; Synonyms=mtg; GN OrderedLocusNames=NMB0357; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00766}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00766}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00766}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00766}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family. CC {ECO:0000255|HAMAP-Rule:MF_00766}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40800.1; -; Genomic_DNA. DR PIR; D81208; D81208. DR RefSeq; NP_273406.1; NC_003112.2. DR RefSeq; WP_002224887.1; NC_003112.2. DR ProteinModelPortal; P0A0Z4; -. DR STRING; 122586.NMB0357; -. DR PaxDb; P0A0Z4; -. DR EnsemblBacteria; AAF40800; AAF40800; NMB0357. DR GeneID; 902473; -. DR KEGG; nme:NMB0357; -. DR PATRIC; 20355867; VBINeiMen85645_0451. DR eggNOG; ENOG4108VKV; Bacteria. DR eggNOG; COG0744; LUCA. DR KO; K03814; -. DR OMA; KEETTFE; -. DR OrthoDB; EOG6HMXCD; -. DR BioCyc; NMEN122586:GHGG-379-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00766; Mono_pep_trsgly; 1. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR011812; Mono_pep_trsgly. DR Pfam; PF00912; Transgly; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR TIGRFAMs; TIGR02070; mono_pep_trsgly; 1. PE 3: Inferred from homology; KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 233 Monofunctional biosynthetic peptidoglycan FT transglycosylase. FT /FTId=PRO_0000083132. FT TRANSMEM 8 28 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00766}. SQ SEQUENCE 233 AA; 26603 MW; 8C85F5BE75417818 CRC64; MFRIIKWLIA LPVGIFIFFN AYVYGNIITY RAVAPHRTAF MSMRMKQFEQ EGRDVALDYR WMPYKRISTN LKKALIASED ARFAGHGGFD WGGIQNAIRR NRNSGKVKAG GSTISQQLAK NLFLNESRSY IRKGEEAAIT AMMEAVTDKD RIFELYLNSI EWHYGVFGAE AASRYFYQIP AAKLTKQQAA KLTARVPAPL YYADHPKSKR LRNKTNIVLK RMGSAELPES DTD // ID MURB_NEIMB Reviewed; 346 AA. AC Q9K016; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase {ECO:0000255|HAMAP-Rule:MF_00037}; DE EC=1.3.1.98 {ECO:0000255|HAMAP-Rule:MF_00037}; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00037}; GN Name=murB {ECO:0000255|HAMAP-Rule:MF_00037}; GN OrderedLocusNames=NMB0811; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00037}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00037}. CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000255|HAMAP- CC Rule:MF_00037}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00037}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41224.1; -; Genomic_DNA. DR PIR; B81156; B81156. DR RefSeq; NP_273853.1; NC_003112.2. DR RefSeq; WP_002225411.1; NC_003112.2. DR ProteinModelPortal; Q9K016; -. DR STRING; 122586.NMB0811; -. DR PaxDb; Q9K016; -. DR EnsemblBacteria; AAF41224; AAF41224; NMB0811. DR GeneID; 902926; -. DR KEGG; nme:NMB0811; -. DR PATRIC; 20357009; VBINeiMen85645_1023. DR eggNOG; ENOG4105D4A; Bacteria. DR eggNOG; COG0812; LUCA. DR HOGENOM; HOG000284356; -. DR KO; K00075; -. DR OMA; MQNIGAY; -. DR OrthoDB; EOG60CWQ3; -. DR BioCyc; NMEN122586:GHGG-842-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; -; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR003170; MurB. DR InterPro; IPR011601; MurB_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR PANTHER; PTHR21071; PTHR21071; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR SUPFAM; SSF56194; SSF56194; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD; KW Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 346 UDP-N-acetylenolpyruvoylglucosamine FT reductase. FT /FTId=PRO_0000179233. FT DOMAIN 18 189 FAD-binding PCMH-type. FT {ECO:0000255|HAMAP-Rule:MF_00037}. FT ACT_SITE 165 165 {ECO:0000255|HAMAP-Rule:MF_00037}. FT ACT_SITE 240 240 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00037}. FT ACT_SITE 336 336 {ECO:0000255|HAMAP-Rule:MF_00037}. SQ SEQUENCE 346 AA; 37961 MW; 91FDFE4842712104 CRC64; MQPIRYRTDL TPYNTFGLRA QARAFIALEH ADELRDIVRL LEFDRDTVLW LGGGSNILLM QDYAGLVVHM ENKGIREIAR SDGMVLIEAQ AGEIWHDFVL HTVALGLSGL ENLSLIPGTV GASPVQNIGA YGVEAKDVIH SVRCFDLDTE TFVELANADC RFAYRESLFK QEGKGRYVIV SVVFALKTHF VPTLGYGDLA AAVAELSAGR VPTAKDVSDA VCAIRNSKLP NPNVLGNVGS FFKNPVVSAE KAATLLQRHP DMPRYPQPDG SVKLAAGWLI DQCRLKGFQI GGAAVHDRQA LVLVNKNNAS ANDVRQLAQH IKFTVFARFQ VELHAEPNWL PASFSL // ID MURC_NEIMB Reviewed; 469 AA. AC Q9K0Y1; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 103. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046}; DE EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046}; GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; GN OrderedLocusNames=NMB0423; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanine. {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP- CC Rule:MF_00046}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40861.1; -; Genomic_DNA. DR PIR; B81201; B81201. DR RefSeq; NP_273471.2; NC_003112.2. DR ProteinModelPortal; Q9K0Y1; -. DR SMR; Q9K0Y1; 5-465. DR STRING; 122586.NMB0423; -. DR PaxDb; Q9K0Y1; -. DR EnsemblBacteria; AAF40861; AAF40861; NMB0423. DR GeneID; 902539; -. DR KEGG; nme:NMB0423; -. DR PATRIC; 20356042; VBINeiMen85645_0536. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR HOGENOM; HOG000256031; -. DR KO; K01924; -. DR OMA; FHFIGIG; -. DR OrthoDB; EOG64BQ73; -. DR BioCyc; NMEN122586:GHGG-447-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01082; murC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 469 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_0000182122. FT NP_BIND 113 119 ATP. {ECO:0000255|HAMAP-Rule:MF_00046}. SQ SEQUENCE 469 AA; 50279 MW; A50C783ACB994ABA CRC64; MMKNRVTNIH FVGIGGVGMS GIAEVLHNLG FKVSGSDQAR NAATEHLGSL GIQVYPGHTA EHVNGADVVV TSTAVKKENP EVVAALEQQI PVIPRALMLA ELMRFRDGIA IAGTHGKTTT TSLTASILGA AGLDPTFVIG GKLNAAGTNA RLGKGEYIVA EADESDASFL HLTPIMSVVT NIDEDHMDTY GHSVEKLHQA FIDFIHRMPF YGKAFLCIDS EHVRAILPKV SKPYATYGLD DTADIYATDI ENVGAQMKFT VHVQMKGHEQ GSFEVVLNMP GRHNVLNALA AIGVALEVGA SVEAIQKGLL GFEGVGRRFQ KYGDIKLPNG GTALLVDDYG HHPVEMAATL AAARGAYLEK RLVLAFQPHR YTRTRDLFED FTKVLNTVDA LVLTEVYAAG EEPIAAADSR ALARAIRVLG KLEPIYCENV ADLPEMLLNV LQDGDIVLNM GAGSINRVPA ALLALSKQI // ID MURA_NEIMB Reviewed; 417 AA. AC Q9K1Q9; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111}; GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; GN OrderedLocusNames=NMB0011; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D- CC glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha- CC D-glucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40490.1; -; Genomic_DNA. DR PIR; A81248; A81248. DR RefSeq; NP_273077.1; NC_003112.2. DR RefSeq; WP_002225755.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q9; -. DR STRING; 122586.NMB0011; -. DR PaxDb; Q9K1Q9; -. DR EnsemblBacteria; AAF40490; AAF40490; NMB0011. DR GeneID; 902113; -. DR KEGG; nme:NMB0011; -. DR PATRIC; 20354951; VBINeiMen85645_0012. DR eggNOG; ENOG4105CDF; Bacteria. DR eggNOG; COG0766; LUCA. DR HOGENOM; HOG000075602; -. DR KO; K00790; -. DR OMA; IRTAPHP; -. DR OrthoDB; EOG68M4GK; -. DR BioCyc; NMEN122586:GHGG-11-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00111; MurA; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01072; murA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase. FT CHAIN 1 417 UDP-N-acetylglucosamine 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000178899. FT ACT_SITE 117 117 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00111}. FT MOD_RES 117 117 2-(S-cysteinyl)pyruvic acid O- FT phosphothioketal. {ECO:0000255|HAMAP- FT Rule:MF_00111}. SQ SEQUENCE 417 AA; 43945 MW; 559002DF2B99FADD CRC64; MDKLKISANG PLNGEITVSG AKNAALPLMC AGLLTSGTLR LKNVPMLADV KTTQKLLQGM GARVLTDNIS EFEINGGTVN NTCAPYELVR TMRASILVLG PTLARFGEAQ VSLPGGCAIG SRPVDQHLKG LEAMGAEIVI EHGYVKAKGK LKGTRVAMDV VTVGGTENLL MAATLAEGTT VLENCAIEPE VVDLAECLVK MGAKISGIGT STMIVEGVDE LQGCEHSVVP DRIEAGTFLC AVAITGGRVV LRNAAPKTME VVLDKLVEAG AVIEAGDDWI AIDMRQRPKA VDIRTVVHPG FPTDMQAQFM ALNAVAEGSC RVVETIFENR FMHVPELNRM GANITTEGNT AFVQGVEQLS GAVVKATDLR ASASLVIAGL AARGETVVEQ IYHLDRGYEN IEKKLGSVGA KIERVSG // ID MUTS_NEIMB Reviewed; 864 AA. AC Q9JX94; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096}; GN Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; GN OrderedLocusNames=NMB2160; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is possible that it carries out the mismatch recognition CC step. This protein has a weak ATPase activity. {ECO:0000255|HAMAP- CC Rule:MF_00096}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. CC {ECO:0000255|HAMAP-Rule:MF_00096}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42468.1; -; Genomic_DNA. DR PIR; A81000; A81000. DR RefSeq; NP_275145.1; NC_003112.2. DR RefSeq; WP_002225746.1; NC_003112.2. DR ProteinModelPortal; Q9JX94; -. DR STRING; 122586.NMB2160; -. DR PaxDb; Q9JX94; -. DR EnsemblBacteria; AAF42468; AAF42468; NMB2160. DR GeneID; 903212; -. DR KEGG; nme:NMB2160; -. DR PATRIC; 20360520; VBINeiMen85645_2756. DR eggNOG; ENOG4105D86; Bacteria. DR eggNOG; COG0249; LUCA. DR HOGENOM; HOG000221407; -. DR KO; K03555; -. DR OMA; CCTTMGS; -. DR OrthoDB; EOG6Q5NPV; -. DR BioCyc; NMEN122586:GHGG-2225-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.110; -; 1. DR Gene3D; 3.40.1170.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00096; MutS; 1. DR InterPro; IPR005748; DNA_mismatch_repair_MutS-1. DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N. DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01624; MutS_I; 1. DR Pfam; PF05188; MutS_II; 1. DR Pfam; PF05192; MutS_III; 1. DR Pfam; PF05190; MutS_IV; 1. DR Pfam; PF00488; MutS_V; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SUPFAM; SSF48334; SSF48334; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF53150; SSF53150; 1. DR SUPFAM; SSF55271; SSF55271; 1. DR TIGRFAMs; TIGR01070; mutS1; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 864 DNA mismatch repair protein MutS. FT /FTId=PRO_0000115112. FT NP_BIND 607 614 ATP. {ECO:0000255|HAMAP-Rule:MF_00096}. SQ SEQUENCE 864 AA; 95227 MW; 4A77EE918F033A40 CRC64; MSKSAVSPMM QQYLGIKAQH TDKLVFYRMG DFYEMFFDDA VEAAKLLDIT LTTRGQVDGE PVKMAGVPFH AAEQYLARLV KLGKSVAICE QVGEVGAGKG PVERKVVRIV TPGTLTDSAL LEDKETNRIV AVSPDKKYIG LAWASLQSGE FKTKLTTVDK LDDELARLQA AEILLPDSKN APQLQTASGV TRLNAWQFAA DAGEKLLTEY FGCQDLRGFG LDGKEHAVAI GAAGALLNYI RLTQNLMPQH LDGLSLETDS QYIGMDAATR RNLEITQTLS GKKSPTLMST LDLCATHMGS RLLALWLHHP LRNRAHIRAR QEAVAALESQ YKPLQCRLKS IADIERIAAR IAVGNARPRD LAALRDSLFA LSEIELSAEC SSLLGTLKAV FPENLSTAEQ LRQAILPEPS VWLKDGNVIN HGFHPELDEL RRIQNHGDEF LLDLEAKERE RTGLSTLKVE FNRVHGFYIE LSKTQAEQAP ADYQRRQTLK NAERFITPEL KAFEDKVLTA QEQALALEKQ LFDGVLKNLQ TALPQLQKAA KAAAALDVLS TFSALAKERN FVRPEFADYP VIHIENGRHP VVEQQVRHFT ANHTDLDHKH RLMLLTGPNM GGKSTYMRQV ALIVLLAHTG CFVPADAATI GPIDQIFTRI GASDDLASNR STFMVEMSET AYILHHATEQ SLVLMDEVGR GTSTFDGLAL AHAVAEHLLQ KNKSFSLFAT HYFELTYLPE AHTAAVNMHL SALEQGQDIV FLHQIQPGPA GKSYGIAVAK LAGLPVRALK SAQKHLNGLE NQAAANRPQL DIFSTMPSEK GDEPNVGNFV DKAEEKHFEG ILAAALEKLD PDSLTPREAL SELYRLKDLC KSVS // ID NADD_NEIMB Reviewed; 201 AA. AC P57090; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase; DE EC=2.7.7.18; DE AltName: Full=Deamido-NAD(+) diphosphorylase; DE AltName: Full=Deamido-NAD(+) pyrophosphorylase; DE AltName: Full=Nicotinate mononucleotide adenylyltransferase; DE Short=NaMN adenylyltransferase; GN Name=nadD; OrderedLocusNames=NMB2024; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide CC (NaAD). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide = CC diphosphate + deamido-NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido- CC NAD(+) from nicotinate D-ribonucleotide: step 1/1. CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42347.1; -; Genomic_DNA. DR PIR; C81015; C81015. DR RefSeq; NP_275016.1; NC_003112.2. DR RefSeq; WP_002223158.1; NC_003112.2. DR ProteinModelPortal; P57090; -. DR STRING; 122586.NMB2024; -. DR PaxDb; P57090; -. DR EnsemblBacteria; AAF42347; AAF42347; NMB2024. DR GeneID; 904082; -. DR KEGG; nme:NMB2024; -. DR PATRIC; 20360163; VBINeiMen85645_2581. DR eggNOG; ENOG4108Z1W; Bacteria. DR eggNOG; COG1057; LUCA. DR HOGENOM; HOG000262779; -. DR KO; K00969; -. DR OMA; HLIMAQY; -. DR OrthoDB; EOG6F55KJ; -. DR BioCyc; NMEN122586:GHGG-2086-MONOMER; -. DR UniPathway; UPA00253; UER00332. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00244; NaMN_adenylyltr; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR005248; NAMN_adtrnsfrase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR12039; PTHR12039; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00482; TIGR00482; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; NAD; Nucleotide-binding; KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 201 Probable nicotinate-nucleotide FT adenylyltransferase. FT /FTId=PRO_0000181430. SQ SEQUENCE 201 AA; 22269 MW; 3AECE2F049B7A9C0 CRC64; MKKIGLFGGT FDPIHNGHLH IARAFADEIG LDAVVFLPTG GPYHKDAASA SAADRLAMVE LATAEDARFA VSDCDIVREG ATYTFDTVQI FRQQFPSAQL WWLMGSDSLM KLHTWKKWQM LVRETNIAVA MRQGDSLHQT PRELHAWLGK SLQDGSVRIL SAPMHNVSST EIRRNLAGQG VSDGIPPAAA RYIREHGLYE K // ID MURE_NEIMB Reviewed; 492 AA. AC Q9K0Y9; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; GN OrderedLocusNames=NMB0414; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl- CC D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + CC UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6- CC diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40853.1; -; Genomic_DNA. DR PIR; C81202; C81202. DR RefSeq; NP_273463.1; NC_003112.2. DR RefSeq; WP_002224920.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y9; -. DR STRING; 122586.NMB0414; -. DR PaxDb; Q9K0Y9; -. DR EnsemblBacteria; AAF40853; AAF40853; NMB0414. DR GeneID; 902530; -. DR KEGG; nme:NMB0414; -. DR PATRIC; 20356017; VBINeiMen85645_0524. DR eggNOG; ENOG4107EEN; Bacteria. DR eggNOG; COG0769; LUCA. DR HOGENOM; HOG000268118; -. DR KO; K01928; -. DR OMA; HNHNIKF; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NMEN122586:GHGG-438-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00208; MurE; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 492 UDP-N-acetylmuramoyl-L-alanyl-D- FT glutamate--2,6-diaminopimelate ligase. FT /FTId=PRO_0000101916. FT NP_BIND 114 120 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 156 157 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 413 416 Meso-diaminopimelate binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT MOTIF 413 416 Meso-diaminopimelate recognition motif. FT BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 183 183 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 189 189 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 191 191 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 389 389 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 462 462 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 466 466 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT MOD_RES 223 223 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 492 AA; 53045 MW; B772F358CA32919E CRC64; MFSKLTPLAE TGIPTLSCAN AAGRLLHSDS RQIKQGDIFV ACPGEYADGR SYIPAAVANG AAFVFWDDDG KFAWNPEWKV PNQGIKDLKH RAGILAAQVY GNVSDGLKVW GVAGTNGKTS ITQWLAQAAD LLGEKTAIVG TVGNGFWGAL EETTHTTPAP VDVQTLLYRF RQQGATVAAM EVSSHGLDQS RVNGVSFRSA IFTNLTRDHL DYHGTMEAYG AIKSRLFYWH GLKHAVINVD DEYGAELVGR LKKDCPDLAV YSYGFSEHAD IRITDFTASS DGIAAVFQTP WGEGKCRTRL LGRFNAQNLA ACIALLCANG YPLDKVLDVL AKIRPASGRM DCIMNSGKPL VVVDYAHTPD ALEKALATLQ EIKPQGAALW CVFGCGGNRD RGKRPLMGAA AVQGADKVVV TSDNPRLENP HDIINDILPA VPAPECVEAD RAAAVRYAVE QAAANDIILI AGKGHENYQD VQGVKHRFSD LEIVGQALLT RK // ID NAGZ_NEIMB Reviewed; 361 AA. AC Q9K0Q4; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; GN Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364}; GN OrderedLocusNames=NMB0530; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from CC peptide-linked peptidoglycan fragments, giving rise to free CC GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic CC acid-linked peptides. {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl- CC D-hexosamine residues in N-acetyl-beta-D-hexosaminides. CC {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00364}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40960.1; -; Genomic_DNA. DR PIR; B81190; B81190. DR RefSeq; NP_273575.1; NC_003112.2. DR RefSeq; WP_002225592.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q4; -. DR STRING; 122586.NMB0530; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR PaxDb; Q9K0Q4; -. DR EnsemblBacteria; AAF40960; AAF40960; NMB0530. DR GeneID; 902646; -. DR KEGG; nme:NMB0530; -. DR PATRIC; 20356311; VBINeiMen85645_0674. DR eggNOG; ENOG4107QPA; Bacteria. DR eggNOG; COG1472; LUCA. DR HOGENOM; HOG000248526; -. DR KO; K01207; -. DR OMA; MIMTSHI; -. DR OrthoDB; EOG6BCT06; -. DR BioCyc; NMEN122586:GHGG-556-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.300; -; 1. DR HAMAP; MF_00364; NagZ; 1. DR InterPro; IPR022956; Beta_hexosaminidase_bac. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00933; Glyco_hydro_3; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Glycosidase; Hydrolase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 361 Beta-hexosaminidase. FT /FTId=PRO_0000210791. FT REGION 174 175 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT ACT_SITE 187 187 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00364}. FT ACT_SITE 258 258 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 69 69 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 144 144 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT SITE 185 185 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00364}. SQ SEQUENCE 361 AA; 39153 MW; 3E066E5B9809033A CRC64; MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAVGGIILFR RNFQNIEQLK TLTAEIKALR TPELIIAVDH EGGRVQRFIE GFTRLPAMST LGEIWDKDGA SAAETAAGQV GRVLATELSA CGIDLSFTPV LDLDWGNCPV IGNRSFHRNP EAVARLALAL QKGLTKGGMK SCGKHFPGHG FVEGDSHLVL PEDWRSLSEL ETADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRE DFRIPDNPTL AQRWQYMANT LGSAAAQAVM QTADFQAAQA FVAGLASPQD TAGGVKVGEA F // ID MURD_NEIMB Reviewed; 445 AA. AC Q9K0Y4; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 100. DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639}; DE EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639}; DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639}; GN Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; GN OrderedLocusNames=NMB0420; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate CC to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). CC {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine CC + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanyl-D-glutamate. {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP- CC Rule:MF_00639}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40858.1; -; Genomic_DNA. DR PIR; G81200; G81200. DR RefSeq; NP_273468.1; NC_003112.2. DR RefSeq; WP_002224926.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y4; -. DR STRING; 122586.NMB0420; -. DR PaxDb; Q9K0Y4; -. DR EnsemblBacteria; AAF40858; AAF40858; NMB0420. DR GeneID; 902536; -. DR KEGG; nme:NMB0420; -. DR PATRIC; 20356034; VBINeiMen85645_0532. DR eggNOG; ENOG4105DMZ; Bacteria. DR eggNOG; COG0771; LUCA. DR HOGENOM; HOG000049427; -. DR KO; K01925; -. DR OMA; PGIPYTN; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NMEN122586:GHGG-444-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00639; MurD; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005762; UDP-N-AcMur-Glu_ligase. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01087; murD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 445 UDP-N-acetylmuramoylalanine--D-glutamate FT ligase. FT /FTId=PRO_0000109049. FT NP_BIND 117 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00639}. SQ SEQUENCE 445 AA; 48163 MW; 9B30F5F67A060393 CRC64; MTFQNKKILV AGLGGTGISM IAYLRKNGAE VAAYDAELKP ERVSQIGKMF DGLVFYTGRL KDALDNGFDI LALSPGISER QPDIEAFKQN GGRVLGDIEL LADIVNRRDD KVIAITGSNG KTTVTSLVGY LCIKCGLDTV IAGNIGTPVL EAEWQREGKK ADVWVLELSS FQLENTESLR PTAATVLNIS EDHLDRYDDL LDYAHTKAKI FRGDGVQVLN ADDAFCRAMK RAGREVKWFS LEHEADFWLE RETGRLKQGN EDLIVTQDIP LQGLHNAANV MAAVALCEAI GLSREALLEH VKTFQGLPHR VEKIGEKNGV VFIDDSKGTN VGATAAAIAG LQNPLFVILG GMGKGQDFTP LRDALVGKAK GVFLIGVDAP QIRRDLDGCG LNMTDCATLG EAVQTAYAQA EAGDIVLLSP ACASFDMFKG YAHRSEVFIE AFKAL // ID MURG_NEIMB Reviewed; 355 AA. AC Q9K0Y2; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033}; DE EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033}; DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033}; GN Name=murG {ECO:0000255|HAMAP-Rule:MF_00033}; GN OrderedLocusNames=NMB0422; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc CC subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid CC intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- CC (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala- CC gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + CC GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphosphoundecaprenol. {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40860.1; -; Genomic_DNA. DR PIR; A81201; A81201. DR RefSeq; NP_273470.1; NC_003112.2. DR RefSeq; WP_002224927.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y2; -. DR STRING; 122586.NMB0422; -. DR PaxDb; Q9K0Y2; -. DR EnsemblBacteria; AAF40860; AAF40860; NMB0422. DR GeneID; 902538; -. DR KEGG; nme:NMB0422; -. DR PATRIC; 20356040; VBINeiMen85645_0535. DR eggNOG; ENOG4105DVQ; Bacteria. DR eggNOG; COG0707; LUCA. DR HOGENOM; HOG000218321; -. DR KO; K02563; -. DR OMA; EQNALPG; -. DR OrthoDB; EOG61VZFD; -. DR BioCyc; NMEN122586:GHGG-446-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0030259; P:lipid glycosylation; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00033; MurG; 1. DR InterPro; IPR006009; GlcNAc_MurG. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR004276; GlycoTrans_28_N. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR Pfam; PF03033; Glyco_transf_28; 1. DR TIGRFAMs; TIGR01133; murG; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase. FT CHAIN 1 355 UDP-N-acetylglucosamine--N-acetylmuramyl- FT (pentapeptide) pyrophosphoryl- FT undecaprenol N-acetylglucosamine FT transferase. FT /FTId=PRO_0000109191. SQ SEQUENCE 355 AA; 38021 MW; 84A9359559062CB5 CRC64; MGGKTFMLMA GGTGGHIFPA LAVADSLRAR GHHVIWLGSK DSMEERIVPQ YGIRLETLAI KGVRGNGIKR KLMLPVTLYQ TVREAQRIIR KHRVECVIGF GGFVTFPGGL AAKLLGVPIV IHEQNAVAGL SNRHLSRWAK RVLYAFPKAF SHEGGLVGNP VRADISNLPV PAERFQGREG RLKILVVGGS LGADVLNKTV PQALALLPDN ARPQMYHQSG RGKLGSLQAD YDALGVKAEC VEFITDMVSA YRDADLVICR AGALTIAELT AAGLGALLVP YPHAVDDHQT ANARFMVQAE AGLLLPQTQL TAEKLAEILG GLNREKCLKW AENARTLALP HSADDVAEAA IACAA // ID MURI_NEIMB Reviewed; 270 AA. AC P0A0R0; Q9RQW7; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 70. DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258}; DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258}; GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; Synonyms=glr; GN OrderedLocusNames=NMB0458; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}. CC -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_00258}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00258}. CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family. CC {ECO:0000255|HAMAP-Rule:MF_00258}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40895.1; -; Genomic_DNA. DR PIR; C81196; C81196. DR RefSeq; NP_273505.1; NC_003112.2. DR RefSeq; WP_002223465.1; NC_003112.2. DR ProteinModelPortal; P0A0R0; -. DR STRING; 122586.NMB0458; -. DR PaxDb; P0A0R0; -. DR EnsemblBacteria; AAF40895; AAF40895; NMB0458. DR GeneID; 902574; -. DR KEGG; nme:NMB0458; -. DR PATRIC; 20356132; VBINeiMen85645_0582. DR eggNOG; ENOG4105F03; Bacteria. DR eggNOG; COG0796; LUCA. DR HOGENOM; HOG000262396; -. DR KO; K01776; -. DR OMA; VYGCTHY; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NMEN122586:GHGG-482-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1860; -; 1. DR HAMAP; MF_00258; Glu_racemase; 1. DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase. DR InterPro; IPR001920; Asp/Glu_race. DR InterPro; IPR033134; Asp/Glu_racemase_AS_2. DR InterPro; IPR004391; Glu_race. DR Pfam; PF01177; Asp_Glu_race; 1. DR SUPFAM; SSF53681; SSF53681; 2. DR TIGRFAMs; TIGR00067; glut_race; 1. DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Isomerase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 270 Glutamate racemase. FT /FTId=PRO_0000095492. FT REGION 14 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 46 47 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 78 79 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 190 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT ACT_SITE 77 77 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. FT ACT_SITE 189 189 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. SQ SEQUENCE 270 AA; 29535 MW; 008ECB673B73FFBD CRC64; MENIGRQRPI GVFDSGIGGL TNVRALMERL PMENIIYFGD TARVPYGTKS KATIENFSMQ IVDFLLEHDV KAMVIACNTI AAVAGQKIRQ KTGNMPVLDV ISAGAKAALA TTRNNKIGII ATNTTVNSNA YARAIHRNNP DTLVRTQAAP LLVPLVEEGW LEHEVTRLTV CEYLKPLLAD GIDTLVLGCT HFPLLKPLIG REAGNVALVD SAITTAEETA RVLAQEGLLN TDNNNPDYRF YVSDIPLKFR TIGERFLGRT MEQIEMVSLG // ID NADB_NEIMB Reviewed; 502 AA. AC Q9K107; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=L-aspartate oxidase; DE Short=LASPO; DE EC=1.4.3.16; DE AltName: Full=Quinolinate synthase B; GN Name=nadB; OrderedLocusNames=NMB0392; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to CC iminoaspartate. CC -!- CATALYTIC ACTIVITY: L-aspartate + O(2) = iminosuccinate + CC H(2)O(2). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; CC iminoaspartate from L-aspartate (oxidase route): step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC NadB subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40832.1; -; Genomic_DNA. DR PIR; H81203; H81203. DR RefSeq; NP_273441.1; NC_003112.2. DR RefSeq; WP_002222010.1; NC_003112.2. DR ProteinModelPortal; Q9K107; -. DR STRING; 122586.NMB0392; -. DR PaxDb; Q9K107; -. DR EnsemblBacteria; AAF40832; AAF40832; NMB0392. DR GeneID; 902507; -. DR KEGG; nme:NMB0392; -. DR PATRIC; 20355947; VBINeiMen85645_0491. DR eggNOG; ENOG4108IYU; Bacteria. DR eggNOG; COG0029; LUCA. DR HOGENOM; HOG000160476; -. DR KO; K00278; -. DR OMA; HCVQWLI; -. DR OrthoDB; EOG696BWH; -. DR BioCyc; NMEN122586:GHGG-414-MONOMER; -. DR UniPathway; UPA00253; UER00326. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR005288; NadB. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. DR Pfam; PF00890; FAD_binding_2; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF56425; SSF56425; 1. DR TIGRFAMs; TIGR00551; nadB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase; KW Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1 502 L-aspartate oxidase. FT /FTId=PRO_0000184392. FT NP_BIND 8 22 FAD. {ECO:0000255}. FT ACT_SITE 228 228 {ECO:0000250}. FT ACT_SITE 249 249 {ECO:0000250}. SQ SEQUENCE 502 AA; 54563 MW; 644152CC3753E294 CRC64; MQTDCDVLIA GNGLAALTLA LSLPESFRIV ILCKNRLDDT ASRHAQGGIA AAWSGEDDIE KHVADTLEAG AGLCDEAAVR AILSQGKPAI EWLLAQGVAF DRNHNGLHLT REGGHTCRRI AHVADYTGEA VMQSLIAQIR RRPNIRVCER QMALDIQTES GAACGLTVLD CRTQETYRIR ARHTVLAGGG LGQIYAATTT PPECTGDAIA MAIRAGCAVG NLEFIQFHPT GLARPSENGR TFLISEAVRG EGGILTNQAG ERFMPHYDRR AELAPRDIVA RAIAAEIAKQ TQDFVSLDIS HQPAAFVRRH FPSIHRHCLS QCGLDITRQA IPVRPVQHYT CGGIQTDPCG RTSLPQLYAL GETACTGLHG ANRLASNSLL ECVVTARLCA QAIADGQAFQ AEPFQRPSES LSAEAGIFSD DLQNTFSRPV LQTFNQRHLG ILRNDTGLRR AIAQLQLWKQ NQAEPHTASE YENRNLLECS LAVAQAAYRR RQNIGAHFNS DC // ID MUTL_NEIMB Reviewed; 658 AA. AC Q9JYT2; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149}; GN Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; GN OrderedLocusNames=NMB1442; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is required for dam-dependent methyl-directed DNA mismatch CC repair. May act as a "molecular matchmaker", a protein that CC promotes the formation of a stable complex between two or more CC DNA-binding proteins in an ATP-dependent manner without itself CC being part of a final effector complex. {ECO:0000255|HAMAP- CC Rule:MF_00149}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family. CC {ECO:0000255|HAMAP-Rule:MF_00149}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41803.1; -; Genomic_DNA. DR PIR; B81084; B81084. DR RefSeq; NP_274454.1; NC_003112.2. DR RefSeq; WP_002222285.1; NC_003112.2. DR ProteinModelPortal; Q9JYT2; -. DR STRING; 122586.NMB1442; -. DR PaxDb; Q9JYT2; -. DR EnsemblBacteria; AAF41803; AAF41803; NMB1442. DR GeneID; 903863; -. DR KEGG; nme:NMB1442; -. DR PATRIC; 20358599; VBINeiMen85645_1811. DR eggNOG; ENOG4105DC6; Bacteria. DR eggNOG; COG0323; LUCA. DR HOGENOM; HOG000256550; -. DR KO; K03572; -. DR OMA; QFLFINN; -. DR OrthoDB; EOG6P8TMH; -. DR BioCyc; NMEN122586:GHGG-1480-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR HAMAP; MF_00149; DNA_mis_repair; 1. DR InterPro; IPR013507; DNA_mismatch_repair_C. DR InterPro; IPR014762; DNA_mismatch_repair_CS. DR InterPro; IPR002099; DNA_mismatch_repair_fam. DR InterPro; IPR020667; DNA_mismatch_repair_MutL. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR014790; MutL_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF01119; DNA_mis_repair; 1. DR Pfam; PF08676; MutL_C; 1. DR SMART; SM01340; DNA_mis_repair; 1. DR SMART; SM00853; MutL_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR00585; mutl; 1. DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Reference proteome. FT CHAIN 1 658 DNA mismatch repair protein MutL. FT /FTId=PRO_0000177956. SQ SEQUENCE 658 AA; 71647 MW; 40EEDC060396DD2F CRC64; MSRIAALPDH LVNQIAAGEV VERPANALKE IVENSIDAGA TAIEVELAGG GIRLIRVSDN GGGIHPDDIE LALHRHATSK IKTLNDLEHV ASMGFRGEGL ASIASVSRLT LTSRQNDSSH ATQVKAEDGK LSSPTAAAHP VGTTIEAAEL FFNTPARRKF LKSENTEYAH CATMLERLAL AHPHIAFSLK RDGKQVFKLP AQSLHERIAA IVGEDFQTAS LGIDSGNGAL RLYGAIAKPT FAKGKTDKQY CFVNHRFVRD KVMLHAVKQA YRDVLHNALT PAFVLFLDLP PEAVDVNVHP TKTEIRFRDS QQVHQLVFHT LNKALADTRA NLTESVGNAG EVLHDITGVV STPMPSENDS ENLFDSVSNY PTGNKSDTHN AFGSSGKTAP MPYQSAYAPQ QRSLSLRESR AAMNTYAELY KKTDDIDLEL SRFEQARFGN MPSETPAPQT DTPLSDGIPS QSELPPLGFA IAQLLGIYIL AQAEDSLLLI DMHAAAERVN YEKMKRQRQE NGNLQSQRLL IPVTFAASHE ECAALADYAE TLAGFGLELS DMGGNTLAVR AVPAMLGKAD VVSLAKDVLN ELAQVGSSQT IEEHENRILA TMSCHGSIRA GRRLTLPEMN ALLRDMENTP RSNQCNHGRP TWVKLTLKEL DALFLRGQ // ID NADA_NEIMB Reviewed; 370 AA. AC Q9K105; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Quinolinate synthase A {ECO:0000255|HAMAP-Rule:MF_00567}; DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00567}; GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00567}; GN OrderedLocusNames=NMB0394; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate. CC {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate = CC pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00567}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00567}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00567}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40834.1; -; Genomic_DNA. DR PIR; B81204; B81204. DR RefSeq; NP_273443.1; NC_003112.2. DR RefSeq; WP_002222012.1; NC_003112.2. DR ProteinModelPortal; Q9K105; -. DR STRING; 122586.NMB0394; -. DR PaxDb; Q9K105; -. DR EnsemblBacteria; AAF40834; AAF40834; NMB0394. DR GeneID; 902509; -. DR KEGG; nme:NMB0394; -. DR PATRIC; 20355951; VBINeiMen85645_0493. DR eggNOG; ENOG4105D0I; Bacteria. DR eggNOG; COG0379; LUCA. DR HOGENOM; HOG000222769; -. DR KO; K03517; -. DR OMA; IAHPECE; -. DR OrthoDB; EOG6DJZ56; -. DR BioCyc; NMEN122586:GHGG-416-MONOMER; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00567; NadA_type1; 1. DR InterPro; IPR003473; NadA. DR InterPro; IPR023513; Quinolinate_synth_A_type1. DR Pfam; PF02445; NadA; 1. DR TIGRFAMs; TIGR00550; nadA; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridine nucleotide biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 370 Quinolinate synthase A. FT /FTId=PRO_0000155764. FT BINDING 62 62 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00567}. FT BINDING 83 83 Iminoaspartate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00567}. FT BINDING 154 154 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00567}. FT BINDING 171 171 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00567}. FT BINDING 241 241 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00567}. FT BINDING 258 258 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00567}. SQ SEQUENCE 370 AA; 40164 MW; AF5295880B777F86 CRC64; MQTAARRSFD YDMPLIQTPT SACQIRQAWA KVADTPDRET ADRLKDEIKA LLKEKNAVLV AHYYVDPLIQ DLALETGGCV GDSLEMARFG AEHEAGTLVV AGVRFMGESA KILCPEKTVL MPDLEAECSL DLGCPEEAFS AFCDQHPDRT VVVYANTSAA VKARADWVVT SSVALEIVSY LKSRGEKLIW GPDRHLGDYI CRETGADMLL WQGSCIVHNE FKGQELAALK AEHPEAVVLV HPESPQSVIE LGDVVGSTSK LLKAAVSRPE KKFIVATDLG ILHEMQKQAP DKQFIAAPTA GNGGSCKSCA FCPWMAMNSL GGIKYALTSG RNEILLDRKL GEAAKLPLQR MLDFAAGLKK KDVFNGMGPA // ID NDK_NEIMB Reviewed; 141 AA. AC P65533; Q9JQU6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDK {ECO:0000255|HAMAP-Rule:MF_00451}; DE Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_00451}; DE AltName: Full=Nucleoside-2-P kinase {ECO:0000255|HAMAP-Rule:MF_00451}; GN Name=ndk {ECO:0000255|HAMAP-Rule:MF_00451}; OrderedLocusNames=NMB1307; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates CC other than ATP. The ATP gamma phosphate is transferred to the NDP CC beta phosphate via a ping-pong mechanism, using a phosphorylated CC active-site intermediate. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00451}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00451}. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000255|HAMAP- CC Rule:MF_00451}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41682.1; -; Genomic_DNA. DR PIR; A81098; A81098. DR RefSeq; NP_274326.1; NC_003112.2. DR RefSeq; WP_002213338.1; NC_003112.2. DR ProteinModelPortal; P65533; -. DR SMR; P65533; 2-138. DR STRING; 122586.NMB1307; -. DR PaxDb; P65533; -. DR EnsemblBacteria; AAF41682; AAF41682; NMB1307. DR GeneID; 903729; -. DR KEGG; nme:NMB1307; -. DR PATRIC; 20358257; VBINeiMen85645_1640. DR eggNOG; ENOG4108UGX; Bacteria. DR eggNOG; COG0105; LUCA. DR HOGENOM; HOG000224565; -. DR KO; K00940; -. DR OMA; AEHSERP; -. DR OrthoDB; EOG67DPRV; -. DR BioCyc; NMEN122586:GHGG-1345-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00451; NDP_kinase; 1. DR InterPro; IPR001564; Nucleoside_diP_kinase. DR InterPro; IPR023005; Nucleoside_diP_kinase_AS. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR PROSITE; PS00469; NDP_KINASES; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1 141 Nucleoside diphosphate kinase. FT /FTId=PRO_0000137013. FT ACT_SITE 117 117 Pros-phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 11 11 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 59 59 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 87 87 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 93 93 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 104 104 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. FT BINDING 114 114 ATP. {ECO:0000255|HAMAP-Rule:MF_00451}. SQ SEQUENCE 141 AA; 15427 MW; C5B8C01ED5463157 CRC64; MAIERTISII KPDAVGKNVI GKIYSRFEEN GLKIVAAKMK QLTLKEAQEF YAVHKDRPFY AGLVEFMTGG PVMIQVLEGE NAVLKNRELM GATNPSEAAE GTIRADFATS VSINAVHGSD SVENAALEIA YFFSQTEICP R // ID NADK_NEIMB Reviewed; 296 AA. AC P65773; Q9JQL9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=NMB0807; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. CC Catalyzes specifically the phosphorylation on 2'-hydroxyl of the CC adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP- CC Rule:MF_00361}. CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). CC {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00361}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41220.1; -; Genomic_DNA. DR PIR; F81155; F81155. DR RefSeq; NP_273849.1; NC_003112.2. DR RefSeq; WP_002213954.1; NC_003112.2. DR ProteinModelPortal; P65773; -. DR STRING; 122586.NMB0807; -. DR PaxDb; P65773; -. DR EnsemblBacteria; AAF41220; AAF41220; NMB0807. DR GeneID; 902922; -. DR KEGG; nme:NMB0807; -. DR PATRIC; 20357001; VBINeiMen85645_1019. DR eggNOG; ENOG4105F91; Bacteria. DR eggNOG; COG0061; LUCA. DR HOGENOM; HOG000227221; -. DR KO; K00858; -. DR OMA; PICPFML; -. DR OrthoDB; EOG6PZXDR; -. DR BioCyc; NMEN122586:GHGG-838-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 1. DR HAMAP; MF_00361; NAD_kinase; 1. DR InterPro; IPR017438; ATP-NAD_kinase_dom_1. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b. DR InterPro; IPR016064; NAD/diacylglycerol_kinase. DR InterPro; IPR002504; NADK. DR PANTHER; PTHR20275; PTHR20275; 1. DR Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 296 NAD kinase. FT /FTId=PRO_0000120640. FT NP_BIND 78 79 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 152 153 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT ACT_SITE 78 78 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT BINDING 180 180 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 182 182 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 251 251 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. SQ SEQUENCE 296 AA; 32853 MW; FCE151130D437713 CRC64; MNSPFHNIGI VTRPNTPDIQ DTAHTLITFL KQHGFTVYLD EVGIKEGCIY TQDTVGCHIV NKTELGQYCD LVAVLGGDGT FLSVAREIAL RAVPIIGINQ GHLGFLTQIP REYMTDKLLP VLEGKYLAEE RILIEAALIR EGKTAERAIA LNDAVLSRGG AGQMIEFEVF VNREFVYTQR SDGLIVSTPT GSTAYSLAAG GPIMQAGLHA FTLVPICPQS MTNRPIAIPD TSEIEILVTQ GGDARVHFDG QTHIDVQNLD RITIRRYRNP LRILHPTDYQ YFKTLRQKLH WGEQLV // ID NEUA_NEIMB Reviewed; 228 AA. AC P0A0Z7; Q57385; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=N-acylneuraminate cytidylyltransferase; DE EC=2.7.7.43; DE AltName: Full=CMP-N-acetylneuraminic acid synthase; DE Short=CMP-NeuNAc synthase; DE AltName: Full=CMP-sialic acid synthase; GN Name=neuA; Synonyms=siaB, synB; OrderedLocusNames=NMB0069; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=1398032; DOI=10.1016/0378-1097(92)90397-7; RA Edwards U., Frosch M.; RT "Sequence and functional analysis of the cloned Neisseria meningitidis RT CMP-NeuNAc synthetase."; RL FEMS Microbiol. Lett. 75:161-166(1992). RN [2] RP SEQUENCE REVISION. RX PubMed=7830552; DOI=10.1111/j.1365-2958.1994.tb01274.x; RA Edwards U., Mueller A., Hammerschmidt S., Gerardy-Schahn R., RA Frosch M.; RT "Molecular analysis of the biosynthesis pathway of the alpha-2,8 RT polysialic acid capsule by Neisseria meningitidis serogroup B."; RL Mol. Microbiol. 14:141-149(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NMB / Serogroup B; RX PubMed=8113198; RA Swartley J.S., Stephens D.S.; RT "Identification of a genetic locus involved in the biosynthesis of N- RT acetyl-D-mannosamine, a precursor of the (alpha 2-->8)-linked RT polysialic acid capsule of serogroup B Neisseria meningitidis."; RL J. Bacteriol. 176:1530-1534(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=NCTC 8249 / Serogroup B; RX PubMed=8045888; RA Ganguli S., Zapata G., Wallis T., Reid C., Boulnois G.J., Vann W.F., RA Roberts I.S.; RT "Molecular cloning and analysis of genes for sialic acid synthesis in RT Neisseria meningitidis group B and purification of the meningococcal RT CMP-NeuNAc synthetase enzyme."; RL J. Bacteriol. 176:4583-4589(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: CTP + N-acylneuraminate = diphosphate + CMP-N- CC acylneuraminate. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M95053; AAA20476.1; -; Genomic_DNA. DR EMBL; U04328; AAA17655.1; -; Unassigned_DNA. DR EMBL; X78068; CAA54983.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40536.1; -; Genomic_DNA. DR PIR; B53384; B53384. DR RefSeq; NP_273133.1; NC_003112.2. DR RefSeq; WP_002215295.1; NC_003112.2. DR ProteinModelPortal; P0A0Z7; -. DR SMR; P0A0Z7; 1-225. DR STRING; 122586.NMB0069; -. DR PaxDb; P0A0Z7; -. DR EnsemblBacteria; AAF40536; AAF40536; NMB0069. DR GeneID; 902175; -. DR KEGG; nme:NMB0069; -. DR PATRIC; 20355139; VBINeiMen85645_0103. DR eggNOG; ENOG4105F0R; Bacteria. DR eggNOG; COG1083; LUCA. DR HOGENOM; HOG000284760; -. DR KO; K00983; -. DR OMA; QPIHELT; -. DR OrthoDB; EOG6HXJ57; -. DR BioCyc; NMEN122586:GHGG-75-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 228 N-acylneuraminate cytidylyltransferase. FT /FTId=PRO_0000213205. SQ SEQUENCE 228 AA; 24892 MW; F2510733EE1C3A31 CRC64; MEKQNIAVIL ARQNSKGLPL KNLRKMNGIS LLGHTINAAI SSKCFDRIIV STDGGLIAEE AKNFGVEVVL RPAELASDTA SSISGVIHAL ETIGSNSGTV TLLQPTSPLR TGAHIREAFS LFDEKIKGSV VSACPMEHHP LKTLLQINNG EYAPMRHLSD LEQPRQQLPQ AFRPNGAIYI NDTASLIANN CFFIAPTKLY IMSHQDSIDI DTELDLQQAE NILNHKES // ID NMFIC_NEIMB Reviewed; 191 AA. AC Q7DDR9; DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=Adenosine monophosphate-protein transferase NmFic; DE EC=2.7.7.n1; DE AltName: Full=AMPylator NmFic; GN OrderedLocusNames=NMB0255; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RA Cuff M.E., Bigelow L., Bargassa M., Joachimiak A.; RT "Structure of a putative cell filamentation protein from Neisseria RT meningitidis."; RL Submitted (FEB-2006) to the PDB data bank. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-167 IN COMPLEX WITH ATP, RP CATALYTIC ACTIVITY, FUNCTION, AMPYLATION AT TYR-183, ENZYME RP REGULATION, AND MUTAGENESIS OF SER-182 AND GLU-186. RC STRAIN=MC58; RX PubMed=22266942; DOI=10.1038/nature10729; RA Engel P., Goepfert A., Stanger F.V., Harms A., Schmidt A., RA Schirmer T., Dehio C.; RT "Adenylylation control by intra- or intermolecular active-site RT obstruction in Fic proteins."; RL Nature 482:107-110(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-191 OF MUTANT GLY-186 IN RP COMPLEX WITH ATP ANALOG, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS RP OF GLU-186. RX PubMed=23738009; DOI=10.1371/journal.pone.0064901; RA Goepfert A., Stanger F.V., Dehio C., Schirmer T.; RT "Conserved inhibitory mechanism and competent ATP binding mode for RT adenylyltransferases with Fic fold."; RL PLoS ONE 8:E64901-E64901(2013). CC -!- FUNCTION: Adenylyltransferase that mediates the addition of CC adenosine 5'-monophosphate (AMP) to specific residues of target CC proteins. {ECO:0000269|PubMed:22266942}. CC -!- CATALYTIC ACTIVITY: ATP + [protein] = diphosphate + [protein]-AMP. CC {ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:23738009}. CC -!- ENZYME REGULATION: Adenylyltransferase activity is inhibited by CC the inhibitory helix present at the C-terminus: Glu-186 binds ATP CC and competes with ATP-binding at Arg-118, thereby preventing CC adenylyltransferase activity. Activation dissociates ATP-binding CC from Glu-186, allowing ordered binding of the entire ATP moiety CC with the alpha-phosphate in an orientation that is productive for CC accepting an incoming target hydroxyl side chain. CC {ECO:0000269|PubMed:22266942}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22266942, CC ECO:0000269|PubMed:23738009}. CC -!- PTM: Auto-AMPylation at Tyr-183 in vitro. CC {ECO:0000269|PubMed:22266942}. CC -!- MISCELLANEOUS: Defined as class III fido-domain containing CC proteins, in which the inhibitory helix is present at the C- CC terminus of the Fido domain. {ECO:0000305|PubMed:22266942}. CC -!- SIMILARITY: Contains 1 fido domain. {ECO:0000255|PROSITE- CC ProRule:PRU00791}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40709.1; -; Genomic_DNA. DR PIR; B81220; B81220. DR RefSeq; NP_273311.1; NC_003112.2. DR RefSeq; WP_002215631.1; NC_003112.2. DR PDB; 2G03; X-ray; 2.20 A; A=1-191. DR PDB; 3S6A; X-ray; 2.20 A; A=11-191. DR PDB; 3SE5; X-ray; 1.70 A; A/B/C/D=11-167. DR PDB; 3SN9; X-ray; 3.03 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=11-191. DR PDB; 3ZLM; X-ray; 2.00 A; A=11-191. DR PDB; 5CGL; X-ray; 2.35 A; A/B=11-191. DR PDB; 5CKL; X-ray; 0.99 A; A=11-191. DR PDB; 5CMT; X-ray; 0.99 A; A=11-191. DR PDBsum; 2G03; -. DR PDBsum; 3S6A; -. DR PDBsum; 3SE5; -. DR PDBsum; 3SN9; -. DR PDBsum; 3ZLM; -. DR PDBsum; 5CGL; -. DR PDBsum; 5CKL; -. DR PDBsum; 5CMT; -. DR ProteinModelPortal; Q7DDR9; -. DR SMR; Q7DDR9; 11-187. DR DIP; DIP-60138N; -. DR STRING; 122586.NMB0255; -. DR PaxDb; Q7DDR9; -. DR EnsemblBacteria; AAF40709; AAF40709; NMB0255. DR GeneID; 902366; -. DR KEGG; nme:NMB0255; -. DR PATRIC; 20355588; VBINeiMen85645_0318. DR eggNOG; ENOG4105MZU; Bacteria. DR eggNOG; COG2184; LUCA. DR HOGENOM; HOG000093879; -. DR KO; K04095; -. DR OMA; REQNISK; -. DR OrthoDB; EOG69976Q; -. DR BioCyc; NMEN122586:GHGG-270-MONOMER; -. DR EvolutionaryTrace; Q7DDR9; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; KW Transferase. FT CHAIN 1 191 Adenosine monophosphate-protein FT transferase NmFic. FT /FTId=PRO_0000417551. FT DOMAIN 37 162 Fido. {ECO:0000255|PROSITE- FT ProRule:PRU00791}. FT NP_BIND 104 107 ATP. {ECO:0000269|PubMed:22266942}. FT NP_BIND 112 118 ATP. {ECO:0000269|PubMed:22266942}. FT NP_BIND 140 143 ATP. {ECO:0000269|PubMed:22266942}. FT MOTIF 182 187 Inhibitory (S/T)XXXE(G/N) motif. FT BINDING 67 67 ATP. {ECO:0000269|PubMed:22266942}. FT BINDING 186 186 ATP. {ECO:0000269|PubMed:22266942}. FT MOD_RES 183 183 O-AMP-tyrosine; in vitro. FT {ECO:0000269|PubMed:22266942}. FT MUTAGEN 182 182 S->A: Promotes adenylyltransferase FT activity; when associated with A-186. FT {ECO:0000269|PubMed:22266942}. FT MUTAGEN 186 186 E->A: Promotes adenylyltransferase FT activity; when associated with A-182. FT {ECO:0000269|PubMed:22266942, FT ECO:0000269|PubMed:23738009}. FT MUTAGEN 186 186 E->G: Promotes adenylyltransferase FT activity. {ECO:0000269|PubMed:22266942, FT ECO:0000269|PubMed:23738009}. FT HELIX 14 27 {ECO:0000244|PDB:5CKL}. FT HELIX 30 33 {ECO:0000244|PDB:5CKL}. FT STRAND 36 38 {ECO:0000244|PDB:5CKL}. FT HELIX 39 50 {ECO:0000244|PDB:5CKL}. FT TURN 51 53 {ECO:0000244|PDB:5CKL}. FT TURN 55 58 {ECO:0000244|PDB:5CKL}. FT HELIX 75 86 {ECO:0000244|PDB:5CKL}. FT HELIX 93 106 {ECO:0000244|PDB:5CKL}. FT STRAND 109 111 {ECO:0000244|PDB:5CKL}. FT HELIX 113 129 {ECO:0000244|PDB:5CKL}. FT HELIX 135 137 {ECO:0000244|PDB:5CKL}. FT HELIX 140 149 {ECO:0000244|PDB:5CKL}. FT TURN 150 152 {ECO:0000244|PDB:5CKL}. FT HELIX 155 162 {ECO:0000244|PDB:5CKL}. FT STRAND 165 167 {ECO:0000244|PDB:5CKL}. FT HELIX 172 185 {ECO:0000244|PDB:5CKL}. SQ SEQUENCE 191 AA; 22190 MW; DAE3849D07424543 CRC64; MPSENPIGKT MKSIDEQSLH NARRLFESGD IDRIEVGTTA GLQQIHRYLF GGLYDFAGQI REDNISKGGF RFANAMYLKE ALVKIEQMPE RTFEEIIAKY VEMNIAHPFL EGNGRSTRIW LDLVLKKNLK KVVNWQNVSK TLYLQAMERS PVNDLELRFL LKDNLTDDVD NREIIFKGIE QSYYYEGYEK G // ID NORM_NEIMB Reviewed; 459 AA. AC Q9K015; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Probable multidrug resistance protein NorM; DE AltName: Full=Multidrug-efflux transporter; GN Name=norM; OrderedLocusNames=NMB0812; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Multidrug efflux pump. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) CC (TC 2.A.66.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41225.1; -; Genomic_DNA. DR PIR; C81156; C81156. DR RefSeq; NP_273854.1; NC_003112.2. DR RefSeq; WP_010980851.1; NC_003112.2. DR STRING; 122586.NMB0812; -. DR PaxDb; Q9K015; -. DR EnsemblBacteria; AAF41225; AAF41225; NMB0812. DR GeneID; 902927; -. DR KEGG; nme:NMB0812; -. DR PATRIC; 20357011; VBINeiMen85645_1024. DR eggNOG; ENOG4107QI1; Bacteria. DR eggNOG; COG0534; LUCA. DR HOGENOM; HOG000038538; -. DR KO; K03327; -. DR OMA; SIVFMLP; -. DR OrthoDB; EOG6423C5; -. DR BioCyc; NMEN122586:GHGG-843-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015238; F:drug transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 3: Inferred from homology; KW Antiport; Cell inner membrane; Cell membrane; Complete proteome; KW Ion transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 459 Probable multidrug resistance protein FT NorM. FT /FTId=PRO_0000164226. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. FT TRANSMEM 395 415 Helical. {ECO:0000255}. FT TRANSMEM 423 443 Helical. {ECO:0000255}. SQ SEQUENCE 459 AA; 50036 MW; F6DC2D21BBC10963 CRC64; MLLDLNRFSF PVFLKEVRLL TTLALPMLLA QVAQVGIGFV DTVMAGGAGK EDLAAVALGS SAFATVYITF MGIMAALNPM IAQLYGAGKT DEVGETGRQG IWFGLFLGVF GMVLMWAAIT PFRNWLTLSD YVEGTMAQYM LFTSLAMPAA MVHRALHAYT SSLNRPRLIM LVSFAAFVLN VPLNYIFVYG KFGMPALGGA GCGLATMAVF WFSALALWIY IAKENFFRPF GLTAKFGKPD WAVFKQIWKI GAPIGLSYFL EASAFSFIVF LIAPFGEDYV AAQQVGISLS GILYMIPQSV GSAGTVRIGF SLGRREFSRA RYISGVSLVL GWMLAVITVL SLVLFRSPLV SMYNNDPAVL SIAATVLLFA GLFQPADFTQ CIASYALRGY KVTKVPMFIH AAAFWGCGLL PGYLLAYRFN MGIYGFWTAL IASLTIAAIA LVWCLELCSR EMVRSHKAV // ID NQRD_NEIMB Reviewed; 208 AA. AC Q9K0M6; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE Short=Na(+)-NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE Short=Na(+)-translocating NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00428}; DE AltName: Full=NQR complex subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE AltName: Full=NQR-1 subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; GN Name=nqrD {ECO:0000255|HAMAP-Rule:MF_00428}; GN OrderedLocusNames=NMB0566; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00428}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00428}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00428}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40994.1; -; Genomic_DNA. DR PIR; A81185; A81185. DR RefSeq; NP_273610.1; NC_003112.2. DR RefSeq; WP_002221365.1; NC_003112.2. DR STRING; 122586.NMB0566; -. DR PaxDb; Q9K0M6; -. DR EnsemblBacteria; AAF40994; AAF40994; NMB0566. DR GeneID; 902681; -. DR KEGG; nme:NMB0566; -. DR PATRIC; 20356411; VBINeiMen85645_0725. DR eggNOG; ENOG4105F5D; Bacteria. DR eggNOG; COG1347; LUCA. DR HOGENOM; HOG000279325; -. DR KO; K00349; -. DR OMA; PSKIRII; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; NMEN122586:GHGG-592-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00428; NqrD; 1. DR InterPro; IPR011292; NqrD. DR InterPro; IPR003667; Rnf-Nqr. DR PANTHER; PTHR30586:SF1; PTHR30586:SF1; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01939; nqrD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 208 Na(+)-translocating NADH-quinone FT reductase subunit D. FT /FTId=PRO_0000214236. FT TRANSMEM 42 62 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 72 92 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 103 123 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 131 151 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 178 198 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. SQ SEQUENCE 208 AA; 22682 MW; 009FA36C9030C11C CRC64; MADMKRLKHL MFSPFIDNNP IALQVLGICS ALAVTTKLQT AIVMGISVAL VTGFSSFFIS LVRNYIPNSI RIIVQMAIIA SLVTLVDQLL QAFAYELSKQ LSVFVGLIIT NCIVMGRAEA FAMKEPPLES LIDGIGNGAG YGIMLLVVAT VRELIGSGKL LGYTVFQTVQ DGGWYQTNGL FLLAPSAFFI IGFLIWGLRT WKPEQAEE // ID NQRB_NEIMB Reviewed; 410 AA. AC Q9K0M4; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE Short=Na(+)-NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE Short=Na(+)-translocating NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR complex subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR-1 subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; GN Name=nqrB {ECO:0000255|HAMAP-Rule:MF_00426}; GN OrderedLocusNames=NMB0568; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00426}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00426}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP- CC Rule:MF_00426}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40996.1; -; Genomic_DNA. DR PIR; C81185; C81185. DR RefSeq; NP_273612.1; NC_003112.2. DR RefSeq; WP_002225562.1; NC_003112.2. DR STRING; 122586.NMB0568; -. DR PaxDb; Q9K0M4; -. DR EnsemblBacteria; AAF40996; AAF40996; NMB0568. DR GeneID; 902683; -. DR KEGG; nme:NMB0568; -. DR PATRIC; 20356415; VBINeiMen85645_0727. DR eggNOG; ENOG4108J5C; Bacteria. DR eggNOG; COG1805; LUCA. DR HOGENOM; HOG000273666; -. DR KO; K00347; -. DR OMA; TVFYTPG; -. DR OrthoDB; EOG65BDMX; -. DR BioCyc; NMEN122586:GHGG-594-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00426; NqrB; 1. DR InterPro; IPR004338; NADH_Q_Rdtase_NQR2_RnfD. DR InterPro; IPR010966; NqrB. DR PANTHER; PTHR30578:SF1; PTHR30578:SF1; 1. DR Pfam; PF03116; NQR2_RnfD_RnfE; 1. DR PIRSF; PIRSF016055; NADH-UbQ_OxRdtase_B_su; 1. DR TIGRFAMs; TIGR01937; nqrB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein; KW FMN; Ion transport; Membrane; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 410 Na(+)-translocating NADH-quinone FT reductase subunit B. FT /FTId=PRO_0000074439. FT TRANSMEM 56 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 119 139 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 266 286 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 293 313 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 318 338 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 347 367 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 377 397 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT MOD_RES 232 232 FMN phosphoryl threonine. FT {ECO:0000255|HAMAP-Rule:MF_00426}. SQ SEQUENCE 410 AA; 44601 MW; F632E12206170B4F CRC64; MGLKHFLEKI EPHFLPGGKH EKWYALYEAA ATIFYTSGAV TRKAAHVRDA LDSKRMMILV WLALFPAMFY GMYNVGAQAF GALTPDLLQQ NIANDWHYAF ANALGINMSS EAGVSDKMLF GAIYFLPIYA TVFVVGGFWE VLFATVRKHE INEGFFVTSI LFALIVPPTL PLWQAALGIS FGVVVAKEVF GGTGKNFMNP ALAGRAFLFF AYPANLSGDA VWTAVDGYSG ATALAQWAAH GADGLKNAVT GQTITWMDAF IGKLPGSIGE VSTLALLIGG AFIVFARIAS WRIIAGVMIG MIAMSSLFNF IGSDTNAMFA MPWYWHLVVG GFAIGMLFMA TDPVSASFTN VGKWWYGALI GVMCVLIRVV NPAYPEGMML AILFANLFAP IFDYFVAQAN IKRRKARSNG // ID NQRC_NEIMB Reviewed; 258 AA. AC Q9K0M5; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE Short=Na(+)-NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE Short=Na(+)-translocating NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR complex subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR-1 subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; GN Name=nqrC {ECO:0000255|HAMAP-Rule:MF_00427}; GN OrderedLocusNames=NMB0567; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00427}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00427}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00427}. CC -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP- CC Rule:MF_00427}. CC -!- CAUTION: The residue potentially involved in the covalent binding CC of FMN is a Ser instead of a Thr. {ECO:0000255|HAMAP- CC Rule:MF_00427, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40995.1; -; Genomic_DNA. DR PIR; B81185; B81185. DR RefSeq; NP_273611.1; NC_003112.2. DR RefSeq; WP_002225563.1; NC_003112.2. DR STRING; 122586.NMB0567; -. DR PaxDb; Q9K0M5; -. DR EnsemblBacteria; AAF40995; AAF40995; NMB0567. DR GeneID; 902682; -. DR KEGG; nme:NMB0567; -. DR PATRIC; 20356413; VBINeiMen85645_0726. DR eggNOG; ENOG4106I92; Bacteria. DR eggNOG; COG2869; LUCA. DR HOGENOM; HOG000273678; -. DR KO; K00348; -. DR OMA; IKGITYY; -. DR OrthoDB; EOG6F2981; -. DR BioCyc; NMEN122586:GHGG-593-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00427; NqrC; 1. DR InterPro; IPR007329; FMN-bd. DR InterPro; IPR010204; NqrC. DR Pfam; PF04205; FMN_bind; 1. DR PIRSF; PIRSF009437; NQR-1_subunit_C; 1. DR SMART; SM00900; FMN_bind; 1. DR TIGRFAMs; TIGR01938; nqrC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein; KW FMN; Ion transport; Membrane; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 258 Na(+)-translocating NADH-quinone FT reductase subunit C. FT /FTId=PRO_0000214218. FT TRANSMEM 14 34 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00427}. FT MOD_RES 226 226 FMN phosphoryl serine. FT {ECO:0000255|HAMAP-Rule:MF_00427}. SQ SEQUENCE 258 AA; 27607 MW; 1F20D8EF011F7C3E CRC64; MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY ILSVAGLMDK DTDIGKTFAE RIEQRVVDLA TGEYVADAPK DFSARIAGKD PAQSIRIKTE DDLAGIKSRA KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV MYGFVAIQPD GNTINGITYY EQGETPGLGG EIGNPLWQQK FVGKKLFDGQ GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF GENGYIPYLN KLKSAGAQ // ID NQRE_NEIMB Reviewed; 197 AA. AC Q9K0M7; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE Short=Na(+)-NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE Short=Na(+)-translocating NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00429}; DE AltName: Full=NQR complex subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE AltName: Full=NQR-1 subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; GN Name=nqrE {ECO:0000255|HAMAP-Rule:MF_00429}; GN OrderedLocusNames=NMB0565; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00429}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00429}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00429}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40993.1; -; Genomic_DNA. DR PIR; H81184; H81184. DR RefSeq; NP_273609.1; NC_003112.2. DR RefSeq; WP_002225564.1; NC_003112.2. DR STRING; 122586.NMB0565; -. DR PaxDb; Q9K0M7; -. DR EnsemblBacteria; AAF40993; AAF40993; NMB0565. DR GeneID; 902680; -. DR KEGG; nme:NMB0565; -. DR PATRIC; 20356409; VBINeiMen85645_0724. DR eggNOG; ENOG4108IUB; Bacteria. DR eggNOG; COG2209; LUCA. DR HOGENOM; HOG000279324; -. DR KO; K00350; -. DR OMA; YFLGMCS; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; NMEN122586:GHGG-591-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00429; NqrE; 1. DR InterPro; IPR010967; NqrE. DR InterPro; IPR003667; Rnf-Nqr. DR PANTHER; PTHR30335:SF1; PTHR30335:SF1; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01940; nqrE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 197 Na(+)-translocating NADH-quinone FT reductase subunit E. FT /FTId=PRO_0000214254. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 35 55 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 76 96 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 108 128 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 139 159 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 175 195 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. SQ SEQUENCE 197 AA; 21179 MW; 768E43B7F8E32326 CRC64; MEHYLSLFIK SVFIENMALS FFLGMCTFLA VSKKVSTAFG LGVAVIFVLG LSVPVNQLVY SLLKDGAIAE GVDLTFLKFI TFIGVIAALV QILEMFLDKF VPALYNALGI YLPLITVNCA IFGAVSFMAQ REYNFGESVV YGFGAGLGWM LAIVALAGIT EKMKYSDAPK GLKGLGITFI AAGLMAMAFM SFSGIQL // ID NQRA_NEIMB Reviewed; 447 AA. AC Q9K0M3; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE Short=Na(+)-NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE Short=Na(+)-translocating NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00425}; DE AltName: Full=NQR complex subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE AltName: Full=NQR-1 subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; GN Name=nqrA {ECO:0000255|HAMAP-Rule:MF_00425}; GN OrderedLocusNames=NMB0569; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000255|HAMAP- CC Rule:MF_00425}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40997.1; -; Genomic_DNA. DR PIR; D81185; D81185. DR RefSeq; NP_273613.1; NC_003112.2. DR RefSeq; WP_002225561.1; NC_003112.2. DR STRING; 122586.NMB0569; -. DR PaxDb; Q9K0M3; -. DR EnsemblBacteria; AAF40997; AAF40997; NMB0569. DR GeneID; 902684; -. DR KEGG; nme:NMB0569; -. DR PATRIC; 20356417; VBINeiMen85645_0728. DR eggNOG; ENOG4105DWQ; Bacteria. DR eggNOG; COG1726; LUCA. DR HOGENOM; HOG000273652; -. DR KO; K00346; -. DR OMA; DYHGMKP; -. DR OrthoDB; EOG6VMTG5; -. DR BioCyc; NMEN122586:GHGG-595-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00425; NqrA; 1. DR InterPro; IPR008703; NqrA. DR InterPro; IPR022615; NqrA_C_domain. DR Pfam; PF05896; NQRA; 1. DR Pfam; PF11973; NQRA_SLBB; 1. DR TIGRFAMs; TIGR01936; nqrA; 1. PE 3: Inferred from homology; KW Complete proteome; Ion transport; NAD; Oxidoreductase; KW Reference proteome; Sodium; Sodium transport; Transport; Ubiquinone. FT CHAIN 1 447 Na(+)-translocating NADH-quinone FT reductase subunit A. FT /FTId=PRO_0000214200. SQ SEQUENCE 447 AA; 48636 MW; BE174A78439BE477 CRC64; MIKIKKGLNL PIAGRPEQAV YDGPAITEVA LLGEEYAGMR PSMKVKEGDA VKKGQVLFED KKNPGVVFTA PASGKIAAIH RGEKRVLQSV VIAVEGNDEI EFERYAPEAL ANLSGEEVRR NLIQSGLWTA LRTRPFSKIP AVDAEPFAIF VNAMDTNPLA ADPTVIIKEA AEDFKRGLLV LSRLTERKIH VCKAAGADVP SENAANIETH EFGGPHPAGL SGTHIHFIEP VGANKTVWTI NYQDVITIGR LFATGRLNTE RVIALGGSQV NKPRLLRTVL GAKVSQITAG ELVDTDNRVI SGSVLNGAIT QGAHDYLGRY HNQISVIEEG RSKELFGWVA PQPDKYSITR TTLGHFLKNK LFKFNTAVNG GDRAMVPIGT YERVMPLDIL PTLLLRDLIV GDTDSAQALG CLELDEEDLA LCSFVCPGKY EYGPLLRKVL ETIEKEG // ID NNRD_NEIMB Reviewed; 296 AA. AC Q9JRZ9; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_01965}; DE EC=4.2.1.136 {ECO:0000255|HAMAP-Rule:MF_01965}; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase {ECO:0000255|HAMAP-Rule:MF_01965}; GN Name=nnrD1 {ECO:0000255|HAMAP-Rule:MF_01965}; GN OrderedLocusNames=NMB1159; GN and GN Name=nnrD2 {ECO:0000255|HAMAP-Rule:MF_01965}; GN OrderedLocusNames=NMB1197; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at CC the expense of ADP, which is converted to AMP. Together with CC NAD(P)HX epimerase, which catalyzes the epimerization of the S- CC and R-forms, the enzyme allows the repair of both epimers of CC NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic CC or heat-dependent hydration. {ECO:0000255|HAMAP-Rule:MF_01965}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + CC NADH. {ECO:0000255|HAMAP-Rule:MF_01965}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + CC phosphate + NADPH. {ECO:0000255|HAMAP-Rule:MF_01965}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01965}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01965}. CC -!- SIMILARITY: Belongs to the NnrD/CARKD family. {ECO:0000255|HAMAP- CC Rule:MF_01965}. CC -!- SIMILARITY: Contains 1 YjeF C-terminal domain. {ECO:0000255|HAMAP- CC Rule:MF_01965}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41545.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41580.1; -; Genomic_DNA. DR PIR; G81111; G81111. DR RefSeq; NP_274187.1; NC_003112.2. DR RefSeq; NP_274223.1; NC_003112.2. DR RefSeq; WP_002225209.1; NC_003112.2. DR ProteinModelPortal; Q9JRZ9; -. DR STRING; 122586.NMB1197; -. DR PaxDb; Q9JRZ9; -. DR EnsemblBacteria; AAF41545; AAF41545; NMB1159. DR EnsemblBacteria; AAF41580; AAF41580; NMB1197. DR GeneID; 903580; -. DR GeneID; 903617; -. DR KEGG; nme:NMB1159; -. DR KEGG; nme:NMB1197; -. DR PATRIC; 20357897; VBINeiMen85645_1464. DR eggNOG; ENOG4105DR1; Bacteria. DR eggNOG; COG0063; LUCA. DR HOGENOM; HOG000024581; -. DR OMA; FTPHQME; -. DR OrthoDB; EOG6C018D; -. DR BioCyc; NMEN122586:GHGG-1195-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1232-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_01965; NADHX_dehydratase; 1. DR InterPro; IPR000631; CARKD. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF01256; Carb_kinase; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00196; yjeF_cterm; 1. DR PROSITE; PS51383; YJEF_C_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Lyase; NAD; NADP; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 296 ADP-dependent (S)-NAD(P)H-hydrate FT dehydratase. FT /FTId=PRO_0000416147. FT DOMAIN 18 292 YjeF C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01965}. FT NP_BIND 202 206 ADP. {ECO:0000255|HAMAP-Rule:MF_01965}. FT NP_BIND 222 231 ADP. {ECO:0000255|HAMAP-Rule:MF_01965}. FT REGION 165 171 NAD(P)HX. {ECO:0000255|HAMAP- FT Rule:MF_01965}. FT BINDING 111 111 NAD(P)HX; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01965}. FT BINDING 232 232 NAD(P)HX. {ECO:0000255|HAMAP- FT Rule:MF_01965}. SQ SEQUENCE 296 AA; 30347 MW; 8A1AEE023D12DA3B CRC64; MFPVFHLSGE SRRQMLQTAL RFPHVFKARA EDSHKGTFGT LAVVGGSAGM SGAPVLAASA AMYLGCGKVW AGFNQDTLPF AVIAGFPEIM LDTADSLAKR QDINAWVVGC GLGTGRAAVG TLAGILTEHT DKPVVLDADA LNILSTDAET RNLARGCKNL ILTPHPAEAA RLLGTTVAQV QADRTAAVRK IGAIFGATVV LKGHKTLVAS PDTEIYVNES GNAGLATAGS GDVLGGIIGS LLAQGVPVFE AACAGAWLHG AAADVIKESA GIAAGLLAGE IAPAARWLRN RITKSM // ID NTPA_NEIMB Reviewed; 199 AA. AC Q9K0G6; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.19 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=NMB0639; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41062.1; -; Genomic_DNA. DR PIR; D81175; D81175. DR RefSeq; NP_273682.1; NC_003112.2. DR RefSeq; WP_002222823.1; NC_003112.2. DR ProteinModelPortal; Q9K0G6; -. DR STRING; 122586.NMB0639; -. DR PaxDb; Q9K0G6; -. DR EnsemblBacteria; AAF41062; AAF41062; NMB0639. DR GeneID; 902750; -. DR KEGG; nme:NMB0639; -. DR PATRIC; 20356577; VBINeiMen85645_0808. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NMEN122586:GHGG-665-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 199 Non-canonical purine NTP pyrophosphatase. FT /FTId=PRO_0000178200. FT REGION 12 17 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 73 74 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 73 73 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT BINDING 160 160 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 180 180 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 186 186 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. SQ SEQUENCE 199 AA; 21508 MW; ECE3BCD8338170D4 CRC64; MSEKPEKIVL ASGNAGKLEE FGNLFKPYSI TVLPQSAFGI PECPEPYPTF VENALAKARH AAKYSGLPAL ADDSGICAAA LNGAPGIHSA RYAGDNPKSD TANNLKLAAE LVGKADKSCC YVCVLVFVRH KDDPRPIIAE GVWHGQWNDT PLGQNGFGYD PYFYLPEHGK TAAELDTEVK NRESHRAQAL AELLRKLAL // ID NUOH_NEIMB Reviewed; 358 AA. AC Q9K1B4; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01350}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01350}; DE AltName: Full=NADH dehydrogenase I subunit H {ECO:0000255|HAMAP-Rule:MF_01350}; DE AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01350}; GN Name=nuoH {ECO:0000255|HAMAP-Rule:MF_01350}; GN OrderedLocusNames=NMB0250; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. This subunit may CC bind ubiquinone. {ECO:0000255|HAMAP-Rule:MF_01350}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01350}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01350}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01350}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01350}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40704.1; -; Genomic_DNA. DR PIR; E81219; E81219. DR RefSeq; NP_273306.1; NC_003112.2. DR RefSeq; WP_002221910.1; NC_003112.2. DR STRING; 122586.NMB0250; -. DR PaxDb; Q9K1B4; -. DR EnsemblBacteria; AAF40704; AAF40704; NMB0250. DR GeneID; 902361; -. DR KEGG; nme:NMB0250; -. DR PATRIC; 20355578; VBINeiMen85645_0313. DR eggNOG; ENOG4105CMZ; Bacteria. DR eggNOG; COG1005; LUCA. DR HOGENOM; HOG000228276; -. DR KO; K00337; -. DR OMA; LDLGWKF; -. DR OrthoDB; EOG6B62B4; -. DR BioCyc; NMEN122586:GHGG-265-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Reference proteome; Transmembrane; KW Transmembrane helix; Ubiquinone. FT CHAIN 1 358 NADH-quinone oxidoreductase subunit H. FT /FTId=PRO_0000240088. FT TRANSMEM 20 40 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 95 115 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 168 188 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 206 226 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 253 273 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 295 315 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. FT TRANSMEM 334 354 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01350}. SQ SEQUENCE 358 AA; 39851 MW; 26C6B7881C64EF66 CRC64; MQEWFQNLFA ATLGLGDLGI TVGLVVSVIV KIVIILIPLI LTVAYLTYFE RKVIGFMQLR VGPNVTGPWG LIQPFADVFK LLFKEVTRPK LSNKALFYIG PIMSLAPSFA AWAVIPFNEE WVLTNINIGL LYILMITSLS VYGVIIAGWA SNSKYSFLGA MRASAQSISY EIAMSAALVC VVMVSGSMNF SDIVAAQAKG IAGGSVFSWN WLPLFPIFIV YLISAVAETN RAPFDVAEGE SEIVAGHHVE YSGFAFALFF LAEYIFMILI AALTSLMFLG GWLSPFPQSW GIVGTPSAFW MFAKMAAVLY WYLWIRATFP RYRYDQIMRL GWKVLIPIGF AYIVILGVWM ISPLNLWK // ID NQRF_NEIMB Reviewed; 405 AA. AC Q9K0M8; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE Short=Na(+)-NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE Short=Na(+)-translocating NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00430}; DE AltName: Full=NQR complex subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE AltName: Full=NQR-1 subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; GN Name=nqrF {ECO:0000255|HAMAP-Rule:MF_00430}; GN OrderedLocusNames=NMB0564; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. The first step CC is catalyzed by NqrF, which accepts electrons from NADH and CC reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer CC pathway. {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00430}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00430}. CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP- CC Rule:MF_00430}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00430}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40992.1; -; Genomic_DNA. DR PIR; G81184; G81184. DR RefSeq; NP_273608.1; NC_003112.2. DR RefSeq; WP_002225565.1; NC_003112.2. DR ProteinModelPortal; Q9K0M8; -. DR SMR; Q9K0M8; 126-404. DR STRING; 122586.NMB0564; -. DR PaxDb; Q9K0M8; -. DR EnsemblBacteria; AAF40992; AAF40992; NMB0564. DR GeneID; 902679; -. DR KEGG; nme:NMB0564; -. DR PATRIC; 20356407; VBINeiMen85645_0723. DR eggNOG; ENOG4105D26; Bacteria. DR eggNOG; COG2871; LUCA. DR HOGENOM; HOG000263661; -. DR KO; K00351; -. DR OMA; EEHGIIM; -. DR OrthoDB; EOG6JHRM2; -. DR BioCyc; NMEN122586:GHGG-590-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.30; -; 1. DR HAMAP; MF_00430; NqrF; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR010205; NqrF. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000044; Cis_Diol_DH_RD; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR TIGRFAMs; TIGR01941; nqrF; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 3: Inferred from homology; KW 2Fe-2S; Cell inner membrane; Cell membrane; Complete proteome; FAD; KW Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 405 Na(+)-translocating NADH-quinone FT reductase subunit F. FT /FTId=PRO_0000074498. FT TRANSMEM 3 23 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT DOMAIN 32 124 2Fe-2S ferredoxin-type. FT {ECO:0000255|HAMAP-Rule:MF_00430}. FT DOMAIN 127 267 FAD-binding FR-type. {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT REGION 270 387 Catalytic. FT METAL 67 67 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 73 73 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 76 76 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 108 108 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. SQ SEQUENCE 405 AA; 45164 MW; 0F93BD48FFC2AFCC CRC64; MEIILGIVMF TVIVLVLALM ILFAKSKLVS EGDITIKVNG EKELTMPAGG KLLGALANEG IFIPSACGGG GSCGQCRVVV KSGGGDILPT ELSHISKREA REGCRLSCQV NVKTDMDIEV PEEVFGVKKW ECTVISNDNK ATFIKELKLA IPEGEEVPFR AGGYIQIEAP PHTVAYKDFD IPKEYHEDWD KYNLWQYVSK VDEPILRAYS MASYPEEKGI IMLNVRIATP PPRVPDAPPG QMSSYIWSLK PGDKVTISGP FGEFFAKDTD AEMVFIGGGA GMAPMRSHIF DQLKRLNSKR KITFWYGARS KREMFYVEDF DQLAAEFPNF TWHVALSDPL PEDNWDGYTG FIHNVVYENH LKNHEAPEDC EFYMCGPPIM NQSVIKMLKD LGVEDENILL DDFGG // ID NRDR_NEIMB Reviewed; 154 AA. AC Q9JXZ9; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN OrderedLocusNames=NMB1816; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Negatively regulates transcription of bacterial CC ribonucleotide reductase nrd genes and operons by binding to NrdR- CC boxes. {ECO:0000255|HAMAP-Rule:MF_00440}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00440}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00440}; CC -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42151.1; -; Genomic_DNA. DR PIR; A81039; A81039. DR RefSeq; NP_274813.1; NC_003112.2. DR RefSeq; WP_002217912.1; NC_003112.2. DR STRING; 122586.NMB1816; -. DR PaxDb; Q9JXZ9; -. DR EnsemblBacteria; AAF42151; AAF42151; NMB1816. DR GeneID; 903284; -. DR KEGG; nme:NMB1816; -. DR PATRIC; 20359617; VBINeiMen85645_2314. DR eggNOG; COG1327; LUCA. DR HOGENOM; HOG000097653; -. DR KO; K07738; -. DR OMA; RFTTYET; -. DR OrthoDB; EOG6XM7J6; -. DR BioCyc; NMEN122586:GHGG-1871-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00440; NrdR; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR003796; RNR_NrdR-like. DR Pfam; PF03477; ATP-cone; 1. DR TIGRFAMs; TIGR00244; TIGR00244; 1. DR PROSITE; PS51161; ATP_CONE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Metal-binding; KW Nucleotide-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 154 Transcriptional repressor NrdR. FT /FTId=PRO_0000182323. FT DOMAIN 49 139 ATP-cone. {ECO:0000255|HAMAP- FT Rule:MF_00440}. FT ZN_FING 3 34 {ECO:0000255|HAMAP-Rule:MF_00440}. SQ SEQUENCE 154 AA; 17285 MW; E6445ECC0EC05885 CRC64; MKCPFCAHPD TRVADSRLME ERNAVRRRRH CPNCGKRFGT LETAELKMPA VIGPDKKRSP FNAQRLRNDL TAAARKSALT PEQIDETVRL TEHRLYTSGQ RDIPSAALAD MVLKELLRQD TEAAVRFAAL HKRFDNPADF ASWLAQAVKT GGKA // ID NUOB_NEIMB Reviewed; 160 AA. AC Q9K1C2; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01356}; DE AltName: Full=NADH dehydrogenase I subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; DE AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356}; GN Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356}; GN OrderedLocusNames=NMB0242; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. CC Couples the redox reaction to proton translocation (for every two CC electrons transferred, four hydrogen ions are translocated across CC the cytoplasmic membrane), and thus conserves the redox energy in CC a proton gradient (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01356}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01356}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01356}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01356}. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01356}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40696.1; -; Genomic_DNA. DR PIR; H81221; H81221. DR RefSeq; NP_273298.1; NC_003112.2. DR RefSeq; WP_002215610.1; NC_003112.2. DR ProteinModelPortal; Q9K1C2; -. DR STRING; 122586.NMB0242; -. DR PaxDb; Q9K1C2; -. DR EnsemblBacteria; AAF40696; AAF40696; NMB0242. DR GeneID; 25048122; -. DR GeneID; 902353; -. DR KEGG; nme:NMB0242; -. DR PATRIC; 20355560; VBINeiMen85645_0304. DR eggNOG; ENOG4105ES3; Bacteria. DR eggNOG; COG0377; LUCA. DR HOGENOM; HOG000228249; -. DR KO; K00331; -. DR OMA; PVMRRVY; -. DR OrthoDB; EOG62K20C; -. DR BioCyc; NMEN122586:GHGG-257-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.700; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron; KW Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; KW Reference proteome; Transport; Ubiquinone. FT CHAIN 1 160 NADH-quinone oxidoreductase subunit B. FT /FTId=PRO_0000358430. FT METAL 37 37 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01356}. FT METAL 38 38 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01356}. FT METAL 102 102 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01356}. FT METAL 132 132 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01356}. SQ SEQUENCE 160 AA; 17630 MW; F1616423A8D799AF CRC64; MGIEGVLKKG FITTSADTVL NYMRTGSLWP VTFGLACCAV EMMHAGMARY DLDRFGIIFR PSPRQADLMI VAGTLTNKMA PALRRVYDQL AEPRWVLSMG SCANGGGYYH YSYSVVRGAD RVVPVDVYVP GCPPTAEALI YGLIQLQQKI KRTSTIARDE // ID NUOC_NEIMB Reviewed; 197 AA. AC Q9K1C1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000255|HAMAP-Rule:MF_01357}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01357}; DE AltName: Full=NADH dehydrogenase I subunit C {ECO:0000255|HAMAP-Rule:MF_01357}; DE AltName: Full=NDH-1 subunit C {ECO:0000255|HAMAP-Rule:MF_01357}; GN Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01357}; GN OrderedLocusNames=NMB0243; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000255|HAMAP-Rule:MF_01357}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01357}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01357}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01357}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01357}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01357}. CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40697.1; -; Genomic_DNA. DR PIR; A81222; A81222. DR RefSeq; NP_273299.1; NC_003112.2. DR RefSeq; WP_002224826.1; NC_003112.2. DR ProteinModelPortal; Q9K1C1; -. DR STRING; 122586.NMB0243; -. DR PaxDb; Q9K1C1; -. DR EnsemblBacteria; AAF40697; AAF40697; NMB0243. DR GeneID; 902354; -. DR KEGG; nme:NMB0243; -. DR PATRIC; 20355562; VBINeiMen85645_0305. DR eggNOG; ENOG4105CYU; Bacteria. DR eggNOG; COG0852; LUCA. DR HOGENOM; HOG000009799; -. DR KO; K00332; -. DR OMA; THNWRLR; -. DR OrthoDB; EOG60PHFK; -. DR BioCyc; NMEN122586:GHGG-258-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS. DR Pfam; PF00329; Complex1_30kDa; 1. DR ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 1. DR TIGRFAMs; TIGR01961; NuoC_fam; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Reference proteome; Transport; Ubiquinone. FT CHAIN 1 197 NADH-quinone oxidoreductase subunit C. FT /FTId=PRO_0000118673. SQ SEQUENCE 197 AA; 23007 MW; 983591220B39E2DC CRC64; MASIQDLYET VSRVLGNQAG KVISALGEIT VECLPEHYIS VMTALRDHEE LHFELLVDLC GVDYSTYKNE AWQGKRFAVV SQLLSVKNNQ RIRVRVWVSD DDFPVVESVV DIYNSADWYE REAFDMYGIM FNNHPDLRRI LTDYGFVGHP FRKDFPISGY VEMRYDEEQK RVIYQPVTIE PREITPRIVR EENYGGQ // ID NUOD_NEIMB Reviewed; 418 AA. AC Q9K1C0; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000255|HAMAP-Rule:MF_01358}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01358}; DE AltName: Full=NADH dehydrogenase I subunit D {ECO:0000255|HAMAP-Rule:MF_01358}; DE AltName: Full=NDH-1 subunit D {ECO:0000255|HAMAP-Rule:MF_01358}; GN Name=nuoD {ECO:0000255|HAMAP-Rule:MF_01358}; GN OrderedLocusNames=NMB0244; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000255|HAMAP-Rule:MF_01358}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01358}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01358}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01358}. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01358}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40698.1; -; Genomic_DNA. DR PIR; B81222; B81222. DR RefSeq; NP_273300.1; NC_003112.2. DR RefSeq; WP_002224828.1; NC_003112.2. DR ProteinModelPortal; Q9K1C0; -. DR STRING; 122586.NMB0244; -. DR PaxDb; Q9K1C0; -. DR EnsemblBacteria; AAF40698; AAF40698; NMB0244. DR GeneID; 902355; -. DR KEGG; nme:NMB0244; -. DR PATRIC; 20355564; VBINeiMen85645_0306. DR eggNOG; ENOG4105CQV; Bacteria. DR eggNOG; COG0649; LUCA. DR HOGENOM; HOG000228264; -. DR KO; K00333; -. DR OMA; IMGTSME; -. DR OrthoDB; EOG62G5MP; -. DR BioCyc; NMEN122586:GHGG-259-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.645.10; -; 2. DR HAMAP; MF_01358; NDH1_NuoD; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR022885; NDH1_su_D/H. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR TIGRFAMs; TIGR01962; NuoD; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Reference proteome; Transport; Ubiquinone. FT CHAIN 1 418 NADH-quinone oxidoreductase subunit D. FT /FTId=PRO_0000357868. SQ SEQUENCE 418 AA; 47710 MW; C207871651F5CA1D CRC64; MANKLRNYTI NFGPQHPAAH GVLRMILELD GEQIVRADPH IGLLHRGTEK LAETKTYLQA LPYMDRLDYV SMMVNEQAYC LAVEKLVGID VPIRAQYIRV MFAEVTRILN HLMGIGSHAF DIGAMTAILY AFRDREELMD LYEAVSGARM HAAYFRPGGV YRDLPDFMPK YEGSKFRNAK VLKQLNESRE GTMLDFIDAF CERFPKNIDT LETLLTDNRI WKQRTVGIGV VSPERAMQKG FTGVMLRGSG VEWDVRKTQP YEVYDKMDFD IPVGVNGDCY DRYLCRMEEM RQSVRIIKQC SEWLRVNPGP VITTNHKFAP PKRTEMKTGM EDLIHHFKLF TEGMHVPEGE TYTAVEHPKG EFGVYIISDG ANKPYRLKIR APGFAHLQGM DEMAKGHMLA DVVAIIGTQD IVFGEVDR // ID NUSG_NEIMB Reviewed; 178 AA. AC P65592; Q9JRD9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN OrderedLocusNames=NMB0126; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates in transcription elongation, termination CC and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}. CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC -!- SIMILARITY: Contains 1 KOW domain. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40585.1; -; Genomic_DNA. DR PIR; C81235; C81235. DR RefSeq; NP_273184.1; NC_003112.2. DR RefSeq; WP_002215369.1; NC_003112.2. DR ProteinModelPortal; P65592; -. DR SMR; P65592; 121-176. DR STRING; 122586.NMB0126; -. DR PaxDb; P65592; -. DR PRIDE; P65592; -. DR EnsemblBacteria; AAF40585; AAF40585; NMB0126. DR GeneID; 902234; -. DR KEGG; nme:NMB0126; -. DR PATRIC; 20355273; VBINeiMen85645_0166. DR eggNOG; ENOG4105E5V; Bacteria. DR eggNOG; COG0250; LUCA. DR HOGENOM; HOG000219265; -. DR KO; K02601; -. DR OMA; EDKIFRI; -. DR OrthoDB; EOG6FFS95; -. DR BioCyc; NMEN122586:GHGG-136-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-1692-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro. DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 3.30.70.940; -; 1. DR HAMAP; MF_00948; NusG; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR001062; Transcrpt_antiterm_NusG. DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF02357; NusG; 1. DR PRINTS; PR00338; NUSGTNSCPFCT. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF82679; SSF82679; 1. DR TIGRFAMs; TIGR00922; nusG; 1. DR PROSITE; PS01014; NUSG; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transcription; KW Transcription antitermination; Transcription regulation; KW Transcription termination. FT CHAIN 1 178 Transcription termination/antitermination FT protein NusG. FT /FTId=PRO_0000113938. FT DOMAIN 126 156 KOW. {ECO:0000255|HAMAP-Rule:MF_00948}. SQ SEQUENCE 178 AA; 20550 MW; 3171F0DC957EFCB3 CRC64; MSKKWYVVQA YSGFEKNVQR ILEERIAREE MGDYFGQILV PVEKVVDIRN GRKTISERKS YPGYVLVEME MTDDSWHLVK STPRVSGFIG GRANRPTPIS QREAEIILQQ VQTGIEKPKP KVEFEVGQQV RVNEGPFADF NGVVEEVNYE RNKLRVSVQI FGRETPVELE FSQVEKIN // ID NUOI_NEIMB Reviewed; 159 AA. AC Q7DDS1; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NDH-1 subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; GN Name=nuoI {ECO:0000255|HAMAP-Rule:MF_01351}; GN OrderedLocusNames=NMB0251; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01351}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01351}. CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40705.1; -; Genomic_DNA. DR RefSeq; NP_273307.1; NC_003112.2. DR RefSeq; WP_002216341.1; NC_003112.2. DR ProteinModelPortal; Q7DDS1; -. DR STRING; 122586.NMB0251; -. DR PaxDb; Q7DDS1; -. DR EnsemblBacteria; AAF40705; AAF40705; NMB0251. DR GeneID; 23783404; -. DR GeneID; 902362; -. DR KEGG; nme:NMB0251; -. DR PATRIC; 20355580; VBINeiMen85645_0314. DR eggNOG; ENOG4105P3U; Bacteria. DR eggNOG; COG1143; LUCA. DR HOGENOM; HOG000228289; -. DR KO; K00338; -. DR OMA; DLFKCIY; -. DR OrthoDB; EOG6XM7H5; -. DR BioCyc; NMEN122586:GHGG-266-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR HAMAP; MF_01351; NDH1_NuoI; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR Pfam; PF12838; Fer4_7; 1. DR TIGRFAMs; TIGR01971; NuoI; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron; KW Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone; KW Reference proteome; Repeat; Ubiquinone. FT CHAIN 1 159 NADH-quinone oxidoreductase subunit I. FT /FTId=PRO_0000250917. FT DOMAIN 50 80 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT DOMAIN 90 119 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 60 60 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 63 63 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 66 66 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 70 70 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 99 99 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 102 102 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 105 105 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. FT METAL 109 109 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_01351}. SQ SEQUENCE 159 AA; 18156 MW; FA5764DAD0009EE9 CRC64; MANLVKTFLL GELVKGMGVT LKNFFARKDT IYFPEEKTPQ SVRFRGLHAQ RRYPNGEERC IACKLCEAVC PAMAINIESE EREDGTRRTK RYDIDLTKCI FCGFCEEACP TDAIVETHIF EYHGEKKGDL HMTKPILLAI GDKYEAEIAK RKAADAPYR // ID NUOK_NEIMB Reviewed; 101 AA. AC Q7DDS0; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=NADH-quinone oxidoreductase subunit K {ECO:0000255|HAMAP-Rule:MF_01456}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_01456}; DE AltName: Full=NADH dehydrogenase I subunit K {ECO:0000255|HAMAP-Rule:MF_01456}; DE AltName: Full=NDH-1 subunit K {ECO:0000255|HAMAP-Rule:MF_01456}; GN Name=nuoK {ECO:0000255|HAMAP-Rule:MF_01456}; GN OrderedLocusNames=NMB0254; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000255|HAMAP-Rule:MF_01456}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|HAMAP-Rule:MF_01456}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000255|HAMAP-Rule:MF_01456}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01456}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01456}. CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. CC {ECO:0000255|HAMAP-Rule:MF_01456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40708.1; -; Genomic_DNA. DR PIR; A81220; A81220. DR RefSeq; NP_273310.1; NC_003112.2. DR RefSeq; WP_002215628.1; NC_003112.2. DR STRING; 122586.NMB0254; -. DR PaxDb; Q7DDS0; -. DR EnsemblBacteria; AAF40708; AAF40708; NMB0254. DR GeneID; 902365; -. DR KEGG; nme:NMB0254; -. DR PATRIC; 20355586; VBINeiMen85645_0317. DR eggNOG; ENOG4105M5H; Bacteria. DR eggNOG; COG0713; LUCA. DR HOGENOM; HOG000066429; -. DR KO; K00340; -. DR OMA; NFVAFSY; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; NMEN122586:GHGG-269-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01456; NDH1_NuoK; 1. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR PANTHER; PTHR11434; PTHR11434; 1. DR Pfam; PF00420; Oxidored_q2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Reference proteome; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 101 NADH-quinone oxidoreductase subunit K. FT /FTId=PRO_0000390142. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01456}. FT TRANSMEM 30 50 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01456}. FT TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01456}. SQ SEQUENCE 101 AA; 11078 MW; BFAF35A0CEDA4087 CRC64; MITLTHYLVL GALLFGISAM GIFMNRKNVL VLLMSIELML LAVNFNFIAF SQHLGDTAGQ IFVFFVLTVA AAESAIGLAI MVLVYRNRQT INVADLDELK G // ID NUOL_NEIMB Reviewed; 674 AA. AC Q9K1B0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=NADH-quinone oxidoreductase subunit L; DE EC=1.6.5.11; DE AltName: Full=NADH dehydrogenase I subunit L; DE AltName: Full=NDH-1 subunit L; GN Name=nuoL; OrderedLocusNames=NMB0257; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40711.1; -; Genomic_DNA. DR PIR; D81220; D81220. DR RefSeq; NP_273313.1; NC_003112.2. DR RefSeq; WP_002221913.1; NC_003112.2. DR STRING; 122586.NMB0257; -. DR PaxDb; Q9K1B0; -. DR EnsemblBacteria; AAF40711; AAF40711; NMB0257. DR GeneID; 902368; -. DR KEGG; nme:NMB0257; -. DR PATRIC; 20355592; VBINeiMen85645_0320. DR eggNOG; ENOG4105D65; Bacteria. DR eggNOG; COG1009; LUCA. DR HOGENOM; HOG000100570; -. DR KO; K00341; -. DR OMA; PESMEGP; -. DR OrthoDB; EOG6FZ48R; -. DR BioCyc; NMEN122586:GHGG-272-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01435; NPOXDRDTASE5. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; NAD; Oxidoreductase; KW Quinone; Reference proteome; Transmembrane; Transmembrane helix; KW Ubiquinone. FT CHAIN 1 674 NADH-quinone oxidoreductase subunit L. FT /FTId=PRO_0000118220. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. FT TRANSMEM 293 313 Helical. {ECO:0000255}. FT TRANSMEM 348 368 Helical. {ECO:0000255}. FT TRANSMEM 385 405 Helical. {ECO:0000255}. FT TRANSMEM 425 445 Helical. {ECO:0000255}. FT TRANSMEM 488 508 Helical. {ECO:0000255}. FT TRANSMEM 549 569 Helical. {ECO:0000255}. FT TRANSMEM 653 673 Helical. {ECO:0000255}. SQ SEQUENCE 674 AA; 74229 MW; C915DA24F0FDE5A3 CRC64; MNDMTLYLII ALVPLAGSLI AGLFGNKIGR AGAHTVTILG VAVSAVLSAY VLWGFIDGSR AKFDENVYTW LTMGGLDFSV GFLVDTMTAM MMVVVTGVSL MVHIYTIGYM HDEKVGYQRF FSYISLFTFS MLMLIMSNNF IQLFFGWEAV GLVSYLLIGF YFKRPSATFA NLKAFLINRV GDFGFLLGIG LVLAYFGGSL RYQDVFAYLP NVQNATIQLF PGVEWSLITV TCLLLFVGAM GKSAQFPLHV WLPDSMEGPT PISALIHAAT MVTAGLFMVS RMSPIYEMSS TALSVIMVIG AITALFMGFL GVIQNDIKRV VAYSTLSQLG YMTVALGASA YSVAMFHVMT HAFFKALLFL AAGSAIIGMH HDQDMRHMGN LKKYMPVTWL TMLIGNLSLI GTPFFSGFYS KDSIIEAAKY STLPGSGFAY FAVLASVFVT AFYAFRQYFM VFHGEEKWRS LPEHHSDGHG EEHHGLGKND NPHESPLVVT LPLILLAVPS VIIGYIAIEP MLYGDFFKDV IFVNADAHPT IHIMKEEFHG ALAMVSHSLH SPVLYLAIAG VLSAWLLYVK LPHLPAKIAQ TFRPIYVLFE NKYYLDALYF NVFAKGTRAL GTFFWKVGDT AIIDNGIVNG SAKLVGAIAA QVRKAQTGFI YTYAAAMVFG VLVLLGMTFW GLFR // ID NUSB_NEIMB Reviewed; 141 AA. AC Q9K0D0; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=N utilization substance protein B homolog {ECO:0000255|HAMAP-Rule:MF_00073}; DE Short=Protein NusB {ECO:0000255|HAMAP-Rule:MF_00073}; GN Name=nusB {ECO:0000255|HAMAP-Rule:MF_00073}; GN OrderedLocusNames=NMB0683; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the transcription termination process. CC {ECO:0000255|HAMAP-Rule:MF_00073}. CC -!- SIMILARITY: Belongs to the NusB family. {ECO:0000255|HAMAP- CC Rule:MF_00073}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41101.1; -; Genomic_DNA. DR PIR; A81172; A81172. DR RefSeq; NP_273725.1; NC_003112.2. DR RefSeq; WP_002214168.1; NC_003112.2. DR ProteinModelPortal; Q9K0D0; -. DR STRING; 122586.NMB0683; -. DR PaxDb; Q9K0D0; -. DR EnsemblBacteria; AAF41101; AAF41101; NMB0683. DR GeneID; 902795; -. DR KEGG; nme:NMB0683; -. DR PATRIC; 20356679; VBINeiMen85645_0857. DR eggNOG; ENOG4107YIM; Bacteria. DR eggNOG; COG0781; LUCA. DR HOGENOM; HOG000281868; -. DR KO; K03625; -. DR OMA; WIGVYEF; -. DR OrthoDB; EOG6RJV9B; -. DR BioCyc; NMEN122586:GHGG-711-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.940.10; -; 1. DR HAMAP; MF_00073; NusB; 1. DR InterPro; IPR011605; NusB_fam. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR PANTHER; PTHR11078; PTHR11078; 1. DR Pfam; PF01029; NusB; 1. DR SUPFAM; SSF48013; SSF48013; 1. DR TIGRFAMs; TIGR01951; nusB; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transcription; KW Transcription regulation; Transcription termination. FT CHAIN 1 141 N utilization substance protein B FT homolog. FT /FTId=PRO_0000176559. SQ SEQUENCE 141 AA; 16039 MW; 8A158E675563FAB2 CRC64; MKTARRRSRE LAVQAVYQSL INRTAAPEIA KNIREMSDFA KADEELFNKL FFGTQTNAAE YIRQIRPLLD RDEKDLNPIE RAVLLTACHE LSAMPETPYP VIINEAIEVT KTFGGTDGHK FVNGILDKLA AQIRPDEPKR R // ID OMP4_NEIMB Reviewed; 242 AA. AC P0A0V3; P38367; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=Outer membrane protein class 4; DE Flags: Precursor; GN Name=rmpM; OrderedLocusNames=NMB0382; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 18241 / M986 / Serogroup B / Serotype 2; RX PubMed=2499543; RA Klugman K.P., Gotschlich E.C., Blake M.S.; RT "Sequence of the structural gene (rmpM) for the class 4 outer membrane RT protein of Neisseria meningitidis, homology of the protein to RT gonococcal protein III and Escherichia coli OmpA, and construction of RT meningococcal strains that lack class 4 protein."; RL Infect. Immun. 57:2066-2071(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the OmpA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 OmpA-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40822.1; -; Genomic_DNA. DR PIR; A37004; A37004. DR PIR; C81205; C81205. DR RefSeq; NP_273431.1; NC_003112.2. DR RefSeq; WP_002212455.1; NC_003112.2. DR ProteinModelPortal; P0A0V3; -. DR SMR; P0A0V3; 90-229. DR STRING; 122586.NMB0382; -. DR PaxDb; P0A0V3; -. DR EnsemblBacteria; AAF40822; AAF40822; NMB0382. DR GeneID; 902497; -. DR KEGG; nme:NMB0382; -. DR PATRIC; 20355931; VBINeiMen85645_0483. DR eggNOG; ENOG4105UYK; Bacteria. DR eggNOG; COG2885; LUCA. DR HOGENOM; HOG000189913; -. DR OMA; CWRTGYW; -. DR OrthoDB; EOG6PP9QB; -. DR BioCyc; NMEN122586:GHGG-404-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR Gene3D; 3.30.1330.60; -; 1. DR InterPro; IPR006664; OMP_bac. DR InterPro; IPR006665; OmpA-like. DR InterPro; IPR006690; OMPA-like_CS. DR Pfam; PF00691; OmpA; 1. DR PRINTS; PR01021; OMPADOMAIN. DR SUPFAM; SSF103088; SSF103088; 1. DR PROSITE; PS01068; OMPA_1; 1. DR PROSITE; PS51123; OMPA_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Disulfide bond; Ion transport; KW Membrane; Porin; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 242 Outer membrane protein class 4. FT /FTId=PRO_0000020112. FT REPEAT 69 70 1. FT REPEAT 71 72 2. FT REPEAT 73 74 3. FT REPEAT 75 76 4. FT REPEAT 77 78 5. FT REPEAT 79 80 6. FT REPEAT 81 82 7. FT DOMAIN 92 229 OmpA-like. {ECO:0000255|PROSITE- FT ProRule:PRU00473}. FT REGION 69 82 7 X 2 AA tandem repeats of X-P. FT DISULFID 191 214 {ECO:0000250}. FT VARIANT 78 79 Missing (in strain: CCUG 18241). FT VARIANT 128 129 SR -> GQ (in strain: CCUG 18241). FT VARIANT 132 132 V -> I (in strain: CCUG 18241). SQ SEQUENCE 242 AA; 26185 MW; 5E108F6D99C1B9E7 CRC64; MTKQLKLSAL FVALLASGTA VAGEASVQGY TVSGQSNEIV RNNYGECWKN AYFDKASQGR VECGDAVAAP EPEPEPEPAP APVVVVEQAP QYVDETISLS AKTLFGFDKD SLRAEAQDNL KVLAQRLSRT NVQSVRVEGH TDFMGSDKYN QALSERRAYV VANNLVSNGV PVSRISAVGL GESQAQMTQV CEAEVAKLGA KVSKAKKREA LIACIEPDRR VDVKIRSIVT RQVVPAHNHH QH // ID OMPB1_NEIMB Reviewed; 331 AA. AC P30690; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 16-MAR-2016, entry version 112. DE RecName: Full=Major outer membrane protein P.IB; DE Short=PIB; DE Short=Protein IB; DE AltName: Full=Class 3 protein; DE AltName: Full=Porin; DE Flags: Precursor; GN Name=porB; OrderedLocusNames=NMB2039; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=1330818; DOI=10.1016/0378-1097(92)90644-4; RA Ward M.J., Lambden P.R., Heckels J.E.; RT "Sequence analysis and relationships between meningococcal class 3 RT serotype proteins and other porins from pathogenic and non-pathogenic RT Neisseria species."; RL FEMS Microbiol. Lett. 73:283-289(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Serves as a slightly cation selective porin. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the Gram-negative porin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65532; CAA46502.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42360.1; -; Genomic_DNA. DR PIR; S21407; S21407. DR RefSeq; NP_275030.1; NC_003112.2. DR RefSeq; WP_002244345.1; NC_003112.2. DR PDB; 3WI4; X-ray; 3.32 A; A=20-331. DR PDB; 3WI5; X-ray; 2.40 A; A=20-331. DR PDBsum; 3WI4; -. DR PDBsum; 3WI5; -. DR ProteinModelPortal; P30690; -. DR STRING; 122586.NMB2039; -. DR PaxDb; P30690; -. DR EnsemblBacteria; AAF42360; AAF42360; NMB2039. DR GeneID; 904054; -. DR KEGG; nme:NMB2039; -. DR PATRIC; 20360214; VBINeiMen85645_2608. DR eggNOG; ENOG4108Z9W; Bacteria. DR eggNOG; ENOG4111NJJ; LUCA. DR HOGENOM; HOG000114654; -. DR KO; K18133; -. DR OMA; ARTPANF; -. DR OrthoDB; EOG6358DM; -. DR BioCyc; NMEN122586:GHGG-2101-MONOMER; -. DR Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane. DR Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade. DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4). DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4). DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.160.10; -; 1. DR InterPro; IPR023614; Porin_dom. DR InterPro; IPR001702; Porin_Gram-ve. DR InterPro; IPR013793; Porin_Gram-ve_CS. DR InterPro; IPR002299; Porin_Neis. DR Pfam; PF00267; Porin_1; 1. DR PRINTS; PR00182; ECOLNEIPORIN. DR PRINTS; PR00184; NEISSPPORIN. DR PROSITE; PS00576; GRAM_NEG_PORIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Ion transport; KW Membrane; Porin; Reference proteome; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 19 {ECO:0000250}. FT CHAIN 20 331 Major outer membrane protein P.IB. FT /FTId=PRO_0000025281. FT STRAND 21 39 {ECO:0000244|PDB:3WI5}. FT STRAND 41 55 {ECO:0000244|PDB:3WI5}. FT STRAND 59 69 {ECO:0000244|PDB:3WI5}. FT STRAND 72 81 {ECO:0000244|PDB:3WI5}. FT STRAND 94 102 {ECO:0000244|PDB:3WI5}. FT STRAND 105 113 {ECO:0000244|PDB:3WI5}. FT HELIX 116 118 {ECO:0000244|PDB:3WI5}. FT TURN 130 134 {ECO:0000244|PDB:3WI5}. FT TURN 136 140 {ECO:0000244|PDB:3WI5}. FT STRAND 143 150 {ECO:0000244|PDB:3WI5}. FT STRAND 157 164 {ECO:0000244|PDB:3WI5}. FT HELIX 166 169 {ECO:0000244|PDB:3WI5}. FT STRAND 176 185 {ECO:0000244|PDB:3WI5}. FT STRAND 188 200 {ECO:0000244|PDB:3WI5}. FT STRAND 203 205 {ECO:0000244|PDB:3WI5}. FT STRAND 208 222 {ECO:0000244|PDB:3WI5}. FT STRAND 225 240 {ECO:0000244|PDB:3WI5}. FT STRAND 245 256 {ECO:0000244|PDB:3WI5}. FT STRAND 262 271 {ECO:0000244|PDB:3WI5}. FT STRAND 277 279 {ECO:0000244|PDB:3WI4}. FT STRAND 285 310 {ECO:0000244|PDB:3WI5}. FT STRAND 314 316 {ECO:0000244|PDB:3WI5}. FT STRAND 318 331 {ECO:0000244|PDB:3WI5}. SQ SEQUENCE 331 AA; 35682 MW; D6945BC81B04B6AF CRC64; MKKSLIALTL AALPVAAMAD VTLYGTIKAG VETSRSVFHQ NGQVTEVTTA TGIVDLGSKI GFKGQEDLGN GLKAIWQVEQ KASIAGTDSG WGNRQSFIGL KGGFGKLRVG RLNSVLKDTG DINPWDSKSD YLGVNKIAEP EARLISVRYD SPEFAGLSGS VQYALNDNAG RHNSESYHAG FNYKNGGFFV QYGGAYKRHH QVQEGLNIEK YQIHRLVSGY DNDALYASVA VQQQDAKLTD ASNSHNSQTE VAATLAYRFG NVTPRVSYAH GFKGLVDDAD IGNEYDQVVV GAEYDFSKRT SALVSAGWLQ EGKGENKFVA TAGGVGLRHK F // ID ORN_NEIMB Reviewed; 187 AA. AC Q9JXW1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Oligoribonuclease {ECO:0000255|HAMAP-Rule:MF_00045}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00045}; GN Name=orn {ECO:0000255|HAMAP-Rule:MF_00045}; OrderedLocusNames=NMB1863; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small CC oligoribonucleotides. {ECO:0000255|HAMAP-Rule:MF_00045}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00045}. CC -!- SIMILARITY: Belongs to the oligoribonuclease family. CC {ECO:0000255|HAMAP-Rule:MF_00045}. CC -!- SIMILARITY: Contains 1 exonuclease domain. {ECO:0000255|HAMAP- CC Rule:MF_00045}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42197.1; -; Genomic_DNA. DR PIR; H81033; H81033. DR RefSeq; NP_274859.1; NC_003112.2. DR RefSeq; WP_002223024.1; NC_003112.2. DR ProteinModelPortal; Q9JXW1; -. DR SMR; Q9JXW1; 5-177. DR STRING; 122586.NMB1863; -. DR PaxDb; Q9JXW1; -. DR EnsemblBacteria; AAF42197; AAF42197; NMB1863. DR GeneID; 904325; -. DR KEGG; nme:NMB1863; -. DR PATRIC; 20359751; VBINeiMen85645_2381. DR eggNOG; ENOG4108RBP; Bacteria. DR eggNOG; COG1949; LUCA. DR HOGENOM; HOG000246596; -. DR KO; K13288; -. DR OMA; AFFHYRN; -. DR OrthoDB; EOG6Z9B51; -. DR BioCyc; NMEN122586:GHGG-1919-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00045; Oligoribonuclease; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR022894; Oligoribonuclease. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 187 Oligoribonuclease. FT /FTId=PRO_0000111054. FT DOMAIN 7 170 Exonuclease. {ECO:0000255|HAMAP- FT Rule:MF_00045}. FT ACT_SITE 128 128 {ECO:0000255|HAMAP-Rule:MF_00045}. SQ SEQUENCE 187 AA; 21760 MW; 039CFF998A4DBCDB CRC64; MQDKNNLCWL DMEMTGLNPE TDRIIEVAMI ITDSDLNVLA QSEVYAVHQS DDVLNKMDEW NTATHGRTGL TQRVRESSHT EAEVEQKLLD FMSEWVPGRA TPMCGNSIHQ DRRFMVKYMP KLENYFHYRN LDVSTLKELA KRWNPPVAKS VVKRGSHKAL DDILESIEEM RHYREHFLIS APRAEAQ // ID OBG_NEIMB Reviewed; 384 AA. AC Q9JXE5; DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454}; DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454}; DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454}; GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=NMB2086; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly CC (p)ppGpp with moderate affinity, with high nucleotide exchange CC rates and a fairly low GTP hydrolysis rate. Plays a role in CC control of the cell cycle, stress response, ribosome biogenesis CC and in those bacteria that undergo differentiation, in CC morphogenesis control. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_01454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42403.1; -; Genomic_DNA. DR PIR; D81007; D81007. DR RefSeq; NP_275074.1; NC_003112.2. DR RefSeq; WP_002223198.1; NC_003112.2. DR ProteinModelPortal; Q9JXE5; -. DR STRING; 122586.NMB2086; -. DR PaxDb; Q9JXE5; -. DR EnsemblBacteria; AAF42403; AAF42403; NMB2086. DR GeneID; 903966; -. DR KEGG; nme:NMB2086; -. DR PATRIC; 20360338; VBINeiMen85645_2666. DR eggNOG; ENOG4105C9R; Bacteria. DR eggNOG; COG0536; LUCA. DR HOGENOM; HOG000019084; -. DR KO; K03979; -. DR OMA; LVDFRYK; -. DR OrthoDB; EOG6H1Q1M; -. DR BioCyc; NMEN122586:GHGG-2151-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.210.12; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01454; GTPase_Obg; 1. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR014100; GTP-bd_Obg/CgtA. DR InterPro; IPR006074; GTP1-OBG_CS. DR InterPro; IPR006169; GTP1_OBG_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11702:SF3; PTHR11702:SF3; 1. DR Pfam; PF01018; GTP1_OBG; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF82051; SSF82051; 1. DR TIGRFAMs; TIGR02729; Obg_CgtA; 1. DR PROSITE; PS51710; G_OBG; 1. DR PROSITE; PS00905; GTP1_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 384 GTPase Obg. FT /FTId=PRO_0000386084. FT DOMAIN 160 348 OBG-type G. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT NP_BIND 166 173 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 191 195 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 213 216 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 284 287 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 329 331 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT METAL 173 173 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT METAL 193 193 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. SQ SEQUENCE 384 AA; 41929 MW; C486D5B8AE5DD68E CRC64; MKFIDEAKIE VAAGKGGNGA TSFRREKFVP RGGPDGGDGG KGGSVWAEAD ENTNTLVEYR FVKRYQAKNG EKGHGSDRYG AGADDIVLKM PVGTLIRDLD TGETVADLTY HGQRVCLAKG GKGGLGNIHF KSSVNRAPKQ STPGEEGEAR SLQLELKVLA DVGLLGMPNA GKSTLITAVS AARPKIANYP FTTLHPNLGV VRIDENHSFV MADIPGLIEG AAEGAGLGHR FLKHLSRTGL LLHVVDLAPF DETVNPAEEA LAIINELRKY DEELYGKPRW LVLNKLDMLD EEEAQTRTAA FLEAVGWDYP KPDDRFQFDM ETPRLFQISA LTHQGTQELV HQINQYLTEK KRIEAEKAEA EKAAANVEII EQQPKTDTGV FKPE // ID PA1_NEIMB Reviewed; 382 AA. AC Q9K0U7; DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Putative phospholipase A1; DE EC=3.1.1.32; DE EC=3.1.1.4; DE AltName: Full=Phosphatidylcholine 1-acylhydrolase; DE Flags: Precursor; GN OrderedLocusNames=NMB0464; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 CC (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 2- CC acylglycerophosphocholine + a carboxylate. CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1- CC acylglycerophosphocholine + a carboxylate. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the CC Ca(2+) is bound by different amino acids with binding of each CC Ca(2+) shared with ligands coming from each monomer. The Ca(2+) CC ion may have a role in catalysis. {ECO:0000250}; CC -!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric CC form is the active one. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. Note=One of the very few CC enzymes located there. {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40901.1; -; Genomic_DNA. DR PIR; E81195; E81195. DR RefSeq; NP_273511.1; NC_003112.2. DR RefSeq; WP_002216585.1; NC_003112.2. DR ProteinModelPortal; Q9K0U7; -. DR STRING; 122586.NMB0464; -. DR PaxDb; Q9K0U7; -. DR EnsemblBacteria; AAF40901; AAF40901; NMB0464. DR GeneID; 902580; -. DR KEGG; nme:NMB0464; -. DR PATRIC; 20356174; VBINeiMen85645_0608. DR eggNOG; ENOG4105HDD; Bacteria. DR eggNOG; COG2829; LUCA. DR HOGENOM; HOG000288150; -. DR KO; K01058; -. DR OMA; SRFWELE; -. DR OrthoDB; EOG6HQSN6; -. DR BioCyc; NMEN122586:GHGG-488-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008970; F:phosphatidylcholine 1-acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.40.230.10; -; 1. DR InterPro; IPR003187; PLipase_A1. DR Pfam; PF02253; PLA1; 1. DR PRINTS; PR01486; PHPHLIPASEA1. DR SUPFAM; SSF56931; SSF56931; 1. PE 1: Evidence at protein level; KW Calcium; Cell outer membrane; Complete proteome; Hydrolase; KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding; KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 382 Putative phospholipase A1. FT /FTId=PRO_0000349892. FT TOPO_DOM 28 65 Periplasmic. {ECO:0000255}. FT TRANSMEM 66 78 Beta stranded. {ECO:0000255}. FT TOPO_DOM 79 168 Extracellular. {ECO:0000255}. FT TRANSMEM 169 183 Beta stranded. {ECO:0000255}. FT TOPO_DOM 184 189 Periplasmic. {ECO:0000255}. FT TRANSMEM 190 202 Beta stranded. {ECO:0000255}. FT TOPO_DOM 203 213 Extracellular. {ECO:0000255}. FT TRANSMEM 214 233 Beta stranded. {ECO:0000255}. FT TOPO_DOM 234 236 Periplasmic. {ECO:0000255}. FT TRANSMEM 237 250 Beta stranded. {ECO:0000255}. FT TOPO_DOM 251 259 Extracellular. {ECO:0000255}. FT TRANSMEM 260 272 Beta stranded. {ECO:0000255}. FT TOPO_DOM 273 274 Periplasmic. {ECO:0000255}. FT TRANSMEM 275 284 Beta stranded. {ECO:0000255}. FT TOPO_DOM 285 306 Extracellular. {ECO:0000255}. FT TRANSMEM 307 313 Beta stranded. {ECO:0000255}. FT TOPO_DOM 314 315 Periplasmic. {ECO:0000255}. FT TRANSMEM 316 325 Beta stranded. {ECO:0000255}. FT TOPO_DOM 326 332 Extracellular. {ECO:0000255}. FT TRANSMEM 333 341 Beta stranded. {ECO:0000255}. FT TOPO_DOM 342 346 Periplasmic. {ECO:0000255}. FT TRANSMEM 347 356 Beta stranded. {ECO:0000255}. FT TOPO_DOM 357 365 Extracellular. {ECO:0000255}. FT TRANSMEM 366 377 Beta stranded. {ECO:0000255}. FT TOPO_DOM 378 382 Periplasmic. {ECO:0000255}. FT ACT_SITE 248 248 Proton acceptor. {ECO:0000250}. FT ACT_SITE 250 250 Nucleophile. {ECO:0000250}. FT METAL 211 211 Calcium 1; via carbonyl oxygen; in FT dimeric form. {ECO:0000250}. FT METAL 258 258 Calcium 2; in dimeric form. FT {ECO:0000250}. FT METAL 294 294 Calcium 3; in monomeric form. FT {ECO:0000250}. SQ SEQUENCE 382 AA; 42714 MW; B468A802F062E836 CRC64; MPTMGAEMNT RNMRYILLTG LLPMASAFGE TALQCAALTD NVTRLACYDR IFAAQLPSSA GQEGQESKAV LNLTETVRSS LDKGEAVIVV EKGGDALPAD SAGETADIYT PLSLMYDLDK NDLRGLLGVR EHNPMYLMPL WYNNSPNYAP GSPTRGTTVQ EKFGQQKRAE TKLQVSFKSK IAEDLFKTRA DLWFGYTQRS DWQIYNQGRK SAPFRNTDYK PEIFLTQPVK ADLPFGGRLR MLGAGFVHQS NGQSRPESRS WNRIYAMAGM EWGKLTVIPR VWVRAFDQSG DKNDNPDIAD YMGYGDVKLQ YRLNDRQNVY SVLRYNPKTG YGAIEAAYTF PIKGKLKGVV RGFHGYGESL IDYNHKQNGI GIGLMFNDLD GI // ID PANB_NEIMB Reviewed; 263 AA. AC Q9JZW6; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156}; DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156}; GN Name=panB {ECO:0000255|HAMAP-Rule:MF_00156}; GN OrderedLocusNames=NMB0870; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-263 IN COMPLEX WITH RP SUBSTRATE AND SODIUM ION, AND SUBUNIT. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl CC group from 5,10-methylenetetrahydrofolate is tranferred onto CC alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + 3-methyl-2- CC oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. CC {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00156}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00156}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. CC {ECO:0000305|PubMed:16021622}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41281.1; -; Genomic_DNA. DR PIR; F81148; F81148. DR RefSeq; NP_273911.1; NC_003112.2. DR RefSeq; WP_002222670.1; NC_003112.2. DR PDB; 1O66; X-ray; 1.75 A; A/B/C/D/E=2-263. DR PDB; 1O68; X-ray; 2.10 A; A/B/C/D/E=2-263. DR PDBsum; 1O66; -. DR PDBsum; 1O68; -. DR ProteinModelPortal; Q9JZW6; -. DR SMR; Q9JZW6; 1-261. DR STRING; 122586.NMB0870; -. DR PaxDb; Q9JZW6; -. DR EnsemblBacteria; AAF41281; AAF41281; NMB0870. DR GeneID; 902986; -. DR KEGG; nme:NMB0870; -. DR PATRIC; 20357133; VBINeiMen85645_1083. DR eggNOG; ENOG4105CCG; Bacteria. DR eggNOG; COG0413; LUCA. DR HOGENOM; HOG000078427; -. DR KO; K00606; -. DR OMA; MAAGAQM; -. DR OrthoDB; EOG63C0WN; -. DR BioCyc; NMEN122586:GHGG-903-MONOMER; -. DR UniPathway; UPA00028; UER00003. DR EvolutionaryTrace; Q9JZW6; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.60; -; 1. DR HAMAP; MF_00156; PanB; 1. DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR20881; PTHR20881; 1. DR Pfam; PF02548; Pantoate_transf; 1. DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR00222; panB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Pantothenate biosynthesis; Reference proteome; Transferase. FT CHAIN 1 263 3-methyl-2-oxobutanoate FT hydroxymethyltransferase. FT /FTId=PRO_0000184867. FT REGION 43 44 Alpha-ketoisovalerate binding. FT ACT_SITE 179 179 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 43 43 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 82 82 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 113 113 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT BINDING 82 82 Alpha-ketoisovalerate. FT BINDING 111 111 Alpha-ketoisovalerate. FT HELIX 4 13 {ECO:0000244|PDB:1O66}. FT STRAND 17 21 {ECO:0000244|PDB:1O66}. FT HELIX 25 33 {ECO:0000244|PDB:1O66}. FT STRAND 38 41 {ECO:0000244|PDB:1O66}. FT HELIX 45 48 {ECO:0000244|PDB:1O66}. FT STRAND 53 55 {ECO:0000244|PDB:1O66}. FT HELIX 60 73 {ECO:0000244|PDB:1O66}. FT STRAND 75 82 {ECO:0000244|PDB:1O66}. FT STRAND 87 90 {ECO:0000244|PDB:1O66}. FT HELIX 92 104 {ECO:0000244|PDB:1O66}. FT STRAND 108 113 {ECO:0000244|PDB:1O66}. FT HELIX 116 118 {ECO:0000244|PDB:1O66}. FT HELIX 119 127 {ECO:0000244|PDB:1O66}. FT STRAND 132 138 {ECO:0000244|PDB:1O66}. FT HELIX 140 142 {ECO:0000244|PDB:1O66}. FT HELIX 158 170 {ECO:0000244|PDB:1O66}. FT STRAND 174 180 {ECO:0000244|PDB:1O66}. FT HELIX 183 192 {ECO:0000244|PDB:1O66}. FT STRAND 197 202 {ECO:0000244|PDB:1O66}. FT STRAND 206 211 {ECO:0000244|PDB:1O66}. FT HELIX 213 216 {ECO:0000244|PDB:1O66}. FT STRAND 220 223 {ECO:0000244|PDB:1O66}. FT HELIX 238 250 {ECO:0000244|PDB:1O66}. FT HELIX 257 259 {ECO:0000244|PDB:1O66}. SQ SEQUENCE 263 AA; 27739 MW; B863D8238F320317 CRC64; MITVNTLQKM KAAGEKIAML TAYESSFAAL MDDAGVEMLL VGDSLGMAVQ GRKSTLPVSL RDMCYHTECV ARGAKNAMIV SDLPFGAYQQ SKEQAFAAAA ELMAAGAHMV KLEGGVWMAE TTEFLQMRGI PVCAHIGLTP QSVFAFGGYK VQGRGGKAQA LLNDAKAHDD AGAAVVLMEC VLAELAKKVT ETVSCPTIGI GAGADCDGQV LVMHDMLGIF PGKTAKFVKN FMQGHDSVQA AVRAYVAEVK AKTFPAAEHI FAD // ID OMPA_NEIMB Reviewed; 392 AA. AC P0DH58; Q51240; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 16-MAR-2016, entry version 27. DE RecName: Full=Major outer membrane protein P.IA; DE Short=PIA; DE Short=Protein IA; DE AltName: Full=Class 1 protein; DE Flags: Precursor; GN Name=porA; OrderedLocusNames=NMB1429; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710308; DOI=10.1126/science.287.5459.1816; RA Pizza M., Scarlato V., Masignani V., Giuliani M.M., Arico' B., RA Comanducci M., Jennings G.T., Baldi L., Bartolini E., Capecchi B., RA Galeotti C.L., Luzzi E., Manetti R., Marchetti E., Mora M., Nuti S., RA Ratti G., Santini L., Savino S., Scarselli M., Storni E., Zuo P., RA Broeker M., Hundt E., Knapp B., Blair E., Mason T., Tettelin H., RA Hood D.W., Jeffries A.C., Saunders N.J., Granoff D.M., Venter J.C., RA Moxon E.R., Grandi G., Rappuoli R.; RT "Identification of vaccine candidates against serogroup B RT meningococcus by whole-genome sequencing."; RL Science 287:1816-1820(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Serves as a slightly cation selective porin. Major CC antigen on the gonococcal cell surface and it may have pathogenic CC properties in addition to its porin activity. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the Gram-negative porin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41790.1; -; Genomic_DNA. DR EMBL; AF226344; AAF42493.1; -; Genomic_DNA. DR PIR; F81084; F81084. DR RefSeq; NP_274441.1; NC_003112.2. DR RefSeq; WP_010980936.1; NC_003112.2. DR ProteinModelPortal; P0DH58; -. DR STRING; 122586.NMB1429; -. DR PaxDb; P0DH58; -. DR EnsemblBacteria; AAF41790; AAF41790; NMB1429. DR GeneID; 903851; -. DR KEGG; nme:NMB1429; -. DR eggNOG; COG3203; LUCA. DR HOGENOM; HOG000114654; -. DR KO; K18132; -. DR OMA; AHGFDFI; -. DR OrthoDB; EOG6358DM; -. DR BioCyc; NMEN122586:GHGG-1467-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.160.10; -; 1. DR InterPro; IPR023614; Porin_dom. DR InterPro; IPR001702; Porin_Gram-ve. DR InterPro; IPR013793; Porin_Gram-ve_CS. DR InterPro; IPR002299; Porin_Neis. DR Pfam; PF00267; Porin_1; 1. DR PRINTS; PR00182; ECOLNEIPORIN. DR PRINTS; PR00184; NEISSPPORIN. DR PROSITE; PS00576; GRAM_NEG_PORIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Ion transport; Membrane; KW Porin; Reference proteome; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 19 {ECO:0000250}. FT CHAIN 20 392 Major outer membrane protein P.IA. FT /FTId=PRO_0000025274. SQ SEQUENCE 392 AA; 42078 MW; 1D78EA55BF76E940 CRC64; MRKKLTALVL SALPLAAVAD VSLYGEIKAG VEGRNYQLQL TEAQAANGGA SGQVKVTKVT KAKSRIRTKI SDFGSFIGFK GSEDLGDGLK AVWQLEQDVS VAGGGATQWG NRESFIGLAG EFGTLRAGRV ANQFDDASQA IDPWDSNNDV ASQLGIFKRH DDMPVSVRYD SPEFSGFSGS VQFVPIQNSK SAYTPAYYTK NTNNNLTLVP AVVGKPGSDV YYAGLNYKNG GFAGNYAFKY ARHANVGRNA FELFLIGSGS DQAKGTDPLK NHQVHRLTGG YEEGGLNLAL AAQLDLSENG DKTKNSTTEI AATASYRFGN AVPRISYAHG FDFIERGKKG ENTSYDQIIA GVDYDFSKRT SAIVSGAWLK RNTGIGNYTQ INAASVGLRH KF // ID OTC_NEIMB Reviewed; 331 AA. AC P0DH57; Q9JYI3; Q9R812; Q9S6H2; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 11-NOV-2015, entry version 33. DE RecName: Full=Ornithine carbamoyltransferase; DE Short=OTCase; DE EC=2.1.3.3; GN Name=argF; OrderedLocusNames=NMB1573; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CDC 8201085 / NMB / Serogroup B; RA Kahler C.M., Stephens D.S.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-314. RC STRAIN=CCUG 23094 / S3446 / Serogroup B / Serotype 14, RC CCUG 23103 / M470 / Serogroup B, HF130 / Serogroup B / Serotype NT, RC and P63 / Serogroup B / Serotype NT / Subtype 2; RX PubMed=1406254; DOI=10.1111/j.1365-2958.1992.tb01387.x; RA Zhou J., Spratt B.G.; RT "Sequence diversity within the argF, fbp and recA genes of natural RT isolates of Neisseria meningitidis: interspecies recombination within RT the argF gene."; RL Mol. Microbiol. 6:2135-2146(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-299. RC STRAIN=NCTC 8249 / Serogroup B; RX PubMed=10368955; DOI=10.1093/oxfordjournals.molbev.a026162; RA Smith N.H., Holmes E.C., Donovan G.M., Carpenter G.A., Spratt B.G.; RT "Networks and groups within the genus Neisseria: analysis of argF, RT recA, rho, and 16S rRNA sequences from human Neisseria species."; RL Mol. Biol. Evol. 16:773-783(1999). CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group CC from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine CC (ORN) to produce L-citrulline. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate CC + L-citrulline. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 1/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF125563; AAD32177.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41926.1; -; Genomic_DNA. DR EMBL; X64861; CAA46073.1; -; Genomic_DNA. DR EMBL; X64862; CAA46074.1; -; Genomic_DNA. DR EMBL; X64863; CAA46075.1; -; Genomic_DNA. DR EMBL; X64868; CAA46080.1; -; Genomic_DNA. DR EMBL; AJ223888; CAA11619.1; -; Genomic_DNA. DR PIR; E81066; E81066. DR PIR; S24734; S24734. DR RefSeq; NP_274579.1; NC_003112.2. DR RefSeq; WP_002212820.1; NC_003112.2. DR ProteinModelPortal; P0DH57; -. DR SMR; P0DH57; 2-331. DR STRING; 122586.NMB1573; -. DR PaxDb; P0DH57; -. DR EnsemblBacteria; AAF41926; AAF41926; NMB1573. DR GeneID; 904168; -. DR KEGG; nme:NMB1573; -. DR eggNOG; ENOG4105DBV; Bacteria. DR eggNOG; COG0078; LUCA. DR HOGENOM; HOG000022686; -. DR KO; K00611; -. DR OMA; DFRIFAP; -. DR OrthoDB; EOG690MGV; -. DR BioCyc; NMEN122586:GHGG-1614-MONOMER; -. DR UniPathway; UPA00068; UER00112. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_01109; OTCase; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR002292; Orn/put_carbamltrans. DR InterPro; IPR024904; OTCase_ArgI. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00658; orni_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 331 Ornithine carbamoyltransferase. FT /FTId=PRO_0000112965. FT REGION 55 59 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 133 136 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 234 235 Ornithine binding. {ECO:0000250}. FT REGION 271 274 Carbamoyl phosphate binding. FT {ECO:0000250}. FT BINDING 9 9 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 71 71 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 82 82 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 106 106 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 166 166 Ornithine. {ECO:0000250}. FT BINDING 230 230 Ornithine. {ECO:0000250}. FT BINDING 299 299 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 317 317 Carbamoyl phosphate. {ECO:0000250}. FT SITE 30 30 Important for structural integrity. FT {ECO:0000250}. FT SITE 146 146 Important for structural integrity. FT {ECO:0000250}. FT VARIANT 302 302 I -> V (in strain: NMB, HF130 and P63). SQ SEQUENCE 331 AA; 36716 MW; B169D6C717FA1C81 CRC64; MNLKNRHFLK LLDFTPEEIT AYLDLAAELK AAKKAGREIQ RMKGKNIALI FEKTSTRTRC AFEVAARDQG AGVTYLEPSA SQIGHKESIK DTARVLGRMY DAIEYRGFGQ EVVEELAKYA GVPVFNGLTN EFHPTQMLAD ALTMREHSGK PLNQTAFAYV GDARYNMGNS LLILGAKLGM DVRIGAPQSL WPSEGIIAAA HAAAKETGAK ITLTENAHEA VKNVDFIHTD VWVSMGEPKE VWQERIDLLK DYRVTPELMA ASGNPQVKFM HCLPAFHNRE TKVGEWIYET FGLNGVEVTE EIFESPASIV FDQAENRMHT IKAVMVAALG D // ID PAND_NEIMB Reviewed; 127 AA. AC Q9JZ56; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446}; DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446}; DE AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446}; DE Flags: Precursor; GN Name=panD {ECO:0000255|HAMAP-Rule:MF_00446}; GN OrderedLocusNames=NMB1282; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of CC aspartate to produce beta-alanine. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00446}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- PTM: Is synthesized initially as an inactive proenzyme, which is CC activated by self-cleavage at a specific serine bond to produce a CC beta-subunit with a hydroxyl group at its C-terminus and an alpha- CC subunit with a pyruvoyl group at its N-terminus. CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41658.1; -; Genomic_DNA. DR PIR; A81100; A81100. DR RefSeq; NP_274302.1; NC_003112.2. DR RefSeq; WP_002217080.1; NC_003112.2. DR ProteinModelPortal; Q9JZ56; -. DR SMR; Q9JZ56; 26-117. DR STRING; 122586.NMB1282; -. DR PaxDb; Q9JZ56; -. DR EnsemblBacteria; AAF41658; AAF41658; NMB1282. DR GeneID; 903704; -. DR KEGG; nme:NMB1282; -. DR PATRIC; 20358191; VBINeiMen85645_1607. DR eggNOG; ENOG4108Z2X; Bacteria. DR eggNOG; COG0853; LUCA. DR HOGENOM; HOG000221007; -. DR KO; K01579; -. DR OMA; LYSKIHR; -. DR OrthoDB; EOG6P5ZMC; -. DR BioCyc; NMEN122586:GHGG-1320-MONOMER; -. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00446; PanD; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR003190; Asp_decarbox. DR PANTHER; PTHR21012; PTHR21012; 1. DR Pfam; PF02261; Asp_decarbox; 1. DR PIRSF; PIRSF006246; Asp_decarbox; 1. DR ProDom; PD009294; Asp_decarbox; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR00223; panD; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase; KW Lyase; Pantothenate biosynthesis; Pyruvate; Reference proteome; KW Schiff base; Zymogen. FT CHAIN 1 24 Aspartate 1-decarboxylase beta chain. FT {ECO:0000255|HAMAP-Rule:MF_00446}. FT /FTId=PRO_0000023127. FT CHAIN 25 127 Aspartate 1-decarboxylase alpha chain. FT {ECO:0000255|HAMAP-Rule:MF_00446}. FT /FTId=PRO_0000023128. FT REGION 73 75 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT ACT_SITE 25 25 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT ACT_SITE 58 58 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT BINDING 57 57 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT MOD_RES 25 25 Pyruvic acid (Ser). {ECO:0000255|HAMAP- FT Rule:MF_00446}. SQ SEQUENCE 127 AA; 13809 MW; F93E4733F5F72B73 CRC64; MFRTMLGGKI HRATVTEADL NYVGSITVDQ DLLDAAGIYP NEKVAIVNNN NGERFETYTI AGKRGSGVIC LNGAAARLVQ KGDIVIIMSY VQLSEPEIAA HEPKVVLVDG NNKIRDIISY EPPHTVL // ID PDXH_NEIMB Reviewed; 210 AA. AC Q9JYZ5; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629}; GN Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629}; GN OrderedLocusNames=NMB1360; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- CC phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal CC 5'-phosphate (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) = CC pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000255|HAMAP- CC Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'- CC phosphate + H(2)O(2). {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01629}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase CC family. {ECO:0000255|HAMAP-Rule:MF_01629}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41734.1; -; Genomic_DNA. DR PIR; A81092; A81092. DR RefSeq; NP_274378.1; NC_003112.2. DR RefSeq; WP_002222336.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ5; -. DR STRING; 122586.NMB1360; -. DR PaxDb; Q9JYZ5; -. DR EnsemblBacteria; AAF41734; AAF41734; NMB1360. DR GeneID; 903782; -. DR KEGG; nme:NMB1360; -. DR PATRIC; 20358381; VBINeiMen85645_1702. DR eggNOG; ENOG4108S7T; Bacteria. DR eggNOG; COG0259; LUCA. DR HOGENOM; HOG000242755; -. DR KO; K00275; -. DR OMA; PEHWGGY; -. DR OrthoDB; EOG60KN2Z; -. DR BioCyc; NMEN122586:GHGG-1398-MONOMER; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 2.30.110.10; -; 1. DR HAMAP; MF_01629; PdxH; 1. DR InterPro; IPR000659; Pyridox_Oxase. DR InterPro; IPR019740; Pyridox_Oxase_CS. DR InterPro; IPR011576; Pyridox_Oxase_FMN-bd. DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR PANTHER; PTHR10851:SF0; PTHR10851:SF0; 1. DR Pfam; PF10590; PNPOx_C; 1. DR Pfam; PF01243; Pyridox_oxidase; 1. DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR00558; pdxH; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Pyridoxine biosynthesis; Reference proteome. FT CHAIN 1 210 Pyridoxine/pyridoxamine 5'-phosphate FT oxidase. FT /FTId=PRO_0000167727. FT NP_BIND 60 65 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 75 76 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 139 140 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT REGION 7 10 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT REGION 189 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 81 81 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 82 82 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 104 104 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 126 126 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 130 130 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 183 183 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 193 193 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. SQ SEQUENCE 210 AA; 24215 MW; F3EF22A9A5024809 CRC64; MDLHNIREDY SKRELSEADC ADNPIEQFER WLDEAVRAQV NEPTAVNVAA VDGRGRPNSR MVLLKEVNSE GFVFFTNYHS RKGRSLDAHP FAAMTFFWPE LERQVRVEGR VERLAEKLSD EYFESRPYQS RLGAWASAQS EVIPNKAVLV AKAAAVGLKH PLHVPRPPHW GGYIVIPDLL EFWQGRPSRL HDRIQYRLLD GGWIRERLSP // ID PARB_NEIMB Reviewed; 286 AA. AC Q9JXP5; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Probable chromosome-partitioning protein ParB; GN Name=parB; OrderedLocusNames=NMB1944; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in chromosome partition. Localize to both poles CC of the predivisional cell following completion of DNA replication. CC Binds to the DNA origin of replication (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42273.1; -; Genomic_DNA. DR PIR; A81026; A81026. DR RefSeq; NP_274938.1; NC_003112.2. DR RefSeq; WP_002223092.1; NC_003112.2. DR ProteinModelPortal; Q9JXP5; -. DR STRING; 122586.NMB1944; -. DR PaxDb; Q9JXP5; -. DR EnsemblBacteria; AAF42273; AAF42273; NMB1944. DR GeneID; 904207; -. DR KEGG; nme:NMB1944; -. DR PATRIC; 20359937; VBINeiMen85645_2473. DR eggNOG; ENOG4105FA0; Bacteria. DR eggNOG; COG1475; LUCA. DR HOGENOM; HOG000088074; -. DR KO; K03497; -. DR OMA; LIQRGKY; -. DR OrthoDB; EOG6Z3KMS; -. DR BioCyc; NMEN122586:GHGG-2001-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR InterPro; IPR004437; ParB/RepB/Spo0J. DR InterPro; IPR003115; ParB/Sulfiredoxin_dom. DR Pfam; PF02195; ParBc; 1. DR SMART; SM00470; ParB; 1. DR SUPFAM; SSF110849; SSF110849; 1. DR TIGRFAMs; TIGR00180; parB_part; 1. PE 3: Inferred from homology; KW Chromosome partition; Complete proteome; DNA-binding; KW Reference proteome. FT CHAIN 1 286 Probable chromosome-partitioning protein FT ParB. FT /FTId=PRO_0000178688. SQ SEQUENCE 286 AA; 31555 MW; BFB3722920546948 CRC64; MAKVKGGLGR GLDSLLANGA DNSSGDRLTT VAVKDIRPGR YQARVQIDDE ALQELADSIK AQGVIQPVIV REHGLSRYEL IAGERRWRAA QIAGLTEIPA VIKTISDETA LAMGLIENLQ RENLNPIEEA QGLKRLADEF GLTHETIAQA VGKSRSAISN SLRLLSLPEP VQEMLYQRRL EMGHARALLT LPVVEQLELA QKAVKNGWSV REVERRSQAA LQNKRPEPKK TAAADIGRLN DLLTEKLGVN AEVKTANHKK GRIVLYFDTP ETFGHLLEQL GIDYRP // ID PBPA_NEIMB Reviewed; 798 AA. AC P0A0Z6; O05194; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Penicillin-binding protein 1A; DE Short=PBP-1a; DE Short=PBP1a; DE Includes: DE RecName: Full=Penicillin-insensitive transglycosylase; DE EC=2.4.2.-; DE AltName: Full=Peptidoglycan TGase; DE Includes: DE RecName: Full=Penicillin-sensitive transpeptidase; DE EC=3.4.-.-; DE AltName: Full=DD-transpeptidase; GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=NMB1807; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked CC peptidoglycan from the lipid intermediates. The enzyme has a CC penicillin-insensitive transglycosylase N-terminal domain CC (formation of linear glycan strands) and a penicillin-sensitive CC transpeptidase C-terminal domain (cross-linking of the peptide CC subunits) (By similarity). {ECO:0000250}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC glycosyltransferase 51 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC transpeptidase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42144.1; -; Genomic_DNA. DR PIR; H81040; H81040. DR RefSeq; NP_274804.1; NC_003112.2. DR RefSeq; WP_002219786.1; NC_003112.2. DR ProteinModelPortal; P0A0Z6; -. DR SMR; P0A0Z6; 63-248. DR STRING; 122586.NMB1807; -. DR PaxDb; P0A0Z6; -. DR EnsemblBacteria; AAF42144; AAF42144; NMB1807. DR GeneID; 903291; -. DR KEGG; nme:NMB1807; -. DR PATRIC; 20359583; VBINeiMen85645_2297. DR eggNOG; ENOG4108JQC; Bacteria. DR eggNOG; COG5009; LUCA. DR HOGENOM; HOG000041138; -. DR KO; K05366; -. DR OMA; ANSGVYI; -. DR OrthoDB; EOG6HMXCD; -. DR BioCyc; NMEN122586:GHGG-1862-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.710.10; -; 2. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR031376; PCB_OB. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF17092; PCB_OB; 1. DR Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF56601; SSF56601; 3. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme; KW Peptidoglycan synthesis; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 798 Penicillin-binding protein 1A. FT /FTId=PRO_0000083172. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 10 30 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 31 798 Periplasmic. {ECO:0000255}. FT REGION 50 218 Transglycosylase. FT REGION 378 700 Transpeptidase. FT ACT_SITE 461 461 Acyl-ester intermediate. {ECO:0000250}. SQ SEQUENCE 798 AA; 88148 MW; 0B4F4EF037A9977B CRC64; MIKKILTTCF GLVFGFCVFG VGLVAIAILV TYPKLPSLDS LQHYQPKMPL TIYSADGEVI GMYGEQRREF TKIGDFPEVL RNAVIAAEDK RFYRHWGVDV WGVARAAVGN VVSGSVQSGA STITQQVAKN FYLSSEKTFT RKFNEVLLAY KIEQSLSKDK ILELYFNQIY LGQRAYGFAS AAQIYFNKNV RDLTLAEAAM LAGLPKAPSA YNPIVNPERA KLRQKYILNN MLEEKMITVQ QRDQALNEEL HYERFVRKID QSALYVAEMV RQELYEKYGE DAYTQGFKVY TTVRADHQKV ATEALRKALR NFDRGSSYRG AENYIDLSKS EDVEETVSQY LSGLYTVDKM VPAVVLDVTK KKNVVIQLPG GRRVTLDRRA LGFAARAVNN EKMGEDRIRR GAVIRVKNNG GRWAVVQEPL LQGALVSLDA KTGAVRALVG GYDFHSKTFN RAVQAMRQPG STFKPFVYSA ALSKGMTAST VVNDAPISLP GKGPNGSVWT PKNSDGRYSG YITLRQALTA SKNMVSIRIL MSIGVGYAQQ YIRRFGFRSS ELPASLSMAL GTGETTPLKV AEAYSVFANG GYRVSSHVID KIYDRDGRLR AQMQPLVAGQ NAPQAIDPRN AYIMYKIMQD VVRVGTARGA AALGRTDIAG KTGTTNDNKD AWFVGFNPDV VTAVYIGFDK PKSMGRVGYG GTIAVPVWVD YMRFALKGKQ GKGMKMPEGV VSSNGEYYMK ERMVTDPGLT LDNSGIAPQP SRRAKEDDGG AAEGGRQAAD DEVRQDMQET PVLPSNTGSK QQQLDSLF // ID PDXJ_NEIMB Reviewed; 242 AA. AC Q9K0V9; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Pyridoxine 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00279}; DE Short=PNP synthase {ECO:0000255|HAMAP-Rule:MF_00279}; DE EC=2.6.99.2 {ECO:0000255|HAMAP-Rule:MF_00279}; GN Name=pdxJ {ECO:0000255|HAMAP-Rule:MF_00279}; GN OrderedLocusNames=NMB0448; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the complicated ring closure reaction between CC the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and CC 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) CC to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2- CC oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00279}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00279}. CC -!- SIMILARITY: Belongs to the PNP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00279}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40885.1; -; Genomic_DNA. DR PIR; B81197; B81197. DR RefSeq; NP_273495.1; NC_003112.2. DR RefSeq; WP_002224937.1; NC_003112.2. DR ProteinModelPortal; Q9K0V9; -. DR SMR; Q9K0V9; 1-239. DR STRING; 122586.NMB0448; -. DR PaxDb; Q9K0V9; -. DR EnsemblBacteria; AAF40885; AAF40885; NMB0448. DR GeneID; 902564; -. DR KEGG; nme:NMB0448; -. DR PATRIC; 20356108; VBINeiMen85645_0570. DR eggNOG; ENOG4105CSZ; Bacteria. DR eggNOG; COG0854; LUCA. DR HOGENOM; HOG000258094; -. DR KO; K03474; -. DR OMA; ERHIRYQ; -. DR OrthoDB; EOG6M9F0H; -. DR BioCyc; NMEN122586:GHGG-472-MONOMER; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033856; F:pyridoxine 5'-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00279; PdxJ; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004569; PyrdxlP_synth_PdxJ. DR Pfam; PF03740; PdxJ; 1. DR SUPFAM; SSF63892; SSF63892; 1. DR TIGRFAMs; TIGR00559; pdxJ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Pyridoxine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 242 Pyridoxine 5'-phosphate synthase. FT /FTId=PRO_0000190120. FT REGION 8 9 1-deoxy-D-xylulose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT REGION 212 213 3-amino-2-oxopropyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT ACT_SITE 42 42 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00279}. FT ACT_SITE 69 69 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00279}. FT ACT_SITE 190 190 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00279}. FT BINDING 6 6 3-amino-2-oxopropyl phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT BINDING 17 17 3-amino-2-oxopropyl phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT BINDING 44 44 1-deoxy-D-xylulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT BINDING 49 49 1-deoxy-D-xylulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT BINDING 99 99 1-deoxy-D-xylulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00279}. FT BINDING 191 191 3-amino-2-oxopropyl phosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00279}. FT SITE 150 150 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00279}. SQ SEQUENCE 242 AA; 26566 MW; 5DA0476728AA1485 CRC64; MLLGVNIDHI ATVRNARGTT YPSPVEAALV AETHGADLIT MHLREDRRHI KDADVFAVKN AIRTRLNLEM ALTEEMLENA LKVMPEDVCI VPEKRQEITT EGGLDVLAQQ EKIAGFTKIL TDAGIRVSLF IDADDRQIQA ARDVGAPVVE LHTGAYADAR SHAEQIRQFE RIQNGAHFAG DLGLVVNAGH GLTIHNVTPI AQILAIRELN IGHSLIAQAL FLGLPEAVRQ MKEAMFRARL LP // ID PANC_NEIMB Reviewed; 278 AA. AC P57036; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158}; DE Short=PS {ECO:0000255|HAMAP-Rule:MF_00158}; DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158}; GN Name=panC {ECO:0000255|HAMAP-Rule:MF_00158}; GN OrderedLocusNames=NMB0871; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine CC in an ATP-dependent reaction via a pantoyl-adenylate intermediate. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + CC diphosphate + (R)-pantothenate. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong CC mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41282.1; -; Genomic_DNA. DR PIR; G81148; G81148. DR RefSeq; NP_273912.1; NC_003112.2. DR RefSeq; WP_002222669.1; NC_003112.2. DR ProteinModelPortal; P57036; -. DR SMR; P57036; 1-277. DR STRING; 122586.NMB0871; -. DR PaxDb; P57036; -. DR EnsemblBacteria; AAF41282; AAF41282; NMB0871. DR GeneID; 902987; -. DR KEGG; nme:NMB0871; -. DR PATRIC; 20357137; VBINeiMen85645_1085. DR eggNOG; ENOG4107R03; Bacteria. DR eggNOG; COG0414; LUCA. DR HOGENOM; HOG000175516; -. DR KO; K01918; -. DR OMA; DMAMLEN; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NMEN122586:GHGG-904-MONOMER; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00158; PanC; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00018; panC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis; Reference proteome. FT CHAIN 1 278 Pantothenate synthetase. FT /FTId=PRO_0000128248. FT NP_BIND 26 33 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT NP_BIND 144 147 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT NP_BIND 181 184 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT ACT_SITE 33 33 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 57 57 Beta-alanine. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 57 57 Pantoate. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 150 150 Pantoate. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 173 173 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00158}. SQ SEQUENCE 278 AA; 31081 MW; 5E71D92FB0E6F6B3 CRC64; MQIIHTIREL RAWRKNAGKV AFVPTMGNLH EGHLALVREA KKRADSVVVS IFVNRLQFGQ GEDFDKYPRT LQQDADKLAA EGIAVVFAPD EKELYPNVEQ RYNVEPPNLQ NELCGKFRPG HFRGVATVVS KLFHIVSPDI ACFGKKDYQQ LAVIKGFVED LNFDVEIVPV DTGRAEDGLA LSSRNQYLSA AERDEAPRLY RELKAVAESL VQGSLDYAGL EKRAVQSLTE YGWVVDYVEI RRADTLEVAR AGDKKLVVLA AACLGTTRLI DNLEIKLP // ID PBP2_NEIMB Reviewed; 581 AA. AC P0A0U9; P11882; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Penicillin-binding protein 2; DE Short=PBP-2; GN Name=penA; OrderedLocusNames=NMB0413; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C311 / Serogroup B; RX PubMed=2503813; DOI=10.1093/nar/17.13.5383; RA Xhang Q.-Y., Spratt B.G.; RT "Nucleotide sequence of the penicillin-binding protein 2 gene of RT Neisseria meningitidis."; RL Nucleic Acids Res. 17:5383-5383(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Synthesis of cross-linked peptidoglycan from the lipid CC intermediates. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. CC -!- DOMAIN: The enzyme has an N-terminal penicillin insensitive CC transglycosylase domain (formation of linear glycan strands) and a CC C-terminal penicillin-sensitive transpeptidase domain (cross- CC linking of the peptide subunits). CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X15276; CAA33347.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40852.1; -; Genomic_DNA. DR PIR; S04857; S04857. DR RefSeq; NP_273462.1; NC_003112.2. DR RefSeq; WP_002218783.1; NC_003112.2. DR ProteinModelPortal; P0A0U9; -. DR STRING; 122586.NMB0413; -. DR PaxDb; P0A0U9; -. DR DNASU; 902529; -. DR EnsemblBacteria; AAF40852; AAF40852; NMB0413. DR GeneID; 902529; -. DR KEGG; nme:NMB0413; -. DR PATRIC; 20356015; VBINeiMen85645_0523. DR eggNOG; ENOG4105CJN; Bacteria. DR eggNOG; COG0768; LUCA. DR HOGENOM; HOG000049554; -. DR KO; K03587; -. DR OMA; FVINREE; -. DR OrthoDB; EOG6N0HHV; -. DR BioCyc; NMEN122586:GHGG-437-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003824; F:catalytic activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR005311; PBP_dimer. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF03717; PBP_dimer; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56519; SSF56519; 1. DR SUPFAM; SSF56601; SSF56601; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell cycle; Cell division; Cell inner membrane; KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Membrane; Multifunctional enzyme; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 581 Penicillin-binding protein 2. FT /FTId=PRO_0000195452. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT ACT_SITE 310 310 Acyl-ester intermediate. SQ SEQUENCE 581 AA; 63604 MW; BABC396F205D2F6B CRC64; MLIKSEYKPR MLPKEEQVKK PMTSNGRISF VLMAIAVLFA GLIARGLYLQ TVTYNFLKEQ GDNRIVRTQT LPATRGTVSD RNGAVLALSA PTESLFAVPK EMKEMPSAAQ LERLSELVDV PVDVLRNKLE QKGKSFIWIK RQLDPKVAEE VKALGLENFV FEKELKRHYP MGNLFAHVIG FTDIDGKGQE GLELSLEDSL HGEDGAEVVL RDRQGNIVDS LDSPRNKAPK NGKDIILSLD QRIQTLAYEE LNKAVEYHQA KAGTVVVLDA RTGEILALAN TPAYDPNRPG RADSEQRRNR AVTDMIEPGS AIKPFVIAKA LDAGKTDLNE RLNTQPYKIG PSPVRDTHVY PSLDVRGIMQ KSSNVGTSKL SARFGAEEMY DFYHELGIGV RMHSGFPGET AGLLRNWRRW RPIEQATMSF GYGLQLSLLQ LARAYTALTH DGVLLPVSFE KQAVAPQGKR IFKESTAREV RNLMVSVTEP GGTGTAGAVD GFDVGAKTGT ARKFVNGRYA DNKHIATFIG FAPAKNPRVI VAVTIDEPTA HGYYGGVVAG PPFKKIMGGS LNILGISPTK PLTAAAVKTP S // ID PDXA_NEIMB Reviewed; 329 AA. AC Q9K1F9; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 13-APR-2016, entry version 94. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536}; GN OrderedLocusNames=NMB0195; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4- CC (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4- CC (phosphohydroxy)butyric acid which spontaneously decarboxylates to CC form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000255|HAMAP- CC Rule:MF_00536}. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino- CC 2-oxopropyl phosphate + CO(2) + NADH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536}; CC Note=Binds 1 divalent metal cation per subunit. Can use ions such CC as Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP- CC Rule:MF_00536}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40652.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40652.1; ALT_INIT; Genomic_DNA. DR PIR; H81227; H81227. DR RefSeq; NP_273253.1; NC_003112.2. DR RefSeq; WP_010980757.1; NC_003112.2. DR ProteinModelPortal; Q9K1F9; -. DR SMR; Q9K1F9; 1-327. DR STRING; 122586.NMB0195; -. DR PaxDb; Q9K1F9; -. DR EnsemblBacteria; AAF40652; AAF40652; NMB0195. DR GeneID; 902303; -. DR KEGG; nme:NMB0195; -. DR PATRIC; 20355423; VBINeiMen85645_0240. DR eggNOG; ENOG4105CEZ; Bacteria. DR eggNOG; COG1995; LUCA. DR HOGENOM; HOG000221592; -. DR KO; K00097; -. DR OMA; YVWDTPL; -. DR OrthoDB; EOG6GN6ZC; -. DR BioCyc; NMEN122586:GHGG-206-MONOMER; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_00536; PdxA; 1. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR005255; PdxA. DR Pfam; PF04166; PdxA; 1. DR TIGRFAMs; TIGR00557; pdxA; 1. PE 3: Inferred from homology; KW Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; NAD; KW NADP; Oxidoreductase; Pyridoxine biosynthesis; Reference proteome; KW Zinc. FT CHAIN 1 329 4-hydroxythreonine-4-phosphate FT dehydrogenase. FT /FTId=PRO_0000188812. FT METAL 166 166 Divalent metal cation; shared with FT dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT METAL 211 211 Divalent metal cation; shared with FT dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT METAL 266 266 Divalent metal cation; shared with FT dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT BINDING 136 136 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT BINDING 137 137 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT BINDING 274 274 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT BINDING 283 283 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00536}. FT BINDING 292 292 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00536}. SQ SEQUENCE 329 AA; 34505 MW; 0126A0A7D7B16DDC CRC64; MKQPVFAVTS GEPAGIGPDI CLDLAFARLP CRCAVLGDKN LLRARAEALG KSVVLRDFDP ESGGAAYGEL EVLHIPAVEA VEAGKLNPAN AAYVLQLLDT ALAGISDGIF DGIVTAPLHK GIINDARAST GFFSGHTEYL AEKSGTGQVV MMLAGKGLRV ALVTTHLPLK DVAAAITQPL IESVARILHH DLKHKFGIKN PKILVAGLNP HAGEGGHLGH EETDTIIPAL ENLRREGINL AGPYPADTLF QPFMLEGADA VLAMYHDQGL PVLKYHSFGQ GVNITLGLPF IRTSVDHGTA LDLAATGRAD SGSLITAVET AVEMARGSL // ID PILQ_NEIMB Reviewed; 769 AA. AC Q70M91; Q4W562; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 16-MAR-2016, entry version 69. DE RecName: Full=Type IV pilus biogenesis and competence protein PilQ; DE Flags: Precursor; GN Name=pilQ; OrderedLocusNames=NMB1812; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ELECTRON CRYOMICROSCOPY. RC STRAIN=CCUG 37602 / M1080 / Serogroup B / Serotype 1; RX PubMed=15254043; DOI=10.1074/jbc.M405971200; RA Collins R.F., Frye S.A., Kitmitto A., Ford R.C., Toenjum T., RA Derrick J.P.; RT "Structure of the Neisseria meningitidis outer membrane PilQ secretin RT complex at 12 A resolution."; RL J. Biol. Chem. 279:39750-39756(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP SUBUNIT. RC STRAIN=CCUG 37602 / M1080 / Serogroup B / Serotype 1; RX PubMed=11395444; DOI=10.1128/JB.183.13.3825-3832.2001; RA Collins R.F., Davidsen L., Derrick J.P., Ford R.C., Toenjum T.; RT "Analysis of the PilQ secretin from Neisseria meningitidis by RT transmission electron microscopy reveals a dodecameric quaternary RT structure."; RL J. Bacteriol. 183:3825-3832(2001). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Required for type IV pilus biogenesis and competence. CC Could function as a pore for exit of the pilus but also as a CC channel for entry of heme and antimicrobial agents and uptake of CC transforming DNA (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homododecamer. Tetramer of trimer. CC {ECO:0000269|PubMed:11395444}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the GSP D family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ564200; CAD91899.1; -; Genomic_DNA. DR EMBL; AE002098; AAY52170.1; -; Genomic_DNA. DR RefSeq; NP_274809.1; NC_003112.2. DR RefSeq; WP_002225652.1; NC_003112.2. DR PDB; 4AQZ; NMR; -; A=224-329. DR PDB; 4AV2; EM; 26.00 A; A/B/C/D/E/F/G/H/I/J/K/L=25-769. DR PDBsum; 4AQZ; -. DR PDBsum; 4AV2; -. DR IntAct; Q70M91; 1. DR STRING; 122586.NMB1812; -. DR PaxDb; Q70M91; -. DR EnsemblBacteria; AAY52170; AAY52170; NMB1812. DR GeneID; 903122; -. DR KEGG; nme:NMB1812; -. DR PATRIC; 20359593; VBINeiMen85645_2302. DR eggNOG; ENOG4105E4G; Bacteria. DR eggNOG; COG4796; LUCA. DR HOGENOM; HOG000255072; -. DR KO; K02666; -. DR OMA; HAIFQAC; -. DR OrthoDB; EOG6423BN; -. DR BioCyc; NMEN122586:GHGG-1867-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0009297; P:pilus assembly; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR021731; AMIN_dom. DR InterPro; IPR001775; GspD/PilQ. DR InterPro; IPR005644; NolW-like. DR InterPro; IPR013355; Pilus_4_PilQ. DR InterPro; IPR011662; Secretin/TonB_short_N. DR InterPro; IPR004846; T2SS/T3SS. DR InterPro; IPR004845; T2SS_GspD_CS. DR Pfam; PF11741; AMIN; 1. DR Pfam; PF00263; Secretin; 1. DR Pfam; PF03958; Secretin_N; 1. DR Pfam; PF07660; STN; 1. DR PRINTS; PR00811; BCTERIALGSPD. DR SMART; SM00965; STN; 1. DR TIGRFAMs; TIGR02515; IV_pilus_PilQ; 1. DR PROSITE; PS00875; T2SP_D; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Competence; Complete proteome; KW Membrane; Protein transport; Reference proteome; Signal; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 769 Type IV pilus biogenesis and competence FT protein PilQ. FT /FTId=PRO_0000013117. FT VARIANT 203 203 A -> T (in strain: CCUG 37602). FT VARIANT 218 225 Missing (in strain: CCUG 37602). FT VARIANT 428 428 L -> F (in strain: CCUG 37602). FT VARIANT 461 461 R -> A (in strain: CCUG 37602). FT VARIANT 475 475 I -> V (in strain: CCUG 37602). FT VARIANT 607 607 T -> P (in strain: CCUG 37602). FT STRAND 227 233 {ECO:0000244|PDB:4AQZ}. FT TURN 234 236 {ECO:0000244|PDB:4AQZ}. FT STRAND 237 243 {ECO:0000244|PDB:4AQZ}. FT STRAND 252 255 {ECO:0000244|PDB:4AQZ}. FT STRAND 257 264 {ECO:0000244|PDB:4AQZ}. FT TURN 271 273 {ECO:0000244|PDB:4AQZ}. FT STRAND 282 293 {ECO:0000244|PDB:4AQZ}. FT STRAND 295 304 {ECO:0000244|PDB:4AQZ}. FT STRAND 306 316 {ECO:0000244|PDB:4AQZ}. FT STRAND 319 326 {ECO:0000244|PDB:4AQZ}. SQ SEQUENCE 769 AA; 82473 MW; 1CC24EF102DC4BC9 CRC64; MNTKLTKIIS GLFVATAAFQ TASAGNITDI KVSSLPNKQK IVKVSFDKEI VNPTGFVTSS PARIALDFEQ TGISMDQQVL EYADPLLSKI SAAQNSSRAR LVLNLNKPGQ YNTEVRGNKV WIFINESDDT VSAPARPAVK AAPAAPAKQQ AAAPSTKSAV SVSEPFTPAK QQAAAPFTES VVSVSAPFSP AKQQAAASAK QQAAAPAKQQ AAAPAKQQAA APAKQTNIDF RKDGKNAGII ELAALGFAGQ PDISQQHDHI IVTLKNHTLP TTLQRSLDVA DFKTPVQKVT LKRLNNDTQL IITTAGNWEL VNKSAAPGYF TFQVLPKKQN LESGGVNNAP KTFTGRKISL DFQDVEIRTI LQILAKESGM NIVASDSVNG KMTLSLKDVP WDQALDLVMQ ARNLDMRQQG NIVNIAPRDE LLAKDKALLQ AEKDIADLGA LYSQNFQLKY KNVEEFRSIL RLDNADTTGN RNTLISGRGS VLIDPATNTL IVTDTRSVIE KFRKLIDELD VPAQQVMIEA RIVEAADGFS RDLGVKFGAT GKKKLKNDTS AFGWGVNSGF GGDDKWGAET KINLPITAAA NSISLVRAIS SGALNLELSA SESLSKTKTL ANPRVLTQNR KEAKIESGYE IPFTVTSIAN GGSSTNTELK KAVLGLTVTP NITPDGQIIM TVKINKDSPA QCASGNQTIL CISTKNLNTQ AMVENGGTLI VGGIYEEDNG NTLTKVPLLG DIPVIGNLFK TRGKKTDRRE LLIFITPRIM GTAGNSLRY // ID PGM_NEIMB Reviewed; 460 AA. AC P40391; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 107. DE RecName: Full=Phosphoglucomutase; DE Short=PGM; DE EC=5.4.2.2; DE AltName: Full=Glucose phosphomutase; GN Name=pgm; OrderedLocusNames=NMB0790; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NMB / Serogroup B; RX PubMed=8157643; RA Zhou D., Stephens D.S., Gibson B.W., Engstrom J.J., McAllister C.F., RA Lee F.K.N., Apicella M.A.; RT "Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning, RT identification, and characterization of the phosphoglucomutase gene."; RL J. Biol. Chem. 269:11162-11169(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This enzyme participates in both the breakdown and CC synthesis of glucose. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose CC 6-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U02490; AAA20589.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41203.1; -; Genomic_DNA. DR PIR; B53614; B53614. DR PIR; C81159; C81159. DR RefSeq; NP_273832.1; NC_003112.2. DR RefSeq; WP_010980847.1; NC_003112.2. DR ProteinModelPortal; P40391; -. DR SMR; P40391; 3-452. DR STRING; 122586.NMB0790; -. DR PaxDb; P40391; -. DR EnsemblBacteria; AAF41203; AAF41203; NMB0790. DR GeneID; 902905; -. DR KEGG; nme:NMB0790; -. DR PATRIC; 20356967; VBINeiMen85645_1002. DR eggNOG; ENOG4107QKV; Bacteria. DR eggNOG; COG1109; LUCA. DR HOGENOM; HOG000268679; -. DR KO; K01835; -. DR OMA; AWFNLRA; -. DR OrthoDB; EOG6W9X55; -. DR BioCyc; NMEN122586:GHGG-821-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Glucose metabolism; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 460 Phosphoglucomutase. FT /FTId=PRO_0000147812. FT REGION 103 104 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT REGION 243 244 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT REGION 322 324 Substrate binding. FT {ECO:0000250|UniProtKB:P00949}. FT ACT_SITE 103 103 Phosphoserine intermediate. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 103 103 Magnesium; via phosphate group. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 239 239 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 241 241 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT METAL 243 243 Magnesium. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 113 113 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT BINDING 303 303 Substrate. FT {ECO:0000250|UniProtKB:P00949}. FT CONFLICT 140 140 A -> R (in Ref. 1; AAA20589). FT {ECO:0000305}. FT CONFLICT 195 195 K -> E (in Ref. 1; AAA20589). FT {ECO:0000305}. FT CONFLICT 277 277 V -> A (in Ref. 1; AAA20589). FT {ECO:0000305}. FT CONFLICT 282 282 K -> E (in Ref. 1; AAA20589). FT {ECO:0000305}. FT CONFLICT 287 287 L -> V (in Ref. 1; AAA20589). FT {ECO:0000305}. FT CONFLICT 357 357 S -> T (in Ref. 1; AAA20589). FT {ECO:0000305}. SQ SEQUENCE 460 AA; 49476 MW; BAA17FD8C6A4A298 CRC64; MASIARDIFK AYDIRGIVGK TLTDEAAYLI GKAIAAKAAE KGITRIALGR DGRLSGPELM EHIRRGFTDS GINVLNVGMV ATPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT LAGEAIQELL SIIEKDGFAA AGKQGSVTEK DISGEYLKHI TGHIRLKRPM NIAIDAGNGV GGAFAGKLYK GLGNKVTELF CDVDGTFPNH HPDPSKPKNL QDLIAALKNG DAEIGLAFDG DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGKAIM EKTGHSFIKS AMKETGAPVA GEMSGHIFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL NNLPQSISTP ELNIALPEGS NGHQVIDELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA SNTTPILVLR FEADTQEAIE RIQNQFKAVI ESNPNLIWPL // ID PLSX_NEIMB Reviewed; 351 AA. AC Q9JXR8; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; DE EC=2.3.1.n2 {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; GN OrderedLocusNames=NMB1913; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate CC (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This CC enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + phosphate = CC acyl-phosphate + [acyl-carrier-protein]. {ECO:0000255|HAMAP- CC Rule:MF_00019}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}. CC Note=Associated with the membrane possibly through PlsY. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP- CC Rule:MF_00019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42243.1; -; Genomic_DNA. DR PIR; H81028; H81028. DR RefSeq; NP_274907.1; NC_003112.2. DR RefSeq; WP_010981006.1; NC_003112.2. DR ProteinModelPortal; Q9JXR8; -. DR STRING; 122586.NMB1913; -. DR PaxDb; Q9JXR8; -. DR EnsemblBacteria; AAF42243; AAF42243; NMB1913. DR GeneID; 904250; -. DR KEGG; nme:NMB1913; -. DR PATRIC; 20359871; VBINeiMen85645_2440. DR eggNOG; ENOG4105C6B; Bacteria. DR eggNOG; COG0416; LUCA. DR HOGENOM; HOG000154730; -. DR KO; K03621; -. DR OMA; KFCLRTM; -. DR OrthoDB; EOG68H88P; -. DR BioCyc; NMEN122586:GHGG-1970-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_00019; PlsX; 1. DR InterPro; IPR003664; FA_synthesis. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR012281; Phospholipid_synth_PlsX-like. DR Pfam; PF02504; FA_synthesis; 1. DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1. DR TIGRFAMs; TIGR00182; plsX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 351 Phosphate acyltransferase. FT /FTId=PRO_0000189912. SQ SEQUENCE 351 AA; 37006 MW; 392B5F6A59023095 CRC64; MITLAVDAMG GDQGLAVTVP GATAFLQAHP DVRLIMTGDE TQLRQALTAA GAPMERIDIC HTTQVVGMDE APQSALKNKK DSSMRVAINQ VKEGKAQAAV SAGNTGALMA TARFVLKTIP GIERPAIAKF LPSDTDHVTL ALDLGANVDC TSEQLAQFAV IGSELVHALH PQKGQPRVGL VNVGTEDIKG TDTVKQTYKL LQNSKLNFIG NIESNGILYG EADVVVADGF VGNVMLKTIE GAVKFMSGAI RREFQSNLFN KLAAVAALPA LKGLKNKLDP RKFNGAILLG LRGIVIKSHG GTDETGFRYA LEEAYHEAKS AGLSKIEQGV AEQLAALETA KAVQNENVGG L // ID PGK_NEIMB Reviewed; 392 AA. AC Q9K1R0; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 2. DT 11-NOV-2015, entry version 84. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=NMB0010; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40489.1; Type=Miscellaneous discrepancy; Note=Probable incorrect perfect sequence repeat which was excised.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40489.1; ALT_SEQ; Genomic_DNA. DR PIR; H81247; H81247. DR RefSeq; NP_273076.1; NC_003112.2. DR ProteinModelPortal; Q9K1R0; -. DR SMR; Q9K1R0; 3-391. DR STRING; 122586.NMB0010; -. DR PaxDb; Q9K1R0; -. DR EnsemblBacteria; AAF40489; AAF40489; NMB0010. DR GeneID; 902112; -. DR KEGG; nme:NMB0010; -. DR PATRIC; 20354949; VBINeiMen85645_0011. DR eggNOG; ENOG4105BZA; Bacteria. DR eggNOG; COG0126; LUCA. DR HOGENOM; HOG000227107; -. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR OrthoDB; EOG64N9Z0; -. DR BioCyc; NMEN122586:GHGG-10-MONOMER; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1260; -; 1. DR Gene3D; 3.40.50.1270; -; 1. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015901; Phosphoglycerate_kinase_C. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR PANTHER; PTHR11406; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; SSF53748; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 392 Phosphoglycerate kinase. FT /FTId=PRO_0000145976. FT NP_BIND 346 349 ATP. {ECO:0000250}. FT REGION 21 23 Substrate binding. {ECO:0000250}. FT REGION 59 62 Substrate binding. {ECO:0000250}. FT BINDING 36 36 Substrate. {ECO:0000250}. FT BINDING 114 114 Substrate. {ECO:0000250}. FT BINDING 147 147 Substrate. {ECO:0000250}. FT BINDING 198 198 ATP. {ECO:0000250}. FT BINDING 320 320 ATP. {ECO:0000250}. FT CONFLICT 281 281 A -> AADAEAVVKDIA (in Ref. 1). FT {ECO:0000305}. SQ SEQUENCE 392 AA; 40632 MW; 9011CDD6661B04BD CRC64; MAFLKLTEQN VQGKTVLIRA DMNVPFKDGK ISDDTRIRAS LASIKYCVDN GASVIVMTHL GRPTEGEFHP EDDVAPVAAH LGSLLGKDVK VLNDWRENKP ALNAGDVVML QNVRINKGEK KNDLELGKAY ASLCDVFVND AFGTAHRAQA STEAVAQAAP VACAGVLMAG ELDALGKALK QPARPMVAIV AGSKVSTKLT ILESLADKVD QLIVGGGIAN TFLLAEGKAI GKSLAEHDLV EESKKIMAKM AAKGGSVPLP TDVVVAKAFA ADAEAVVKDI ADVAEDEMIL DIGPKSAAAL ADLLKAAGTV VWNGPVGVFE FDQFAGGTKA LAEAIAQSKA FSIAGGGDTL AAIAKFGVTE QIGYISTGGG AFLEFLEGKE LPAVAALEKR GA // ID PIP_NEIMB Reviewed; 310 AA. AC Q9JZR6; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Proline iminopeptidase; DE Short=PIP; DE EC=3.4.11.5; DE AltName: Full=Prolyl aminopeptidase; DE Short=PAP; GN Name=pip; OrderedLocusNames=NMB0927; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline CC residues from peptides. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41334.1; -; Genomic_DNA. DR PIR; B81141; B81141. DR RefSeq; NP_273966.1; NC_003112.2. DR RefSeq; WP_002225339.1; NC_003112.2. DR ProteinModelPortal; Q9JZR6; -. DR STRING; 122586.NMB0927; -. DR ESTHER; neigo-pip; Proline_iminopeptidase. DR MEROPS; S33.001; -. DR PaxDb; Q9JZR6; -. DR EnsemblBacteria; AAF41334; AAF41334; NMB0927. DR GeneID; 903048; -. DR KEGG; nme:NMB0927; -. DR PATRIC; 20357323; VBINeiMen85645_1176. DR eggNOG; ENOG4108HGY; Bacteria. DR eggNOG; COG0596; LUCA. DR HOGENOM; HOG000171480; -. DR KO; K01259; -. DR OMA; VSEMFPD; -. DR OrthoDB; EOG6BPDDC; -. DR BioCyc; NMEN122586:GHGG-965-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR InterPro; IPR005944; Pro_iminopeptidase. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF006431; Pept_S33; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 310 Proline iminopeptidase. FT /FTId=PRO_0000080843. FT ACT_SITE 107 107 Nucleophile. {ECO:0000250}. FT ACT_SITE 260 260 {ECO:0000250}. FT ACT_SITE 287 287 Proton donor. {ECO:0000250}. SQ SEQUENCE 310 AA; 34957 MW; 9F883415B1C7B4A2 CRC64; MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI VIIDQRGCGR SRPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH PERVKGLVLR GIFLCRPSET VWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL FHQDEEVCLS AAKAWADWES YLIRFEPEEV DEDAYASLAI ARLENHYFVN GGWLQGDRAI LNNIGKIRHI PTIIVQGRYD LCTPMQSAWA LSKAFPEAEL RVVQAGHRAF DPPLVDALVQ AVEDILPHLL // ID PNP_NEIMB Reviewed; 707 AA. AC Q9K062; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595}; DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595}; DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595}; DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595}; GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=NMB0758; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the CC phosphorolysis of single-stranded polyribonucleotides processively CC in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the polyribonucleotide CC nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41171.1; -; Genomic_DNA. DR PIR; C81161; C81161. DR RefSeq; NP_273800.1; NC_003112.2. DR RefSeq; WP_010980838.1; NC_003112.2. DR ProteinModelPortal; Q9K062; -. DR SMR; Q9K062; 618-693. DR STRING; 122586.NMB0758; -. DR PaxDb; Q9K062; -. DR EnsemblBacteria; AAF41171; AAF41171; NMB0758. DR GeneID; 902873; -. DR KEGG; nme:NMB0758; -. DR PATRIC; 20356887; VBINeiMen85645_0962. DR eggNOG; ENOG4105C62; Bacteria. DR eggNOG; COG1185; LUCA. DR HOGENOM; HOG000218327; -. DR KO; K00962; -. DR OMA; RFMFHYN; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NMEN122586:GHGG-789-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 1.10.10.400; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1370.10; -; 1. DR Gene3D; 3.30.230.70; -; 2. DR HAMAP; MF_01595; PNPase; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012162; PNPase. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR PANTHER; PTHR11252; PTHR11252; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF03726; PNPase; 1. DR Pfam; PF01138; RNase_PH; 2. DR Pfam; PF03725; RNase_PH_C; 2. DR Pfam; PF00575; S1; 1. DR PIRSF; PIRSF005499; PNPase; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR SUPFAM; SSF54791; SSF54791; 1. DR SUPFAM; SSF55666; SSF55666; 2. DR TIGRFAMs; TIGR03591; polynuc_phos; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase. FT CHAIN 1 707 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000320268. FT DOMAIN 554 613 KH. {ECO:0000255|HAMAP-Rule:MF_01595}. FT DOMAIN 623 693 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 488 488 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 494 494 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. SQ SEQUENCE 707 AA; 76422 MW; 89ED8E26B9C6C46F CRC64; MMFDKHVKTF QYGNQTVTLE TGEIARQAAA AVKVSMGDTV VLVAVTTNKE VKEGQDFFPL TVDYLERTYA AGKIPGGFFK REGKQSEKEI LTSRLIDRPI RPLFPEGFYH DIQIVAMVVS VDPEIDSDIP AMLGASAALV LSGVPFAGPI GAARVGYVNG VYVLNPTKAE LAKSQLDLVV AGTSKAVLMV ESEAKILPED VMLGAVVYGH DQMQVAINAI NEFADEVNPE LWDWKAPETN EELVAKVRGI AGETIKEAFK IRQKQARSAK LDEAWSAVKE ALITEETDTL AANEIKGIFK HLEADVVRSQ ILDGQPRIDG RDTRTVRPLN IQTSVLPRTH GSALFTRGET QALAVATLGT SRDEQIIDAL SGEYTDRFML HYNFPPYSTG EVGRMGAPKR REIGHGRLAK RALLAVLPKP EDFSYTMRVV SEITESNGSS SMASVCGGCL SLLSAGVPLK AHVAGIAMGL ILEGNKFAVL TDILGDEDHL GDMDFKVAGT TEGVTALQMD IKIQGITKEI MQIALAQAKE ARLHILDQMK AAVAGPQELS AHAPRLFTMK INQDKIREVI GKGGETIRSI TAETGTEINI AEDGTITIAA TTQEAGDAAK KRIEQITAEV EVGKVYEGTV VKILDNNVGA IVSVMPGKDG LVHISQIAHE RVRNVGDYLQ VGQVVNVKAL EVDDRGRVRL SIKALLDAPA REENAAE // ID PLSC_NEIMB Reviewed; 255 AA. AC Q9JZ47; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase; DE Short=1-AGP acyltransferase; DE Short=1-AGPAT; DE EC=2.3.1.51; DE AltName: Full=Lysophosphatidic acid acyltransferase; DE Short=LPAAT; GN Name=plsC; OrderedLocusNames=NMB1294; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic CC acid by incorporating acyl moiety at the 2 position. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity CC and may constitute the binding site for the phosphate moiety of CC the glycerol-3-phosphate. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41670.1; -; Genomic_DNA. DR PIR; A81099; A81099. DR RefSeq; NP_274314.1; NC_003112.2. DR RefSeq; WP_002217072.1; NC_003112.2. DR ProteinModelPortal; Q9JZ47; -. DR STRING; 122586.NMB1294; -. DR PaxDb; Q9JZ47; -. DR EnsemblBacteria; AAF41670; AAF41670; NMB1294. DR GeneID; 903716; -. DR KEGG; nme:NMB1294; -. DR PATRIC; 20358215; VBINeiMen85645_1619. DR eggNOG; ENOG4108Z20; Bacteria. DR eggNOG; COG0204; LUCA. DR HOGENOM; HOG000220746; -. DR KO; K00655; -. DR OMA; EMAPRRQ; -. DR OrthoDB; EOG654P6D; -. DR BioCyc; NMEN122586:GHGG-1332-MONOMER; -. DR UniPathway; UPA00557; UER00613. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR004552; AGP_acyltrans. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 255 1-acyl-sn-glycerol-3-phosphate FT acyltransferase. FT /FTId=PRO_0000208176. FT MOTIF 78 83 HXXXXD motif. SQ SEQUENCE 255 AA; 27943 MW; F262C2BE7B2F2AD7 CRC64; MSSNKASFFT RLRRLCRLAV WLFKTGKNLR GIDGGCPESR NRAVIELGRG VLAALDIGLE VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIRVDF VCVADAAESE DRYALKDKIE ESIRAVVADD ADIAV // ID PLSY_NEIMB Reviewed; 200 AA. AC Q9JZG9; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=G3P acyltransferase {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=GPAT {ECO:0000255|HAMAP-Rule:MF_01043}; DE EC=2.3.1.n3 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Lysophosphatidic acid synthase {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=LPA synthase {ECO:0000255|HAMAP-Rule:MF_01043}; GN Name=plsY {ECO:0000255|HAMAP-Rule:MF_01043}; GN OrderedLocusNames=NMB1062; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl- CC phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form CC lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate CC as fatty acyl donor, but not acyl-CoA or acyl-ACP. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1- CC acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41458.1; -; Genomic_DNA. DR PIR; H81126; H81126. DR RefSeq; NP_274095.1; NC_003112.2. DR RefSeq; WP_002225265.1; NC_003112.2. DR STRING; 122586.NMB1062; -. DR PaxDb; Q9JZG9; -. DR EnsemblBacteria; AAF41458; AAF41458; NMB1062. DR GeneID; 903479; -. DR KEGG; nme:NMB1062; -. DR PATRIC; 20357667; VBINeiMen85645_1350. DR eggNOG; ENOG4105K7Z; Bacteria. DR eggNOG; COG0344; LUCA. DR HOGENOM; HOG000283806; -. DR KO; K08591; -. DR OMA; HIWPVWL; -. DR OrthoDB; EOG6M6JSX; -. DR BioCyc; NMEN122586:GHGG-1099-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01043; PlsY; 1. DR InterPro; IPR003811; G3P_acylTferase_PlsY. DR PANTHER; PTHR30309:SF0; PTHR30309:SF0; 1. DR Pfam; PF02660; G3P_acyltransf; 1. DR SMART; SM01207; G3P_acyltransf; 1. DR TIGRFAMs; TIGR00023; TIGR00023; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 200 Glycerol-3-phosphate acyltransferase. FT /FTId=PRO_0000188411. FT TRANSMEM 2 22 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 51 71 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 84 104 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 114 134 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 159 179 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 200 AA; 20685 MW; 6C46910188A6DA45 CRC64; MFNIPAVAVS YLIGSLSFAV IVSKYYGMDD PRTYGSGNPG ATNVLRSGKK KAAALTLLGD AAKGLVAVLL ARVLQEPLGL SDSAIAAVAL AALVGHMWPV FFGFKGGKGV ATALGVLLAL SPATALVCAL IWLVMAFGFK VSSLAALTAT IAAPVAASFF MPHVSWVWAT VAIALLVLFR HKSNIVKLLE GRESKIGGSR // ID PRMB_NEIMB Reviewed; 303 AA. AC Q9JYC0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=50S ribosomal protein L3 glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02125}; DE Short=L3 MTase {ECO:0000255|HAMAP-Rule:MF_02125}; DE EC=2.1.1.298 {ECO:0000255|HAMAP-Rule:MF_02125}; DE AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000255|HAMAP-Rule:MF_02125}; GN Name=prmB {ECO:0000255|HAMAP-Rule:MF_02125}; GN OrderedLocusNames=NMB1655; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on CC a specific glutamine residue. {ECO:0000255|HAMAP-Rule:MF_02125}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [ribosomal protein CC L3]-L-glutamine = S-adenosyl-L-homocysteine + [ribosomal protein CC L3]-N(5)-methyl-L-glutamine. {ECO:0000255|HAMAP-Rule:MF_02125}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmB subfamily. {ECO:0000255|HAMAP-Rule:MF_02125}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42004.1; -; Genomic_DNA. DR PIR; F81057; F81057. DR RefSeq; NP_274660.1; NC_003112.2. DR RefSeq; WP_002223537.1; NC_003112.2. DR ProteinModelPortal; Q9JYC0; -. DR STRING; 122586.NMB1655; -. DR PaxDb; Q9JYC0; -. DR EnsemblBacteria; AAF42004; AAF42004; NMB1655. DR GeneID; 903461; -. DR KEGG; nme:NMB1655; -. DR PATRIC; 20359236; VBINeiMen85645_2130. DR eggNOG; ENOG4105C76; Bacteria. DR eggNOG; COG2890; LUCA. DR HOGENOM; HOG000076275; -. DR KO; K07320; -. DR OMA; VLVCEVG; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; NMEN122586:GHGG-1704-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02125; L3_methyltr_PrmB; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004556; Modification_methylase_HemK. DR InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03533; L3_gln_methyl; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 303 50S ribosomal protein L3 glutamine FT methyltransferase. FT /FTId=PRO_0000088008. SQ SEQUENCE 303 AA; 33955 MW; 0D35DDFF0EC95805 CRC64; MVHIMFNQAA QELTTIRDIL RFAVSRFNEA GLFFGHGTDN AHDEAAYLIL HTLNLPLDML APYLDAKLLE AEKEEVLAVI ERRAVEHIPA AYLTHQAWQG EFDFYVDERV IIPRSFIYEL LGDGLRPWIE YDELVHNALD LCTGSGCLAI QMAHHYPDAQ IDAVDVSLDA LEVAGINVED YGLEERIRLI HTDLFEGLEG TYDLIVSNPP YVDAESVELL PEEYLHEPEL ALGSGADGLD ATRQILLNAA KFLNPKGVLL VEIGHNRDVL EAAYPELPFT WLETSGGDGF VFLLTREQLL GEE // ID PROB_NEIMB Reviewed; 369 AA. AC Q9JZG2; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Glutamate 5-kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456}; DE AltName: Full=Gamma-glutamyl kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00456}; GN Name=proB {ECO:0000255|HAMAP-Rule:MF_00456}; GN OrderedLocusNames=NMB1069; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate CC to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41464.1; -; Genomic_DNA. DR PIR; F81125; F81125. DR RefSeq; NP_274102.1; NC_003112.2. DR RefSeq; WP_002213646.1; NC_003112.2. DR ProteinModelPortal; Q9JZG2; -. DR STRING; 122586.NMB1069; -. DR PaxDb; Q9JZG2; -. DR DNASU; 903487; -. DR EnsemblBacteria; AAF41464; AAF41464; NMB1069. DR GeneID; 903487; -. DR KEGG; nme:NMB1069; -. DR PATRIC; 20357687; VBINeiMen85645_1360. DR eggNOG; ENOG4105CGT; Bacteria. DR eggNOG; COG0263; LUCA. DR HOGENOM; HOG000246369; -. DR KO; K00931; -. DR OMA; KMNKQWI; -. DR OrthoDB; EOG6PGK7G; -. DR BioCyc; NMEN122586:GHGG-1106-MONOMER; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00456; ProB; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR011529; Glu_5kinase. DR InterPro; IPR005715; Glu_5kinase/COase_Synthase. DR InterPro; IPR019797; Glutamate_5-kinase_CS. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR01027; proB; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 369 Glutamate 5-kinase. FT /FTId=PRO_0000109698. FT DOMAIN 275 355 PUA. {ECO:0000255|HAMAP-Rule:MF_00456}. FT NP_BIND 168 169 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT NP_BIND 210 216 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 9 9 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 49 49 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 136 136 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 148 148 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00456}. SQ SEQUENCE 369 AA; 39320 MW; A4ACA2C449FE0427 CRC64; MKYKRIVFKV GTSSITHSDG SLSRGKIQTI TCQLAALHHA GHELVLVSSG AVAAGFGALG FKKRPVKIAD KQASAAVGQG LLMEEYTANL SSDGIVSAQI LLSRADFADK RRYQNAGGAL SVLLQRRAVP IINENDTVSV EELKIGDNDT LSAQVAAMIQ ADLLVLLTDI DGLYTGNPNS NPDAVRLDKI EHINHEIIEM AGGSGSANGT GGMLTKIKAA TIAAESGVPV YICSSLKPDA LAEAAEHQAD GSFFVPRAKG LRTQKQWLAF YSESRGSVYV DEGAEHALSE QGKSLLMSGI AGIEGHFSRM DTVTVYSKAT KQPLGKGRVL FGSAAAEDLL KSRKAKGVFI HRDDWISITP EIRLLLTEF // ID PRMA_NEIMB Reviewed; 295 AA. AC Q9JXW2; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735}; DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735}; GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735}; GN OrderedLocusNames=NMB1862; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|HAMAP- CC Rule:MF_00735}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA CC family. {ECO:0000255|HAMAP-Rule:MF_00735}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42196.1; -; Genomic_DNA. DR PIR; G81033; G81033. DR RefSeq; NP_274858.1; NC_003112.2. DR RefSeq; WP_002223022.1; NC_003112.2. DR ProteinModelPortal; Q9JXW2; -. DR STRING; 122586.NMB1862; -. DR PaxDb; Q9JXW2; -. DR EnsemblBacteria; AAF42196; AAF42196; NMB1862. DR GeneID; 904326; -. DR KEGG; nme:NMB1862; -. DR PATRIC; 20359749; VBINeiMen85645_2380. DR eggNOG; ENOG4105F59; Bacteria. DR eggNOG; COG2264; LUCA. DR HOGENOM; HOG000007390; -. DR KO; K02687; -. DR OMA; FVHKIEQ; -. DR OrthoDB; EOG6N684G; -. DR BioCyc; NMEN122586:GHGG-1918-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00735; Methyltr_PrmA; 1. DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF000401; RPL11_MTase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00406; prmA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 295 Ribosomal protein L11 methyltransferase. FT /FTId=PRO_0000192282. SQ SEQUENCE 295 AA; 31951 MW; EA2318BE01D3591A CRC64; MPYQQITVNV NDAVAERLAD ALMEHGALSA AIEDAYAGTQ NEQAIFGEPG MPAEQIWQQS KVIALFGEHD EAAAIIQTAT QECGLKDLAY TGETIEDQDW VRLTQSQFDP IRISDRLWIT PSWHEVPEGS AVNLRLDPGL AFGTGSHPTT RLCLKWLDTQ LKNGESVLDY GCGSGILTIA ALKLGAGFAV GVDIDEQAVR AGKDNAAQNN VDAQFFLPDG LPQGQFDVVV ANILANPLRM LGEMLAARTK QGGRIVLSGL LDEQAEELGG IYSQWFDLDP AETEEGWARL SGVKR // ID PNCB_NEIMB Reviewed; 402 AA. AC Q9JYM9; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570}; DE Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570}; DE EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570}; GN Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570}; GN OrderedLocusNames=NMB1505; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D- CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate CC at the expense of ATP. {ECO:0000255|HAMAP-Rule:MF_00570}. CC -!- CATALYTIC ACTIVITY: Nicotinate + 5-phospho-alpha-D-ribose 1- CC diphosphate + ATP + H(2)O = beta-nicotinate D-ribonucleotide + CC diphosphate + ADP + phosphate. {ECO:0000255|HAMAP-Rule:MF_00570}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- CC ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00570}. CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP- CC Rule:MF_00570}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41861.1; -; Genomic_DNA. DR PIR; E81075; E81075. DR RefSeq; NP_274513.1; NC_003112.2. DR RefSeq; WP_002225072.1; NC_003112.2. DR ProteinModelPortal; Q9JYM9; -. DR STRING; 122586.NMB1505; -. DR PaxDb; Q9JYM9; -. DR EnsemblBacteria; AAF41861; AAF41861; NMB1505. DR GeneID; 903949; -. DR KEGG; nme:NMB1505; -. DR PATRIC; 20358792; VBINeiMen85645_1906. DR eggNOG; ENOG4107RH7; Bacteria. DR eggNOG; COG1488; LUCA. DR HOGENOM; HOG000284928; -. DR KO; K00763; -. DR OMA; PFIKPDF; -. DR OrthoDB; EOG6X10XB; -. DR BioCyc; NMEN122586:GHGG-1545-MONOMER; -. DR UniPathway; UPA00253; UER00457. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019357; P:nicotinate nucleotide biosynthetic process; IEA:InterPro. DR HAMAP; MF_00570; NAPRTase; 1. DR InterPro; IPR006406; Nic_PRibTrfase. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR PANTHER; PTHR11098; PTHR11098; 1. DR Pfam; PF04095; NAPRTase; 1. DR PIRSF; PIRSF000484; NAPRT; 1. DR SUPFAM; SSF51690; SSF51690; 1. DR TIGRFAMs; TIGR01514; NAPRTase; 1. PE 3: Inferred from homology; KW Complete proteome; Ligase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 402 Nicotinate phosphoribosyltransferase. FT /FTId=PRO_0000205834. SQ SEQUENCE 402 AA; 46310 MW; D6B618EEC5CC4A86 CRC64; MTGIIHSLLD TDLYKFTMLQ VVLHQFPQTH SLYEFRCRNA STVYPLADIR EDLEAELDAL CQLRFTHDEL GYLRSLRFIK SDFVDYLELF QLQRRFVEIG TDDKDRLNIR IEGPMIQAMF FEIFILAIVN ELYFRRLETP AVIEEGERRL QAKAARLKEI AAAQNPDEPP FLISDFGTRR RYKLAWQEHV IRTLLEAAPG IVRGTSNVFL AKKLGITPIG TMAHEFLQAF QALDVRLRNF QKAALESWVH EYRGDLGVAL TDVVGMDAFL RDFDLYFAKL FDGLRHDSGD PYVWGDKAYA HYQKLKIDSR TKMLTFSDGL DIERSWALHQ YFKDRFKTGF GIGTNLTNDM GHTPLNIVLK LVECNGQSVA KLSDSPGKTM TNNSTFLAYL RQVFDVPEPE TP // ID PPSA_NEIMB Reviewed; 794 AA. AC Q9K0I2; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Phosphoenolpyruvate synthase; DE Short=PEP synthase; DE EC=2.7.9.2; DE AltName: Full=Pyruvate, water dikinase; GN Name=ppsA; OrderedLocusNames=NMB0618; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to CC phosphoenolpyruvate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + H(2)O = AMP + CC phosphoenolpyruvate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, CC the central domain the pyrophosphate/phosphate carrier histidine, CC and the C-terminal domain the pyruvate binding site. CC {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated CC by a phosphocarrier histidine residue located on the surface of CC the central domain. The two first partial reactions are catalyzed CC at an active site located on the N-terminal domain, and the third CC partial reaction is catalyzed at an active site located on the C- CC terminal domain. For catalytic turnover, the central domain CC swivels from the concave surface of the N-terminal domain to that CC of the C-terminal domain (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41044.1; -; Genomic_DNA. DR PIR; G81177; G81177. DR RefSeq; NP_273662.1; NC_003112.2. DR RefSeq; WP_002222834.1; NC_003112.2. DR PDB; 2OLS; X-ray; 2.40 A; A=1-794. DR PDBsum; 2OLS; -. DR ProteinModelPortal; Q9K0I2; -. DR SMR; Q9K0I2; 4-792. DR STRING; 122586.NMB0618; -. DR PaxDb; Q9K0I2; -. DR PRIDE; Q9K0I2; -. DR EnsemblBacteria; AAF41044; AAF41044; NMB0618. DR GeneID; 902731; -. DR KEGG; nme:NMB0618; -. DR PATRIC; 20356525; VBINeiMen85645_0782. DR eggNOG; ENOG4108HRN; Bacteria. DR eggNOG; COG0574; LUCA. DR HOGENOM; HOG000230913; -. DR KO; K01007; -. DR OMA; DELHTAC; -. DR OrthoDB; EOG632CZ4; -. DR BioCyc; NMEN122586:GHGG-644-MONOMER; -. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; Q9K0I2; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.50.30.10; -; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR006319; PEP_synth. DR InterPro; IPR018274; PEP_util_AS. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR002192; PPDK_PEP-bd. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 1. DR PIRSF; PIRSF000854; PEP_synthase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01418; PEP_synth; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 794 Phosphoenolpyruvate synthase. FT /FTId=PRO_0000320270. FT ACT_SITE 422 422 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 752 752 Proton donor. {ECO:0000250}. FT METAL 681 681 Magnesium. {ECO:0000250}. FT METAL 705 705 Magnesium. {ECO:0000250}. FT BINDING 512 512 Substrate. {ECO:0000250}. FT BINDING 579 579 Substrate. {ECO:0000250}. FT BINDING 681 681 Substrate. {ECO:0000250}. FT BINDING 702 702 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 703 703 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 704 704 Substrate. {ECO:0000250}. FT BINDING 705 705 Substrate; via amide nitrogen. FT {ECO:0000250}. FT STRAND 6 8 {ECO:0000244|PDB:2OLS}. FT HELIX 9 11 {ECO:0000244|PDB:2OLS}. FT HELIX 14 16 {ECO:0000244|PDB:2OLS}. FT HELIX 17 34 {ECO:0000244|PDB:2OLS}. FT HELIX 35 37 {ECO:0000244|PDB:2OLS}. FT STRAND 44 47 {ECO:0000244|PDB:2OLS}. FT HELIX 49 56 {ECO:0000244|PDB:2OLS}. FT HELIX 58 60 {ECO:0000244|PDB:2OLS}. FT HELIX 61 70 {ECO:0000244|PDB:2OLS}. FT HELIX 77 92 {ECO:0000244|PDB:2OLS}. FT HELIX 98 114 {ECO:0000244|PDB:2OLS}. FT STRAND 122 128 {ECO:0000244|PDB:2OLS}. FT STRAND 144 148 {ECO:0000244|PDB:2OLS}. FT HELIX 151 164 {ECO:0000244|PDB:2OLS}. FT HELIX 168 177 {ECO:0000244|PDB:2OLS}. FT STRAND 186 192 {ECO:0000244|PDB:2OLS}. FT STRAND 198 207 {ECO:0000244|PDB:2OLS}. FT TURN 209 211 {ECO:0000244|PDB:2OLS}. FT STRAND 215 224 {ECO:0000244|PDB:2OLS}. FT HELIX 227 230 {ECO:0000244|PDB:2OLS}. FT STRAND 237 242 {ECO:0000244|PDB:2OLS}. FT HELIX 243 247 {ECO:0000244|PDB:2OLS}. FT STRAND 253 257 {ECO:0000244|PDB:2OLS}. FT STRAND 263 267 {ECO:0000244|PDB:2OLS}. FT STRAND 272 274 {ECO:0000244|PDB:2OLS}. FT STRAND 277 281 {ECO:0000244|PDB:2OLS}. FT HELIX 284 287 {ECO:0000244|PDB:2OLS}. FT HELIX 294 311 {ECO:0000244|PDB:2OLS}. FT STRAND 315 321 {ECO:0000244|PDB:2OLS}. FT TURN 323 325 {ECO:0000244|PDB:2OLS}. FT STRAND 328 335 {ECO:0000244|PDB:2OLS}. FT STRAND 392 396 {ECO:0000244|PDB:2OLS}. FT HELIX 400 402 {ECO:0000244|PDB:2OLS}. FT HELIX 404 407 {ECO:0000244|PDB:2OLS}. FT STRAND 410 416 {ECO:0000244|PDB:2OLS}. FT HELIX 422 426 {ECO:0000244|PDB:2OLS}. FT STRAND 434 436 {ECO:0000244|PDB:2OLS}. FT HELIX 441 444 {ECO:0000244|PDB:2OLS}. FT STRAND 484 491 {ECO:0000244|PDB:2OLS}. FT HELIX 494 496 {ECO:0000244|PDB:2OLS}. FT HELIX 497 501 {ECO:0000244|PDB:2OLS}. FT STRAND 506 511 {ECO:0000244|PDB:2OLS}. FT HELIX 514 519 {ECO:0000244|PDB:2OLS}. FT HELIX 525 529 {ECO:0000244|PDB:2OLS}. FT HELIX 531 533 {ECO:0000244|PDB:2OLS}. FT HELIX 536 545 {ECO:0000244|PDB:2OLS}. FT TURN 546 548 {ECO:0000244|PDB:2OLS}. FT STRAND 549 551 {ECO:0000244|PDB:2OLS}. FT HELIX 552 571 {ECO:0000244|PDB:2OLS}. FT STRAND 574 579 {ECO:0000244|PDB:2OLS}. FT HELIX 585 589 {ECO:0000244|PDB:2OLS}. FT HELIX 595 597 {ECO:0000244|PDB:2OLS}. FT HELIX 604 606 {ECO:0000244|PDB:2OLS}. FT HELIX 611 615 {ECO:0000244|PDB:2OLS}. FT TURN 617 619 {ECO:0000244|PDB:2OLS}. FT HELIX 620 635 {ECO:0000244|PDB:2OLS}. FT STRAND 642 646 {ECO:0000244|PDB:2OLS}. FT HELIX 652 664 {ECO:0000244|PDB:2OLS}. FT HELIX 671 673 {ECO:0000244|PDB:2OLS}. FT STRAND 676 680 {ECO:0000244|PDB:2OLS}. FT HELIX 683 687 {ECO:0000244|PDB:2OLS}. FT HELIX 689 693 {ECO:0000244|PDB:2OLS}. FT STRAND 696 702 {ECO:0000244|PDB:2OLS}. FT HELIX 703 711 {ECO:0000244|PDB:2OLS}. FT TURN 718 720 {ECO:0000244|PDB:2OLS}. FT HELIX 721 723 {ECO:0000244|PDB:2OLS}. FT HELIX 729 743 {ECO:0000244|PDB:2OLS}. FT TURN 744 746 {ECO:0000244|PDB:2OLS}. FT STRAND 748 754 {ECO:0000244|PDB:2OLS}. FT HELIX 755 758 {ECO:0000244|PDB:2OLS}. FT HELIX 760 769 {ECO:0000244|PDB:2OLS}. FT STRAND 773 776 {ECO:0000244|PDB:2OLS}. FT HELIX 778 780 {ECO:0000244|PDB:2OLS}. FT HELIX 781 791 {ECO:0000244|PDB:2OLS}. SQ SEQUENCE 794 AA; 87170 MW; 2165BDF3CFA67E56 CRC64; MADNYVIWFE NLRMTDVERV GGKNASLGEM ISQLTEKGVR VPGGFATTAE AYRAFLAHNG LSERISAALA KLDVEDVAEL ARVGKEIRQW ILDTPFPEQL DAEIEAAWNK MVADAGGADI SVAVRSSATA EDLPDASFAG QQETFLNING LDNVKEAMHH VFASLYNDRA ISYRVHKGFE HDIVALSAGV QRMVRSDSGA SGVMFTLDTE SGYDQVVFVT SSYGLGENVV QGAVNPDEFY VFKPTLKAGK PAILRKTMGS KHIKMIFTDK AEAGKSVTNV DVPEEDRNRF SITDEEITEL AHYALTIEKH YGRPMDIEWG RDGLDGKLYI LQARPETVKS QEEGNRNLRR FAINGDKTVL CEGRAIGQKV GQGKVRLIKD ASEMDSVEAG DVLVTDMTDP DWEPVMKRAS AIVTNRGGRT CHAAIIAREL GIPAVVGCGN ATELLKNGQE VTVSCAEGDT GFIYAGLLDV QITDVALDNM PKAPVKVMMN VGNPELAFSF ANLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDDELKA EITRRIAGYA SPVDFYVDKI AEGVATLAAS VYPRKTIVRM SDFKSNEYAN LVGGNVYEPH EENPMLGFRG AARYVADNFK DCFALECKAL KRVRDEMGLT NVEIMIPFVR TLGEAEAVVK ALKENGLERG KNGLRLIMMC ELPSNAVLAE QFLQYFDGFS IGSNDMTQLT LGLDRDSGLV SESFDERNPA VKVMLHLAIS ACRKQNKYVG ICGQGPSDHP DFAKWLVEEG IESVSLNPDT VIETWLYLAN ELNK // ID PPK_NEIMB Reviewed; 685 AA. AC Q9JXS9; Q59616; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 11-MAY-2016, entry version 86. DE RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347}; DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347}; DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347}; DE AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347}; GN Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347}; OrderedLocusNames=NMB1900; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BNCV / Serogroup B; RX PubMed=7729865; RA Tinsley C.R., Gotschlich E.C.; RT "Cloning and characterization of the meningococcal polyphosphate RT kinase gene: production of polyphosphate synthesis mutants."; RL Infect. Immun. 63:1624-1630(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-208. RX PubMed=9501229; DOI=10.1073/pnas.95.6.3140; RA Maiden M.C.J., Bygraves J.A., Feil E., Morelli G., Russell J.E., RA Urwin R., Zhang Q., Zhou J., Zurth K., Caugant D.A., Feavers I.M., RA Achtman M., Spratt B.G.; RT "Multilocus sequence typing: a portable approach to the identification RT of clones within populations of pathogenic microorganisms."; RL Proc. Natl. Acad. Sci. U.S.A. 95:3140-3145(1998). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate of ATP to form a long-chain polyphosphate (polyP). CC -!- CATALYTIC ACTIVITY: ATP + (phosphate)(n) = ADP + (phosphate)(n+1). CC {ECO:0000255|HAMAP-Rule:MF_00347}. CC -!- PTM: An intermediate of this reaction is the autophosphorylated CC ppk in which a phosphate is covalently linked to histidine CC residues through a N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347}. CC -!- SIMILARITY: Belongs to the polyphosphate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00347}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42231.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42231.1; ALT_INIT; Genomic_DNA. DR EMBL; U16262; AAA85674.1; -; Genomic_DNA. DR EMBL; AF037931; AAC08915.1; -; Genomic_DNA. DR PIR; B81030; B81030. DR RefSeq; NP_274895.1; NC_003112.2. DR RefSeq; WP_010981005.1; NC_003112.2. DR ProteinModelPortal; Q9JXS9; -. DR STRING; 122586.NMB1900; -. DR PaxDb; Q9JXS9; -. DR EnsemblBacteria; AAF42231; AAF42231; NMB1900. DR GeneID; 904271; -. DR KEGG; nme:NMB1900; -. DR PATRIC; 20359841; VBINeiMen85645_2425. DR eggNOG; ENOG4105CUU; Bacteria. DR eggNOG; COG0855; LUCA. DR HOGENOM; HOG000248948; -. DR KO; K00937; -. DR OMA; VRLMQVP; -. DR OrthoDB; EOG65TRRG; -. DR BioCyc; NMEN122586:GHGG-1957-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1840.10; -; 1. DR HAMAP; MF_00347; Polyphosphate_kinase; 1. DR InterPro; IPR003414; PP_kinase. DR InterPro; IPR024953; PP_kinase_middle. DR InterPro; IPR025200; PPK_C_dom. DR InterPro; IPR025198; PPK_N_dom. DR Pfam; PF02503; PP_kinase; 1. DR Pfam; PF13090; PP_kinase_C; 1. DR Pfam; PF13089; PP_kinase_N; 1. DR PIRSF; PIRSF015589; PP_kinase; 1. DR SUPFAM; SSF140356; SSF140356; 1. DR TIGRFAMs; TIGR03705; poly_P_kin; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1 685 Polyphosphate kinase. FT /FTId=PRO_0000128651. FT ACT_SITE 435 435 Phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00347}. FT ACT_SITE 454 454 Phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00347}. FT CONFLICT 28 28 Q -> K (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 61 66 HKRCPQ -> NKLHPR (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 107 109 QEG -> RES (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 120 120 D -> G (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 360 360 A -> R (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 365 365 A -> D (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 473 473 L -> I (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 486 486 I -> T (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 586 586 V -> I (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 597 597 Y -> C (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 603 603 T -> A (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 626 626 T -> A (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 629 629 T -> A (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 639 639 H -> R (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 643 643 T -> E (in Ref. 2; AAA85674). FT {ECO:0000305}. FT CONFLICT 647 647 D -> A (in Ref. 2; AAA85674). FT {ECO:0000305}. SQ SEQUENCE 685 AA; 77258 MW; 192D5B8F5B6370D6 CRC64; MPEQNRILCR ELSLLAFNRR VLAQAEDQNV PLLERLRFLC IVSSNLDEFF EVRMAWLKRE HKRCPQRRLD NGKMPSETIA DVTEAARSLI RHQYDLFNNV LQPELAQEGI HFYRRRNWTD TQKKWIEDYF DRELLPILTP IGLDPSHPFP RPLNKSLNFA VELDGTDAFG RPSGMAIVQA PRILPRVVPL PSELCGGGHG FVFLSSILHA HVGKLFPGMN VKGCHQFRLT RDSDLTVDEE DLQNLRAAIQ NELHDREYGD GVRLEVADTC PAYIRDFLLA QFKLTAAELY QVKGPVNLVR LNAVPDLVNR PDLKFPTHTP GRLKALGKTA SIFDLVRQSP ILLHHPYQSF DPVVEMMREA AADPAVLAVK MTIYRTGTRS ELVRALMKAA LAGKQVTVVV ELMARFDEAN NVNWAKQLEE AGAHVVYGVF GYKVHAKMAL VIRREDGVLK RYAHLGTGNY HQGTSRIYTD FGLITADEQI TADVNILFME ITGLGKPGRL NKLYQSPFTL HKMVIDRIAR ETEHAKAGKP ARITAKMNSL IEPTVIEALY RASAAGVQID LIVRGMCTLR PGVKGLSENI RVRSIVGRQL EHARVYYFHN NGTDDTFISS ADWMGRNFFR RIETATPITA PELKKRVIHE GLTMALDDNT HAWLMQPDGG YIRAAPAEGE SEADLQNDLW TLLGG // ID PRIB_NEIMB Reviewed; 100 AA. AC Q9JZ30; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Primosomal replication protein n {ECO:0000255|HAMAP-Rule:MF_00720}; GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; GN OrderedLocusNames=NMB1322; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site CC (PAS). {ECO:0000255|HAMAP-Rule:MF_00720}. CC -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, CC PriB, PriC, DnaB and DnaT. Upon transient interaction with DnaG it CC forms the primosome. {ECO:0000255|HAMAP-Rule:MF_00720}. CC -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP- CC Rule:MF_00720}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|HAMAP- CC Rule:MF_00720}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41697.1; -; Genomic_DNA. DR PIR; A81097; A81097. DR RefSeq; NP_274341.1; NC_003112.2. DR RefSeq; WP_002213304.1; NC_003112.2. DR ProteinModelPortal; Q9JZ30; -. DR STRING; 122586.NMB1322; -. DR PaxDb; Q9JZ30; -. DR EnsemblBacteria; AAF41697; AAF41697; NMB1322. DR GeneID; 903744; -. DR KEGG; nme:NMB1322; -. DR PATRIC; 20358293; VBINeiMen85645_1658. DR eggNOG; COG2965; LUCA. DR HOGENOM; HOG000261222; -. DR KO; K02686; -. DR OMA; HESWQKE; -. DR OrthoDB; EOG654P86; -. DR BioCyc; NMEN122586:GHGG-1360-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00720; PriB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR023646; Prisomal_replication_PriB. DR PIRSF; PIRSF003135; Primosomal_n; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR04418; PriB_gamma; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; Primosome; KW Reference proteome. FT CHAIN 1 100 Primosomal replication protein n. FT /FTId=PRO_0000199055. FT DOMAIN 1 99 SSB. {ECO:0000255|HAMAP-Rule:MF_00720}. SQ SEQUENCE 100 AA; 11594 MW; 5AE2CAFDCCF16A50 CRC64; MGFNNLVSLA ALIEKVFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ AEEWQYRQGV YVHVEGFLAQ KSRRSLMPML RIQNIQEYKG // ID PROA_NEIMB Reviewed; 420 AA. AC Q9JZG3; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412}; DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; GN OrderedLocusNames=NMB1068; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate CC 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The CC product spontaneously undergoes cyclization to form 1-pyrroline-5- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00412}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase CC family. {ECO:0000255|HAMAP-Rule:MF_00412}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62324.1; -; Genomic_DNA. DR RefSeq; NP_274101.1; NC_003112.2. DR RefSeq; WP_002244113.1; NC_003112.2. DR ProteinModelPortal; Q9JZG3; -. DR STRING; 122586.NMB1068; -. DR PaxDb; Q9JZG3; -. DR EnsemblBacteria; AAF62324; AAF62324; NMB1068. DR GeneID; 903486; -. DR KEGG; nme:NMB1068; -. DR PATRIC; 20357685; VBINeiMen85645_1359. DR eggNOG; ENOG4105C2S; Bacteria. DR eggNOG; COG0014; LUCA. DR HOGENOM; HOG000246356; -. DR KO; K00147; -. DR OMA; CNAIETL; -. DR OrthoDB; EOG6FFSCX; -. DR BioCyc; NMEN122586:GHGG-1105-MONOMER; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 2. DR HAMAP; MF_00412; ProA; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR012134; Glu-5-SA_DH. DR InterPro; IPR000965; GPR_dom. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS01223; PROA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Proline biosynthesis; Reference proteome. FT CHAIN 1 420 Gamma-glutamyl phosphate reductase. FT /FTId=PRO_0000189756. SQ SEQUENCE 420 AA; 45257 MW; 009996E9CF6B1118 CRC64; MSNTQKQLAL AKAAKKSVNT ADTEEKNRAL LAMADSLEAA TADILAANRQ DLEAAAGNIP ESMTDRLLLD GKRICAMADG IRAVAALPNP VGEILETSTL PNGLEIVKKR VAMGVIGIIY ESRPNVTSDA AALALKSGSA VVLRSGKDAF QSARAIVAAL KTGLAQTRID PDALQLIEDT GRESSYEMMR AKDYLDLLIP RGGAGLIRAV VENAVVPVIE TGTGIVHIYI DKDADWDKAL RIVYNAKTSR PSVCNSMEVL LVHEDIAADF LPKLERLLVR DRIEAGLPPI RFRLDPQAAR HIGGEAAGAD DFDTEFLDYI LAVKTVASVE EAVWHIETHS THHSDGIVTE NRHAADYFTT HIDSAAVYVN ASTRFTDGGE FGLGCEMGIS TQKLHARGPM GLKELTSYKY IVQGTGQVRE // ID PSRP_NEIMB Reviewed; 273 AA. AC Q9K0I1; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062}; DE Short=PEP synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062}; DE Short=PSRP {ECO:0000255|HAMAP-Rule:MF_01062}; DE EC=2.7.11.33 {ECO:0000255|HAMAP-Rule:MF_01062}; DE EC=2.7.4.28 {ECO:0000255|HAMAP-Rule:MF_01062}; DE AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062}; GN OrderedLocusNames=NMB0619; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase CC involved in the regulation of the phosphoenolpyruvate synthase CC (PEPS) by catalyzing its phosphorylation/dephosphorylation. CC {ECO:0000255|HAMAP-Rule:MF_01062}. CC -!- CATALYTIC ACTIVITY: ADP + [pyruvate, water dikinase] = AMP + CC [pyruvate, water dikinase] phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01062}. CC -!- CATALYTIC ACTIVITY: [Pyruvate, water dikinase] phosphate + CC phosphate = [pyruvate, water dikinase] + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01062}. CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase CC regulatory protein family. PSRP subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01062}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41045.1; -; Genomic_DNA. DR PIR; H81177; H81177. DR RefSeq; NP_273663.1; NC_003112.2. DR RefSeq; WP_002217768.1; NC_003112.2. DR STRING; 122586.NMB0619; -. DR PaxDb; Q9K0I1; -. DR EnsemblBacteria; AAF41045; AAF41045; NMB0619. DR GeneID; 902732; -. DR KEGG; nme:NMB0619; -. DR PATRIC; 20356527; VBINeiMen85645_0783. DR eggNOG; ENOG4105CF9; Bacteria. DR eggNOG; COG1806; LUCA. DR HOGENOM; HOG000218053; -. DR KO; K09773; -. DR OMA; EVEMMYK; -. DR OrthoDB; EOG6KHG2N; -. DR BioCyc; NMEN122586:GHGG-645-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043531; F:ADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006470; P:protein dephosphorylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01062; PSRP; 1. DR InterPro; IPR005177; Kinase-pyrophosphorylase. DR InterPro; IPR026530; PSRP. DR Pfam; PF03618; Kinase-PPPase; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 273 Putative phosphoenolpyruvate synthase FT regulatory protein. FT /FTId=PRO_0000196679. FT NP_BIND 154 161 ADP. {ECO:0000255|HAMAP-Rule:MF_01062}. SQ SEQUENCE 273 AA; 30894 MW; 1A705A88863FC57A CRC64; MSSPRHVFYI SDRTGLTAEN IGEALLNQFG NLSFKRHTHP FVDTPEKARA VVEKVNRSRQ ENGQRPIAFV SVVDDEIRRI IKGADAFQIN FFETFLGLLE KELNTEATAS GQGHHSIGNT KRYDARMEAV NFSLNHDDGV SDKNLQEADV ILMGVSRSGK TPTCLYLALQ YGIRAANYPL IPDDLESADL PRMVKPYRDK LFGLTIQPER LQAIRQERRP NSTYAKIDTC RSEVADAQSM FRRHGIPFAN TTDKSVEELA VHILQACKLK RRF // ID PSD_NEIMB Reviewed; 265 AA. AC Q9JZP0; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664}; DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00664}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664}; GN Name=psd {ECO:0000255|HAMAP-Rule:MF_00664}; OrderedLocusNames=NMB0963; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine CC (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine = CC phosphatidylethanolamine + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00664}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00664}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: CC step 2/2. {ECO:0000255|HAMAP-Rule:MF_00664}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit CC and a small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00664}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The post-translation cleavage follows an CC unusual pathway, termed non-hydrolytic serinolysis, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom CC to form the C-terminus of the beta chain, while the remainder of CC the serine residue undergoes an oxidative deamination to produce CC ammonia and the pyruvoyl prosthetic group on the alpha chain. CC {ECO:0000255|HAMAP-Rule:MF_00664}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase CC family. PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41369.1; -; Genomic_DNA. DR PIR; B81138; B81138. DR RefSeq; NP_274001.1; NC_003112.2. DR RefSeq; WP_002225313.1; NC_003112.2. DR STRING; 122586.NMB0963; -. DR PaxDb; Q9JZP0; -. DR EnsemblBacteria; AAF41369; AAF41369; NMB0963. DR GeneID; 903083; -. DR KEGG; nme:NMB0963; -. DR PATRIC; 20357409; VBINeiMen85645_1219. DR eggNOG; ENOG41071I4; Bacteria. DR eggNOG; COG0688; LUCA. DR HOGENOM; HOG000229359; -. DR KO; K01613; -. DR OMA; FNVHSNR; -. DR OrthoDB; EOG6KT2P7; -. DR BioCyc; NMEN122586:GHGG-1000-MONOMER; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00664; PS_decarb_PSD_A; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033175; PSD-A. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR TIGRFAMs; TIGR00164; PS_decarb_rel; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Decarboxylase; Lipid biosynthesis; KW Lipid metabolism; Lyase; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Pyruvate; Reference proteome; Zymogen. FT CHAIN 1 182 Phosphatidylserine decarboxylase beta FT chain. {ECO:0000255|HAMAP-Rule:MF_00664}. FT /FTId=PRO_0000029787. FT CHAIN 183 265 Phosphatidylserine decarboxylase alpha FT chain. {ECO:0000255|HAMAP-Rule:MF_00664}. FT /FTId=PRO_0000029788. FT ACT_SITE 183 183 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000255|HAMAP- FT Rule:MF_00664}. FT SITE 182 183 Cleavage (non-hydrolytic); by FT autocatalysis. {ECO:0000255|HAMAP- FT Rule:MF_00664}. FT MOD_RES 183 183 Pyruvic acid (Ser); by autocatalysis. FT {ECO:0000255|HAMAP-Rule:MF_00664}. SQ SEQUENCE 265 AA; 28955 MW; 10609DBF3CFD9EAF CRC64; MNRLYPHPII AREGWPIIGG GLALSLLVSI CCGWWSLPFW VFTVFALQFF RDPAREIPLN PEAVLSPVDG RIVVVERARD PYRDVDALKI SIFMNVFNVH SQKSPADCTV TKVVYNKGKF VNADLDKAST ENERNAVLAT TASGREITFV QVAGLVARRI LCYTQAGAKL SRGERYGFIR FGSRVDMYLP VDAQAQVAIG DKVTGVSTVL ARLPLTAPQT ESEPESEPAL QTAPVETAAN PSAEQRQIEA AAAKIQAAVQ DVLKD // ID PTHP_NEIMB Reviewed; 89 AA. AC P65877; Q9JQN1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Phosphocarrier protein HPr; DE EC=2.7.11.-; DE AltName: Full=Histidine-containing protein; GN Name=ptsH; OrderedLocusNames=NMB2045; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (sugar PTS). This major carbohydrate active-transport system CC catalyzes the phosphorylation of incoming sugar substrates CC concomitantly with their translocation across the cell membrane. CC The phosphoryl group from phosphoenolpyruvate (PEP) is transferred CC to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr CC then transfers it to the permease (enzymes II/III) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein HPr N(pi)-phospho-L-histidine + CC protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L- CC histidine. CC -!- ENZYME REGULATION: Phosphorylation on Ser-46 inhibits the CC phosphoryl transfer from enzyme I to HPr. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HPr family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HPr domain. {ECO:0000255|PROSITE- CC ProRule:PRU00681}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42365.1; -; Genomic_DNA. DR PIR; A81013; A81013. DR RefSeq; NP_275035.1; NC_003112.2. DR RefSeq; WP_002218178.1; NC_003112.2. DR ProteinModelPortal; P65877; -. DR STRING; 122586.NMB2045; -. DR PaxDb; P65877; -. DR EnsemblBacteria; AAF42365; AAF42365; NMB2045. DR GeneID; 904045; -. DR KEGG; nme:NMB2045; -. DR PATRIC; 20360244; VBINeiMen85645_2622. DR eggNOG; ENOG41080Z8; Bacteria. DR eggNOG; COG1925; LUCA. DR HOGENOM; HOG000278398; -. DR KO; K11189; -. DR OMA; AEVWVTR; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; NMEN122586:GHGG-2108-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1340.10; -; 1. DR InterPro; IPR000032; HPr_prot-like. DR InterPro; IPR001020; PTS_HPr_His_P_site. DR InterPro; IPR002114; PTS_HPr_Ser_P_site. DR Pfam; PF00381; PTS-HPr; 1. DR PRINTS; PR00107; PHOSPHOCPHPR. DR SUPFAM; SSF55594; SSF55594; 1. DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1. DR PROSITE; PS51350; PTS_HPR_DOM; 1. DR PROSITE; PS00369; PTS_HPR_HIS; 1. DR PROSITE; PS00589; PTS_HPR_SER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Phosphoprotein; KW Phosphotransferase system; Reference proteome; KW Serine/threonine-protein kinase; Sugar transport; Transferase; KW Transport. FT CHAIN 1 89 Phosphocarrier protein HPr. FT /FTId=PRO_0000107866. FT DOMAIN 1 88 HPr. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT ACT_SITE 15 15 Pros-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. FT MOD_RES 46 46 Phosphoserine; by HPrK/P. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. SQ SEQUENCE 89 AA; 9693 MW; F4A3563301E24616 CRC64; MLKQSIEIIN KLGLHARASN KFTQTASQFK SEVWVTKNDS RVNGKSIMGL MMLAAAKGTV IELETDGADE AEAMRALTDL INGYFGEGE // ID PUR4_NEIMB Reviewed; 1320 AA. AC Q9JXK5; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; GN OrderedLocusNames=NMB1996; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in CC the purines biosynthetic pathway. Catalyzes the ATP-dependent CC conversion of formylglycinamide ribonucleotide (FGAR) and CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00419}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS CC family. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00419}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42323.1; -; Genomic_DNA. DR PIR; G81017; G81017. DR RefSeq; NP_274988.1; NC_003112.2. DR RefSeq; WP_002225870.1; NC_003112.2. DR ProteinModelPortal; Q9JXK5; -. DR STRING; 122586.NMB1996; -. DR PaxDb; Q9JXK5; -. DR EnsemblBacteria; AAF42323; AAF42323; NMB1996. DR GeneID; 904131; -. DR KEGG; nme:NMB1996; -. DR PATRIC; 20360091; VBINeiMen85645_2550. DR eggNOG; ENOG4107QIK; Bacteria. DR eggNOG; COG0046; LUCA. DR eggNOG; COG0047; LUCA. DR HOGENOM; HOG000261359; -. DR KO; K01952; -. DR OMA; LSANWMW; -. DR OrthoDB; EOG6FNHHR; -. DR BioCyc; NMEN122586:GHGG-2053-MONOMER; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00419; PurL_1; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010073; PRibForGlyAmidine_synth. DR InterPro; IPR016188; PurM-like_N. DR Pfam; PF02769; AIRS_C; 2. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF56042; SSF56042; 3. DR TIGRFAMs; TIGR01735; FGAM_synt; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 1320 Phosphoribosylformylglycinamidine FT synthase. FT /FTId=PRO_0000100411. FT DOMAIN 1069 1320 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00419}. FT NP_BIND 311 322 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1162 1162 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT ACT_SITE 1285 1285 {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1287 1287 {ECO:0000255|HAMAP-Rule:MF_00419}. FT METAL 679 679 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 718 718 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 722 722 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 884 884 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT BINDING 678 678 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00419}. FT BINDING 886 886 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. SQ SEQUENCE 1320 AA; 143853 MW; B6B873913EBB06BD CRC64; MSVVLPLRGV TALSDFRVEK LLQKAAALGL PEVKLSSEFW YFVGSEKALD AATVEKLQAL LAAQSVEQTP KAREGLHLFL VTPRLGTISP WASKATNIAE NCGLAGIERI ERGMAVWLEG RLNDEQKQQW AALLHDRMTE SVLPDFQTAS KLFHHLESET FSGVDVLGGG KEALVKANTE MGLALSADEI DYLVENYQAL QRNPSDVELM MFAQANSEHC RHKIFNADFI LNGEKQPKSL FGMIRDTHNA HPEGTVVAYK DNSSVIEGAK IERFYPNAAE NQGYRFHEED THIIMKVETH NHPTAIAPFA GAATGAGGEI RDEGATGKGS RPKAGLTGFT VSNLNIPDLK QPWEQDYGKP EHISSPLDIM IEGPIGGAAF NNEFGRPNLL GYFRTFEEKF DGQVRGYHKP IMIAGGLGSI QAQQTHKDEI PEGALLIQLG GPGMLIGLGG GAASSMDTGT NDASLDFNSV QRGNPEIERR AQEVIDRCWQ LGGKNPIISI HDVGAGGLSN AFPELVNDAR RGAVFKLREV PLEEHGLNPL QIWCNESQER YVLSILEKDL DAFRAICERE RCPFAVVGTA TDDGHLKVRD DLFANNPVDL PLNVLLGKLP KTTRTDKTVA PSKKPFHAGD IDITEAAYRV LRLPAVAAKN FLITIGDRSV GGLTHRDQMV GKYQTPVADC AVTMMGFNTY RGEAMSMGEK PTVALFDAPA SGRMCVGEAI TNIAAVNIGD IGNIKLSANW MAACGNEGED EKLYRTVEAV SKACQALDLS IPVGKDSLSM KTVWQDGEEK KSVVSPLSLI ISAFAPVKDV RKTVTPELKN VEDSVLLFVD LGFGKARMGG SAFGQVYNNM SGDAPDLDDT GRLKAFYSVI QQLVAENKLL AYHDRSDGGL FAVLVEMAFA GRCGLDIDLN LLLAQTFITN HTALSQSLRT EEVKALAEWQ ETIARTLFNE ELGAVIQVRK QDVADIINLF YQQQLHHNVF EIGTLTDENT LIIRDGQTHL ISDNLIKLQQ TWQETSHQIQ RLRDNPACAD SEFALIGDNE RSALFADVKF DVNEDIAAPF INSGAKPKIA ILREQGVNGQ IEMAAAFTRA GFDAYDVHMS DLMAGRIHLA DFKMLAACGG FSYGDVLGAG EGWAKSILFH PALRDQFAAF FADPDTLTLG VCNGCQMVSN LAEIIPGTAG WPKFKRNLSE QFEARLSMVH VPKSASLILN EMQGSSLPVV VSHGEGRADF ALHGGNISAD LGIALQYIDG QNQVTQTYPL NPNGSPQGIA GVTNADGRIT IMMPHPERVY RAAQMSWKPE GWTELSGWYR LFAGARKALG // ID PUR9_NEIMB Reviewed; 526 AA. AC Q9JZM7; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139}; GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; GN OrderedLocusNames=NMB0983; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. {ECO:0000255|HAMAP- CC Rule:MF_00139}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl CC THF route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP- CC Rule:MF_00139}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41387.1; -; Genomic_DNA. DR PIR; A81135; A81135. DR RefSeq; NP_274020.1; NC_003112.2. DR RefSeq; WP_010980881.1; NC_003112.2. DR ProteinModelPortal; Q9JZM7; -. DR STRING; 122586.NMB0983; -. DR PaxDb; Q9JZM7; -. DR EnsemblBacteria; AAF41387; AAF41387; NMB0983. DR GeneID; 903103; -. DR KEGG; nme:NMB0983; -. DR PATRIC; 20357457; VBINeiMen85645_1243. DR eggNOG; ENOG4105DC1; Bacteria. DR eggNOG; COG0138; LUCA. DR HOGENOM; HOG000230372; -. DR KO; K00602; -. DR OMA; PCGVAEG; -. DR OrthoDB; EOG6QCDFF; -. DR BioCyc; NMEN122586:GHGG-1020-MONOMER; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dom. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR PANTHER; PTHR11692; PTHR11692; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00355; purH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 526 Bifunctional purine biosynthesis protein FT PurH. FT /FTId=PRO_0000192109. SQ SEQUENCE 526 AA; 56803 MW; E7EF33E3EEFC65A8 CRC64; MSSIKRALIS LSDKTGAVEF AQTLHKLGVE ILSTGGTAKL LADAGVPVIE VADYTGFPEM LDGRVKTLHP KIHGGILGRR DLDEHVAKME EHGIGNIDLV CVNLYLFAAT IAKPNCTLED AIENIDIGGP TMVRSAAKNW KHVAIVTDTA DFPAIAAELE ANNGALSDKT RFNLSRKAFS HTAQYDGMIS NYLTSLSDDV LSGTPEIAGF PGRFNQSWIK VQDMRYGENP HQRAAFYRDI DPAAGSLAAY KQLQGKELSY NNIADADAAW EAVKSFDVPA CVIVKHANPC GVAIASNTLD AYKLAYATDT TSAFGGIIAF NREVDGATVK QITDNQFMEV LMAPKFTAEA LEIAAAKKNV RVLEVPLEAG ANRFELKRVG GGLLVQTPDI HRISRADLKV VSKRQPTEQE WNDLLFVWNV AKYVKSNAIV FGKGGQTYGI GAGQMSRVDS TRIAARKAQD AGLDLNGACA ASDAFFPFRD GVDVIAEQGI KAIIHPAGSM RDQEVFDAAD EHGIAMVVTG IRHFRH // ID PTH_NEIMB Reviewed; 192 AA. AC Q9K029; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083}; DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083}; DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083}; GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=NMB0795; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl- CC tRNAs which drop off the ribosome during protein synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N- CC substituted amino acid + tRNA. {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP- CC Rule:MF_00083}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41208.1; -; Genomic_DNA. DR PIR; B81157; B81157. DR RefSeq; NP_273837.1; NC_003112.2. DR RefSeq; WP_002221185.1; NC_003112.2. DR ProteinModelPortal; Q9K029; -. DR SMR; Q9K029; 4-191. DR STRING; 122586.NMB0795; -. DR PaxDb; Q9K029; -. DR EnsemblBacteria; AAF41208; AAF41208; NMB0795. DR GeneID; 902910; -. DR KEGG; nme:NMB0795; -. DR PATRIC; 20356977; VBINeiMen85645_1007. DR eggNOG; ENOG4108ZPD; Bacteria. DR eggNOG; COG0193; LUCA. DR HOGENOM; HOG000004796; -. DR KO; K01056; -. DR OMA; FMNRSGL; -. DR OrthoDB; EOG6C5RTR; -. DR BioCyc; NMEN122586:GHGG-826-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1470; -; 1. DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1. DR InterPro; IPR001328; Pept_tRNA_hydro. DR InterPro; IPR018171; Pept_tRNA_hydro_CS. DR PANTHER; PTHR17224; PTHR17224; 1. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR SUPFAM; SSF53178; SSF53178; 1. DR TIGRFAMs; TIGR00447; pth; 1. DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 192 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000187783. SQ SEQUENCE 192 AA; 21474 MW; 11ED239E968CFCA7 CRC64; MSNTIKMVVG LGNPGKEYEQ TRHNAGFWFL DELAWKWKAS FKEEKKFFGE VARAALPDGD VWLLKPATFM NRSGQAVAAL AQFYKIKPEE ILVVHDELDI PCGRIKFKLG GGNGGHNGLK DIQAKLGTAD YYRLRLGIGH PGDRNLVVGY VLNKPSTEHR RQIDDAVAKS LQAIPDILAG KWEEATRFLH SK // ID PUR5_NEIMB Reviewed; 344 AA. AC Q9JZ80; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741}; DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741}; GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; GN OrderedLocusNames=NMB1252; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. {ECO:0000255|HAMAP-Rule:MF_00741}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_00741}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}. CC -!- SIMILARITY: Belongs to the AIR synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00741}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41632.1; -; Genomic_DNA. DR PIR; E81104; E81104. DR RefSeq; NP_274275.1; NC_003112.2. DR RefSeq; WP_002222409.1; NC_003112.2. DR ProteinModelPortal; Q9JZ80; -. DR SMR; Q9JZ80; 3-337. DR STRING; 122586.NMB1252; -. DR PaxDb; Q9JZ80; -. DR EnsemblBacteria; AAF41632; AAF41632; NMB1252. DR GeneID; 903674; -. DR KEGG; nme:NMB1252; -. DR PATRIC; 20358105; VBINeiMen85645_1565. DR eggNOG; ENOG4105CXB; Bacteria. DR eggNOG; COG0150; LUCA. DR HOGENOM; HOG000229091; -. DR KO; K01933; -. DR OMA; NHCVNDI; -. DR OrthoDB; EOG61CM1V; -. DR BioCyc; NMEN122586:GHGG-1289-MONOMER; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR004733; PurM_cligase. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00878; purM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 344 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_0000148225. SQ SEQUENCE 344 AA; 36974 MW; D71654C401BEA862 CRC64; MSTSLSYRDA GVDIDAGDQL VENIKPFAKR TMRPEVLGDL GGFGALVEIG KKYQNPVLVS GTDGVGTKLK LAFDWDKHDT VGIDLVAMSV NDILVQGAEP LFFLDYFACG KLDVPRATDV IKGIAQGCEE SGCALIGGET AEMPGMYPVG EYDLAGFAVG VVEKENVITG RSIGVGDVVL GLASNGAHSN GYSLIRKIIE RDNPDLDAEF DNGKTLREAV IAPTRLYVKP ILAALEKFTI KGMAHITGGG ITENVPRVLP ENTVAQIDAK SWELPKLFQW LQKAGNVETQ EMYRTFNCGI GMVVIVAAED ADAVQGLLGE QGETVYRLGL IRERQGDEHQ TQVA // ID PYRC_NEIMB Reviewed; 344 AA. AC Q9K0D1; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219}; DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219}; DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219}; GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219}; GN OrderedLocusNames=NMB0682; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00219}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3. CC {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00219}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41100.1; -; Genomic_DNA. DR PIR; H81171; H81171. DR RefSeq; NP_273724.1; NC_003112.2. DR RefSeq; WP_002222782.1; NC_003112.2. DR ProteinModelPortal; Q9K0D1; -. DR SMR; Q9K0D1; 2-343. DR STRING; 122586.NMB0682; -. DR PaxDb; Q9K0D1; -. DR EnsemblBacteria; AAF41100; AAF41100; NMB0682. DR GeneID; 902794; -. DR KEGG; nme:NMB0682; -. DR PATRIC; 20356675; VBINeiMen85645_0855. DR eggNOG; ENOG4105EKE; Bacteria. DR eggNOG; COG0418; LUCA. DR HOGENOM; HOG000256259; -. DR KO; K01465; -. DR OMA; YAEAFEQ; -. DR OrthoDB; EOG6TFCMH; -. DR BioCyc; NMEN122586:GHGG-710-MONOMER; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR HAMAP; MF_00219; PyrC_type1; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR004721; DHOdimr. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR032466; Metal_Hydrolase. DR PANTHER; PTHR11647:SF59; PTHR11647:SF59; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF001237; DHOdimr; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00856; pyrC_dimer; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 344 Dihydroorotase. FT /FTId=PRO_0000147211. FT METAL 13 13 Zinc 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 15 15 Zinc 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 98 98 Zinc 1; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 98 98 Zinc 2; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 135 135 Zinc 2; via pros nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 173 173 Zinc 2; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00219}. FT METAL 247 247 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00219}. FT MOD_RES 98 98 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_00219}. SQ SEQUENCE 344 AA; 37084 MW; 39FC78FD93A73DD8 CRC64; MQTLTIIRPD DMHLHLRDGD ALKAVAPYTA RQMGRAVIMP NLKPPVVSVA DALAYKARIM AALPEGSAFE PLMTLYLTDN ATPELVREAK AAGIVAFKLY PAGATTNSDS GVTDLFKLIP VLEEMAKQGI LFLVHGEVTD PEIDIFDREA AFIGRVMKPV LAQVPNLKVV FEHITTAEAA RLVLEAGDNV AATVTPQHLL LNRNDLLVGG VRPHHFCLPV LKRETHRQAL VAAVTGEKAH KFFLGTDSAP HAKSAKENAC GCAGMFSAMT AIELYAEVFE KAGALDKLEA FASKNGARFY GIPENTDTIT LVKQSQTVPA SVPYGDGELV PMRAGGEIGW TVQY // ID PYRD_NEIMB Reviewed; 335 AA. AC Q9K1D7; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_00225}; DE EC=1.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00225}; DE AltName: Full=DHOdehase {ECO:0000255|HAMAP-Rule:MF_00225}; DE Short=DHOD {ECO:0000255|HAMAP-Rule:MF_00225}; DE Short=DHODase {ECO:0000255|HAMAP-Rule:MF_00225}; DE AltName: Full=Dihydroorotate oxidase {ECO:0000255|HAMAP-Rule:MF_00225}; GN Name=pyrD {ECO:0000255|HAMAP-Rule:MF_00225}; GN OrderedLocusNames=NMB0221; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate CC with quinone as electron acceptor. {ECO:0000255|HAMAP- CC Rule:MF_00225}. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a CC quinol. {ECO:0000255|HAMAP-Rule:MF_00225}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00225}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_00225}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (quinone route): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00225}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00225}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00225}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00225}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00225}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40677.1; -; Genomic_DNA. DR PIR; G81222; G81222. DR RefSeq; NP_273278.1; NC_003112.2. DR RefSeq; WP_002243962.1; NC_003112.2. DR ProteinModelPortal; Q9K1D7; -. DR SMR; Q9K1D7; 2-333. DR STRING; 122586.NMB0221; -. DR PaxDb; Q9K1D7; -. DR EnsemblBacteria; AAF40677; AAF40677; NMB0221. DR GeneID; 902333; -. DR KEGG; nme:NMB0221; -. DR PATRIC; 20355514; VBINeiMen85645_0281. DR eggNOG; ENOG4107QYT; Bacteria. DR eggNOG; COG0167; LUCA. DR HOGENOM; HOG000225103; -. DR KO; K00254; -. DR OMA; TLVRHKM; -. DR OrthoDB; EOG65BDN8; -. DR BioCyc; NMEN122586:GHGG-236-MONOMER; -. DR UniPathway; UPA00070; UER00946. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00225; DHO_dh_type2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR005719; Dihydroorotate_DH_2. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR TIGRFAMs; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane; KW Oxidoreductase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 335 Dihydroorotate dehydrogenase (quinone). FT /FTId=PRO_0000148460. FT NP_BIND 59 63 FMN. {ECO:0000255|HAMAP-Rule:MF_00225}. FT NP_BIND 315 316 FMN. {ECO:0000255|HAMAP-Rule:MF_00225}. FT REGION 108 112 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT REGION 243 244 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT ACT_SITE 172 172 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT BINDING 63 63 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT BINDING 83 83 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 136 136 FMN. {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 169 169 FMN. {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT BINDING 174 174 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00225}. FT BINDING 214 214 FMN. {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 242 242 FMN; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 265 265 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00225}. FT BINDING 294 294 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00225}. SQ SEQUENCE 335 AA; 35889 MW; 52316AD774B1905C CRC64; MYPLARRILF ALDAEKAHHF TLDALYTVYK LGLIPVTDNR TKPVKLMGMD LPNPVGLAAG LDKNGEYIDA LGALGFGFIE IGTVTPNPQP GNPQPRLFRV PEHQGIINRM GFNNHGIDTM IRNIEKSKFS GVLGINIGKN AVTPIENAAD DYLICLEKAY AHASYITVNI SSPNTKNLRA LQGGDELSAL LEALKNKQAQ LASVHGKYVP LAVKIAPDLD EAQIEDIAHV VKSVEMDGII ATNTTIDKSS LGSHPLAGEQ GGLSGLPVHE KSNRVLKLLA DHIDGKLPII GVGGIMEGED SADKIRLGAT AVQVYSGLIY KGPALVKECL KALAR // ID PUR2_NEIMB Reviewed; 423 AA. AC Q9JXA3; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; GN OrderedLocusNames=NMB2151; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42459.1; -; Genomic_DNA. DR PIR; E81000; E81000. DR RefSeq; NP_275136.1; NC_003112.2. DR RefSeq; WP_002225741.1; NC_003112.2. DR ProteinModelPortal; Q9JXA3; -. DR SMR; Q9JXA3; 1-423. DR STRING; 122586.NMB2151; -. DR PaxDb; Q9JXA3; -. DR EnsemblBacteria; AAF42459; AAF42459; NMB2151. DR GeneID; 903221; -. DR KEGG; nme:NMB2151; -. DR PATRIC; 20360498; VBINeiMen85645_2745. DR eggNOG; ENOG4105C12; Bacteria. DR eggNOG; COG0151; LUCA. DR HOGENOM; HOG000033463; -. DR KO; K01945; -. DR OMA; DYQNFTE; -. DR OrthoDB; EOG69SKD1; -. DR BioCyc; NMEN122586:GHGG-2216-MONOMER; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 423 Phosphoribosylamine--glycine ligase. FT /FTId=PRO_0000151467. FT DOMAIN 107 314 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00138}. FT NP_BIND 133 194 ATP. {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 284 284 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 286 286 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. SQ SEQUENCE 423 AA; 44975 MW; 7203DDCAEC2D38E2 CRC64; MKLLVIGNGG REHALAWKLA QSPKVETVFV APGNAGTAIE PKLQNIDLTA HQDLIEFCRK ENIVFTVVGP EAPLAAGIVD DFRAAGLKIF GPTQYAAQLE SSKDFAKAFM AKYNIPTAQY QTFENADAAH DYVNQKGAPI VIKADGLAAG KGVIVAMTLD EAHAAIDDML LDNKMGNAGA RVVIEDFLQG EEASFIVMVD GNNVLPMATS QDHKRLLDGD KGLNTGGMGA YSPAPVVTPV VYERAMNEII LPTVAGMKAE GHEFTGFLYA GLMIDQSGAP YTIEFNCRFG DPETQPIMSR LNSDLSDLVE AAIDGKLDSV TAEWSPQTAV GVVLAAQNYP ETPKKGDIIS GLDAANQIGK VFHAGTTANE KGDVLTNGGR VLCVVGLGDN VAQAKAKAYG ALEKISFDGM QYRKDIADKA INR // ID PYRB_NEIMB Reviewed; 306 AA. AC P65616; Q9JQU5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_00001}; DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001}; DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001}; DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001}; GN Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; GN OrderedLocusNames=NMB0106; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. {ECO:0000255|HAMAP-Rule:MF_00001}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00001}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. CC {ECO:0000255|HAMAP-Rule:MF_00001}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40565.1; -; Genomic_DNA. DR PIR; A81238; A81238. DR RefSeq; NP_273164.1; NC_003112.2. DR RefSeq; WP_002215336.1; NC_003112.2. DR ProteinModelPortal; P65616; -. DR SMR; P65616; 3-306. DR STRING; 122586.NMB0106; -. DR PaxDb; P65616; -. DR EnsemblBacteria; AAF40565; AAF40565; NMB0106. DR GeneID; 902210; -. DR KEGG; nme:NMB0106; -. DR PATRIC; 20355225; VBINeiMen85645_0146. DR eggNOG; ENOG4105CXT; Bacteria. DR eggNOG; COG0540; LUCA. DR HOGENOM; HOG000022685; -. DR KO; K00609; -. DR OMA; KQSFYGV; -. DR OrthoDB; EOG61KBJZ; -. DR BioCyc; NMEN122586:GHGG-112-MONOMER; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_00001; Asp_carb_tr; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR002082; Asp_carbamoyltransf. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00101; ATCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00670; asp_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Complete proteome; Pyrimidine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 306 Aspartate carbamoyltransferase. FT /FTId=PRO_0000113165. SQ SEQUENCE 306 AA; 34205 MW; C6865145E0B7F8C9 CRC64; MPNPLYRQHI ISISDLSREQ LECLLQTALK LKAHPRGDLL EGKLIGSCFF EPSTRTRLSF ETAVQRLGGK VIGFSDGANT SAKKGETLAD TARIISGYTD AIIQRHPKDG AARVAAEFSR VPVINAGDGT NQHPSQTLLD LVTIYETQGR LDKLKIAMAG DLKYGRTVHS LCQALKRWNC EFAFVSPPSL AMPDYITEEL DEAGCRYRIL GSLEEAAEWA DILYMTRVQR ERFDEQEFAK IQGKFNLEAS MLARAKPNLR VLHPLPRVDE IHPDVDATPH AYYFEQATNG VYARMAILSL VLNEEV // ID PYRE_NEIMB Reviewed; 213 AA. AC P65915; Q9JR25; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; GN OrderedLocusNames=NMB1874; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation CC of orotidine monophosphate (OMP). {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate CC + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42208.1; -; Genomic_DNA. DR PIR; H81032; H81032. DR RefSeq; NP_274870.1; NC_003112.2. DR RefSeq; WP_002217982.1; NC_003112.2. DR ProteinModelPortal; P65915; -. DR SMR; P65915; 1-212. DR STRING; 122586.NMB1874; -. DR PaxDb; P65915; -. DR EnsemblBacteria; AAF42208; AAF42208; NMB1874. DR GeneID; 904314; -. DR KEGG; nme:NMB1874; -. DR PATRIC; 20359779; VBINeiMen85645_2395. DR eggNOG; ENOG4107QP2; Bacteria. DR eggNOG; COG0461; LUCA. DR HOGENOM; HOG000037974; -. DR KO; K00762; -. DR OMA; MKAYQRQ; -. DR OrthoDB; EOG6091H8; -. DR BioCyc; NMEN122586:GHGG-1930-MONOMER; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01208; PyrE; 1. DR InterPro; IPR023031; OPRT. DR InterPro; IPR004467; Or_phspho_trans_dom. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Magnesium; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 213 Orotate phosphoribosyltransferase. FT /FTId=PRO_0000110715. FT REGION 34 35 Orotate binding. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT REGION 72 73 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT REGION 123 131 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 26 26 5-phosphoribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 98 98 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 99 99 5-phosphoribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 102 102 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 104 104 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 127 127 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 155 155 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. SQ SEQUENCE 213 AA; 23262 MW; 77750D345A8265BC CRC64; MTDFRQDFLK FSLAQNVLKF GEFTTKAGRR SPYFFNAGLF NDGLSTLQLA KFYAQSIIES GIRFDMLFGP AYKGIILAAA TAMMLAEKGV NVPFAYNRKE AKDHGEGGVL VGAPLKGRVL IIDDVISAGT SVRESIKLIE AEGATPAGVA IALDRMEKGT GELSAVQEVE KQYGLPVAPI ASLNDLFILL QNNPEFGQFL EPVRAYRRQY GVE // ID PYRI_NEIMB Reviewed; 152 AA. AC Q9K1K9; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002}; GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; GN OrderedLocusNames=NMB0107; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in allosteric regulation of aspartate CC carbamoyltransferase. {ECO:0000255|HAMAP-Rule:MF_00002}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00002}; CC -!- SUBUNIT: Contains catalytic and regulatory chains. CC {ECO:0000255|HAMAP-Rule:MF_00002}. CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000255|HAMAP- CC Rule:MF_00002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40566.1; -; Genomic_DNA. DR PIR; B81238; B81238. DR RefSeq; NP_273165.1; NC_003112.2. DR RefSeq; WP_002216215.1; NC_003112.2. DR ProteinModelPortal; Q9K1K9; -. DR SMR; Q9K1K9; 13-151. DR STRING; 122586.NMB0107; -. DR PaxDb; Q9K1K9; -. DR EnsemblBacteria; AAF40566; AAF40566; NMB0107. DR GeneID; 902211; -. DR KEGG; nme:NMB0107; -. DR PATRIC; 20355227; VBINeiMen85645_0147. DR eggNOG; ENOG4108R9M; Bacteria. DR eggNOG; COG1781; LUCA. DR HOGENOM; HOG000113530; -. DR KO; K00610; -. DR OMA; MNVPSDR; -. DR OrthoDB; EOG6JX7QS; -. DR BioCyc; NMEN122586:GHGG-113-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.20; -; 1. DR Gene3D; 3.30.70.140; -; 1. DR HAMAP; MF_00002; Asp_carb_tr_reg; 1. DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N. DR InterPro; IPR002801; Asp_carbamoylTrfase_reg. DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C. DR Pfam; PF01948; PyrI; 1. DR Pfam; PF02748; PyrI_C; 1. DR ProDom; PD006194; Asp_carbamoylTrfase_reg; 1. DR SUPFAM; SSF54893; SSF54893; 1. DR SUPFAM; SSF57825; SSF57825; 1. DR TIGRFAMs; TIGR00240; ATCase_reg; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 152 Aspartate carbamoyltransferase regulatory FT chain. FT /FTId=PRO_0000142308. FT METAL 108 108 Zinc. {ECO:0000255|HAMAP-Rule:MF_00002}. FT METAL 113 113 Zinc. {ECO:0000255|HAMAP-Rule:MF_00002}. FT METAL 137 137 Zinc. {ECO:0000255|HAMAP-Rule:MF_00002}. FT METAL 140 140 Zinc. {ECO:0000255|HAMAP-Rule:MF_00002}. SQ SEQUENCE 152 AA; 16904 MW; 7E838D72FF83A73E CRC64; METPKLSVEA IEKGTVIDHI PAGRGLTILR QFKLLHYGNA VTVGFNLPSK TQGSKDIIKI KGVCLDDKAA DRLALFAPEA VVNTIDNFKV VQKRHLNLPD EIAEVFRCPN TNCAGHGEPV KSRFYVKKHN GQTRLKCHYC EKTYSRDSVA EA // ID PUR7_NEIMB Reviewed; 287 AA. AC Q9K063; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137}; DE EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137}; DE AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137}; GN Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; GN OrderedLocusNames=NMB0757; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. {ECO:0000255|HAMAP-Rule:MF_00137}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00137}. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00137}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41170.1; -; Genomic_DNA. DR PIR; B81161; B81161. DR RefSeq; NP_273799.1; NC_003112.2. DR RefSeq; WP_002225440.1; NC_003112.2. DR ProteinModelPortal; Q9K063; -. DR STRING; 122586.NMB0757; -. DR PaxDb; Q9K063; -. DR EnsemblBacteria; AAF41170; AAF41170; NMB0757. DR GeneID; 902872; -. DR KEGG; nme:NMB0757; -. DR PATRIC; 20356885; VBINeiMen85645_0961. DR eggNOG; ENOG4105C8V; Bacteria. DR eggNOG; COG0152; LUCA. DR HOGENOM; HOG000230360; -. DR KO; K01923; -. DR OMA; WNKQPPA; -. DR OrthoDB; EOG69SKD1; -. DR BioCyc; NMEN122586:GHGG-788-MONOMER; -. DR UniPathway; UPA00074; UER00131. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.470.20; -; 1. DR HAMAP; MF_00137; SAICAR_synth; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR028923; SAICAR_synt/ADE2_N. DR InterPro; IPR001636; SAICAR_synth. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Pfam; PF01259; SAICAR_synt; 1. DR TIGRFAMs; TIGR00081; purC; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 287 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_0000100846. SQ SEQUENCE 287 AA; 32283 MW; D3BEC1DAEEE4014C CRC64; MSEIGLVKIY FGKVRDLYEI DDKRMLMVAS DRLSAFDVIL DDPIPSKGEI LTQISNFWFK KLAHIMPNHF TGQTVYDVLP ENEAKALEKR AVVAKKLTPV KVEAIVRGYL AGSGWKDYQK TGSVCGIQLP EGMQEAQQLP EVIFTPSTKA AVGDHDENIS FEECGRIIGK ELAEEVRAKA VRLYTEAAEY AKSRGIIICD TKFEFGLDEN GTLTLMDEVL TPDSSRFWPA DQYKVGTNPP SFDKQFVRDW LEQSGWNKKA PAPKVPADVI QKTVEKYREA LTLLTQD // ID PURA_NEIMB Reviewed; 432 AA. AC Q9K012; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 11-MAY-2016, entry version 100. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; GN OrderedLocusNames=NMB0815; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. Catalyzes the first committed step in the CC biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + CC N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41228.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41228.1; ALT_INIT; Genomic_DNA. DR PIR; F81153; F81153. DR RefSeq; NP_273857.1; NC_003112.2. DR ProteinModelPortal; Q9K012; -. DR SMR; Q9K012; 2-432. DR STRING; 122586.NMB0815; -. DR PaxDb; Q9K012; -. DR EnsemblBacteria; AAF41228; AAF41228; NMB0815. DR GeneID; 902930; -. DR KEGG; nme:NMB0815; -. DR PATRIC; 20357017; VBINeiMen85645_1027. DR eggNOG; ENOG4105C91; Bacteria. DR eggNOG; COG0104; LUCA. DR HOGENOM; HOG000260959; -. DR KO; K01939; -. DR OMA; FHHAKPI; -. DR OrthoDB; EOG68Q0QG; -. DR BioCyc; NMEN122586:GHGG-846-MONOMER; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 432 Adenylosuccinate synthetase. FT /FTId=PRO_0000095203. FT NP_BIND 13 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 41 43 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 333 335 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 416 418 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT REGION 14 17 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 39 42 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 301 307 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 14 14 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 42 42 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 14 14 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 41 41 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 131 131 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 145 145 IMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 226 226 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 241 241 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 305 305 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 307 307 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. SQ SEQUENCE 432 AA; 46048 MW; 5D0CA7E83F0EF776 CRC64; MAKNVVVIGA QWGDEGKGKI VDWLAEEAGG VVRFQGGHNA GHTLVVGGKK TILRLIPSGI LHESLDCFIG SGVVVSPEAL LGEIDELNAA GVKNVEGRLK IAPTCPLILP YHIALDQARE ASRGKGKIGT TGRGIGPAYE DKVARRAIRA ADLLHPEKLR EKLDAVLAYY NVQLQHLHNA EPVKAEDVMA VIEKVAPRIA PMITDVSRVL NEKNKNGEKL LFEGAQGALL DIDYGTYPFV TSSNCLAGAA SAGAGVGPQM LDYVLGIVKA YTTRVGSGPF PTELFDEVGV GLAERGHEFG SVTGRARRCG WFDAAALKRS IQINGISGMC ITKLDVMDGV ETINICVGYE LPDGGKTDIL PCGSDAVETC KPIYETMPGW RESTFGVKDY GALPENAKAY LKRIEEVCGA PVAIVSTGPD REETIVLHHP FA // ID PYRH_NEIMB Reviewed; 239 AA. AC P65932; Q9JQT5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uridylate kinase; DE Short=UK; DE EC=2.7.4.22; DE AltName: Full=Uridine monophosphate kinase; DE Short=UMP kinase; DE Short=UMPK; GN Name=pyrH; OrderedLocusNames=NMB2103; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION, ENZYME REGULATION, KINETIC PARAMETERS, IDENTIFICATION BY RP MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=17210578; DOI=10.1074/jbc.M606963200; RA Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., RA Assairi L., Ionescu M., Palibroda N., Barzu O., Gilles A.-M.; RT "Regulatory mechanisms differ in UMP kinases from Gram-negative and RT Gram-positive bacteria."; RL J. Biol. Chem. 282:7242-7253(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RG New York structural genomics research consortium (NYSGRC); RT "Crystal structure analysis of uridylate kinase from Neisseria RT meningitidis."; RL Submitted (FEB-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000269|PubMed:17210578}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. CC -!- ENZYME REGULATION: Allosterically activated by GTP. Inhibited by CC UTP. {ECO:0000269|PubMed:17210578}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.98 mM for ATP (in the absence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=0.83 mM for ATP (in the presence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=8.7 uM for UMP {ECO:0000269|PubMed:17210578}; CC Vmax=35 umol/min/mg enzyme (in the absence of GTP) CC {ECO:0000269|PubMed:17210578}; CC Vmax=66 umol/min/mg enzyme (in the presence of GTP) CC {ECO:0000269|PubMed:17210578}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17210578}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42420.1; -; Genomic_DNA. DR PIR; H81006; H81006. DR RefSeq; NP_275091.1; NC_003112.2. DR RefSeq; WP_002215090.1; NC_003112.2. DR PDB; 1YBD; X-ray; 2.60 A; A/B/C=1-239. DR PDBsum; 1YBD; -. DR ProteinModelPortal; P65932; -. DR SMR; P65932; 4-239. DR STRING; 122586.NMB2103; -. DR PaxDb; P65932; -. DR DNASU; 903933; -. DR EnsemblBacteria; AAF42420; AAF42420; NMB2103. DR GeneID; 903933; -. DR KEGG; nme:NMB2103; -. DR PATRIC; 20360376; VBINeiMen85645_2685. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR HOGENOM; HOG000047187; -. DR KO; K09903; -. DR OMA; RSRADYM; -. DR OrthoDB; EOG6M0T8S; -. DR BioCyc; NMEN122586:GHGG-2168-MONOMER; -. DR BRENDA; 2.7.4.22; 3593. DR SABIO-RK; P65932; -. DR UniPathway; UPA00159; UER00275. DR EvolutionaryTrace; P65932; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_B; PyrH_B; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR015963; Uridylate_kinase_bac. DR PANTHER; PTHR21499:SF23; PTHR21499:SF23; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02075; pyrH_bact; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Pyrimidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 239 Uridylate kinase. FT /FTId=PRO_0000143866. FT NP_BIND 13 16 ATP. {ECO:0000250}. FT NP_BIND 136 143 UMP. {ECO:0000250}. FT BINDING 55 55 UMP; via amide nitrogen. {ECO:0000250}. FT BINDING 56 56 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 60 60 ATP. {ECO:0000250}. FT BINDING 75 75 UMP. {ECO:0000250}. FT BINDING 163 163 ATP. {ECO:0000250}. FT BINDING 164 164 ATP. {ECO:0000250}. FT BINDING 169 169 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 172 172 ATP. {ECO:0000250}. FT STRAND 8 14 {ECO:0000244|PDB:1YBD}. FT HELIX 16 20 {ECO:0000244|PDB:1YBD}. FT STRAND 23 26 {ECO:0000244|PDB:1YBD}. FT HELIX 29 44 {ECO:0000244|PDB:1YBD}. FT STRAND 48 53 {ECO:0000244|PDB:1YBD}. FT HELIX 56 66 {ECO:0000244|PDB:1YBD}. FT HELIX 71 95 {ECO:0000244|PDB:1YBD}. FT STRAND 100 106 {ECO:0000244|PDB:1YBD}. FT STRAND 108 111 {ECO:0000244|PDB:1YBD}. FT HELIX 117 125 {ECO:0000244|PDB:1YBD}. FT STRAND 129 134 {ECO:0000244|PDB:1YBD}. FT HELIX 143 153 {ECO:0000244|PDB:1YBD}. FT STRAND 157 162 {ECO:0000244|PDB:1YBD}. FT STRAND 164 167 {ECO:0000244|PDB:1YBD}. FT STRAND 169 171 {ECO:0000244|PDB:1YBD}. FT HELIX 173 175 {ECO:0000244|PDB:1YBD}. FT STRAND 183 186 {ECO:0000244|PDB:1YBD}. FT HELIX 187 192 {ECO:0000244|PDB:1YBD}. FT HELIX 200 208 {ECO:0000244|PDB:1YBD}. FT STRAND 213 216 {ECO:0000244|PDB:1YBD}. FT HELIX 223 229 {ECO:0000244|PDB:1YBD}. FT STRAND 234 238 {ECO:0000244|PDB:1YBD}. SQ SEQUENCE 239 AA; 25700 MW; CB08FD7E1AFBC5FE CRC64; MTQQIKYKRV LLKLSGESLM GSDPFGINHD TIVQTVGEIA EVVKMGVQVG IVVGGGNIFR GVSAQAGSMD RATADYMGMM ATVMNALALK DAFETLGIKA RVQSALSMQQ IAETYARPKA IQYLEEGKVV IFAAGTGNPF FTTDTAAALR GAEMNCDVML KATNVDGVYT ADPKKDPSAT RYETITFDEA LLKNLKVMDA TAFALCRERK LNIVVFGIAK EGSLKRVITG EDEGTLVHC // ID PYRF_NEIMB Reviewed; 246 AA. AC Q9K005; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; GN OrderedLocusNames=NMB0824; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'- CC monophosphate (OMP) to uridine 5'-monophosphate (UMP). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01200}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41237.1; -; Genomic_DNA. DR PIR; G81154; G81154. DR RefSeq; NP_273866.1; NC_003112.2. DR RefSeq; WP_002217549.1; NC_003112.2. DR ProteinModelPortal; Q9K005; -. DR STRING; 122586.NMB0824; -. DR PaxDb; Q9K005; -. DR EnsemblBacteria; AAF41237; AAF41237; NMB0824. DR GeneID; 902939; -. DR KEGG; nme:NMB0824; -. DR PATRIC; 20357033; VBINeiMen85645_1035. DR eggNOG; ENOG4106EG9; Bacteria. DR eggNOG; COG0284; LUCA. DR HOGENOM; HOG000226071; -. DR KO; K01591; -. DR OMA; NFKIFLD; -. DR OrthoDB; EOG6N6815; -. DR BioCyc; NMEN122586:GHGG-855-MONOMER; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01200_B; OMPdecase_type1_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis; KW Reference proteome. FT CHAIN 1 246 Orotidine 5'-phosphate decarboxylase. FT /FTId=PRO_0000134557. FT REGION 71 80 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT ACT_SITE 73 73 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 22 22 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 44 44 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 130 130 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 191 191 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 201 201 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 221 221 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01200}. FT BINDING 222 222 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. SQ SEQUENCE 246 AA; 26485 MW; 1493F78D78767264 CRC64; MNPLISDFQT PQQRTPVIVA LDFSNEKDTL GFVRNLDPTL CQIKIGKELF TATGRNLAES LINQGFKLFL DLKYHDIPHT VAQACKVAAD MGVWMVDMHA SGGRRMMEAA AEAVAGYGTK PLLIGVTVLT SMEQSDLAEI GLNTAPEEQV IRLAKLAQSS GLDGVVCSAQ EAAPLRRELG QDFVLVTPGI RLDVAGNNDD QRRIMTPAEA LAAGSTYLVM GRPVTQAADP VAVLREVNRV ANLEAN // ID QUEC_NEIMB Reviewed; 219 AA. AC Q9K0Q9; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633}; GN Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; GN OrderedLocusNames=NMB0525; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- CATALYTIC ACTIVITY: 7-carboxy-7-carbaguanine + NH(3) + ATP = 7- CC cyano-7-carbaguanine + ADP + phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01633}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP- CC Rule:MF_01633}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40955.1; -; Genomic_DNA. DR PIR; E81189; E81189. DR RefSeq; NP_273570.1; NC_003112.2. DR RefSeq; WP_002225597.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q9; -. DR SMR; Q9K0Q9; 5-217. DR STRING; 122586.NMB0525; -. DR PaxDb; Q9K0Q9; -. DR EnsemblBacteria; AAF40955; AAF40955; NMB0525. DR GeneID; 902640; -. DR KEGG; nme:NMB0525; -. DR PATRIC; 20356295; VBINeiMen85645_0667. DR eggNOG; ENOG4105FD2; Bacteria. DR eggNOG; COG0603; LUCA. DR HOGENOM; HOG000110563; -. DR KO; K06920; -. DR OMA; AYGYGCD; -. DR OrthoDB; EOG6091HB; -. DR BioCyc; NMEN122586:GHGG-550-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01633; QueC; 1. DR InterPro; IPR018317; QueC. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF06508; QueC; 1. DR PIRSF; PIRSF006293; ExsB; 1. DR TIGRFAMs; TIGR00364; TIGR00364; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Metal-binding; KW Nucleotide-binding; Queuosine biosynthesis; Reference proteome; Zinc. FT CHAIN 1 219 7-cyano-7-deazaguanine synthase. FT /FTId=PRO_0000246865. FT NP_BIND 10 20 ATP. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 188 188 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 196 196 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 199 199 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 202 202 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. SQ SEQUENCE 219 AA; 24473 MW; 6E23DAB40E55C7C0 CRC64; MSNQQALVIF SGGQDSTTCL IQAIQTYGRE NVQAITFQYG QRHAVELERA RWIAQDLGVK QTVLDLSLMR QITHNALMDD TAAIETAENG VPNTFVDGRN ALFLLYAAIY AKGQGIRHII AGVCETDFSG YPDCRDVFVK SMNVTLNLAM DYDFQIHTPL MYLTKAQTWA LADEMGVLDY IREQTHTCYN GIVGGCRECP SCILRERGLA EYLESKKAV // ID QUEA_NEIMB Reviewed; 346 AA. AC Q9JXW4; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113}; DE EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113}; DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113}; GN Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; GN OrderedLocusNames=NMB1859; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet CC to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give CC epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 7-aminomethyl-7- CC carbaguanosine(34) in tRNA = L-methionine + adenine + CC epoxyqueuosine(34) in tRNA. {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|HAMAP- CC Rule:MF_00113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42193.1; -; Genomic_DNA. DR PIR; D81033; D81033. DR RefSeq; NP_274855.1; NC_003112.2. DR RefSeq; WP_002248769.1; NC_003112.2. DR ProteinModelPortal; Q9JXW4; -. DR STRING; 122586.NMB1859; -. DR PaxDb; Q9JXW4; -. DR EnsemblBacteria; AAF42193; AAF42193; NMB1859. DR GeneID; 903239; -. DR KEGG; nme:NMB1859; -. DR PATRIC; 20359741; VBINeiMen85645_2376. DR eggNOG; ENOG4105E2N; Bacteria. DR eggNOG; COG0809; LUCA. DR HOGENOM; HOG000004401; -. DR KO; K07568; -. DR OMA; YGDAMFL; -. DR OrthoDB; EOG6X6RBB; -. DR BioCyc; NMEN122586:GHGG-1915-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00113; QueA; 1. DR InterPro; IPR003699; QueA. DR Pfam; PF02547; Queuosine_synth; 1. DR SUPFAM; SSF111337; SSF111337; 1. DR TIGRFAMs; TIGR00113; queA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Queuosine biosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 346 S-adenosylmethionine:tRNA FT ribosyltransferase-isomerase. FT /FTId=PRO_0000165417. SQ SEQUENCE 346 AA; 38168 MW; A172B80D032BC2E4 CRC64; MDISDFDFTL PEKLIAQHPP EVRGSSRLLV ALPDMPLQDR VFGDLPDYVE AGDVLVFNNT KVMKARLFGQ KDSGGRIEAL IERVLDNHTA LAHIRSSKSP KPGMGLVFEG GIRAVTVGRE GELFCLRFEG GETVYELLEQ NGHLPLPPYI ERAADADDDS RYQTVYAKYQ GAVAAPTAGL HFTEELLHRL KDKGAVTAEV TLHVGAGTFQ PVRVDKIEEH KMHSEWFEVP SETAAAVEAA KARGNKVWAV GTTSMRALES AARATGRLKA GQGDTDIFIT PGYRFNVVDR LVTNFHLPKS TLLMLVSAFS GMGHIRAAYR HAVEREYRFF SYGDAMVLGR NEGVVR // ID RBFA_NEIMB Reviewed; 123 AA. AC Q9JYY2; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; GN OrderedLocusNames=NMB1373; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Associates with free 30S ribosomal subunits (but not CC with 30S subunits that are part of 70S ribosomes or polysomes). CC Essential for efficient processing of 16S rRNA. May interact with CC the 5'-terminal helix region of 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00003}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003}. CC -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP- CC Rule:MF_00003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41747.1; -; Genomic_DNA. DR PIR; B81091; B81091. DR RefSeq; NP_274391.1; NC_003112.2. DR RefSeq; WP_002220822.1; NC_003112.2. DR ProteinModelPortal; Q9JYY2; -. DR STRING; 122586.NMB1373; -. DR PaxDb; Q9JYY2; -. DR EnsemblBacteria; AAF41747; AAF41747; NMB1373. DR GeneID; 903795; -. DR KEGG; nme:NMB1373; -. DR PATRIC; 20358419; VBINeiMen85645_1721. DR eggNOG; ENOG4105KG7; Bacteria. DR eggNOG; COG0858; LUCA. DR HOGENOM; HOG000218325; -. DR KO; K02834; -. DR OMA; GFIRSEV; -. DR OrthoDB; EOG6XQ3TJ; -. DR BioCyc; NMEN122586:GHGG-1411-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_00003; RbfA; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR000238; Ribosome-bd_facA. DR InterPro; IPR023799; Ribosome-bd_facA_dom. DR InterPro; IPR020053; Ribosome-bd_factorA_CS. DR Pfam; PF02033; RBFA; 1. DR ProDom; PD007327; Rib_bd_factA; 1. DR SUPFAM; SSF89919; SSF89919; 1. DR TIGRFAMs; TIGR00082; rbfA; 1. DR PROSITE; PS01319; RBFA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; rRNA processing. FT CHAIN 1 123 Ribosome-binding factor A. FT /FTId=PRO_0000102701. SQ SEQUENCE 123 AA; 14334 MW; EEA68B175A98D32E CRC64; MRKPQRGYAR QDRVKEQIMR ELAELVRTGL KDPRAGFITV NEVEVTRDYS HATVFYTILN QDAREITEEV LEHARGHLRS ELAKRIKLFK TPELHFKYDE SLERGLNLSA LIDQVAAEKP VED // ID PYRG_NEIMB Reviewed; 544 AA. AC Q9JYJ8; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; GN OrderedLocusNames=NMB1554; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41908.1; -; Genomic_DNA. DR PIR; F81070; F81070. DR RefSeq; NP_274561.1; NC_003112.2. DR RefSeq; WP_002225042.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ8; -. DR SMR; Q9JYJ8; 2-543. DR STRING; 122586.NMB1554; -. DR MEROPS; C26.964; -. DR PaxDb; Q9JYJ8; -. DR EnsemblBacteria; AAF41908; AAF41908; NMB1554. DR GeneID; 904105; -. DR KEGG; nme:NMB1554; -. DR PATRIC; 20358962; VBINeiMen85645_2000. DR eggNOG; ENOG4105C8D; Bacteria. DR eggNOG; COG0504; LUCA. DR HOGENOM; HOG000077515; -. DR KO; K01937; -. DR OMA; MRLGEYE; -. DR OrthoDB; EOG6RC3NR; -. DR BioCyc; NMEN122586:GHGG-1595-MONOMER; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 544 CTP synthase. FT /FTId=PRO_0000138206. FT DOMAIN 290 544 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT REGION 1 252 Aminator domain. FT ACT_SITE 380 380 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 517 517 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 519 519 {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 544 AA; 59929 MW; E3C67621DF52E69C CRC64; MTKFIFVTGG VVSSLGKGIA AASIAAILES RGLNVTMLKL DPYINVDPGT MSPFQHGEVF VTDDGAETDL DLGHYERFID STMTRRNSFS TGQVYENVIA KERRGDYLGG TVQVIPHITD EIKRRIHEGA AGYDVAIVEI GGTVGDIESL PFLEAIRQMR SQLGRNNTLF AHLSYVPYIA AAGEIKTKPT QHTVKEMLSI GLQPDILICR MDRTMPADER RKIALFCNVE ERAIVGSYDV DSIYECPEML HDQGIDNIIT EQLQLNVQQA DLTAWKKIVH AIQNPKHTVK IAMVGKYVDL TESYKSLIEA LKHAGIHTET DVQITFVDSE NIEKNKGDVS MLKDMDAILV PGGFGSRGVE GKIAAVRYAR ENNVPYLGIC LGMQIALIEY ARDVAGLKGA NSTEFDLKCA APVVALIDEW QTADGSVETR DESTDLGGTM RLGAQEVELK AGSLAAKIYG SGHIRERHRH RYEVNNNYVP TLEQAGLVIG GVSAGRERLV ETIELPNHPW FFACQFHPEF TSNPRKGHPL FTAFVKAALN NKKA // ID QUEE_NEIMB Reviewed; 212 AA. AC Q9K0Q5; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917}; DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917}; GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917}; GN OrderedLocusNames=NMB0529; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- CC carboxy-7-deazaguanine (CDG), a step common to the biosynthetic CC pathways of all 7-deazapurine-containing compounds. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7- CC carboxy-7-carbaguanine + NH(3). {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- CC deazaguanine synthase family. {ECO:0000255|HAMAP-Rule:MF_00917}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40959.1; -; Genomic_DNA. DR PIR; A81190; A81190. DR RefSeq; NP_273574.1; NC_003112.2. DR RefSeq; WP_002225593.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q5; -. DR STRING; 122586.NMB0529; -. DR PaxDb; Q9K0Q5; -. DR DNASU; 902644; -. DR EnsemblBacteria; AAF40959; AAF40959; NMB0529. DR GeneID; 902644; -. DR KEGG; nme:NMB0529; -. DR PATRIC; 20356305; VBINeiMen85645_0672. DR eggNOG; ENOG4105EIZ; Bacteria. DR eggNOG; COG0602; LUCA. DR HOGENOM; HOG000266142; -. DR OMA; RYYLSPC; -. DR OrthoDB; EOG6RJV40; -. DR BioCyc; NMEN122586:GHGG-554-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00917; QueE; 1. DR InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF000370; QueE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium; KW Metal-binding; Queuosine biosynthesis; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 212 7-carboxy-7-deazaguanine synthase. FT /FTId=PRO_0000416209. FT REGION 22 24 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT REGION 122 124 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 48 48 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 50 50 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 37 37 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 78 78 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 80 80 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00917}. SQ SEQUENCE 212 AA; 23710 MW; 4327B364909E0317 CRC64; MKKINVAPEN PQYRIVEIFE SLQGEGWNTG MPAVFVRLGK CNLACGWCDT DYLTFGMMGL SDILGRLKTY AARNIIITGG EPTIQPHLDM LLDTLKAEGY FLCLETNGLN PAPPQIDYVA TSPKACYAAK YENSCIETAD EVRIVADGDV LAFCENMERK IRAHHYYLSP CEQDGAMNIY DTIRQIGILN SRPDASVHWQ LSVQTHKWAG IE // ID QUEF_NEIMB Reviewed; 157 AA. AC Q9K161; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818}; GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; GN OrderedLocusNames=NMB0317; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7- CC cyano-7-carbaguanine + 2 NADPH. {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type CC 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40762.1; -; Genomic_DNA. DR PIR; H81211; H81211. DR RefSeq; NP_273366.1; NC_003112.2. DR RefSeq; WP_002224865.1; NC_003112.2. DR ProteinModelPortal; Q9K161; -. DR STRING; 122586.NMB0317; -. DR PaxDb; Q9K161; -. DR EnsemblBacteria; AAF40762; AAF40762; NMB0317. DR GeneID; 902433; -. DR KEGG; nme:NMB0317; -. DR PATRIC; 20355763; VBINeiMen85645_0401. DR eggNOG; ENOG4107YRI; Bacteria. DR eggNOG; COG0780; LUCA. DR HOGENOM; HOG000009528; -. DR KO; K09457; -. DR OMA; LITLECK; -. DR OrthoDB; EOG6D5G0M; -. DR BioCyc; NMEN122586:GHGG-337-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00818; QueF_type1; 1. DR InterPro; IPR029500; QueF. DR InterPro; IPR016856; QueF_type1. DR Pfam; PF14489; QueF; 1. DR PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1. DR TIGRFAMs; TIGR03139; QueF-II; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Queuosine biosynthesis; Reference proteome. FT CHAIN 1 157 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_0000162982. FT REGION 77 79 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00818}. FT REGION 96 97 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00818}. FT ACT_SITE 55 55 Thioimide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00818}. FT ACT_SITE 62 62 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00818}. SQ SEQUENCE 157 AA; 18107 MW; 73FCA24971D9E54D CRC64; MSRNNEELQG ISLLGNQKTQ YPTGYAPEIL EAFDNKHPDN DYFVKFVCPE FTSLCPMTGQ PDFATIYIRY IPHIKMVESK SLKLYLFSFR NHGDFHEDCV NIIMKDLIAL MDPKYIEVFG EFTPRGGIAI HPFANYGKAG TEFETLARKR LFEHDAQ // ID RECO_NEIMB Reviewed; 263 AA. AC Q9K0W0; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=DNA repair protein RecO; DE AltName: Full=Recombination protein O; GN Name=recO; OrderedLocusNames=NMB0447; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in DNA repair and RecF pathway recombination. CC Involved in pilin antigenic variation (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecO family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40884.1; -; Genomic_DNA. DR PIR; A81197; A81197. DR RefSeq; NP_273494.1; NC_003112.2. DR RefSeq; WP_002224936.1; NC_003112.2. DR ProteinModelPortal; Q9K0W0; -. DR STRING; 122586.NMB0447; -. DR PaxDb; Q9K0W0; -. DR EnsemblBacteria; AAF40884; AAF40884; NMB0447. DR GeneID; 902563; -. DR KEGG; nme:NMB0447; -. DR PATRIC; 20356106; VBINeiMen85645_0569. DR eggNOG; ENOG41071DT; Bacteria. DR eggNOG; COG1381; LUCA. DR HOGENOM; HOG000245560; -. DR KO; K03584; -. DR OMA; TALFCAM; -. DR OrthoDB; EOG6X10W9; -. DR BioCyc; NMEN122586:GHGG-471-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00201; RecO; 1. DR InterPro; IPR022572; DNA_rep/recomb_RecO_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR003717; RecO. DR Pfam; PF02565; RecO_C; 1. DR Pfam; PF11967; RecO_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00613; reco; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Reference proteome. FT CHAIN 1 263 DNA repair protein RecO. FT /FTId=PRO_0000204975. SQ SEQUENCE 263 AA; 29330 MW; 2119476724A4AD52 CRC64; MSEYRVNHEP VFMLASSPWR ESSLWVEAFS RRYGRVALLA RSARKRQSEL RGVLVPFVPV SVSWYGSQEL KTLHRAEWVG GWRQPQGRAL FGGLYVNELV LKLTAREDPV PELYDALAEV MEAVCCKAAY IDDLRRFEWR LLNLLGVAPD LNRDGDGGTI AAGGTYLVRP ETAVFPVGKG FAVPPHAAGV VAPGQSLIDL REGSFRTAES LQQALKITRL FIRHLLPEGL KSRQVLEQIR QFDRKETARE TVPTSDGTAS NAV // ID RECR_NEIMB Reviewed; 206 AA. AC Q9JZ92; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017}; GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; GN OrderedLocusNames=NMB1237; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May play a role in DNA repair. It seems to be involved CC in an RecBC-independent recombinational process of DNA repair. It CC may act with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}. CC -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP- CC Rule:MF_00017}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00017}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41618.1; -; Genomic_DNA. DR PIR; B81105; B81105. DR RefSeq; NP_274261.1; NC_003112.2. DR RefSeq; WP_002225195.1; NC_003112.2. DR ProteinModelPortal; Q9JZ92; -. DR STRING; 122586.NMB1237; -. DR PaxDb; Q9JZ92; -. DR EnsemblBacteria; AAF41618; AAF41618; NMB1237. DR GeneID; 903659; -. DR KEGG; nme:NMB1237; -. DR PATRIC; 20358071; VBINeiMen85645_1548. DR eggNOG; ENOG4105F3K; Bacteria. DR eggNOG; COG0353; LUCA. DR HOGENOM; HOG000103272; -. DR KO; K06187; -. DR OMA; DVMAIEN; -. DR OrthoDB; EOG62NX85; -. DR BioCyc; NMEN122586:GHGG-1274-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00017; RecR; 1. DR InterPro; IPR000093; DNA_Rcmb_RecR. DR InterPro; IPR023627; Rcmb_RecR. DR InterPro; IPR023628; Rcmb_RecR_C4-type_Zn. DR InterPro; IPR015967; Rcmb_RecR_CS. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF02132; RecR; 1. DR Pfam; PF13662; Toprim_4; 1. DR SUPFAM; SSF111304; SSF111304; 1. DR TIGRFAMs; TIGR00615; recR; 1. DR PROSITE; PS01300; RECR; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Metal-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 206 Recombination protein RecR. FT /FTId=PRO_0000190355. FT DOMAIN 83 178 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00017}. FT ZN_FING 60 75 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00017}. SQ SEQUENCE 206 AA; 22490 MW; 66B5E9376E335949 CRC64; MMSHKKQDAF QGLIDALKVL PNVGPKSAQR IAYHLLQHKR KEAEKLVDAL QTALKQVYHC AMCNTFCEGG LCDICADETR DGRRLMVVHM PADVSNMEAA NCHDGLYFVL MGQINTALGM DVSAIALDRL AQRLGGGEVE EIIIATAFTA EGNATAYVLS EFFKNLPYKV SRLSQGIPLG GELEYVDAGT LAQAVYERRL IKEGGA // ID RECX_NEIMB Reviewed; 153 AA. AC Q9JYQ3; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Regulatory protein RecX; GN Name=recX; OrderedLocusNames=NMB1479; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Modulates RecA activity. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RecX family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41835.1; -; Genomic_DNA. DR PIR; D81079; D81079. DR RefSeq; NP_274487.1; NC_003112.2. DR RefSeq; WP_002225089.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ3; -. DR STRING; 122586.NMB1479; -. DR PaxDb; Q9JYQ3; -. DR EnsemblBacteria; AAF41835; AAF41835; NMB1479. DR GeneID; 903901; -. DR KEGG; nme:NMB1479; -. DR PATRIC; 20358724; VBINeiMen85645_1871. DR eggNOG; ENOG4108004; Bacteria. DR eggNOG; COG2137; LUCA. DR HOGENOM; HOG000242561; -. DR KO; K03565; -. DR OMA; EVWRRKF; -. DR OrthoDB; EOG693GQ0; -. DR BioCyc; NMEN122586:GHGG-1519-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006282; P:regulation of DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 3. DR HAMAP; MF_01114; RecX; 1. DR InterPro; IPR003783; Regulatory_RecX. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02631; RecX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 153 Regulatory protein RecX. FT /FTId=PRO_0000162454. SQ SEQUENCE 153 AA; 17717 MW; 740F49970EC31E9F CRC64; MKPQKSLRAR AMDILSRQEL SRIGLKRKLA PHAESEEELE NVLNEFAERN WQSDLRYAEA YIRSKSRKHG SLRLKQALAQ QGIDEETSRN LLPDRSSEKL AAIAVLRKKF KHPAADLKEK QKQARFLAYR GFDADTVQTA LKHAWDDGWE EDC // ID RDGC_NEIMB Reviewed; 299 AA. AC Q9JZY2; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Recombination-associated protein RdgC {ECO:0000255|HAMAP-Rule:MF_00194}; GN Name=rdgC {ECO:0000255|HAMAP-Rule:MF_00194}; GN OrderedLocusNames=NMB0851; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May be involved in recombination. {ECO:0000255|HAMAP- CC Rule:MF_00194}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_00194}. CC -!- SIMILARITY: Belongs to the RdgC family. {ECO:0000255|HAMAP- CC Rule:MF_00194}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41262.1; -; Genomic_DNA. DR PIR; F81149; F81149. DR RefSeq; NP_273892.1; NC_003112.2. DR RefSeq; WP_002219474.1; NC_003112.2. DR ProteinModelPortal; Q9JZY2; -. DR STRING; 122586.NMB0851; -. DR PaxDb; Q9JZY2; -. DR EnsemblBacteria; AAF41262; AAF41262; NMB0851. DR GeneID; 902965; -. DR KEGG; nme:NMB0851; -. DR PATRIC; 20357093; VBINeiMen85645_1065. DR eggNOG; ENOG4105DH7; Bacteria. DR eggNOG; COG2974; LUCA. DR HOGENOM; HOG000117544; -. DR KO; K03554; -. DR OMA; PCSSQDI; -. DR OrthoDB; EOG6WX4MD; -. DR BioCyc; NMEN122586:GHGG-882-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00194; RdgC; 1. DR InterPro; IPR007476; RdgC. DR Pfam; PF04381; RdgC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA recombination; Reference proteome. FT CHAIN 1 299 Recombination-associated protein RdgC. FT /FTId=PRO_0000211743. SQ SEQUENCE 299 AA; 33264 MW; F239DE3B2747151A CRC64; MWFKQISFYP LNKEKLPEAD VLADKLAEAE FTHCQGLDWF SEGFTAPVSF SPELVFPADF TLRVALKKEE KVLPAGVIRD ILEEKVAEIQ NNEARNVGRK EKQELKEQIT DDLLPRAFTR SSRTEAVFNT RHGYLLVNNA ASAKAENILT KLREALGGLE ASLPNTKQSP SSLMTGWLLQ GHCEGGFELD SDCELKGTGD IVPVVKVSKQ DLTADEVVQH VKNGKTVTQL GLVWREQIAF ILTQDFTLKR IQYLDVLQEE AESNGDDAAG LAFASQILMA ESVSTMLEEL VSYLGGWQD // ID RECA_NEIMB Reviewed; 348 AA. AC P0DH59; P49984; P56988; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 11-NOV-2015, entry version 31. DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268}; DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268}; GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; GN OrderedLocusNames=NMB1445; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-297. RC STRAIN=CCUG 23094 / S3446 / Serogroup B / Serotype 14, RC HF116 / Serogroup Z / Serotype NT, HF130 / Serogroup B / Serotype NT, RC N94II / Serogroup Y / Serotype NT, and RC P63 / Serogroup B / Serotype NT / Subtype 2; RX PubMed=1406254; DOI=10.1111/j.1365-2958.1992.tb01387.x; RA Zhou J., Spratt B.G.; RT "Sequence diversity within the argF, fbp and recA genes of natural RT isolates of Neisseria meningitidis: interspecies recombination within RT the argF gene."; RL Mol. Microbiol. 6:2135-2146(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-297. RC STRAIN=CCUG 23094 / S3446 / Serogroup B / Serotype 14; RX PubMed=8995060; DOI=10.1007/BF02202111; RA Feil E., Zhou J., Maynard Smith J., Spratt B.G.; RT "A comparison of the nucleotide sequences of the adk and recA genes of RT pathogenic and commensal Neisseria species: evidence for extensive RT interspecies recombination within adk."; RL J. Mol. Evol. 43:631-640(1996). CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of CC single-stranded DNA, the ATP-dependent uptake of single-stranded CC DNA by duplex DNA, and the ATP-dependent hybridization of CC homologous single-stranded DNAs. It interacts with LexA causing CC its activation and leading to its autocatalytic cleavage. CC {ECO:0000255|HAMAP-Rule:MF_00268}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}. CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP- CC Rule:MF_00268}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41805.1; -; Genomic_DNA. DR EMBL; X64843; CAA46055.1; -; Genomic_DNA. DR EMBL; X64844; CAA46056.1; -; Genomic_DNA. DR EMBL; X64845; CAA46057.1; -; Genomic_DNA. DR EMBL; X64846; CAA46058.1; -; Genomic_DNA. DR EMBL; X64848; CAA46060.1; -; Genomic_DNA. DR EMBL; U57903; AAB49196.1; -; Genomic_DNA. DR PIR; F81082; F81082. DR PIR; S24745; S24745. DR RefSeq; NP_274457.1; NC_003112.2. DR RefSeq; WP_002213013.1; NC_003112.2. DR ProteinModelPortal; P0DH59; -. DR SMR; P0DH59; 1-326. DR STRING; 122586.NMB1445; -. DR PaxDb; P0DH59; -. DR EnsemblBacteria; AAF41805; AAF41805; NMB1445. DR GeneID; 903865; -. DR KEGG; nme:NMB1445; -. DR eggNOG; ENOG4105C68; Bacteria. DR eggNOG; COG0468; LUCA. DR HOGENOM; HOG000264120; -. DR KO; K03553; -. DR OMA; IRQNAGL; -. DR OrthoDB; EOG6ZKXNZ; -. DR BioCyc; NMEN122586:GHGG-1483-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.250.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00268; RecA; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013765; DNA_recomb/repair_RecA. DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR023400; RecA_C. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR PANTHER; PTHR22942:SF1; PTHR22942:SF1; 1. DR Pfam; PF00154; RecA; 1. DR PRINTS; PR00142; RECA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54752; SSF54752; 1. DR TIGRFAMs; TIGR02012; tigrfam_recA; 1. DR PROSITE; PS00321; RECA_1; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 348 Protein RecA. FT /FTId=PRO_0000122778. FT NP_BIND 66 73 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. FT VARIANT 138 138 I -> V (in strain: P63). SQ SEQUENCE 348 AA; 37612 MW; A6597854E45D7BA5 CRC64; MSDDKSKALA AALAQIEKSF GKGAIMKMDG SQQEENLEVI STGSLGLDLA LGVGGLPRGR IVEIFGPESS GKTTLCLEAV AQCQKNGGVC AFVDAEHAFD PVYARKLGVK VEELYLSQPD TGEQALEICD TLVRSGGIDM VVVDSVAALV PKAEIEGDMG DSHVGLQARL MSQALRKLTG HIKKTNTLVV FINQIRMKIG VMFGSPETTT GGNALKFYSS VRLDIRRTGS IKKGEEVLGN ETRVKVIKNK VAPPFRQAEF DILYGEGISW EGELIDIGVK NDIINKSGAW YSYNGAKIGQ GKDNVRVWLK ENPEVANEID AKIRALNGVE MHITEGTQDE TDGERPEE // ID RF3_NEIMB Reviewed; 531 AA. AC Q9K0H6; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Peptide chain release factor 3 {ECO:0000255|HAMAP-Rule:MF_00072}; DE Short=RF-3 {ECO:0000255|HAMAP-Rule:MF_00072}; GN Name=prfC {ECO:0000255|HAMAP-Rule:MF_00072}; GN OrderedLocusNames=NMB0626; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Increases the formation of ribosomal termination CC complexes and stimulates activities of RF-1 and RF-2. It binds CC guanine nucleotides and has strong preference for UGA stop codons. CC It may interact directly with the ribosome. The stimulation of RF- CC 1 and RF-2 is significantly reduced by GTP and GDP, but not by CC GMP. {ECO:0000255|HAMAP-Rule:MF_00072}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00072}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. PrfC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00072}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41051.1; -; Genomic_DNA. DR PIR; F81176; F81176. DR RefSeq; NP_273669.1; NC_003112.2. DR RefSeq; WP_002225531.1; NC_003112.2. DR ProteinModelPortal; Q9K0H6; -. DR SMR; Q9K0H6; 1-527. DR STRING; 122586.NMB0626; -. DR PaxDb; Q9K0H6; -. DR EnsemblBacteria; AAF41051; AAF41051; NMB0626. DR GeneID; 902739; -. DR KEGG; nme:NMB0626; -. DR PATRIC; 20356549; VBINeiMen85645_0794. DR eggNOG; ENOG4105C8A; Bacteria. DR eggNOG; COG4108; LUCA. DR HOGENOM; HOG000236725; -. DR KO; K02837; -. DR OMA; DFAEDTY; -. DR OrthoDB; EOG6677Q1; -. DR BioCyc; NMEN122586:GHGG-652-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. DR GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00072; Rel_fac_3; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004548; PrfC. DR InterPro; IPR032090; RF3_C. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF16658; RF3_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR00503; prfC; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 531 Peptide chain release factor 3. FT /FTId=PRO_0000210951. FT DOMAIN 10 278 tr-type G. FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00072}. FT NP_BIND 87 91 GTP. {ECO:0000255|HAMAP-Rule:MF_00072}. FT NP_BIND 141 144 GTP. {ECO:0000255|HAMAP-Rule:MF_00072}. SQ SEQUENCE 531 AA; 59588 MW; 4CD316A2C717E5A8 CRC64; MSQEILDQVR RRRTFAIISH PDAGKTTLTE KLLLFSGAIQ SAGTVKGKKT GKFATSDWME IEKQRGISVA SSVMQFDYKD HTVNLLDTPG HQDFSEDTYR VLTAVDSALM VIDAAKGVEA QTIKLLNVCR LRDTPIVTFM NKYDREVRDS LELLDEVENI LKIRCAPVTW PIGMGKNFKG VYHILNDEIY LFEAGGERLP HEFDIIKGID NPELEQRFPL EIQQLRDEIE LVQAASNEFN LDEFLAGELT PVFFGSAINN FGIQEILNSL IDWAPAPKPR DATVRMVEPD EPKFSGFIFK IQANMDPKHR DRIAFLRVCS GKFERGMKMK HLRINREIAA SSVVTFMSHD RELVEEAYAG DIIGIPNHGN IQIGDSFSEG EQLAFTGIPF FAPELFRSVR IKNPLKIKQL QKGLQQLGEE GAVQVFKPMS GADLILGAVG VLQFEVVTSR LANEYGVEAV FDSASIWSAR WVSCDDKKKL AEFEKANAGN LAIDAGGNLA YLAPNRVNLG LTQERWPDIV FHETREHSVK L // ID RIBA_NEIMB Reviewed; 197 AA. AC Q9JZ78; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_00179}; DE EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_00179}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_00179}; GN Name=ribA {ECO:0000255|HAMAP-Rule:MF_00179}; GN OrderedLocusNames=NMB1254; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00179}. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6- CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00179}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00179}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00179}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_00179}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. CC {ECO:0000255|HAMAP-Rule:MF_00179}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41634.1; -; Genomic_DNA. DR PIR; G81104; G81104. DR RefSeq; NP_274277.1; NC_003112.2. DR RefSeq; WP_002220947.1; NC_003112.2. DR ProteinModelPortal; Q9JZ78; -. DR SMR; Q9JZ78; 5-174. DR STRING; 122586.NMB1254; -. DR PaxDb; Q9JZ78; -. DR EnsemblBacteria; AAF41634; AAF41634; NMB1254. DR GeneID; 903677; -. DR KEGG; nme:NMB1254; -. DR PATRIC; 20358113; VBINeiMen85645_1568. DR eggNOG; ENOG4107QJN; Bacteria. DR eggNOG; COG0807; LUCA. DR HOGENOM; HOG000115442; -. DR KO; K01497; -. DR OMA; PTPFGVF; -. DR OrthoDB; EOG679TK8; -. DR BioCyc; NMEN122586:GHGG-1292-MONOMER; -. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00179; RibA; 1. DR InterPro; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR TIGRFAMs; TIGR00505; ribA; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Riboflavin biosynthesis; Zinc. FT CHAIN 1 197 GTP cyclohydrolase-2. FT /FTId=PRO_0000151765. FT NP_BIND 50 54 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT NP_BIND 93 95 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT ACT_SITE 127 127 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT ACT_SITE 129 129 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 55 55 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 66 66 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 68 68 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT BINDING 71 71 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 115 115 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 150 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 155 155 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. SQ SEQUENCE 197 AA; 21930 MW; FDC2DA4AF94C61EF CRC64; MSEMLNHVAS CRLPTEWGVF TMHGFEEANG QEHVALTVGN FSDGNPVLTR IHSECLTGDA LFSRKCDCGP QLEAAMRAVQ TEGRGIIVYL RQEGRGIGLI NKIRAYHLQD QGMDTVEANL ALGLPVDARD FRLAQSIYEY LGIRSVKLLT NNPEKIQTLK DAGINVVERI PLHVGENLEN KRYLQTKADK LGHLMSE // ID RIMP_NEIMB Reviewed; 149 AA. AC P67217; Q9JR05; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Ribosome maturation factor RimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN Name=rimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN OrderedLocusNames=NMB1641; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for maturation of 30S ribosomal subunits. CC {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SIMILARITY: Belongs to the RimP family. {ECO:0000255|HAMAP- CC Rule:MF_01077}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41990.1; -; Genomic_DNA. DR PIR; A81060; A81060. DR RefSeq; NP_274646.1; NC_003112.2. DR RefSeq; WP_002212689.1; NC_003112.2. DR ProteinModelPortal; P67217; -. DR STRING; 122586.NMB1641; -. DR PaxDb; P67217; -. DR EnsemblBacteria; AAF41990; AAF41990; NMB1641. DR GeneID; 903938; -. DR KEGG; nme:NMB1641; -. DR PATRIC; 20359202; VBINeiMen85645_2113. DR eggNOG; ENOG4105K7D; Bacteria. DR eggNOG; COG0779; LUCA. DR HOGENOM; HOG000242360; -. DR KO; K09748; -. DR OMA; GLKEFEG; -. DR OrthoDB; EOG6NSGP3; -. DR BioCyc; NMEN122586:GHGG-1690-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.180; -; 1. DR Gene3D; 3.30.300.70; -; 1. DR HAMAP; MF_01077; RimP; 1. DR InterPro; IPR003728; Ribosome_maturation_RimP. DR InterPro; IPR028998; RimP_C. DR InterPro; IPR028989; RimP_N. DR Pfam; PF02576; DUF150; 1. DR SUPFAM; SSF74942; SSF74942; 1. DR SUPFAM; SSF75420; SSF75420; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Ribosome biogenesis. FT CHAIN 1 149 Ribosome maturation factor RimP. FT /FTId=PRO_0000181895. SQ SEQUENCE 149 AA; 16636 MW; 898EC4CEDD50072D CRC64; MYIGSSMDIQ TILEKTLPGL GYELVDFELT AQGTLRVFID KESGITVEDC ATVSNHLSRV FMVEDIDYKN LEISSPGLDR PLKKAADFVR FAGQNAKIKT RLPIDGQKNF IGKIEGCEND TVTVSFDGKT VQIELGNIDK ARLRPEFKF // ID RF1_NEIMB Reviewed; 358 AA. AC Q9JY93; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093}; DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093}; GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; GN OrderedLocusNames=NMB1686; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Peptide chain release factor 1 directs the termination CC of translation in response to the peptide chain termination codons CC UAG and UAA. {ECO:0000255|HAMAP-Rule:MF_00093}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor family. {ECO:0000255|HAMAP-Rule:MF_00093}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42034.1; -; Genomic_DNA. DR PIR; G81053; G81053. DR RefSeq; NP_274690.1; NC_003112.2. DR RefSeq; WP_002222130.1; NC_003112.2. DR ProteinModelPortal; Q9JY93; -. DR SMR; Q9JY93; 8-354. DR STRING; 122586.NMB1686; -. DR PaxDb; Q9JY93; -. DR EnsemblBacteria; AAF42034; AAF42034; NMB1686. DR GeneID; 903421; -. DR KEGG; nme:NMB1686; -. DR PATRIC; 20359323; VBINeiMen85645_2168. DR eggNOG; ENOG4105C8K; Bacteria. DR eggNOG; COG0216; LUCA. DR HOGENOM; HOG000074815; -. DR KO; K02835; -. DR OMA; NRLSEHR; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; NMEN122586:GHGG-1741-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00093; Rel_fac_1; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR004373; PrfA. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00019; prfA; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 358 Peptide chain release factor 1. FT /FTId=PRO_0000177714. FT MOD_RES 235 235 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_00093}. SQ SEQUENCE 358 AA; 39793 MW; F7B51A5C6BAC9D53 CRC64; MKPSILEKLQ QLSDRLEEVT HLLGQPEATS DMDNYRKLTR EHAELTPVVE VFQNYRLAQS DLADAEEMLS DPEMKDFAAE EIEAAKAKIG ELDTELQKLL LPKDADDDKN IFIEIRAGTG GDEAALFAGD LLRMYSRYAE RNRWQVEIVS ANESELGGYK EVIARIVGLG AYSRLKFESG GHRVQRVPAT ESQGRIHTSA CTVAVMPEAD ELEDIELNPA DLRIDTFRAS GAGGQHINKT DSAVRITHLP TGMVVECQDG RSQHANKAQA MKVLAARLND AQKREAQAKE AAERKSLIGS GDRSERIRTY NYPQGRVTDH RINLTLHKLD FVMDGDLEEI TNALIAEHQA ELLAAMGD // ID RF2_NEIMB Reviewed; 367 AA. AC Q9JXB3; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094}; DE Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094}; GN Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; GN OrderedLocusNames=NMB2138; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Peptide chain release factor 2 directs the termination CC of translation in response to the peptide chain termination codons CC UGA and UAA. {ECO:0000255|HAMAP-Rule:MF_00094}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor family. {ECO:0000255|HAMAP-Rule:MF_00094}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42446.1; -; Genomic_DNA. DR PIR; H81001; H81001. DR RefSeq; NP_275123.1; NC_003112.2. DR RefSeq; WP_002225736.1; NC_003112.2. DR ProteinModelPortal; Q9JXB3; -. DR SMR; Q9JXB3; 6-367. DR STRING; 122586.NMB2138; -. DR PaxDb; Q9JXB3; -. DR EnsemblBacteria; AAF42446; AAF42446; NMB2138. DR GeneID; 903234; -. DR KEGG; nme:NMB2138; -. DR PATRIC; 20360466; VBINeiMen85645_2729. DR eggNOG; ENOG4105CG1; Bacteria. DR eggNOG; COG1186; LUCA. DR HOGENOM; HOG000074814; -. DR KO; K02836; -. DR OMA; RLYEHEM; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; NMEN122586:GHGG-2203-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00094; Rel_fac_2; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR020853; Peptide_chain_release_fac2_bac. DR InterPro; IPR004374; PrfB. DR PANTHER; PTHR11075:SF6; PTHR11075:SF6; 1. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00020; prfB; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 367 Peptide chain release factor 2. FT /FTId=PRO_0000166835. FT MOD_RES 254 254 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_00094}. SQ SEQUENCE 367 AA; 41489 MW; DC5D4417C6FAC72B CRC64; MEAEVINQLN NTLNDLEKRS EDIRVYMDYQ GKKDRLEEVI GLSEDPELWN DPKRAQEIGK ERKILEGIVL TLDNIASGIE DNRMLIEMTV EENDEEGFAA VQEDVAGLEK QMADLEFKRM FNQPADPNNC FIDITAGAGG TEAEDWAGML FRMYSRYAER KGFRIEILEE DDGEIAGINR ATIRVEGEYA YGLLRTETGV HRLVRYSPFD SNNKRHTSFA SVFVYPEIDD SIEIEINPAD LRIDTYRASG AGGQHINKTD SAVRITHEPT GIVVQCQNDR SQHANKAAAM EMLKSKLYEL EMRKRNEEKQ ALEEGKSDVG WGSQIRSYVL DSSRIKDLRT GYEVGNTKAV LDGDLDGFIE ASLKQGV // ID RIBB_NEIMB Reviewed; 363 AA. AC Q9JZ77; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; DE Short=DHBP synthase; DE EC=4.1.99.12; GN Name=ribB; OrderedLocusNames=NMB1256; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41635.1; -; Genomic_DNA. DR PIR; H81104; H81104. DR RefSeq; NP_274278.1; NC_003112.2. DR RefSeq; WP_010980912.1; NC_003112.2. DR ProteinModelPortal; Q9JZ77; -. DR STRING; 122586.NMB1256; -. DR PaxDb; Q9JZ77; -. DR EnsemblBacteria; AAF41635; AAF41635; NMB1256. DR GeneID; 903679; -. DR KEGG; nme:NMB1256; -. DR PATRIC; 20358121; VBINeiMen85645_1572. DR eggNOG; ENOG4105C66; Bacteria. DR eggNOG; COG0108; LUCA. DR eggNOG; COG0807; LUCA. DR HOGENOM; HOG000115440; -. DR KO; K14652; -. DR OMA; ECKLPTE; -. DR OrthoDB; EOG679TK8; -. DR BioCyc; NMEN122586:GHGG-1294-MONOMER; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00180; RibB; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR032677; GTP_cyclohydro_II. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Magnesium; Manganese; Metal-binding; KW Reference proteome; Riboflavin biosynthesis. FT CHAIN 1 363 3,4-dihydroxy-2-butanone 4-phosphate FT synthase. FT /FTId=PRO_0000151730. FT REGION 1 202 DHBP synthase. FT REGION 28 29 Substrate binding. {ECO:0000250}. FT REGION 141 145 Substrate binding. {ECO:0000250}. FT REGION 205 363 GTP cyclohydrolase II-like. FT METAL 29 29 Magnesium or manganese 1. {ECO:0000250}. FT METAL 29 29 Magnesium or manganese 2. {ECO:0000250}. FT METAL 144 144 Magnesium or manganese 2. {ECO:0000250}. FT BINDING 33 33 Substrate. {ECO:0000250}. FT BINDING 165 165 Substrate. {ECO:0000250}. FT SITE 127 127 Essential for catalytic activity. FT {ECO:0000250}. FT SITE 165 165 Essential for catalytic activity. FT {ECO:0000250}. SQ SEQUENCE 363 AA; 39335 MW; A12BFA091C5E2DBC CRC64; MSHISPIPEI LADIKAGKMV IITDAEDREN EGDLLMAAQF VTPEAINFMI KHARGLVCLP MDGEMVEKLG LPMMTQKNGA QYGTNFTVSI EAAHGITTGI SAADRALTIQ TAVSPTAKPE DIVQPGHIFP LRAQKGGVLV RAGHTEAGVD LAQMNGLIPA SVICEIINDD GTMARMPELM KFAEEHKLKI GTIADLIEYR SRTESLLEDM GNAPVQTPWG EFQQHVYVDK LSGETHLALV KGTPAADTET LVRVHEPFSV MDFIQANPRH SWSLPKALEH IQQAESGVVI LLHRTEDGAS LLDRTLPKGA NQAYKWDSKS YGIGAQILAG LNVKKLRVLG QPSSFTGLTG FGLEVVGFEE AEK // ID RIMM_NEIMB Reviewed; 169 AA. AC Q9K0K3; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN OrderedLocusNames=NMB0591; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: An accessory protein needed during the final step in the CC assembly of 30S ribosomal subunit, possibly for assembly of the CC head region. Probably interacts with S19. Essential for efficient CC processing of 16S rRNA. May be needed both before and after RbfA CC during the maturation of 16S rRNA. It has affinity for free CC ribosomal 30S subunits but not for 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SUBUNIT: Binds ribosomal protein S19. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SIMILARITY: Contains 1 PRC barrel domain. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41019.1; -; Genomic_DNA. DR PIR; D81180; D81180. DR RefSeq; NP_273635.1; NC_003112.2. DR RefSeq; WP_002214316.1; NC_003112.2. DR ProteinModelPortal; Q9K0K3; -. DR STRING; 122586.NMB0591; -. DR PaxDb; Q9K0K3; -. DR EnsemblBacteria; AAF41019; AAF41019; NMB0591. DR GeneID; 902706; -. DR KEGG; nme:NMB0591; -. DR PATRIC; 20356467; VBINeiMen85645_0753. DR eggNOG; ENOG4108ZR6; Bacteria. DR eggNOG; COG0806; LUCA. DR HOGENOM; HOG000220989; -. DR KO; K02860; -. DR OMA; QPWFIQR; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; NMEN122586:GHGG-617-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR Gene3D; 2.40.30.60; -; 1. DR HAMAP; MF_00014; Ribosome_mat_RimM; 1. DR InterPro; IPR011961; 16S_RimM. DR InterPro; IPR027275; PRC-brl_dom. DR InterPro; IPR011033; PRC_barrel-like. DR InterPro; IPR002676; RimM. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF05239; PRC; 1. DR Pfam; PF01782; RimM; 1. DR SUPFAM; SSF50346; SSF50346; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR02273; 16S_RimM; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 169 Ribosome maturation factor RimM. FT /FTId=PRO_0000163323. FT DOMAIN 97 169 PRC barrel. {ECO:0000255|HAMAP- FT Rule:MF_00014}. SQ SEQUENCE 169 AA; 18875 MW; 66C6F6B9D4864CB8 CRC64; MTDTQNRVAM GYIKGVFGIK GWLKIAANTE YSDSLLDYPE WHLVKDGKTI SVTLEAGKVV NGELQVKFEG INDRDLAFSL RGYTIEIPRE AFAPTEEDEY YWTDLVGMTV VNKDHTVLGK VSNLMETGAN DVLMIDGEHG QILIPFVSQY IETVDTGSKT ITADWGLDY // ID RL10_NEIMB Reviewed; 166 AA. AC P66047; Q9JQP7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 61. DE RecName: Full=50S ribosomal protein L10; GN Name=rplJ; OrderedLocusNames=NMB0130; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central CC role in the interaction of the ribosome with GTP-bound translation CC factors. {ECO:0000250}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC The N-terminus interacts with L11 and the large rRNA to form the CC base of the stalk. The C-terminus forms an elongated spine to CC which L12 dimers bind in a sequential fashion forming a multimeric CC L10(L12)X complex (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40589.1; -; Genomic_DNA. DR PIR; G81235; G81235. DR RefSeq; NP_273188.1; NC_003112.2. DR RefSeq; WP_002215373.1; NC_003112.2. DR ProteinModelPortal; P66047; -. DR STRING; 122586.NMB0130; -. DR PaxDb; P66047; -. DR PRIDE; P66047; -. DR EnsemblBacteria; AAF40589; AAF40589; NMB0130. DR GeneID; 902238; -. DR KEGG; nme:NMB0130; -. DR PATRIC; 20355279; VBINeiMen85645_0169. DR eggNOG; ENOG4108VZM; Bacteria. DR eggNOG; COG0244; LUCA. DR HOGENOM; HOG000004851; -. DR KO; K02864; -. DR OMA; GVYIRVV; -. DR OrthoDB; EOG6DNTDR; -. DR BioCyc; NMEN122586:GHGG-140-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00362; Ribosomal_L10; 1. DR InterPro; IPR022973; Ribosomal_L10. DR InterPro; IPR002363; Ribosomal_L10_eubac_CS. DR InterPro; IPR001790; Ribosomal_L10P. DR Pfam; PF00466; Ribosomal_L10; 1. DR PROSITE; PS01109; RIBOSOMAL_L10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 166 50S ribosomal protein L10. FT /FTId=PRO_0000154676. SQ SEQUENCE 166 AA; 17594 MW; E90B1423F65317EE CRC64; MSLNIETKKV AVEEISAAIA NAQTLVVAEY RGISVSSMTE LRANARKEGV YLRVLKNTLA RRAVQGTSFA ELADQMVGPL VYAASEDAVA AAKVLHQFAK KDDKIVVKAG SYNGEVMNAA QVAELASIPS REELLSKLLF VMQAPVSGFA RGLAALAEKK AGEEAA // ID RL14_NEIMB Reviewed; 122 AA. AC Q7DDT2; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=NMB0152; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit CC bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and CC together make contacts with the 16S rRNA in bridges B5 and B8. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein L14P family. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40610.1; -; Genomic_DNA. DR RefSeq; NP_273210.1; NC_003112.2. DR RefSeq; WP_002215434.1; NC_003112.2. DR ProteinModelPortal; Q7DDT2; -. DR SMR; Q7DDT2; 2-122. DR STRING; 122586.NMB0152; -. DR PaxDb; Q7DDT2; -. DR PRIDE; Q7DDT2; -. DR EnsemblBacteria; AAF40610; AAF40610; NMB0152. DR GeneID; 25048753; -. DR GeneID; 902259; -. DR KEGG; nme:NMB0152; -. DR PATRIC; 20355327; VBINeiMen85645_0193. DR eggNOG; ENOG4108UNN; Bacteria. DR eggNOG; COG0093; LUCA. DR HOGENOM; HOG000183702; -. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR BioCyc; NMEN122586:GHGG-162-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.150.20; -; 1. DR HAMAP; MF_01367; Ribosomal_L14; 1. DR InterPro; IPR000218; Ribosomal_L14P. DR InterPro; IPR005745; Ribosomal_L14P_bac-type. DR InterPro; IPR019972; Ribosomal_L14P_CS. DR PANTHER; PTHR11761; PTHR11761; 1. DR Pfam; PF00238; Ribosomal_L14; 1. DR SMART; SM01374; Ribosomal_L14; 1. DR SUPFAM; SSF50193; SSF50193; 1. DR TIGRFAMs; TIGR01067; rplN_bact; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 122 50S ribosomal protein L14. FT /FTId=PRO_0000266511. SQ SEQUENCE 122 AA; 13375 MW; 9B972CB38B626A08 CRC64; MIQMQTILDV ADNSGARRVM CIKVLGGSKR RYASVGDIIK VAVKDAAPRG RVKKGDVYNA VVVRTAKGVR RPDGALIKFD NNAAVLLNNK LEPLGTRIFG PVTRELRTER FMKIVSLAPE VL // ID RL17_NEIMB Reviewed; 122 AA. AC Q9K1I1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; GN OrderedLocusNames=NMB0169; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L32. CC {ECO:0000255|HAMAP-Rule:MF_01368}. CC -!- SIMILARITY: Belongs to the ribosomal protein L17P family. CC {ECO:0000255|HAMAP-Rule:MF_01368}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40626.1; -; Genomic_DNA. DR PIR; A81230; A81230. DR RefSeq; NP_273227.1; NC_003112.2. DR RefSeq; WP_002224774.1; NC_003112.2. DR ProteinModelPortal; Q9K1I1; -. DR SMR; Q9K1I1; 1-118. DR STRING; 122586.NMB0169; -. DR PaxDb; Q9K1I1; -. DR EnsemblBacteria; AAF40626; AAF40626; NMB0169. DR GeneID; 902276; -. DR KEGG; nme:NMB0169; -. DR PATRIC; 20355361; VBINeiMen85645_0210. DR eggNOG; ENOG4108ZT0; Bacteria. DR eggNOG; COG0203; LUCA. DR HOGENOM; HOG000019780; -. DR KO; K02879; -. DR OMA; KEGTLCA; -. DR OrthoDB; EOG6GR3GR; -. DR BioCyc; NMEN122586:GHGG-179-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1030.10; -; 1. DR HAMAP; MF_01368; Ribosomal_L17; 1. DR InterPro; IPR000456; Ribosomal_L17. DR PANTHER; PTHR14413; PTHR14413; 1. DR Pfam; PF01196; Ribosomal_L17; 1. DR SUPFAM; SSF64263; SSF64263; 1. DR TIGRFAMs; TIGR00059; L17; 1. DR PROSITE; PS01167; RIBOSOMAL_L17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 122 50S ribosomal protein L17. FT /FTId=PRO_0000267899. SQ SEQUENCE 122 AA; 13772 MW; D46FDBA374CC270F CRC64; MRHRNGNRKL NRTSSHRAAM LRNMANSLLT HEAIVTTLPK AKELRRVVEP LITLGKKPSL ANRRLAFDRT RDRDVVVKLF GDLGPRFTAR NGGYVRVLKY GFRKGDNAPL ALVELVDKPA AE // ID RL1_NEIMB Reviewed; 231 AA. AC P66088; Q9JRJ1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; GN OrderedLocusNames=NMB0128; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile CC in the ribosome, and is involved in E site tRNA release. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of the L11 operon by binding to its mRNA. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01318}. CC -!- SIMILARITY: Belongs to the ribosomal protein L1P family. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40587.1; -; Genomic_DNA. DR PIR; E81235; E81235. DR RefSeq; NP_273186.1; NC_003112.2. DR RefSeq; WP_002218415.1; NC_003112.2. DR ProteinModelPortal; P66088; -. DR SMR; P66088; 6-227. DR STRING; 122586.NMB0128; -. DR PaxDb; P66088; -. DR PRIDE; P66088; -. DR EnsemblBacteria; AAF40587; AAF40587; NMB0128. DR GeneID; 902236; -. DR KEGG; nme:NMB0128; -. DR PATRIC; 20355277; VBINeiMen85645_0168. DR eggNOG; ENOG4105C64; Bacteria. DR eggNOG; COG0081; LUCA. DR HOGENOM; HOG000207015; -. DR KO; K02863; -. DR OMA; NEGWTDF; -. DR OrthoDB; EOG6FBX2G; -. DR BioCyc; NMEN122586:GHGG-138-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.190.20; -; 2. DR Gene3D; 3.40.50.790; -; 1. DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1. DR InterPro; IPR005878; Ribosom_L1_bac-type. DR InterPro; IPR002143; Ribosomal_L1. DR InterPro; IPR023674; Ribosomal_L1-like. DR InterPro; IPR028364; Ribosomal_L1/biogenesis. DR InterPro; IPR016094; Ribosomal_L1_2-a/b-sand. DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand. DR InterPro; IPR023673; Ribosomal_L1_CS. DR Pfam; PF00687; Ribosomal_L1; 1. DR PIRSF; PIRSF002155; Ribosomal_L1; 1. DR SUPFAM; SSF56808; SSF56808; 1. DR TIGRFAMs; TIGR01169; rplA_bact; 1. DR PROSITE; PS01199; RIBOSOMAL_L1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repressor; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation; KW tRNA-binding. FT CHAIN 1 231 50S ribosomal protein L1. FT /FTId=PRO_0000125699. SQ SEQUENCE 231 AA; 24102 MW; 09D8CC821DC607C0 CRC64; MAKVSKRLKA LRSSVEANKL YAIDEAIALV KKAATAKFDE SVDVSFNLGV DPRKSDQVIR GSVVLPKGTG KITRVAVFTQ GANAEAAKEA GADIVGFEDL AAEIKAGNLN FDVVIASPDA MRIVGQLGTI LGPRGLMPNP KVGTVTPNVA EAVKNAKAGQ VQYRTDKAGI VHATIGRASF AEADLKENFD ALLDAIVKAK PAAAKGQYLK KVAVSSTMGL GIRVDTSSVN N // ID RISB_NEIMB Reviewed; 158 AA. AC P66037; Q9JQV6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178}; GN Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178}; Synonyms=ribE; GN OrderedLocusNames=NMB0684; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8- CC ribityllumazine by condensation of 5-amino-6-(D- CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. CC This is the penultimate step in the biosynthesis of riboflavin. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5- CC amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D- CC ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00178}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- SIMILARITY: Belongs to the DMRL synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41102.1; -; Genomic_DNA. DR PIR; B81172; B81172. DR RefSeq; NP_273726.1; NC_003112.2. DR RefSeq; WP_002222781.1; NC_003112.2. DR ProteinModelPortal; P66037; -. DR STRING; 122586.NMB0684; -. DR PaxDb; P66037; -. DR EnsemblBacteria; AAF41102; AAF41102; NMB0684. DR GeneID; 902796; -. DR KEGG; nme:NMB0684; -. DR PATRIC; 20356681; VBINeiMen85645_0858. DR eggNOG; ENOG4108UTT; Bacteria. DR eggNOG; COG0054; LUCA. DR HOGENOM; HOG000229250; -. DR KO; K00794; -. DR OMA; SHVAMNS; -. DR OrthoDB; EOG6RC3WC; -. DR BioCyc; NMEN122586:GHGG-712-MONOMER; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.960; -; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR002180; DMRL_synthase. DR PANTHER; PTHR21058; PTHR21058; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; SSF52121; 1. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Riboflavin biosynthesis; KW Transferase. FT CHAIN 1 158 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_0000134775. FT REGION 56 58 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 80 82 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 85 86 1-deoxy-L-glycero-tetrulose 4-phosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT ACT_SITE 88 88 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT BINDING 22 22 5-amino-6-(D-ribitylamino)uracil. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 113 113 5-amino-6-(D-ribitylamino)uracil; via FT amide nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 127 127 1-deoxy-L-glycero-tetrulose 4-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00178}. SQ SEQUENCE 158 AA; 17073 MW; B8A5A74E79185FAC CRC64; MNTIAPNLDG KHLRIGIVQA RFTNEIGSEM LKVCCRTLQE LGVADENITV ATVPGALEIP IALMNFASSE KFDALIAIGV VIRGETYHFE LVSNESGAGV SRVALDYNIP IANAVLTTEN DAQAIERIEE KASDAAKVAV ECANLVNLLL EEQFEDEE // ID RL11_NEIMB Reviewed; 144 AA. AC Q9K1J3; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=NMB0127; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC Interacts with L10 and the large rRNA to form the base of the CC stalk. L10 forms an elongated spine to which L12 dimers bind in a CC sequential fashion forming a multimeric L10(L12)X complex. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- PTM: One or more lysine residues are methylated. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40586.1; -; Genomic_DNA. DR PIR; D81235; D81235. DR RefSeq; NP_273185.1; NC_003112.2. DR RefSeq; WP_002218414.1; NC_003112.2. DR ProteinModelPortal; Q9K1J3; -. DR SMR; Q9K1J3; 2-141. DR STRING; 122586.NMB0127; -. DR PaxDb; Q9K1J3; -. DR EnsemblBacteria; AAF40586; AAF40586; NMB0127. DR GeneID; 902235; -. DR KEGG; nme:NMB0127; -. DR PATRIC; 20355275; VBINeiMen85645_0167. DR eggNOG; ENOG4108UIK; Bacteria. DR eggNOG; COG0080; LUCA. DR HOGENOM; HOG000082123; -. DR KO; K02867; -. DR OMA; CKQFNAK; -. DR OrthoDB; EOG69PQ9D; -. DR BioCyc; NMEN122586:GHGG-137-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.250; -; 1. DR Gene3D; 3.30.1550.10; -; 1. DR HAMAP; MF_00736; Ribosomal_L11; 1. DR InterPro; IPR000911; Ribosomal_L11/L12. DR InterPro; IPR006519; Ribosomal_L11_bac-typ. DR InterPro; IPR020783; Ribosomal_L11_C. DR InterPro; IPR020785; Ribosomal_L11_CS. DR InterPro; IPR020784; Ribosomal_L11_N. DR PANTHER; PTHR11661; PTHR11661; 1. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR SMART; SM00649; RL11; 1. DR SUPFAM; SSF46906; SSF46906; 1. DR SUPFAM; SSF54747; SSF54747; 1. DR TIGRFAMs; TIGR01632; L11_bact; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; 1. PE 3: Inferred from homology; KW Complete proteome; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 144 50S ribosomal protein L11. FT /FTId=PRO_0000104327. SQ SEQUENCE 144 AA; 14986 MW; 1B222AEF28D2F7FD CRC64; MAKKIIGYIK LQIPAGKANP SPPVGPALGQ RGLNIMEFCK AFNAATQGME PGLPIPVVIT AFADKSFTFV MKTPPASILL KKAAGLQKGS SNPLTNKVGK LTRAQLEEIA KTKDPDLTAA DLDAAVRTIA GSARSMGLDV EGVV // ID RL13_NEIMB Reviewed; 143 AA. AC Q7DD49; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=NMB2057; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein is one of the early assembly proteins of CC the 50S ribosomal subunit, although it is not seen to bind rRNA by CC itself. It is important during the early stages of 50S assembly. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01366}. CC -!- SIMILARITY: Belongs to the ribosomal protein L13P family. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42377.1; -; Genomic_DNA. DR RefSeq; NP_275047.1; NC_003112.2. DR RefSeq; WP_002215010.1; NC_003112.2. DR ProteinModelPortal; Q7DD49; -. DR SMR; Q7DD49; 1-142. DR STRING; 122586.NMB2057; -. DR PaxDb; Q7DD49; -. DR EnsemblBacteria; AAF42377; AAF42377; NMB2057. DR GeneID; 904023; -. DR KEGG; nme:NMB2057; -. DR PATRIC; 20360270; VBINeiMen85645_2635. DR eggNOG; ENOG4108UM5; Bacteria. DR eggNOG; COG0102; LUCA. DR HOGENOM; HOG000225286; -. DR KO; K02871; -. DR OMA; GMLPHNR; -. DR OrthoDB; EOG628FBD; -. DR BioCyc; NMEN122586:GHGG-2120-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1180.10; -; 1. DR HAMAP; MF_01366; Ribosomal_L13; 1. DR InterPro; IPR005822; Ribosomal_L13. DR InterPro; IPR005823; Ribosomal_L13_bac-type. DR InterPro; IPR023564; Ribosomal_L13_dom. DR PANTHER; PTHR11545; PTHR11545; 1. DR Pfam; PF00572; Ribosomal_L13; 1. DR PIRSF; PIRSF002181; Ribosomal_L13; 1. DR SUPFAM; SSF52161; SSF52161; 1. DR TIGRFAMs; TIGR01066; rplM_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 143 50S ribosomal protein L13. FT /FTId=PRO_0000261755. SQ SEQUENCE 143 AA; 16222 MW; F6718B35186CFBC7 CRC64; MKTFSAKPHE VKREWFVIDA QDKVLGRVAA EVASRLRGKH KPEYTPHVDT GDYIIVINAD KLRVTGAKFE DKKYFRHSGF PGGIYERTFR EMQEQFPGRA LEQAVKGMLP KGPLGYAMIK KLKVYAGAEH AHAAQQPKVL ELK // ID RL16_NEIMB Reviewed; 138 AA. AC Q7DDT4; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; GN OrderedLocusNames=NMB0149; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with CC the A and possibly P site tRNAs. {ECO:0000255|HAMAP- CC Rule:MF_01342}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01342}. CC -!- SIMILARITY: Belongs to the ribosomal protein L16P family. CC {ECO:0000255|HAMAP-Rule:MF_01342}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40607.1; -; Genomic_DNA. DR RefSeq; NP_273207.1; NC_003112.2. DR RefSeq; WP_002215430.1; NC_003112.2. DR ProteinModelPortal; Q7DDT4; -. DR SMR; Q7DDT4; 1-136. DR STRING; 122586.NMB0149; -. DR PaxDb; Q7DDT4; -. DR PRIDE; Q7DDT4; -. DR EnsemblBacteria; AAF40607; AAF40607; NMB0149. DR GeneID; 902256; -. DR KEGG; nme:NMB0149; -. DR PATRIC; 20355321; VBINeiMen85645_0190. DR eggNOG; ENOG4108R70; Bacteria. DR eggNOG; COG0197; LUCA. DR HOGENOM; HOG000164573; -. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR BioCyc; NMEN122586:GHGG-159-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1170.10; -; 1. DR HAMAP; MF_01342; Ribosomal_L16; 1. DR InterPro; IPR016180; Ribosomal_L10e/L16. DR InterPro; IPR000114; Ribosomal_L16. DR InterPro; IPR020798; Ribosomal_L16_CS. DR PANTHER; PTHR12220; PTHR12220; 1. DR Pfam; PF00252; Ribosomal_L16; 1. DR PRINTS; PR00060; RIBOSOMALL16. DR SUPFAM; SSF54686; SSF54686; 1. DR TIGRFAMs; TIGR01164; rplP_bact; 1. DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 138 50S ribosomal protein L16. FT /FTId=PRO_0000062153. SQ SEQUENCE 138 AA; 15519 MW; 7529F4E9F2131F9A CRC64; MLQPTRLKYR KQQKGRNTGI ATRGNKVSFG EFGLKAVGRG RLTARQIEAA RRAMTRHIKR GGRIWIRVFP DKPITEKPIQ VRMGGGKGNV EYYIAEIKPG KVLYEMDGVP EELAREAFEL AAAKLPIPTT FVVRQVGQ // ID RL19_NEIMB Reviewed; 121 AA. AC Q9K0K5; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE RecName: Full=50S ribosomal protein L19 {ECO:0000255|HAMAP-Rule:MF_00402}; GN Name=rplS {ECO:0000255|HAMAP-Rule:MF_00402}; GN OrderedLocusNames=NMB0589; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: This protein is located at the 30S-50S ribosomal subunit CC interface and may play a role in the structure and function of the CC aminoacyl-tRNA binding site. {ECO:0000255|HAMAP-Rule:MF_00402}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein L19P family. CC {ECO:0000255|HAMAP-Rule:MF_00402}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41017.1; -; Genomic_DNA. DR PIR; B81180; B81180. DR RefSeq; NP_273633.1; NC_003112.2. DR RefSeq; WP_002217809.1; NC_003112.2. DR ProteinModelPortal; Q9K0K5; -. DR SMR; Q9K0K5; 2-116. DR STRING; 122586.NMB0589; -. DR PaxDb; Q9K0K5; -. DR PRIDE; Q9K0K5; -. DR EnsemblBacteria; AAF41017; AAF41017; NMB0589. DR GeneID; 902704; -. DR KEGG; nme:NMB0589; -. DR PATRIC; 20356463; VBINeiMen85645_0751. DR eggNOG; ENOG4108YY1; Bacteria. DR eggNOG; COG0335; LUCA. DR HOGENOM; HOG000016264; -. DR KO; K02884; -. DR OMA; EAEQCAK; -. DR OrthoDB; EOG6DZF5W; -. DR BioCyc; NMEN122586:GHGG-615-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00402; Ribosomal_L19; 1. DR InterPro; IPR001857; Ribosomal_L19. DR InterPro; IPR018257; Ribosomal_L19_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR15680; PTHR15680; 1. DR Pfam; PF01245; Ribosomal_L19; 1. DR PIRSF; PIRSF002191; Ribosomal_L19; 1. DR PRINTS; PR00061; RIBOSOMALL19. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01024; rplS_bact; 1. DR PROSITE; PS01015; RIBOSOMAL_L19; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 121 50S ribosomal protein L19. FT /FTId=PRO_0000163496. SQ SEQUENCE 121 AA; 13768 MW; 63E5A110F5F96E77 CRC64; MNLIQQLEQE EIARLNKEIP EFAPGDTVVV SVRVVEGTRS RLQAYEGVVI ARRNRGLNSN FIVRKISSGE GVERTFQLYS PTVEKIEVKR RGDVRRAKLY YLRGLTGKAA RIKEKLPARK G // ID RL27_NEIMB Reviewed; 90 AA. AC P66130; Q9JRI8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=50S ribosomal protein L27 {ECO:0000255|HAMAP-Rule:MF_00539}; GN Name=rpmA {ECO:0000255|HAMAP-Rule:MF_00539}; GN OrderedLocusNames=NMB0324; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L27P family. CC {ECO:0000255|HAMAP-Rule:MF_00539}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40769.1; -; Genomic_DNA. DR PIR; G81212; G81212. DR RefSeq; NP_273373.1; NC_003112.2. DR RefSeq; WP_002212328.1; NC_003112.2. DR ProteinModelPortal; P66130; -. DR SMR; P66130; 2-82. DR STRING; 122586.NMB0324; -. DR PaxDb; P66130; -. DR EnsemblBacteria; AAF40769; AAF40769; NMB0324. DR GeneID; 25048335; -. DR GeneID; 902440; -. DR KEGG; nme:NMB0324; -. DR PATRIC; 20355783; VBINeiMen85645_0411. DR eggNOG; ENOG4105K46; Bacteria. DR eggNOG; COG0211; LUCA. DR HOGENOM; HOG000111610; -. DR KO; K02899; -. DR OMA; NGRNNKK; -. DR OrthoDB; EOG6N94H6; -. DR BioCyc; NMEN122586:GHGG-344-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00539; Ribosomal_L27; 1. DR InterPro; IPR001684; Ribosomal_L27. DR InterPro; IPR018261; Ribosomal_L27_CS. DR PANTHER; PTHR15893; PTHR15893; 1. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR TIGRFAMs; TIGR00062; L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 90 50S ribosomal protein L27. FT /FTId=PRO_0000181133. SQ SEQUENCE 90 AA; 9685 MW; 0A919D71A89E8295 CRC64; MASKKAGGST RNGRDSEAKR LGVKAYGNEL IPAGSIIVRQ RGTKFHAGDN VGMGKDHTLF AKVDGYVEFK TKGALNRKTV SIRPYTGSEE // ID RL18_NEIMB Reviewed; 117 AA. AC Q7DDT0; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 61. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=NMB0158; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This is one of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SIMILARITY: Belongs to the ribosomal protein L18P family. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40616.1; -; Genomic_DNA. DR RefSeq; NP_273216.1; NC_003112.2. DR RefSeq; WP_002215441.1; NC_003112.2. DR ProteinModelPortal; Q7DDT0; -. DR SMR; Q7DDT0; 2-117. DR STRING; 122586.NMB0158; -. DR PaxDb; Q7DDT0; -. DR EnsemblBacteria; AAF40616; AAF40616; NMB0158. DR GeneID; 902265; -. DR KEGG; nme:NMB0158; -. DR PATRIC; 20355339; VBINeiMen85645_0199. DR eggNOG; ENOG4105K4C; Bacteria. DR eggNOG; COG0256; LUCA. DR HOGENOM; HOG000248742; -. DR KO; K02881; -. DR OMA; KSTRSHI; -. DR OrthoDB; EOG64NB48; -. DR BioCyc; NMEN122586:GHGG-168-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1. DR InterPro; IPR005484; Ribosomal_L18. DR InterPro; IPR004389; Ribosomal_L18_bac-type. DR Pfam; PF00861; Ribosomal_L18p; 1. DR TIGRFAMs; TIGR00060; L18_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 117 50S ribosomal protein L18. FT /FTId=PRO_0000131308. SQ SEQUENCE 117 AA; 12798 MW; E1E329739EB3ED83 CRC64; MDKHTTRLRR ARKTRARIAD LKMVRLCVFR SNNHIYAQVI SAEGDKVLAQ ASTLEAEVRG SLKSGSNVEA AAIVGKRIAE KAKAAGVEKV AFDRSGFQYH GRVKALAEAA RENGLSF // ID RL33_NEIMB Reviewed; 51 AA. AC P66226; Q9JQX1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=50S ribosomal protein L33; GN Name=rpmG; OrderedLocusNames=NMB0322; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L33P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40767.1; -; Genomic_DNA. DR PIR; E81212; E81212. DR RefSeq; NP_273371.1; NC_003112.2. DR RefSeq; WP_002212306.1; NC_003112.2. DR ProteinModelPortal; P66226; -. DR SMR; P66226; 1-51. DR STRING; 122586.NMB0322; -. DR PaxDb; P66226; -. DR EnsemblBacteria; AAF40767; AAF40767; NMB0322. DR GeneID; 902438; -. DR KEGG; nme:NMB0322; -. DR PATRIC; 20355775; VBINeiMen85645_0407. DR eggNOG; ENOG4105W0E; Bacteria. DR eggNOG; COG0267; LUCA. DR HOGENOM; HOG000004839; -. DR KO; K02913; -. DR OMA; ARKHVLY; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; NMEN122586:GHGG-342-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00294; Ribosomal_L33; 1. DR InterPro; IPR001705; Ribosomal_L33. DR InterPro; IPR018264; Ribosomal_L33_CS. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF00471; Ribosomal_L33; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01023; rpmG_bact; 1. DR PROSITE; PS00582; RIBOSOMAL_L33; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 51 50S ribosomal protein L33. FT /FTId=PRO_0000170197. SQ SEQUENCE 51 AA; 5937 MW; A98181586FB41701 CRC64; MRDKIKLESS AGTGHFYTTT KNKRTMPGKL EIKKFDPVAR KHVVYKETKL K // ID RL15_NEIMB Reviewed; 144 AA. AC Q9K1I2; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; GN OrderedLocusNames=NMB0161; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SIMILARITY: Belongs to the ribosomal protein L15P family. CC {ECO:0000255|HAMAP-Rule:MF_01341}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40619.1; -; Genomic_DNA. DR PIR; C81233; C81233. DR RefSeq; NP_273219.1; NC_003112.2. DR RefSeq; WP_002215449.1; NC_003112.2. DR ProteinModelPortal; Q9K1I2; -. DR SMR; Q9K1I2; 1-143. DR STRING; 122586.NMB0161; -. DR PaxDb; Q9K1I2; -. DR EnsemblBacteria; AAF40619; AAF40619; NMB0161. DR GeneID; 902268; -. DR KEGG; nme:NMB0161; -. DR PATRIC; 20355345; VBINeiMen85645_0202. DR eggNOG; ENOG4108UZ0; Bacteria. DR eggNOG; COG0200; LUCA. DR HOGENOM; HOG000231262; -. DR KO; K02876; -. DR OMA; HKGQWAR; -. DR OrthoDB; EOG6CGCM5; -. DR BioCyc; NMEN122586:GHGG-171-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01341; Ribosomal_L15; 1. DR InterPro; IPR030878; Ribosomal_L15. DR InterPro; IPR005749; Ribosomal_L15_bac-type. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR PANTHER; PTHR12934; PTHR12934; 1. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR TIGRFAMs; TIGR01071; rplO_bact; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 144 50S ribosomal protein L15. FT /FTId=PRO_0000104770. SQ SEQUENCE 144 AA; 14882 MW; 276926308D6C33C2 CRC64; MFLNTIQPAV GATHAGRRVG RGIGSGLGKT GGRGHKGQKS RSGGFHKVGF EGGQMPLQRR LPKRGFKSLT ASANAQLRLS ELESIAVNEI DILVLKQAGL IASTVSNVKV IASGEISKAV ALKGIKVTKG ARAAIEAVGG KIEM // ID RL20_NEIMB Reviewed; 119 AA. AC Q9K093; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382}; GN Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; GN OrderedLocusNames=NMB0723; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for CC the in vitro assembly process of the 50S ribosomal subunit. It is CC not involved in the protein synthesizing functions of that CC subunit. {ECO:0000255|HAMAP-Rule:MF_00382}. CC -!- SIMILARITY: Belongs to the ribosomal protein L20P family. CC {ECO:0000255|HAMAP-Rule:MF_00382}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41136.1; -; Genomic_DNA. DR PIR; F81165; F81165. DR RefSeq; NP_273765.1; NC_003112.2. DR RefSeq; WP_002225461.1; NC_003112.2. DR ProteinModelPortal; Q9K093; -. DR SMR; Q9K093; 3-117. DR STRING; 122586.NMB0723; -. DR PaxDb; Q9K093; -. DR PRIDE; Q9K093; -. DR EnsemblBacteria; AAF41136; AAF41136; NMB0723. DR GeneID; 902836; -. DR KEGG; nme:NMB0723; -. DR PATRIC; 20356801; VBINeiMen85645_0921. DR eggNOG; ENOG4108YZX; Bacteria. DR eggNOG; COG0292; LUCA. DR HOGENOM; HOG000035046; -. DR KO; K02887; -. DR OMA; WIRNRGP; -. DR OrthoDB; EOG6CGCMB; -. DR BioCyc; NMEN122586:GHGG-752-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:InterPro. DR HAMAP; MF_00382; Ribosomal_L20; 1. DR InterPro; IPR005813; Ribosomal_L20. DR PANTHER; PTHR10986; PTHR10986; 1. DR Pfam; PF00453; Ribosomal_L20; 1. DR PRINTS; PR00062; RIBOSOMALL20. DR TIGRFAMs; TIGR01032; rplT_bact; 1. DR PROSITE; PS00937; RIBOSOMAL_L20; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 119 50S ribosomal protein L20. FT /FTId=PRO_0000177193. SQ SEQUENCE 119 AA; 13710 MW; 9B98430B554A6650 CRC64; MPRVKRGVTA RARHQKIFAL AKGYRGRRKN VYRVAKQAVM KAGQYAYRDR RQRKRQFRQL WIVRINAGTR ENGLSYSKFM NGLKRASIEI DRKVLADLAV FDKAAFAQLV EKAKAALAA // ID RL30_NEIMB Reviewed; 61 AA. AC Q7DDS9; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371}; GN Name=rpmD {ECO:0000255|HAMAP-Rule:MF_01371}; GN OrderedLocusNames=NMB0160; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01371}. CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family. CC {ECO:0000255|HAMAP-Rule:MF_01371}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40618.1; -; Genomic_DNA. DR RefSeq; NP_273218.1; NC_003112.2. DR RefSeq; WP_002215447.1; NC_003112.2. DR ProteinModelPortal; Q7DDS9; -. DR SMR; Q7DDS9; 5-61. DR STRING; 122586.NMB0160; -. DR PaxDb; Q7DDS9; -. DR EnsemblBacteria; AAF40618; AAF40618; NMB0160. DR GeneID; 902267; -. DR KEGG; nme:NMB0160; -. DR PATRIC; 20355343; VBINeiMen85645_0201. DR eggNOG; ENOG4105VPB; Bacteria. DR eggNOG; COG1841; LUCA. DR HOGENOM; HOG000039916; -. DR KO; K02907; -. DR OMA; IRKVDYL; -. DR OrthoDB; EOG6BGP7P; -. DR BioCyc; NMEN122586:GHGG-170-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1390.20; -; 1. DR HAMAP; MF_01371_B; Ribosomal_L30_B; 1. DR InterPro; IPR005996; Ribosomal_L30_bac-type. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR Pfam; PF00327; Ribosomal_L30; 1. DR PIRSF; PIRSF002211; Ribosomal_L30_bac-type; 1. DR SUPFAM; SSF55129; SSF55129; 1. DR TIGRFAMs; TIGR01308; rpmD_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 61 50S ribosomal protein L30. FT /FTId=PRO_0000273812. SQ SEQUENCE 61 AA; 6946 MW; CB7930DD00DBEE32 CRC64; MAEQKKIRVT LVKSLIGTIE SHRACARGLG LRRREHTVEV LDTPENRGMI NKISYLLKVE S // ID RL361_NEIMB Reviewed; 37 AA. AC P66293; Q9JRB2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=50S ribosomal protein L36 1 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ1 {ECO:0000255|HAMAP-Rule:MF_00251}; Synonyms=rpmJ; GN OrderedLocusNames=NMB0164; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L36P family. CC {ECO:0000255|HAMAP-Rule:MF_00251}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62305.1; -; Genomic_DNA. DR RefSeq; NP_273222.1; NC_003112.2. DR RefSeq; WP_002216248.1; NC_003112.2. DR ProteinModelPortal; P66293; -. DR SMR; P66293; 1-37. DR STRING; 122586.NMB0164; -. DR PaxDb; P66293; -. DR EnsemblBacteria; AAF62305; AAF62305; NMB0164. DR GeneID; 902271; -. DR KEGG; nme:NMB0164; -. DR PATRIC; 20355351; VBINeiMen85645_0205. DR HOGENOM; HOG000111584; -. DR KO; K02919; -. DR BioCyc; NMEN122586:GHGG-174-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00251; Ribosomal_L36; 1. DR InterPro; IPR000473; Ribosomal_L36. DR PANTHER; PTHR18804; PTHR18804; 1. DR Pfam; PF00444; Ribosomal_L36; 1. DR SUPFAM; SSF57840; SSF57840; 1. DR TIGRFAMs; TIGR01022; rpmJ_bact; 1. DR PROSITE; PS00828; RIBOSOMAL_L36; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 37 50S ribosomal protein L36 1. FT /FTId=PRO_0000126225. SQ SEQUENCE 37 AA; 4489 MW; 3FBD743EF9940F1D CRC64; MRVQPSVKKI CRNCKIIRRN RVVRVICTDL RHKQRQG // ID RL21_NEIMB Reviewed; 102 AA. AC Q7DDR4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; GN OrderedLocusNames=NMB0325; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This protein binds to 23S rRNA in the presence of CC protein L20. {ECO:0000255|HAMAP-Rule:MF_01363}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L20. CC {ECO:0000255|HAMAP-Rule:MF_01363}. CC -!- SIMILARITY: Belongs to the ribosomal protein L21P family. CC {ECO:0000255|HAMAP-Rule:MF_01363}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40770.1; -; Genomic_DNA. DR RefSeq; NP_273374.1; NC_003112.2. DR RefSeq; WP_002216394.1; NC_003112.2. DR ProteinModelPortal; Q7DDR4; -. DR STRING; 122586.NMB0325; -. DR PaxDb; Q7DDR4; -. DR EnsemblBacteria; AAF40770; AAF40770; NMB0325. DR GeneID; 902441; -. DR KEGG; nme:NMB0325; -. DR PATRIC; 20355785; VBINeiMen85645_0412. DR eggNOG; ENOG4105KK9; Bacteria. DR eggNOG; COG0261; LUCA. DR HOGENOM; HOG000036265; -. DR KO; K02888; -. DR OMA; QGHRQPF; -. DR OrthoDB; EOG6TJ84X; -. DR BioCyc; NMEN122586:GHGG-345-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01363; Ribosomal_L21; 1. DR InterPro; IPR028909; L21p-like. DR InterPro; IPR001787; Ribosomal_L21. DR InterPro; IPR018258; Ribosomal_L21_CS. DR Pfam; PF00829; Ribosomal_L21p; 1. DR SUPFAM; SSF141091; SSF141091; 1. DR TIGRFAMs; TIGR00061; L21; 1. DR PROSITE; PS01169; RIBOSOMAL_L21; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 102 50S ribosomal protein L21. FT /FTId=PRO_0000269349. SQ SEQUENCE 102 AA; 11448 MW; 26842402762BF8AC CRC64; MYAVVKTGGK QYKVSVGEKL KVEQIPAELD SQIELTEVLM IADGESVKVG APFIEGAKVT AKVVAHGRGE KVRIFKMRRR KHYQKRQGHR QNFTQIEIVA IA // ID RL22_NEIMB Reviewed; 109 AA. AC Q7DDT5; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; GN OrderedLocusNames=NMB0147; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding CC is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. CC It is important during the early stages of 50S assembly. It makes CC multiple contacts with different domains of the 23S rRNA in the CC assembled 50S subunit and ribosome (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_01331}. CC -!- FUNCTION: The globular domain of the protein is located near the CC polypeptide exit tunnel on the outside of the subunit, while an CC extended beta-hairpin is found that lines the wall of the exit CC tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family. CC {ECO:0000255|HAMAP-Rule:MF_01331}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40605.1; -; Genomic_DNA. DR RefSeq; NP_273205.1; NC_003112.2. DR RefSeq; WP_002215424.1; NC_003112.2. DR ProteinModelPortal; Q7DDT5; -. DR SMR; Q7DDT5; 1-109. DR STRING; 122586.NMB0147; -. DR PaxDb; Q7DDT5; -. DR PRIDE; Q7DDT5; -. DR EnsemblBacteria; AAF40605; AAF40605; NMB0147. DR GeneID; 902254; -. DR KEGG; nme:NMB0147; -. DR PATRIC; 20355317; VBINeiMen85645_0188. DR eggNOG; ENOG4105KAP; Bacteria. DR eggNOG; COG0091; LUCA. DR HOGENOM; HOG000205046; -. DR KO; K02890; -. DR OMA; MKRIQPR; -. DR OrthoDB; EOG6V4GKB; -. DR BioCyc; NMEN122586:GHGG-157-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.470.10; -; 1. DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1. DR InterPro; IPR001063; Ribosomal_L22. DR InterPro; IPR018260; Ribosomal_L22/L17_CS. DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type. DR PANTHER; PTHR13501; PTHR13501; 1. DR Pfam; PF00237; Ribosomal_L22; 1. DR SUPFAM; SSF54843; SSF54843; 1. DR TIGRFAMs; TIGR01044; rplV_bact; 1. DR PROSITE; PS00464; RIBOSOMAL_L22; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 109 50S ribosomal protein L22. FT /FTId=PRO_0000125189. SQ SEQUENCE 109 AA; 11909 MW; 318AAFB9E515E7C2 CRC64; MRVNAQHKNA RISAQKARLV ADLIRGKDVA QALNILAFSP KKGAELIKKV LESAIANAEH NNGADIDELK VVTIFVDKGP SLKRFQARAK GRGNRIEKQT CHINVTVGN // ID RL28_NEIMB Reviewed; 77 AA. AC P66151; Q9JQQ3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=50S ribosomal protein L28 {ECO:0000255|HAMAP-Rule:MF_00373}; GN Name=rpmB {ECO:0000255|HAMAP-Rule:MF_00373}; GN OrderedLocusNames=NMB0321; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L28P family. CC {ECO:0000255|HAMAP-Rule:MF_00373}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40766.1; -; Genomic_DNA. DR PIR; D81212; D81212. DR RefSeq; NP_273370.1; NC_003112.2. DR RefSeq; WP_002216391.1; NC_003112.2. DR ProteinModelPortal; P66151; -. DR SMR; P66151; 2-76. DR STRING; 122586.NMB0321; -. DR PaxDb; P66151; -. DR EnsemblBacteria; AAF40766; AAF40766; NMB0321. DR GeneID; 25048560; -. DR GeneID; 902437; -. DR KEGG; nme:NMB0321; -. DR PATRIC; 20355773; VBINeiMen85645_0406. DR eggNOG; ENOG4105KDC; Bacteria. DR eggNOG; COG0227; LUCA. DR HOGENOM; HOG000040462; -. DR KO; K02902; -. DR OMA; WLPSERR; -. DR OrthoDB; EOG6W727M; -. DR BioCyc; NMEN122586:GHGG-341-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00373; Ribosomal_L28; 1. DR InterPro; IPR026569; Ribo_L28/L24. DR InterPro; IPR001383; Ribosomal_L28. DR PANTHER; PTHR13528; PTHR13528; 1. DR Pfam; PF00830; Ribosomal_L28; 1. DR TIGRFAMs; TIGR00009; L28; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 77 50S ribosomal protein L28. FT /FTId=PRO_0000178516. SQ SEQUENCE 77 AA; 8818 MW; E3C08F654DF9871A CRC64; MARVCKVTGK RPMSGNNVSH ANNKTKRRFL PNLQSRRFWV ESENRWVRLR VSNAALRTID KVGIDVVLAD LRARGEA // ID RL31B_NEIMB Reviewed; 91 AA. AC Q9JZQ4; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=50S ribosomal protein L31 type B {ECO:0000255|HAMAP-Rule:MF_00502}; GN Name=rpmE2 {ECO:0000255|HAMAP-Rule:MF_00502}; GN OrderedLocusNames=NMB0942; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00502}. CC -!- SIMILARITY: Belongs to the ribosomal protein L31P family. Type B CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00502}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41348.1; -; Genomic_DNA. DR PIR; C81140; C81140. DR RefSeq; NP_273980.1; NC_003112.2. DR RefSeq; WP_002217400.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ4; -. DR STRING; 122586.NMB0942; -. DR PaxDb; Q9JZQ4; -. DR EnsemblBacteria; AAF41348; AAF41348; NMB0942. DR GeneID; 903062; -. DR KEGG; nme:NMB0942; -. DR PATRIC; 20357365; VBINeiMen85645_1197. DR eggNOG; ENOG4105NRA; Bacteria. DR eggNOG; COG0254; LUCA. DR HOGENOM; HOG000284894; -. DR KO; K02909; -. DR OMA; ARFQQRF; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; NMEN122586:GHGG-979-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00502; Ribosomal_L31_2; 1. DR InterPro; IPR002150; Ribosomal_L31. DR InterPro; IPR027493; Ribosomal_L31_B. DR Pfam; PF01197; Ribosomal_L31; 1. DR PRINTS; PR01249; RIBOSOMALL31. DR TIGRFAMs; TIGR00105; L31; 1. DR PROSITE; PS01143; RIBOSOMAL_L31; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 91 50S ribosomal protein L31 type B. FT /FTId=PRO_0000173240. SQ SEQUENCE 91 AA; 10465 MW; 5B08932DEFC4A6CD CRC64; MKPNIHPDNY RTVLFFDSSA NEGWLIRSCA ETHGKTMVWT DGKEYPLFSL DTSSASHPVY TGKQRNVNTE GRASKFNQRF QSVMSSFRKD K // ID RL29_NEIMB Reviewed; 63 AA. AC P66169; Q9JQX4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=50S ribosomal protein L29; GN Name=rpmC; OrderedLocusNames=NMB0150; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L29P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40608.1; -; Genomic_DNA. DR PIR; H81231; H81231. DR RefSeq; NP_273208.1; NC_003112.2. DR RefSeq; WP_002215432.1; NC_003112.2. DR ProteinModelPortal; P66169; -. DR STRING; 122586.NMB0150; -. DR PaxDb; P66169; -. DR EnsemblBacteria; AAF40608; AAF40608; NMB0150. DR GeneID; 902257; -. DR KEGG; nme:NMB0150; -. DR PATRIC; 20355323; VBINeiMen85645_0191. DR eggNOG; ENOG41083MP; Bacteria. DR eggNOG; COG0255; LUCA. DR HOGENOM; HOG000248754; -. DR KO; K02904; -. DR OMA; MRMQAST; -. DR OrthoDB; EOG6VTK8Z; -. DR BioCyc; NMEN122586:GHGG-160-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.310; -; 1. DR HAMAP; MF_00374; Ribosomal_L29; 1. DR InterPro; IPR001854; Ribosomal_L29. DR InterPro; IPR018254; Ribosomal_L29_CS. DR Pfam; PF00831; Ribosomal_L29; 1. DR SUPFAM; SSF46561; SSF46561; 1. DR TIGRFAMs; TIGR00012; L29; 1. DR PROSITE; PS00579; RIBOSOMAL_L29; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 63 50S ribosomal protein L29. FT /FTId=PRO_0000130427. SQ SEQUENCE 63 AA; 7078 MW; A7B1633418280B9B CRC64; MKANELKDKS VEQLNADLLD LLKAQFGLRM QNATGQLGKP SELKRVRRDI ARIKTVLTEK GAK // ID RL34_NEIMB Reviewed; 44 AA. AC P66251; Q9JRA1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 13-APR-2016, entry version 58. DE RecName: Full=50S ribosomal protein L34; GN Name=rpmH; OrderedLocusNames=NMB1904; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L34P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42234.1; -; Genomic_DNA. DR PIR; G81027; G81027. DR RefSeq; NP_274898.1; NC_003112.2. DR RefSeq; WP_002214728.1; NC_003112.2. DR ProteinModelPortal; P66251; -. DR SMR; P66251; 1-44. DR STRING; 122586.NMB1904; -. DR PaxDb; P66251; -. DR EnsemblBacteria; AAF42234; AAF42234; NMB1904. DR GeneID; 25048442; -. DR GeneID; 904264; -. DR KEGG; nme:NMB1904; -. DR PATRIC; 20359851; VBINeiMen85645_2430. DR eggNOG; ENOG4105VG0; Bacteria. DR eggNOG; COG0230; LUCA. DR HOGENOM; HOG000111572; -. DR KO; K02914; -. DR BioCyc; NMEN122586:GHGG-1961-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00391; Ribosomal_L34; 1. DR InterPro; IPR000271; Ribosomal_L34. DR InterPro; IPR020939; Ribosomal_L34_CS. DR PANTHER; PTHR14503; PTHR14503; 1. DR Pfam; PF00468; Ribosomal_L34; 1. DR ProDom; PD003101; Ribosomal_L34; 1. DR TIGRFAMs; TIGR01030; rpmH_bact; 1. DR PROSITE; PS00784; RIBOSOMAL_L34; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 44 50S ribosomal protein L34. FT /FTId=PRO_0000187427. SQ SEQUENCE 44 AA; 5051 MW; 464395813C8808DA CRC64; MKRTYQPSVT KRKRTHGFLV RSKTRGGRAV LAARRAKGRK RLAV // ID RL23_NEIMB Reviewed; 104 AA. AC Q9K1I6; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=NMB0144; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. CC One of the proteins that surrounds the polypeptide exit tunnel on CC the outside of the ribosome. Forms the main docking site for CC trigger factor binding to the ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01369}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, CC and trigger factor when it is bound to the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40602.1; -; Genomic_DNA. DR PIR; B81231; B81231. DR RefSeq; NP_273202.1; NC_003112.2. DR RefSeq; WP_002243944.1; NC_003112.2. DR ProteinModelPortal; Q9K1I6; -. DR SMR; Q9K1I6; 1-92. DR STRING; 122586.NMB0144; -. DR PaxDb; Q9K1I6; -. DR PRIDE; Q9K1I6; -. DR EnsemblBacteria; AAF40602; AAF40602; NMB0144. DR GeneID; 902251; -. DR KEGG; nme:NMB0144; -. DR PATRIC; 20355311; VBINeiMen85645_0185. DR eggNOG; ENOG41080KG; Bacteria. DR eggNOG; COG0089; LUCA. DR HOGENOM; HOG000231364; -. DR KO; K02892; -. DR OMA; KGIVGRQ; -. DR OrthoDB; EOG6HTP4P; -. DR BioCyc; NMEN122586:GHGG-154-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 104 50S ribosomal protein L23. FT /FTId=PRO_0000272783. SQ SEQUENCE 104 AA; 11268 MW; DD24B74FFB62D049 CRC64; MNQQRLTQVI LAPIVSEKSN VLAEKRNQMT FKVLANATKP EIKAAVELLF GVQVADVTTV TIKGKVKRFG RTLGRRSDVK KAYVSLAAGQ ELDLEAAAAA ADKE // ID RL24_NEIMB Reviewed; 107 AA. AC P60733; Q9JQQ7; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=NMB0153; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of two assembly initiator proteins, it binds CC directly to the 5'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit CC tunnel on the outside of the subunit. {ECO:0000255|HAMAP- CC Rule:MF_01326}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01326}. CC -!- SIMILARITY: Belongs to the ribosomal protein L24P family. CC {ECO:0000255|HAMAP-Rule:MF_01326}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40611.1; -; Genomic_DNA. DR PIR; C81232; C81232. DR RefSeq; NP_273211.1; NC_003112.2. DR RefSeq; WP_002215435.1; NC_003112.2. DR ProteinModelPortal; P60733; -. DR STRING; 122586.NMB0153; -. DR PaxDb; P60733; -. DR EnsemblBacteria; AAF40611; AAF40611; NMB0153. DR GeneID; 902260; -. DR KEGG; nme:NMB0153; -. DR PATRIC; 20355329; VBINeiMen85645_0194. DR eggNOG; ENOG4105KAR; Bacteria. DR eggNOG; COG0198; LUCA. DR HOGENOM; HOG000039892; -. DR KO; K02895; -. DR OMA; NVNIVKR; -. DR OrthoDB; EOG6FFSDM; -. DR BioCyc; NMEN122586:GHGG-163-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR003256; Ribosomal_L24. DR InterPro; IPR005825; Ribosomal_L24/26_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF17136; ribosomal_L24; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01079; rplX_bact; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 107 50S ribosomal protein L24. FT /FTId=PRO_0000130686. SQ SEQUENCE 107 AA; 11667 MW; E1CEAA2F0A93A24C CRC64; MNKIIKGDRV VVIAGKDKGK QGQVVRVLGD KVVVEGVNVV KRHQKPNPMR GIEGGIITKE MPLDISNIAI LNPETNKADR VGIKLIENEG KVKRVRFFKS NGSIIGA // ID RL31_NEIMB Reviewed; 71 AA. AC P66190; Q9JR74; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; GN OrderedLocusNames=NMB1956; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00501}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}. CC -!- SIMILARITY: Belongs to the ribosomal protein L31P family. Type A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00501}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42285.1; -; Genomic_DNA. DR PIR; E81021; E81021. DR RefSeq; NP_274950.1; NC_003112.2. DR RefSeq; WP_002218070.1; NC_003112.2. DR ProteinModelPortal; P66190; -. DR STRING; 122586.NMB1956; -. DR PaxDb; P66190; -. DR EnsemblBacteria; AAF42285; AAF42285; NMB1956. DR GeneID; 904194; -. DR KEGG; nme:NMB1956; -. DR PATRIC; 20359971; VBINeiMen85645_2490. DR eggNOG; ENOG4105VFB; Bacteria. DR eggNOG; COG0254; LUCA. DR HOGENOM; HOG000284895; -. DR KO; K02909; -. DR OMA; EMITANC; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; NMEN122586:GHGG-2013-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00501; Ribosomal_L31_1; 1. DR InterPro; IPR002150; Ribosomal_L31. DR InterPro; IPR027491; Ribosomal_L31_A. DR Pfam; PF01197; Ribosomal_L31; 1. DR PRINTS; PR01249; RIBOSOMALL31. DR TIGRFAMs; TIGR00105; L31; 1. DR PROSITE; PS01143; RIBOSOMAL_L31; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc. FT CHAIN 1 71 50S ribosomal protein L31. FT /FTId=PRO_0000173136. FT METAL 16 16 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 18 18 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 38 38 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 41 41 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. SQ SEQUENCE 71 AA; 8118 MW; 59331C1E436792CC CRC64; MKQGIHPNYH EVNVTCSCGN KFATKSAMEK ENFNIEVCSL CHPFYTGTQK IVDTTGRVDK FNNKFGNLFK R // ID RL25_NEIMB Reviewed; 190 AA. AC Q9JZW3; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334}; DE AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334}; GN Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334}; GN Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334}; GN OrderedLocusNames=NMB0876; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in CC the ribosome where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01334}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S CC rRNA independently of L5 and L18. {ECO:0000255|HAMAP- CC Rule:MF_01334}. CC -!- SIMILARITY: Belongs to the ribosomal protein L25P family. CTC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41287.1; -; Genomic_DNA. DR PIR; G81146; G81146. DR RefSeq; NP_273917.1; NC_003112.2. DR RefSeq; WP_002213865.1; NC_003112.2. DR ProteinModelPortal; Q9JZW3; -. DR STRING; 122586.NMB0876; -. DR PaxDb; Q9JZW3; -. DR EnsemblBacteria; AAF41287; AAF41287; NMB0876. DR GeneID; 902995; -. DR KEGG; nme:NMB0876; -. DR PATRIC; 20357157; VBINeiMen85645_1092. DR eggNOG; ENOG4105KW6; Bacteria. DR eggNOG; COG1825; LUCA. DR HOGENOM; HOG000214907; -. DR KO; K02897; -. DR OMA; CVLYGGD; -. DR OrthoDB; EOG6SZ1PC; -. DR BioCyc; NMEN122586:GHGG-912-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.170.120.20; -; 1. DR Gene3D; 2.40.240.10; -; 1. DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1. DR HAMAP; MF_01336; Ribosomal_L25; 1. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR029751; Ribosomal_L25. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR020057; Ribosomal_L25_b-dom. DR InterPro; IPR001021; Ribosomal_L25_long. DR InterPro; IPR020055; Ribosomal_L25_short. DR Pfam; PF01386; Ribosomal_L25p; 1. DR Pfam; PF14693; Ribosomal_TL5_C; 1. DR ProDom; PD012503; Ribosomal_L25; 1. DR SUPFAM; SSF50715; SSF50715; 1. DR TIGRFAMs; TIGR00731; bL25_bact_ctc; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 190 50S ribosomal protein L25. FT /FTId=PRO_0000181573. SQ SEQUENCE 190 AA; 20956 MW; 7086A835B920F63B CRC64; MTYEIQASVR EAQGTGASRR LRREGQIPGI LYGEGQEPVA IAVDHKTVFY ALEKESFHTA LIKLSLNGET KDVIVRDFQM HPFRREVQHI DFQAVKADQL VRIRVPLHIV NAENSQAVKL QGGRVSLLNT SVEVVALPAN IPAFLDLDCA EVVAGDILHL SDIKLPEGVE SVSLKRNENL AVATVTGKKR // ID RL32_NEIMB Reviewed; 59 AA. AC Q9JXS0; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 79. DE RecName: Full=50S ribosomal protein L32; GN Name=rpmF; OrderedLocusNames=NMB1911; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L32P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42241.1; -; Genomic_DNA. DR PIR; F81028; F81028. DR RefSeq; NP_274905.1; NC_003112.2. DR RefSeq; WP_002214744.1; NC_003112.2. DR ProteinModelPortal; Q9JXS0; -. DR SMR; Q9JXS0; 2-54. DR STRING; 122586.NMB1911; -. DR PaxDb; Q9JXS0; -. DR EnsemblBacteria; AAF42241; AAF42241; NMB1911. DR GeneID; 904253; -. DR KEGG; nme:NMB1911; -. DR PATRIC; 20359865; VBINeiMen85645_2437. DR eggNOG; ENOG4105VGS; Bacteria. DR eggNOG; COG0333; LUCA. DR HOGENOM; HOG000040269; -. DR KO; K02911; -. DR OMA; HRAHDFL; -. DR OrthoDB; EOG6VMTT4; -. DR BioCyc; NMEN122586:GHGG-1968-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00340; Ribosomal_L32; 1. DR InterPro; IPR002677; Ribosomal_L32p. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01783; Ribosomal_L32p; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01031; rpmF_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 59 50S ribosomal protein L32. FT /FTId=PRO_0000172376. SQ SEQUENCE 59 AA; 6473 MW; A40C6A906CD631E1 CRC64; MAVQQNKKSP SKRGMHRSHD ALTAPALSVD STTGEVHRPH HISPNGMYRG RKVVKAKGE // ID RL3_NEIMB Reviewed; 214 AA. AC P60444; Q9JRH6; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=NMB0142; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly near the 3'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SIMILARITY: Belongs to the ribosomal protein L3P family. CC {ECO:0000255|HAMAP-Rule:MF_01325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40600.1; -; Genomic_DNA. DR PIR; H81230; H81230. DR RefSeq; NP_273200.1; NC_003112.2. DR RefSeq; WP_002215400.1; NC_003112.2. DR ProteinModelPortal; P60444; -. DR SMR; P60444; 3-211. DR STRING; 122586.NMB0142; -. DR PaxDb; P60444; -. DR PRIDE; P60444; -. DR EnsemblBacteria; AAF40600; AAF40600; NMB0142. DR GeneID; 902249; -. DR KEGG; nme:NMB0142; -. DR PATRIC; 20355307; VBINeiMen85645_0183. DR eggNOG; ENOG4105EEE; Bacteria. DR eggNOG; COG0087; LUCA. DR HOGENOM; HOG000100368; -. DR KO; K02906; -. DR OMA; NVVMIKG; -. DR OrthoDB; EOG6WDSMH; -. DR BioCyc; NMEN122586:GHGG-152-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1. DR InterPro; IPR000597; Ribosomal_L3. DR InterPro; IPR019927; Ribosomal_L3_bac/org-type. DR InterPro; IPR019926; Ribosomal_L3_CS. DR InterPro; IPR009000; Transl_B-barrel. DR PANTHER; PTHR11229; PTHR11229; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR03625; L3_bact; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. PE 3: Inferred from homology; KW Complete proteome; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 214 50S ribosomal protein L3. FT /FTId=PRO_0000077127. FT MOD_RES 153 153 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_01325}. SQ SEQUENCE 214 AA; 22678 MW; 11B5CB61336FD378 CRC64; MTLGLVGRKV GMTRVFDEQG VSVPVTVLDM SANRVTQVKS KDTDGYTAVQ VTFGQKKANR VNKAEAGHFA KAGVEAGRGL IEFALTEEKL AELKAGDEIT VSMFEVGQLV DVTGTSKGKG FSGTIKRHNF GAQRTSHGNS RSHRVPGSIG MAQDPGRVFP GKRMAGQYGN TKATVQKLEV VRVDAERQLL LVKGAVPGAV NSDVVVRPSV KVGA // ID RLMN_NEIMB Reviewed; 364 AA. AC Q9JZ42; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849}; GN OrderedLocusNames=NMB1308; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 CC modification seems to play a crucial role in the proofreading step CC occurring at the peptidyl transferase center and thus would serve CC to optimize ribosomal fidelity. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in CC 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L- CC homocysteine + L-methionine + 5'-deoxyadenosine + 2- CC methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in CC tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + CC L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism CC involving intermediate methylation of a conserved cysteine CC residue. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41683.1; -; Genomic_DNA. DR PIR; B81098; B81098. DR RefSeq; NP_274327.1; NC_003112.2. DR RefSeq; WP_002219171.1; NC_003112.2. DR ProteinModelPortal; Q9JZ42; -. DR STRING; 122586.NMB1308; -. DR PaxDb; Q9JZ42; -. DR EnsemblBacteria; AAF41683; AAF41683; NMB1308. DR GeneID; 903730; -. DR KEGG; nme:NMB1308; -. DR PATRIC; 20358261; VBINeiMen85645_1642. DR eggNOG; ENOG4105C55; Bacteria. DR eggNOG; COG0820; LUCA. DR HOGENOM; HOG000217992; -. DR KO; K06941; -. DR OMA; IYHFGVS; -. DR OrthoDB; EOG6DJZ2N; -. DR BioCyc; NMEN122586:GHGG-1346-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR30544; PTHR30544; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron; KW Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 364 Dual-specificity RNA methyltransferase FT RlmN. FT /FTId=PRO_0000350278. FT REGION 164 165 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT REGION 218 220 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT ACT_SITE 91 91 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01849}. FT ACT_SITE 338 338 S-methylcysteine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 196 196 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 295 295 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT DISULFID 104 338 (transient). {ECO:0000255|HAMAP- FT Rule:MF_01849}. SQ SEQUENCE 364 AA; 40935 MW; C79777AFE7391A86 CRC64; MKTNLLNYDL QGLTRHFADM GEKPFRAKQV MRWMHQSGAQ NFDEMTDLAK SLRHKLNEQA GIEIPKLMMS QKSSDGTRKW LLDVGTGNGV ETVFIPESDR GTLCISSQVG CALECTFCST GRQGFNRNLT AAEIIGQLWW ANKAMGVTPK NERVISNVVM MGMGEPMANF DNVVTALSIM LDDHGYGLSR RRVTVSTSGM VPQMDRLRDV MPVALAVSLH ASNDEVRNQI VPLNKKYPLK ELMAACQRYL VKAPRDFITF EYVMLDGIND KAQHARELIE LVTDVPCKFN LIPFNPFPNS GYERSSNENI RVFRDILQQA GFVVTVRKTR GDDIDAACGQ LAGQVQDKTR RQQKWQQILI GQQG // ID RLPA_NEIMB Reviewed; 239 AA. AC Q9K1A0; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=RlpA-like protein; DE Flags: Precursor; GN OrderedLocusNames=NMB0267; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SPOR domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40721.1; -; Genomic_DNA. DR PIR; D81218; D81218. DR RefSeq; NP_273323.1; NC_003112.2. DR RefSeq; WP_002221924.1; NC_003112.2. DR ProteinModelPortal; Q9K1A0; -. DR STRING; 122586.NMB0267; -. DR PaxDb; Q9K1A0; -. DR DNASU; 902378; -. DR EnsemblBacteria; AAF40721; AAF40721; NMB0267. DR GeneID; 902378; -. DR KEGG; nme:NMB0267; -. DR PATRIC; 20355616; VBINeiMen85645_0332. DR eggNOG; ENOG4105K6T; Bacteria. DR eggNOG; COG0797; LUCA. DR HOGENOM; HOG000254768; -. DR KO; K03642; -. DR OMA; QARGMIQ; -. DR OrthoDB; EOG6X3W9K; -. DR BioCyc; NMEN122586:GHGG-282-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR Gene3D; 2.40.40.10; -; 1. DR InterPro; IPR009009; RlpA-like_DPBB. DR InterPro; IPR012997; RplA. DR InterPro; IPR007730; SPOR_dom. DR Pfam; PF03330; DPBB_1; 1. DR Pfam; PF05036; SPOR; 1. DR SUPFAM; SSF50685; SSF50685; 1. DR TIGRFAMs; TIGR00413; rlpA; 1. DR PROSITE; PS51724; SPOR; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 239 RlpA-like protein. FT /FTId=PRO_0000030807. FT DOMAIN 160 239 SPOR. SQ SEQUENCE 239 AA; 25994 MW; 629EA8EFB7DF693A CRC64; MTLTRKTLFL LTAAFGTHSL QTASADAVVK AEKLHASANR SYKVAGKRYT PKNQVAEFTQ TGNASWYGGR FHGRKTSGGE RYDMNAFTAA HKTLPIPSYV RVTNTKNGKS VIVRVNDRGP FHGNRIIDVS KAAAQKLGFV NQGTAHVKIE QIVPGQSAPV AENKDIFIDL KSFGTEHEAQ AYLNQAAQNF AVSSSGTNLS VEKRRYEYVV KMGPFTSQER AAEAEAQARG MVRAVLTAG // ID RLUD_NEIMB Reviewed; 374 AA. AC Q9K0B0; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribosomal large subunit pseudouridine synthase D; DE EC=5.4.99.23; DE AltName: Full=23S rRNA pseudouridine(1911/1915/1917) synthase; DE AltName: Full=rRNA pseudouridylate synthase D; DE AltName: Full=rRNA-uridine isomerase D; GN Name=rluD; OrderedLocusNames=NMB0704; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil CC at positions 1911, 1915 and 1917 in 23S ribosomal RNA. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 23S rRNA CC uridine(1911)/uridine(1915)/uridine(1917) = 23S rRNA CC pseudouridine(1911)/pseudouridine(1915)/pseudouridine(1917). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41121.1; -; Genomic_DNA. DR PIR; A81168; A81168. DR RefSeq; NP_273746.1; NC_003112.2. DR RefSeq; WP_002247551.1; NC_003112.2. DR ProteinModelPortal; Q9K0B0; -. DR SMR; Q9K0B0; 98-334. DR STRING; 122586.NMB0704; -. DR PaxDb; Q9K0B0; -. DR EnsemblBacteria; AAF41121; AAF41121; NMB0704. DR GeneID; 902816; -. DR KEGG; nme:NMB0704; -. DR PATRIC; 20356749; VBINeiMen85645_0896. DR eggNOG; ENOG4105C34; Bacteria. DR eggNOG; COG0564; LUCA. DR HOGENOM; HOG000275919; -. DR KO; K06180; -. DR OMA; TYGGRPR; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NMEN122586:GHGG-732-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; RNA-binding; KW rRNA processing. FT CHAIN 1 374 Ribosomal large subunit pseudouridine FT synthase D. FT /FTId=PRO_0000162694. FT DOMAIN 39 112 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 160 160 {ECO:0000250}. SQ SEQUENCE 374 AA; 41453 MW; E5648CACB9A1A9DF CRC64; MQNTSFDNES DYSDDSDFAS ASETENRIGL TVPLELAGGR LDAVLAKLLP DYSRSRLTSW IKEGAVIVND KPSQPKDKMI GGEQICVTVR PSEENLAFVP EPMALDIVYE DDTVIVVNKP AGLVVHPAAG NWTGTLLNGL LAHCPELSQV PRAGIVHRLD KETSGLMVVA KTLPAQNSLV RQLQERTVKR IYRAVANGIV PFDGKIETQI GRDPHNRLKM AVVKFGGKPA VTHVKVLERY LTHSYIECSL ETGRTHQIRV HMREANHPLA ADPVYGNPRH PCGDTVKEAV KSLGARQALH AYRLSFTHPE SGETVSFEAP IPNDIYHLLS VLRLEAGLDS SLSNEEEWQD KFGADDDDDW NEDDYDVEVV YVRE // ID RL2_NEIMB Reviewed; 277 AA. AC Q9K1I5; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; GN OrderedLocusNames=NMB0145; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for CC association of the 30S and 50S subunits to form the 70S ribosome, CC for tRNA binding and peptide bond formation. It has been suggested CC to have peptidyltransferase activity; this is somewhat CC controversial. Makes several contacts with the 16S rRNA in the 70S CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the CC 30S subunit in the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01320}. CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family. CC {ECO:0000255|HAMAP-Rule:MF_01320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40603.1; -; Genomic_DNA. DR PIR; C81231; C81231. DR RefSeq; NP_273203.1; NC_003112.2. DR RefSeq; WP_002221850.1; NC_003112.2. DR ProteinModelPortal; Q9K1I5; -. DR SMR; Q9K1I5; 2-272. DR STRING; 122586.NMB0145; -. DR PaxDb; Q9K1I5; -. DR EnsemblBacteria; AAF40603; AAF40603; NMB0145. DR GeneID; 902252; -. DR KEGG; nme:NMB0145; -. DR PATRIC; 20355313; VBINeiMen85645_0186. DR eggNOG; ENOG4105CFD; Bacteria. DR eggNOG; COG0090; LUCA. DR HOGENOM; HOG000232982; -. DR KO; K02886; -. DR OMA; HNRGVTM; -. DR OrthoDB; EOG6TR0J1; -. DR BioCyc; NMEN122586:GHGG-155-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 4.10.950.10; -; 1. DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR005880; Ribosomal_L2_bac/org-type. DR InterPro; IPR022669; Ribosomal_L2_C. DR InterPro; IPR022671; Ribosomal_L2_CS. DR InterPro; IPR014726; Ribosomal_L2_dom3. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR13691; PTHR13691; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SMART; SM01383; Ribosomal_L2; 1. DR SMART; SM01382; Ribosomal_L2_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR01171; rplB_bact; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 277 50S ribosomal protein L2. FT /FTId=PRO_0000129589. SQ SEQUENCE 277 AA; 30125 MW; 121EB985B7B67E58 CRC64; MAIVKMKPTS AGRRGMVRVV TEGLYKGAPY APLLEKKNST AGRNNNGHIT TRHKGGGHKH HYRVVDFKRN KDGIPAKVER IEYDPNRTAF IALLCYADGE RRYIIAPRGI QAGAVLVSGA EAAIKVGNTL PIRNIPVGTT IHCIEMKPGK GAQIARSAGA SAVLLAKEGA YAQVRLRSGE VRKINVDCRA TIGEVGNEEQ SLKKIGKAGA NRWRGIRPTV RGVVMNPVDH PHGGGEGRTG EAREPVSPWG TPAKGYRTRN NKRTDNMIVR RRYSNKG // ID RL362_NEIMB Reviewed; 41 AA. AC P66295; Q9JQV0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=50S ribosomal protein L36 2 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ2 {ECO:0000255|HAMAP-Rule:MF_00251}; GN OrderedLocusNames=NMB0941; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L36P family. CC {ECO:0000255|HAMAP-Rule:MF_00251}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41347.1; -; Genomic_DNA. DR PIR; B81140; B81140. DR RefSeq; NP_273979.1; NC_003112.2. DR RefSeq; WP_002213788.1; NC_003112.2. DR ProteinModelPortal; P66295; -. DR STRING; 122586.NMB0941; -. DR PaxDb; P66295; -. DR EnsemblBacteria; AAF41347; AAF41347; NMB0941. DR GeneID; 903061; -. DR KEGG; nme:NMB0941; -. DR PATRIC; 20357363; VBINeiMen85645_1196. DR eggNOG; ENOG4105YK5; Bacteria. DR eggNOG; COG0257; LUCA. DR HOGENOM; HOG000111585; -. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR BioCyc; NMEN122586:GHGG-978-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00251; Ribosomal_L36; 1. DR InterPro; IPR000473; Ribosomal_L36. DR PANTHER; PTHR18804; PTHR18804; 1. DR Pfam; PF00444; Ribosomal_L36; 1. DR SUPFAM; SSF57840; SSF57840; 1. DR TIGRFAMs; TIGR01022; rpmJ_bact; 1. DR PROSITE; PS00828; RIBOSOMAL_L36; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 41 50S ribosomal protein L36 2. FT /FTId=PRO_0000126226. SQ SEQUENCE 41 AA; 4943 MW; BC02610F493EAA31 CRC64; MQVLSSLKTA KQRHRDCQIV RRRGKVYVIC KSNPRFKARQ R // ID RLMK_NEIMB Reviewed; 354 AA. AC Q9JYY8; DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Ribosomal RNA large subunit methyltransferase K; DE EC=2.1.1.264; DE AltName: Full=23S rRNA m7G2069 methyltransferase; DE AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK; GN Name=rlmK; OrderedLocusNames=NMB1367; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22210896; DOI=10.1093/nar/gkr1287; RA Kimura S., Ikeuchi Y., Kitahara K., Sakaguchi Y., Suzuki T., RA Suzuki T.; RT "Base methylations in the double-stranded RNA by a fused RT methyltransferase bearing unwinding activity."; RL Nucleic Acids Res. 40:4071-4085(2012). CC -!- FUNCTION: Specifically methylates the guanine in position 2069 CC (m7G2069) of 23S rRNA. {ECO:0000269|PubMed:22210896}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(2069) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(2069) in 23S CC rRNA. {ECO:0000269|PubMed:22210896}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41741.1; -; Genomic_DNA. DR PIR; D81090; D81090. DR RefSeq; NP_274385.1; NC_003112.2. DR RefSeq; WP_010980927.1; NC_003112.2. DR ProteinModelPortal; Q9JYY8; -. DR STRING; 122586.NMB1367; -. DR PaxDb; Q9JYY8; -. DR EnsemblBacteria; AAF41741; AAF41741; NMB1367. DR GeneID; 903789; -. DR KEGG; nme:NMB1367; -. DR PATRIC; 20358399; VBINeiMen85645_1711. DR eggNOG; ENOG4105DR4; Bacteria. DR eggNOG; COG1092; LUCA. DR HOGENOM; HOG000218999; -. DR KO; K06969; -. DR OMA; LMKWAKR; -. DR OrthoDB; EOG6HJ238; -. DR BioCyc; NMEN122586:GHGG-1405-MONOMER; -. DR BRENDA; 2.1.1.264; 3593. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10672; Methyltrans_SAM; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 354 Ribosomal RNA large subunit FT methyltransferase K. FT /FTId=PRO_0000419971. SQ SEQUENCE 354 AA; 41086 MW; C822861032B3C8C3 CRC64; MASYDKISDG WYRVCPKRSS NRALITVKLP FSTLFRLKPM TDITPFANRL GKNIKHLMKW AKRNGIEAWR IYDRDIPQFP FAADVYGDRI HLQEYDTGWL MRPEEYEAWL AEVLEAVAFV TGFAPEQIRL KRRERQKGLQ QYEKTGKAGD DFVITENGRK FWVNLDKYLD TGLFLDHRNT RKKVGETAAG KRFLNLFSYT GSFTVYAATG GAASSETVDL SNTYLDWAKR NFELNGIDTE RHKIVRADVF QYLQTAYGEG RRFDLIVMDP PSFSNSKKMS DILDIQRDHK KLIDGAVKLL ASDGILYFSN NLRSFVLDDL VSEQYAVKDI SKQSVPEDFR NKKIHRCWEI RHKS // ID RMLB_NEIMB Reviewed; 355 AA. AC P55294; Q9JS14; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 09-DEC-2015, entry version 102. DE RecName: Full=dTDP-glucose 4,6-dehydratase; DE EC=4.2.1.46; GN Name=rfbB1; OrderedLocusNames=NMB0063; GN and GN Name=rfbB2; OrderedLocusNames=NMB0079; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=8022265; DOI=10.1111/j.1365-2958.1994.tb00367.x; RA Hammerschmidt S., Birkholz C., Zaehringer U., Robertson B.D., RA van Putten J.P.M., Ebeling O., Frosch M.; RT "Contribution of genes from the capsule gene complex (cps) to RT lipooligosaccharide biosynthesis and serum resistance in Neisseria RT meningitidis."; RL Mol. Microbiol. 11:885-896(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form CC dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving CC oxidation, dehydration and reduction. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy- CC alpha-D-glucose + H(2)O. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L09188; AAA63157.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40531.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40543.1; -; Genomic_DNA. DR PIR; G81242; G81242. DR PIR; S42431; S42431. DR RefSeq; NP_273127.1; NC_003112.2. DR RefSeq; NP_273142.1; NC_003112.2. DR RefSeq; WP_002224748.1; NC_003112.2. DR ProteinModelPortal; P55294; -. DR SMR; P55294; 1-350. DR STRING; 122586.NMB0079; -. DR PaxDb; P55294; -. DR EnsemblBacteria; AAF40531; AAF40531; NMB0063. DR EnsemblBacteria; AAF40543; AAF40543; NMB0079. DR GeneID; 902170; -. DR GeneID; 902183; -. DR KEGG; nme:NMB0063; -. DR KEGG; nme:NMB0079; -. DR PATRIC; 20355131; VBINeiMen85645_0099. DR eggNOG; ENOG4105C1B; Bacteria. DR eggNOG; COG1088; LUCA. DR HOGENOM; HOG000168006; -. DR KO; K01710; -. DR OMA; DYEIICL; -. DR OrthoDB; EOG6PZXCX; -. DR BioCyc; NMEN122586:GHGG-69-MONOMER; -. DR BioCyc; NMEN122586:GHGG-85-MONOMER; -. DR UniPathway; UPA00124; -. DR UniPathway; UPA00281; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB. DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005888; dTDP_Gluc_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10366:SF41; PTHR10366:SF41; 1. DR Pfam; PF16363; GDP_Man_Dehyd; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1. PE 3: Inferred from homology; KW Complete proteome; Lipopolysaccharide biosynthesis; Lyase; NAD; KW Reference proteome. FT CHAIN 1 355 dTDP-glucose 4,6-dehydratase. FT /FTId=PRO_0000183242. FT NP_BIND 8 14 NAD. {ECO:0000255}. FT NP_BIND 33 36 NAD. {ECO:0000250}. FT NP_BIND 59 60 NAD. {ECO:0000250}. FT NP_BIND 160 164 NAD. {ECO:0000250}. FT REGION 134 136 Substrate binding. {ECO:0000250}. FT REGION 199 200 Substrate binding. {ECO:0000250}. FT REGION 215 217 Substrate binding. {ECO:0000250}. FT REGION 294 297 Substrate binding. {ECO:0000250}. FT ACT_SITE 135 135 Proton donor. {ECO:0000250}. FT ACT_SITE 136 136 Proton acceptor. {ECO:0000250}. FT ACT_SITE 160 160 Proton acceptor. {ECO:0000250}. FT BINDING 81 81 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 85 85 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 100 100 NAD. {ECO:0000250}. FT BINDING 189 189 Substrate. {ECO:0000250}. FT BINDING 190 190 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 224 224 Substrate. {ECO:0000250}. FT BINDING 259 259 Substrate. {ECO:0000250}. FT CONFLICT 1 3 MRK -> MQTANKKT (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 26 28 RDA -> QDS (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 32 32 V -> L (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 46 47 EV -> DI (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 73 73 Y -> H (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 142 142 G -> H (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 152 152 A -> T (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 268 268 A -> T (in Ref. 1; AAA63157). FT {ECO:0000305}. FT CONFLICT 274 274 A -> V (in Ref. 1; AAA63157). FT {ECO:0000305}. SQ SEQUENCE 355 AA; 39865 MW; 631AA0EDA02B6F41 CRC64; MRKILVTGGA GFIGSAVVRH IIRNTRDAVV NVDKLTYAGN LESLTEVADN PRYAFEQVDI CDRAELDRVF AQYRPDAVMH LAAESHVDRS IGSAGEFIQT NIVGTFNLLE AARAYWQQMP SEQHEAFRFH HISTDEVYGD LGGTDDLFTE TAPYAPSSPY SASKASSDHL VRAWLRTYGL PTIVTNCSNN YGPYHFPEKL IPLMILNALD GKPLPVYGDG MQIRDWLFVE DHARALYQVV TEGVVGETYN IGGHNEKANI EVVKTICALL EELAPEKPAG VARYEDLITF VQDRPGHDVR YAVDAAKIRR DLGWLPLETF ESGLRKTVQW YLDNKTWWQN VLNGSYRLER LGTGK // ID RL9_NEIMB Reviewed; 150 AA. AC Q9JZ31; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=NMB1320; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00503}. CC -!- SIMILARITY: Belongs to the ribosomal protein L9P family. CC {ECO:0000255|HAMAP-Rule:MF_00503}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41695.1; -; Genomic_DNA. DR PIR; G81096; G81096. DR RefSeq; NP_274339.1; NC_003112.2. DR RefSeq; WP_002213307.1; NC_003112.2. DR ProteinModelPortal; Q9JZ31; -. DR STRING; 122586.NMB1320; -. DR PaxDb; Q9JZ31; -. DR PRIDE; Q9JZ31; -. DR EnsemblBacteria; AAF41695; AAF41695; NMB1320. DR GeneID; 903742; -. DR KEGG; nme:NMB1320; -. DR PATRIC; 20358289; VBINeiMen85645_1656. DR eggNOG; ENOG4105K9Q; Bacteria. DR eggNOG; COG0359; LUCA. DR HOGENOM; HOG000040337; -. DR KO; K02939; -. DR OMA; AIRWTKG; -. DR OrthoDB; EOG6D8BH0; -. DR BioCyc; NMEN122586:GHGG-1358-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.430.100; -; 1. DR Gene3D; 3.40.5.10; -; 1. DR HAMAP; MF_00503; Ribosomal_L9; 1. DR InterPro; IPR000244; Ribosomal_L9. DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N. DR InterPro; IPR020594; Ribosomal_L9_bac/chp. DR InterPro; IPR020069; Ribosomal_L9_C. DR InterPro; IPR020070; Ribosomal_L9_N. DR PANTHER; PTHR21368; PTHR21368; 1. DR Pfam; PF03948; Ribosomal_L9_C; 1. DR Pfam; PF01281; Ribosomal_L9_N; 1. DR SUPFAM; SSF55653; SSF55653; 1. DR SUPFAM; SSF55658; SSF55658; 1. DR TIGRFAMs; TIGR00158; L9; 1. DR PROSITE; PS00651; RIBOSOMAL_L9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 150 50S ribosomal protein L9. FT /FTId=PRO_0000176659. SQ SEQUENCE 150 AA; 15747 MW; FFE4F2A760260429 CRC64; MQIILLEKIG GLGNLGDIVT VKNGYARNFL IPAGKAKRAT EANMKEFEAR RAELEAKQAE ILADARVRQE KLDGQTVTVA QKAGVDGRLF GSVTNADIAA AIVAAGIEAV KANVRLPNGP LKAVGEYEVE VALHTDAVAK ITVAVVAATE // ID RLME_NEIMB Reviewed; 206 AA. AC Q7DDL2; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547}; DE EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; GN Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547}; GN Synonyms=ftsJ {ECO:0000255|HAMAP-Rule:MF_01547}, GN rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=NMB0799; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the uridine in position 2552 of CC 23S rRNA at the 2'-O position of the ribose in the fully assembled CC 50S ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uridine(2552) in 23S CC rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase RlmE family. CC {ECO:0000255|HAMAP-Rule:MF_01547}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41212.1; -; Genomic_DNA. DR RefSeq; NP_273841.1; NC_003112.2. DR RefSeq; WP_002213963.1; NC_003112.2. DR ProteinModelPortal; Q7DDL2; -. DR STRING; 122586.NMB0799; -. DR PaxDb; Q7DDL2; -. DR EnsemblBacteria; AAF41212; AAF41212; NMB0799. DR GeneID; 902914; -. DR KEGG; nme:NMB0799; -. DR PATRIC; 20356985; VBINeiMen85645_1011. DR eggNOG; ENOG4105F7M; Bacteria. DR eggNOG; COG0293; LUCA. DR HOGENOM; HOG000162367; -. DR KO; K02427; -. DR OMA; ERQINDP; -. DR OrthoDB; EOG657JC0; -. DR BioCyc; NMEN122586:GHGG-830-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01547; RNA_methyltr_E; 1. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR10920; PTHR10920; 1. DR Pfam; PF01728; FtsJ; 1. DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 206 Ribosomal RNA large subunit FT methyltransferase E. FT /FTId=PRO_0000155513. FT ACT_SITE 162 162 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 61 61 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 63 63 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 81 81 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 97 97 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 122 122 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. SQ SEQUENCE 206 AA; 22721 MW; A6CF0CC91BAA8AAE CRC64; MAVRSKSSKA WLHEHVNDHY VHMAQKDGYR ARAAYKLLEI NEKDKLIKPG TVLADLGSAP GSWSQVAAKL TGTSGAVFAL DILPMEAIGG VSFIQGDFRE NDVLAQFETL LDNRPLDLVI CDMAPNMSGN AVSDQARSFY LCELALDFAS QHLKTGGSFL VKVFQGAGYQ EYMAAMREIF GTVQTRKPEA SRNRSSEIYL LGKNKR // ID RLMH_NEIMB Reviewed; 156 AA. AC P67519; Q9JR59; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_00658}; DE EC=2.1.1.177 {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN Name=rlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN OrderedLocusNames=NMB2022; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the pseudouridine at position CC 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + pseudouridine(1915) CC in 23S rRNA = S-adenosyl-L-homocysteine + N(3)- CC methylpseudouridine(1915) in 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00658}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family. CC {ECO:0000255|HAMAP-Rule:MF_00658}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42345.1; -; Genomic_DNA. DR PIR; A81015; A81015. DR RefSeq; NP_275014.1; NC_003112.2. DR RefSeq; WP_002225675.1; NC_003112.2. DR ProteinModelPortal; P67519; -. DR STRING; 122586.NMB2022; -. DR PaxDb; P67519; -. DR EnsemblBacteria; AAF42345; AAF42345; NMB2022. DR GeneID; 904088; -. DR KEGG; nme:NMB2022; -. DR PATRIC; 20360159; VBINeiMen85645_2579. DR eggNOG; ENOG4108UXA; Bacteria. DR eggNOG; COG1576; LUCA. DR HOGENOM; HOG000218434; -. DR KO; K00783; -. DR OMA; NGEPYHK; -. DR OrthoDB; EOG6S26HR; -. DR BioCyc; NMEN122586:GHGG-2084-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00658; 23SrRNA_methyltr_H; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR003742; SPOUT_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF02590; SPOUT_MTase; 1. DR PIRSF; PIRSF004505; MT_bac; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 156 Ribosomal RNA large subunit FT methyltransferase H. FT /FTId=PRO_0000198151. SQ SEQUENCE 156 AA; 17510 MW; 63DE283F1D5A6266 CRC64; MNITVLAVGT KMPRWVDEAV AEYAKRFGRD VAYALKEIKP EKRGAGVNAA QGMAAEEKRI LEAIPQGAFL VVLDERGKAP TSVELAEHLK SWRQNGEHVC FVIGGADGMT DRLKQQARMM MRLSSLTLPH GMVRVFLTEQ LYRAVSILHN HPYHRE // ID RNH2_NEIMB Reviewed; 194 AA. AC Q9K1G1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Ribonuclease HII; DE Short=RNase HII; DE EC=3.1.26.4; GN Name=rnhB; OrderedLocusNames=NMB0192; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per CC monomer in the absence of substrate. May bind a second metal ion CC after substrate binding. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40649.1; -; Genomic_DNA. DR PIR; E81227; E81227. DR RefSeq; NP_273250.1; NC_003112.2. DR RefSeq; WP_002221870.1; NC_003112.2. DR ProteinModelPortal; Q9K1G1; -. DR STRING; 122586.NMB0192; -. DR PaxDb; Q9K1G1; -. DR EnsemblBacteria; AAF40649; AAF40649; NMB0192. DR GeneID; 902300; -. DR KEGG; nme:NMB0192; -. DR PATRIC; 20355417; VBINeiMen85645_0237. DR eggNOG; ENOG4108UH2; Bacteria. DR eggNOG; COG0164; LUCA. DR HOGENOM; HOG000100288; -. DR KO; K03470; -. DR OMA; LSWAYLD; -. DR OrthoDB; EOG6BKJC8; -. DR BioCyc; NMEN122586:GHGG-203-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00052_B; RNase_HII_B; 1. DR InterPro; IPR022898; RNase_HII. DR InterPro; IPR001352; RNase_HII/HIII. DR InterPro; IPR024567; RNase_HII/HIII_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR PANTHER; PTHR10954; PTHR10954; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Manganese; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 194 Ribonuclease HII. FT /FTId=PRO_0000111595. FT METAL 9 9 Divalent metal cation. {ECO:0000250}. FT METAL 10 10 Divalent metal cation. {ECO:0000250}. FT METAL 101 101 Divalent metal cation. {ECO:0000250}. SQ SEQUENCE 194 AA; 21206 MW; 3BBC84BA1FD01B1E CRC64; MHILTAGVDE AGRGPLVGSV FAAAVILPET FDLPGLTDSK KLSEKKRDAL AEMIKNQAVE WHVAAASPEE IASLNILHAT MLAMKRAVDG LAVRPEKIFI DGNRIPEHLN IPAEAVVKGD SKIIEISAAS VLAKTARDAE MYALAQRHPQ YGFDKHKGYG TKQHLEALEK YGVLPEHRRD FAPVRNLLAQ QALF // ID RL35_NEIMB Reviewed; 65 AA. AC P66274; Q9JQN7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=50S ribosomal protein L35 {ECO:0000255|HAMAP-Rule:MF_00514}; GN Name=rpmI {ECO:0000255|HAMAP-Rule:MF_00514}; GN OrderedLocusNames=NMB0722; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein L35P family. CC {ECO:0000255|HAMAP-Rule:MF_00514}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41135.1; -; Genomic_DNA. DR PIR; E81165; E81165. DR RefSeq; NP_273764.1; NC_003112.2. DR RefSeq; WP_002232040.1; NC_003112.2. DR ProteinModelPortal; P66274; -. DR SMR; P66274; 2-65. DR STRING; 122586.NMB0722; -. DR PaxDb; P66274; -. DR EnsemblBacteria; AAF41135; AAF41135; NMB0722. DR GeneID; 23782750; -. DR GeneID; 902835; -. DR KEGG; nme:NMB0722; -. DR PATRIC; 20356799; VBINeiMen85645_0920. DR eggNOG; ENOG4105VJV; Bacteria. DR eggNOG; COG0291; LUCA. DR HOGENOM; HOG000040108; -. DR KO; K02916; -. DR OMA; AYKRHIL; -. DR OrthoDB; EOG651T3B; -. DR BioCyc; NMEN122586:GHGG-751-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00514; Ribosomal_L35; 1. DR InterPro; IPR021137; Ribosomal_L35. DR InterPro; IPR018265; Ribosomal_L35_CS. DR InterPro; IPR001706; Ribosomal_L35_non-mt. DR Pfam; PF01632; Ribosomal_L35p; 1. DR PRINTS; PR00064; RIBOSOMALL35. DR TIGRFAMs; TIGR00001; rpmI_bact; 1. DR PROSITE; PS00936; RIBOSOMAL_L35; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 65 50S ribosomal protein L35. FT /FTId=PRO_0000177390. SQ SEQUENCE 65 AA; 7357 MW; EF7E775093C90473 CRC64; MPKMKTKSSA KKRFKVLGNG GVKRAHAFKR HILTKKTTKN KRQLRGTSMV NDRDLASVAK MLPYA // ID RL6_NEIMB Reviewed; 177 AA. AC Q9K1I3; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; GN OrderedLocusNames=NMB0157; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in CC its secondary structure. It is located near the subunit interface CC in the base of the L7/L12 stalk, and near the tRNA binding site of CC the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01365}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein L6P family. CC {ECO:0000255|HAMAP-Rule:MF_01365}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40615.1; -; Genomic_DNA. DR PIR; G81232; G81232. DR RefSeq; NP_273215.1; NC_003112.2. DR RefSeq; WP_002224773.1; NC_003112.2. DR ProteinModelPortal; Q9K1I3; -. DR SMR; Q9K1I3; 2-177. DR STRING; 122586.NMB0157; -. DR PaxDb; Q9K1I3; -. DR EnsemblBacteria; AAF40615; AAF40615; NMB0157. DR GeneID; 902264; -. DR KEGG; nme:NMB0157; -. DR PATRIC; 20355337; VBINeiMen85645_0198. DR eggNOG; ENOG4108R5J; Bacteria. DR eggNOG; COG0097; LUCA. DR HOGENOM; HOG000039903; -. DR KO; K02933; -. DR OMA; TIGYSHP; -. DR OrthoDB; EOG67DPRD; -. DR BioCyc; NMEN122586:GHGG-167-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.930.12; -; 2. DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR020040; Ribosomal_L6_a/b-dom. DR InterPro; IPR019906; Ribosomal_L6_bac-type. DR InterPro; IPR002358; Ribosomal_L6_CS. DR PANTHER; PTHR11655; PTHR11655; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR PRINTS; PR00059; RIBOSOMALL6. DR SUPFAM; SSF56053; SSF56053; 2. DR TIGRFAMs; TIGR03654; L6_bact; 1. DR PROSITE; PS00525; RIBOSOMAL_L6_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 177 50S ribosomal protein L6. FT /FTId=PRO_0000260901. SQ SEQUENCE 177 AA; 18904 MW; 9D4AE698E30A0E10 CRC64; MSRVAKNPVT VPAGVEVKFG AEALVIKGKN GELSFPLHSD VAIEFNDGKL TFVANNSSKQ ANAMSGTARA LVSNMVKGVS EGFEKRLQLI GVGYRAQAQG KILNLSLGFS HPIVYEMPEG VSVQTPSQTE IVLTGSDKQV VGQVAAEIRA FRAPEPYKGK GVRYVGEVVV MKEAKKK // ID RL7_NEIMB Reviewed; 123 AA. AC P0A0X1; P80716; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 70. DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368}; GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; GN OrderedLocusNames=NMB0131; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. Is thus CC essential for accurate translation. {ECO:0000255|HAMAP- CC Rule:MF_00368}. CC -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S CC ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 CC forms an elongated spine to which 2 to 4 L12 dimers bind in a CC sequential fashion. Binds GTP-bound translation factors. CC {ECO:0000255|HAMAP-Rule:MF_00368}. CC -!- SIMILARITY: Belongs to the ribosomal protein L7/L12P family. CC {ECO:0000255|HAMAP-Rule:MF_00368}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40590.1; -; Genomic_DNA. DR PIR; H81235; H81235. DR RefSeq; NP_273189.1; NC_003112.2. DR RefSeq; WP_002215374.1; NC_003112.2. DR ProteinModelPortal; P0A0X1; -. DR SMR; P0A0X1; 3-123. DR STRING; 122586.NMB0131; -. DR PaxDb; P0A0X1; -. DR EnsemblBacteria; AAF40590; AAF40590; NMB0131. DR GeneID; 902239; -. DR KEGG; nme:NMB0131; -. DR PATRIC; 20355281; VBINeiMen85645_0170. DR eggNOG; ENOG4105KBC; Bacteria. DR eggNOG; COG0222; LUCA. DR HOGENOM; HOG000248813; -. DR KO; K02935; -. DR OMA; GLKETWG; -. DR OrthoDB; EOG6WMJ69; -. DR BioCyc; NMEN122586:GHGG-141-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1390.10; -; 1. DR HAMAP; MF_00368; Ribosomal_L7_L12; 1. DR InterPro; IPR000206; Ribosomal_L7/12. DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like. DR InterPro; IPR013823; Ribosomal_L7/L12_C. DR InterPro; IPR008932; Ribosomal_L7/L12_oligo. DR Pfam; PF00542; Ribosomal_L12; 1. DR Pfam; PF16320; Ribosomal_L12_N; 1. DR ProDom; PD001326; Ribosomal_L7/L12_C; 1. DR SUPFAM; SSF48300; SSF48300; 1. DR SUPFAM; SSF54736; SSF54736; 1. DR TIGRFAMs; TIGR00855; L12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 123 50S ribosomal protein L7/L12. FT /FTId=PRO_0000157557. SQ SEQUENCE 123 AA; 12622 MW; 5A6607CA5CB6F535 CRC64; MAITKEDILE AVGSLTVMEL NDLVKAFEEK FGVSAAAVAV AGPAGAGAAD AEEKTEFDVV LASAGDQKVG VIKVVRAITG LGLKEAKDIV DGAPKTIKEG VSKAEAEDIQ KQLEEAGAKV EIK // ID RL4_NEIMB Reviewed; 206 AA. AC P61057; Q9JRA2; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=NMB0143; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein CC initially binds near the 5'-end of the 23S rRNA. It is important CC during the early stages of 50S assembly. It makes multiple CC contacts with different domains of the 23S rRNA in the assembled CC 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01328}. CC -!- SIMILARITY: Belongs to the ribosomal protein L4P family. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40601.1; -; Genomic_DNA. DR PIR; A81231; A81231. DR RefSeq; NP_273201.1; NC_003112.2. DR RefSeq; WP_002215402.1; NC_003112.2. DR ProteinModelPortal; P61057; -. DR SMR; P61057; 1-205. DR STRING; 122586.NMB0143; -. DR PaxDb; P61057; -. DR PRIDE; P61057; -. DR EnsemblBacteria; AAF40601; AAF40601; NMB0143. DR GeneID; 902250; -. DR KEGG; nme:NMB0143; -. DR PATRIC; 20355309; VBINeiMen85645_0184. DR eggNOG; ENOG4106U5A; Bacteria. DR eggNOG; COG0088; LUCA. DR HOGENOM; HOG000248766; -. DR KO; K02926; -. DR OMA; VVRSHEH; -. DR OrthoDB; EOG6M0T9G; -. DR BioCyc; NMEN122586:GHGG-153-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1370.10; -; 1. DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1. DR InterPro; IPR002136; Ribosomal_L4/L1e. DR InterPro; IPR023574; Ribosomal_L4_dom. DR InterPro; IPR013005; Ribosomal_uL4/L1e. DR PANTHER; PTHR10746; PTHR10746; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03953; rplD_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 206 50S ribosomal protein L4. FT /FTId=PRO_0000129249. SQ SEQUENCE 206 AA; 23263 MW; 45FDA7EBE045F2CC CRC64; MELKVIDAKG QVSGSLSVSD ALFAREYNEA LVHQLVNAYL ANARSGNRAQ KTRAEVKHST KKPWRQKGTG RARSGMTSSP LWRKGGRAFP NKPDENFTQK VNRKMYRAGM ATILSQLTRD ERLFAIEALT AETPKTKVFA EQVKNLGLEQ VLFVTKQLDE NVYLASRNLP NVLVLEAQQV DPYSLLRYKK VIITKDAVAQ LEEQWV // ID RL5_NEIMB Reviewed; 179 AA. AC Q9K1I4; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=NMB0154; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: This is 1 of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. In the CC 70S ribosome it contacts protein S13 of the 30S subunit (bridge CC B1b), connecting the 2 subunits; this bridge is implicated in CC subunit movement. Contacts the P site tRNA; the 5S rRNA and some CC of its associated proteins might help stabilize positioning of CC ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site CC tRNA. Forms a bridge to the 30S subunit in the 70S ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SIMILARITY: Belongs to the ribosomal protein L5P family. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40612.1; -; Genomic_DNA. DR PIR; D81232; D81232. DR RefSeq; NP_273212.1; NC_003112.2. DR RefSeq; WP_002215436.1; NC_003112.2. DR ProteinModelPortal; Q9K1I4; -. DR SMR; Q9K1I4; 2-178. DR STRING; 122586.NMB0154; -. DR PaxDb; Q9K1I4; -. DR EnsemblBacteria; AAF40612; AAF40612; NMB0154. DR GeneID; 902261; -. DR KEGG; nme:NMB0154; -. DR PATRIC; 20355331; VBINeiMen85645_0195. DR eggNOG; ENOG4105CW6; Bacteria. DR eggNOG; COG0094; LUCA. DR HOGENOM; HOG000231311; -. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR BioCyc; NMEN122586:GHGG-164-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR020930; Ribosomal_L5_bac-type. DR InterPro; IPR031309; Ribosomal_L5_C. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR031310; Ribosomal_L5_N. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; SSF55282; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 179 50S ribosomal protein L5. FT /FTId=PRO_0000124958. SQ SEQUENCE 179 AA; 20323 MW; 95FF7F5E4F4F2C2F CRC64; MARLREFYKE TVVPELVKQF GYKSVMEVPR IEKITLNMGV GEAVADKKVM EHAVSDLEKI AGQKPVVTVA RKSIAGFKIR DNYPVGCKVT LRRDQMFEFL DRLITIALPR VRDFRGVSGK SFDGRGNYNM GVREQIIFPE IEYDKIDALR GLNITITTTA KTDEEAKALL SLFKFPFKG // ID RNH_NEIMB Reviewed; 145 AA. AC Q9JYE5; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Ribonuclease HI {ECO:0000255|HAMAP-Rule:MF_00042}; DE Short=RNase HI {ECO:0000255|HAMAP-Rule:MF_00042}; DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00042}; GN Name=rnhA {ECO:0000255|HAMAP-Rule:MF_00042}; GN OrderedLocusNames=NMB1618; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000255|HAMAP-Rule:MF_00042}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00042}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00042}; CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion CC at a regulatory site, or after substrate binding. CC {ECO:0000255|HAMAP-Rule:MF_00042}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00042}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00042}. CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000255|HAMAP- CC Rule:MF_00042}. CC -!- SIMILARITY: Contains 1 RNase H domain. {ECO:0000255|HAMAP- CC Rule:MF_00042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41970.1; -; Genomic_DNA. DR PIR; H81061; H81061. DR RefSeq; NP_274624.1; NC_003112.2. DR RefSeq; WP_002225009.1; NC_003112.2. DR ProteinModelPortal; Q9JYE5; -. DR STRING; 122586.NMB1618; -. DR PaxDb; Q9JYE5; -. DR EnsemblBacteria; AAF41970; AAF41970; NMB1618. DR GeneID; 904120; -. DR KEGG; nme:NMB1618; -. DR PATRIC; 20359136; VBINeiMen85645_2079. DR eggNOG; ENOG4108UMW; Bacteria. DR eggNOG; COG0328; LUCA. DR HOGENOM; HOG000040465; -. DR KO; K03469; -. DR OMA; NGWKTSE; -. DR OrthoDB; EOG696BTR; -. DR BioCyc; NMEN122586:GHGG-1667-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00042; RNase_H; 1. DR InterPro; IPR022892; RNaseH. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR002156; RNaseH_domain. DR Pfam; PF00075; RNase_H; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50879; RNASE_H; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 145 Ribonuclease HI. FT /FTId=PRO_0000195385. FT DOMAIN 1 142 RNase H. {ECO:0000255|HAMAP- FT Rule:MF_00042}. FT METAL 10 10 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00042}. FT METAL 10 10 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00042}. FT METAL 48 48 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00042}. FT METAL 70 70 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00042}. FT METAL 134 134 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00042}. SQ SEQUENCE 145 AA; 16251 MW; 3E2EA6BED17D5E91 CRC64; MNQTVYLYTD GACKGNPGAG GWGVLMRYGS HEKELFGGEA QTTNNRMELT AVIEGLKSLK RRCTVIICTD SQYVKNGMEN WIHGWKRNGW KTASKQPVKN DDLWKELDAL VGRHQVSWTW VKGHAGHAEN ERADDLANRG AAQFS // ID RLMB_NEIMB Reviewed; 250 AA. AC Q9JZR3; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000255|HAMAP-Rule:MF_01887}; DE EC=2.1.1.185 {ECO:0000255|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887}; GN Name=rlmB {ECO:0000255|HAMAP-Rule:MF_01887}; GN OrderedLocusNames=NMB0931; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in CC 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(2251) in CC 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(2251) CC in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC RlmB subfamily. {ECO:0000255|HAMAP-Rule:MF_01887}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41338.1; -; Genomic_DNA. DR PIR; F81141; F81141. DR RefSeq; NP_273970.1; NC_003112.2. DR RefSeq; WP_002231513.1; NC_003112.2. DR ProteinModelPortal; Q9JZR3; -. DR SMR; Q9JZR3; 6-243. DR STRING; 122586.NMB0931; -. DR PaxDb; Q9JZR3; -. DR EnsemblBacteria; AAF41338; AAF41338; NMB0931. DR GeneID; 903052; -. DR KEGG; nme:NMB0931; -. DR PATRIC; 20357331; VBINeiMen85645_1180. DR eggNOG; ENOG4105C2N; Bacteria. DR eggNOG; COG0566; LUCA. DR HOGENOM; HOG000218798; -. DR KO; K03218; -. DR OMA; WVEGVHQ; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; NMEN122586:GHGG-969-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_01887; 23SrRNA_methyltr_B; 1. DR InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR004441; rRNA_MeTrfase_TrmH. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR013123; SpoU_subst-bd. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR Pfam; PF08032; SpoU_sub_bind; 1. DR SMART; SM00967; SpoU_sub_bind; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 250 23S rRNA (guanosine-2'-O-)- FT methyltransferase RlmB. FT /FTId=PRO_0000159792. FT BINDING 197 197 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01887}. FT BINDING 217 217 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01887}. FT BINDING 226 226 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01887}. SQ SEQUENCE 250 AA; 27467 MW; B4E908AACC3B71CB CRC64; MANQRPIYGF HAVNARLWQN PKSIVELYIQ EGKSDARTRE VLEKAANENI RVYFADADRL NAISKGARHQ GVVGFIDASK NHVHLEDVLE NLSEPPLLLI LDGITDPHNL GACLRTADAM GVHAVIAPKD KSAGLNATVS KVACGAAETV PYITVTNLAR TLRELKEYGI WIIGTDMSGE SDLYHCNLPD SAAWVMGNEG DGMRRLTREH CDMLVSIPMF GTVESMNVSV SAGMVLSETR RQRVLKNEKV // ID RLML_NEIMB Reviewed; 380 AA. AC Q9K0V4; DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Ribosomal RNA large subunit methyltransferase L; DE EC=2.1.1.173; DE AltName: Full=23S rRNA m2G2445 methyltransferase; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL; GN Name=rlmL; OrderedLocusNames=NMB0455; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22210896; DOI=10.1093/nar/gkr1287; RA Kimura S., Ikeuchi Y., Kitahara K., Sakaguchi Y., Suzuki T., RA Suzuki T.; RT "Base methylations in the double-stranded RNA by a fused RT methyltransferase bearing unwinding activity."; RL Nucleic Acids Res. 40:4071-4085(2012). CC -!- FUNCTION: Specifically methylates the guanine in position 2445 CC (m2G2445) of 23S rRNA. {ECO:0000269|PubMed:22210896}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(2445) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(2445) in 23S CC rRNA. {ECO:0000269|PubMed:22210896}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00529}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40892.1; -; Genomic_DNA. DR PIR; A81198; A81198. DR RefSeq; NP_273502.1; NC_003112.2. DR RefSeq; WP_002224938.1; NC_003112.2. DR ProteinModelPortal; Q9K0V4; -. DR STRING; 122586.NMB0455; -. DR PaxDb; Q9K0V4; -. DR DNASU; 902571; -. DR EnsemblBacteria; AAF40892; AAF40892; NMB0455. DR GeneID; 902571; -. DR KEGG; nme:NMB0455; -. DR PATRIC; 20356124; VBINeiMen85645_0578. DR eggNOG; ENOG4105C4H; Bacteria. DR eggNOG; COG0116; LUCA. DR HOGENOM; HOG000040915; -. DR KO; K07444; -. DR OMA; GFMYKAN; -. DR OrthoDB; EOG6HJ238; -. DR BioCyc; NMEN122586:GHGG-479-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR000241; RNA_methylase_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF02926; THUMP; 1. DR Pfam; PF01170; UPF0020; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS51165; THUMP; 1. DR PROSITE; PS01261; UPF0020; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 380 Ribosomal RNA large subunit FT methyltransferase L. FT /FTId=PRO_0000419972. FT DOMAIN 46 157 THUMP. {ECO:0000255|PROSITE- FT ProRule:PRU00529}. SQ SEQUENCE 380 AA; 42664 MW; 735727D9F504204D CRC64; MNTLYTLFAT CPRGLETVLS QELESLGCTD VQVFDGGVSC RGGLEQVYAA NLHSRTASRI LLRLTKGTYR NERDIYKLAK NINWFNWFTL QQTFKVKVEA KRANVKSIQF VGLTVKDAVC DAFRDIYDAR PSVDKAAPDV RIHAFLNERN VEIFIDTSGE ALFKRGYRLD TGEAPLRENL AAGLLLSAGY DGTQPFQDPF CGSGTIAIEA AWIAARRAPG MMRRFGFEKL QNFDKTLWSD LRRRAEAQTR PVRAPIAGSD NDRRIVQTAL DNARRAGVDD IVSFSVADAQ SVRPNGENGI MVSNPPYGVR LEEVRALQAL YPQLGTWLKK HYAGWLAAMF TGDREMPKFM CLSPKRKIPL YNGNIDCRLF LIDMVEGSNR // ID RMLA_NEIMB Reviewed; 288 AA. AC P55255; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=Glucose-1-phosphate thymidylyltransferase; DE EC=2.7.7.24; DE AltName: Full=dTDP-glucose pyrophosphorylase; DE AltName: Full=dTDP-glucose synthase; GN Name=rmlA1; Synonyms=rfbA1; OrderedLocusNames=NMB0062; GN and GN Name=rmlA2; Synonyms=rfbA2; OrderedLocusNames=NMB0080; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=8022265; DOI=10.1111/j.1365-2958.1994.tb00367.x; RA Hammerschmidt S., Birkholz C., Zaehringer U., Robertson B.D., RA van Putten J.P.M., Ebeling O., Frosch M.; RT "Contribution of genes from the capsule gene complex (cps) to RT lipooligosaccharide biosynthesis and serum resistance in Neisseria RT meningitidis."; RL Mol. Microbiol. 11:885-896(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and CC glucose 1-phosphate, as well as its pyrophosphorolysis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate = CC diphosphate + dTDP-alpha-D-glucose. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glucose-1-phosphate CC thymidylyltransferase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37050.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L09189; AAC37050.1; ALT_INIT; Genomic_DNA. DR EMBL; AE002098; AAF40530.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40544.1; -; Genomic_DNA. DR PIR; B81240; B81240. DR RefSeq; NP_273126.1; NC_003112.2. DR RefSeq; NP_273143.1; NC_003112.2. DR RefSeq; WP_002224747.1; NC_003112.2. DR ProteinModelPortal; P55255; -. DR SMR; P55255; 1-287. DR STRING; 122586.NMB0080; -. DR PaxDb; P55255; -. DR EnsemblBacteria; AAF40530; AAF40530; NMB0062. DR EnsemblBacteria; AAF40544; AAF40544; NMB0080. DR GeneID; 902169; -. DR GeneID; 902184; -. DR KEGG; nme:NMB0062; -. DR KEGG; nme:NMB0080; -. DR PATRIC; 20355129; VBINeiMen85645_0098. DR eggNOG; ENOG4108I19; Bacteria. DR eggNOG; COG1209; LUCA. DR HOGENOM; HOG000283473; -. DR KO; K00973; -. DR OMA; PHDAEQF; -. DR OrthoDB; EOG6RC3RN; -. DR BioCyc; NMEN122586:GHGG-68-MONOMER; -. DR BioCyc; NMEN122586:GHGG-86-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005907; G1P_thy_trans_s. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR22572:SF105; PTHR22572:SF105; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01207; rmlA; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 288 Glucose-1-phosphate FT thymidylyltransferase. FT /FTId=PRO_0000207998. FT METAL 108 108 Magnesium. {ECO:0000250}. FT METAL 223 223 Magnesium. {ECO:0000250}. FT CONFLICT 125 125 A -> R (in Ref. 1; AAC37050). FT {ECO:0000305}. FT CONFLICT 198 198 T -> S (in Ref. 1; AAC37050). FT {ECO:0000305}. SQ SEQUENCE 288 AA; 32162 MW; 8A65B50B531F2907 CRC64; MKGIILAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLSV LMLAGIRDIL VITAPEDNAS FKRLLGDGSD FGISISYAVQ PSPDGLAQAF IIGEEFIGND NVCLVLGDNI FYGQSFTQTL KQAAAQTHGA TVFAYQVKNP ERFGVVEFNE NFRAVSIEEK PQRPKSDWAV TGLYFYDNRA VEFAKQLKPS ARGELEITDL NRMYLEDGSL SVQILGRGFA WLDTGTHESL HEAASFVQTV QNIQNLHIAC LEEIAWRNGW LSDEKLEELA RPMAKNQYGQ YLLRLLKK // ID RMUC_NEIMB Reviewed; 594 AA. AC Q9JXH2; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=DNA recombination protein RmuC homolog; GN Name=rmuC; OrderedLocusNames=NMB2050; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in DNA recombination. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RmuC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42370.1; -; Genomic_DNA. DR PIR; C81011; C81011. DR RefSeq; NP_275040.1; NC_003112.2. DR RefSeq; WP_002225695.1; NC_003112.2. DR ProteinModelPortal; Q9JXH2; -. DR STRING; 122586.NMB2050; -. DR PaxDb; Q9JXH2; -. DR EnsemblBacteria; AAF42370; AAF42370; NMB2050. DR GeneID; 904037; -. DR KEGG; nme:NMB2050; -. DR PATRIC; 20360254; VBINeiMen85645_2627. DR eggNOG; ENOG4105CGY; Bacteria. DR eggNOG; COG1322; LUCA. DR HOGENOM; HOG000270056; -. DR KO; K09760; -. DR OMA; HGKLMAA; -. DR OrthoDB; EOG6T4S02; -. DR BioCyc; NMEN122586:GHGG-2113-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR InterPro; IPR003798; DNA_recombination_RmuC. DR Pfam; PF02646; RmuC; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA recombination; Reference proteome. FT CHAIN 1 594 DNA recombination protein RmuC homolog. FT /FTId=PRO_0000202046. FT COILED 66 330 {ECO:0000255}. SQ SEQUENCE 594 AA; 66655 MW; 3A307F5571600D14 CRC64; MELMTVLLPL AALVSGVLFT WLLMKGRFQG EFAGLNAHLA EKAARCDFVE QAHGKTVSEL AVLDGKYRHL QDENYALGNR FSAAEKQIAH LQEKEAESAR LKQSYIELQE KAQGLAVENE RLATQLGQER KAFADQYALE RQIRQRIETD LEESRQTVRD VQNDLSDVGN RFAAAEKQIA HLQEKEAEAE RLRQSHTELQ EKAQGLAVEN ERLATQIEQE RLASEEKLSL LGEARKSLSD QFQNLANTIL EEKSRRFTEQ NREQLHQVLN PLNERIHGFG ELVKQTYDKE SRERLTLENE LKRLQGLNAQ LHSEAKALTN ALTGTQNKVQ GNWGEMILET VLENSGLQKG REYVVQAASV RKEEDGGTRR LQPDVLVNLP DNKQIVIDSK VSLTAYVRYT QAADADTAAR ELAAHVASIR AHMKGLSLKD YTDLEGVNTL DFVFMFIPVE PAYLLALQND AGLFQECFDK RIMLVGPSTL LATLRTVANI WRNEQQNQNA LAIADEGGKL YDKFVGFVQT LESVGKGIDQ AQSSFQTAFK QLAEGRGNLV GRAEKLRLLG VKAGKQLQRD LVERSNETTA LSESLEYAAE DEAV // ID RPOB_NEIMB Reviewed; 1392 AA. AC Q59622; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 17-FEB-2016, entry version 105. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; GN OrderedLocusNames=NMB0132; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT RIFAMPICIN RESISTANT. RC STRAIN=BNCV / Serogroup B; RX PubMed=9222044; DOI=10.1093/jac/39.6.747; RA Nolte O.J.; RT "Rifampicin resistance in Neisseria meningitidis: evidence from a RT study of sibling strains, description of new mutations and notes on RT population genetics."; RL J. Antimicrob. Chemother. 39:747-755(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF40591.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z54353; CAA91164.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40591.1; ALT_INIT; Genomic_DNA. DR PIR; A81236; A81236. DR PIR; T30824; T30824. DR RefSeq; NP_273190.1; NC_003112.2. DR RefSeq; WP_010980755.1; NC_003112.2. DR ProteinModelPortal; Q59622; -. DR STRING; 122586.NMB0132; -. DR PaxDb; Q59622; -. DR PRIDE; Q59622; -. DR EnsemblBacteria; AAF40591; AAF40591; NMB0132. DR GeneID; 902240; -. DR KEGG; nme:NMB0132; -. DR PATRIC; 20355283; VBINeiMen85645_0171. DR eggNOG; ENOG4107QIH; Bacteria. DR eggNOG; COG0085; LUCA. DR HOGENOM; HOG000218612; -. DR KO; K03043; -. DR OMA; YFNPKRY; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; NMEN122586:GHGG-142-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.150.10; -; 1. DR Gene3D; 2.40.270.10; -; 2. DR Gene3D; 2.40.50.150; -; 2. DR Gene3D; 3.90.1110.10; -; 2. DR HAMAP; MF_01321; RNApol_bact_RpoB; 1. DR InterPro; IPR010243; DNA-dir_RNA_pol_bsu. DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR PANTHER; PTHR20856; PTHR20856; 6. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 2. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF10385; RNA_pol_Rpb2_45; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR TIGRFAMs; TIGR02013; rpoB; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 1392 DNA-directed RNA polymerase subunit beta. FT /FTId=PRO_0000047930. FT VARIANT 549 549 S -> P (rifampicin resistant). FT CONFLICT 2 2 N -> S (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 28 28 L -> I (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 224 252 ILDIFYDKETFYLSSNGVQTDLVADRLKG -> NLGYFLRQ FT RNVLFVFKRCSNRFGRRPSES (in Ref. 1; FT CAA91164). {ECO:0000305}. FT CONFLICT 284 284 N -> L (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 350 360 AYISNTLRTDE -> VISPIPCVRMK (in Ref. 1; FT CAA91164). {ECO:0000305}. FT CONFLICT 378 378 Missing (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 648 648 A -> G (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 706 706 A -> P (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 717 718 VP -> SA (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 748 749 GG -> A (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 818 818 F -> L (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 836 837 GY -> VN (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 1190 1192 YNG -> SR (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 1201 1201 A -> S (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 1244 1246 DDP -> EDA (in Ref. 1; CAA91164). FT {ECO:0000305}. FT CONFLICT 1373 1373 F -> L (in Ref. 1; CAA91164). FT {ECO:0000305}. SQ SEQUENCE 1392 AA; 155710 MW; 92AA331A597898F1 CRC64; MNYSFTEKKR IRKSFAKREN VLEVPFLLAT QIDSYAKFLQ LENAFDKRTD DGLQAAFNSI FPIVSHNGYA RLEFVHYTLG EPLFDIPECQ LRGITYAAPL RARIRLVILD KEASKPTVKE VRENEVYMGE IPLMTPSGSF VINGTERVIV SQLHRSPGVF FEHDKGKTHS SGKLLFSARI IPYRGSWLDF EFDPKDLLYF RIDRRRKMPV TILLKALGYN NEQILDIFYD KETFYLSSNG VQTDLVADRL KGETAKVDIL DKEGNVLVAK GKRITAKNIR DITNAGLTRL DVEPESLLGK ALAADLIDSE TGEVLASAND EITEELLAKF DINGVKEITT LYINELDQGA YISNTLRTDE TAGRQAARVA IYRMMRPGEP PTEEAVEQLF NRLFFSEDSY DLSRVGRMKF NTRTYEQKLS EAQQNSWYGR LLNETFAGAA DKGGYVLSVE DIVASIATLV ELRNGHGEVD DIDHLGNRRV RSVGELTENQ FRSGLARVER AVKERLNQAE SENLMPHDLI NAKPVSAAIK EFFGSSQLSQ FMDQTNPLSE VTHKRRVSAL GPGGLTRERA GFEVRDVHPT HYGRVCPIET PEGPNIGLIN SLSVYARTND YGFLETPYRR VIDGKVTEEI DYLSAIEEGR YVIAQANADL DSDGNLIGDL VTCREKGETI MATPDRVQYM DVATGQVVSV AASLIPFLEH DDANRALMGA NMQRQAVPCL RPEKPMVGTG IERSVAVDSA TAIVARRGGV VEYVDANRVV IRVHDDEATA GEVGVDIYNL VKFTRSNQST NINQRPAVKA GDVLQRGDLV ADGASTDFGE LALGQNMTIA FMPWNGYNYE DSILISEKVA ADDRYTSIHI EELNVVARDT KLGAEDITRD IPNLSERMQN RLDESGIVYI GAEVEAGDVL VGKVTPKGET QLTPEEKLLR AIFGEKASDV KDTSLRMPTG MSGTVIDVQV FTREGIQRDK RAQSIIDSEL KRYRLDLNDQ LRIFDNDAFD RIERMIVGQK ANGGPMKLAK GSEITTEYLA GLPSRHDWFD IRLTDEDLAK QLELIKVSLQ QKREEADELY EIKKKKLTQG DELQPGVQKM VKVFIAIKRR LQAGDKMAGR HGNKGVVSRI LPVEDMPYMA DGRPVDIVLN PLGVPSRMNI GQILEVHLGW AAKGIGERID RMLKEQRKAG ELREFLNRLY NGSGKKEDLD ALTDEEIIEL ASNLRKGASF ASPVFDGAKE SEIREMLNLA YPSDDPEVEK LGFNDSKTQI TLYDGRSGEA FDRKVTVGVM HYLKLHHLVD EKMHARSTGP YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYENIVK GEHKIDAGMP ESFNVLVKEI RSLGLDIDLE RY // ID RNC_NEIMB Reviewed; 239 AA. AC Q9K0C8; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104}; DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104}; DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104}; GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=NMB0686; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing CC of primary rRNA transcript to yield the immediate precursors to CC the large and small rRNAs (23S and 16S). Processes some mRNAs, and CC tRNAs when they are encoded in the rRNA operon. Processes pre- CC crRNA and tracrRNA of type II CRISPR loci if present in the CC organism. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain. CC {ECO:0000255|HAMAP-Rule:MF_00104}. CC -!- SIMILARITY: Contains 1 RNase III domain. {ECO:0000255|HAMAP- CC Rule:MF_00104}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41104.1; -; Genomic_DNA. DR PIR; E81169; E81169. DR RefSeq; NP_273728.1; NC_003112.2. DR RefSeq; WP_002225498.1; NC_003112.2. DR ProteinModelPortal; Q9K0C8; -. DR STRING; 122586.NMB0686; -. DR PaxDb; Q9K0C8; -. DR EnsemblBacteria; AAF41104; AAF41104; NMB0686. DR GeneID; 902798; -. DR KEGG; nme:NMB0686; -. DR PATRIC; 20356685; VBINeiMen85645_0860. DR eggNOG; ENOG4108ZBM; Bacteria. DR eggNOG; COG0571; LUCA. DR HOGENOM; HOG000246809; -. DR KO; K03685; -. DR OMA; LTHKSCK; -. DR OrthoDB; EOG6T1WVS; -. DR BioCyc; NMEN122586:GHGG-714-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 1.10.1520.10; -; 1. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; mRNA processing; Nuclease; Reference proteome; KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1 239 Ribonuclease 3. FT /FTId=PRO_0000180416. FT DOMAIN 11 133 RNase III. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT DOMAIN 160 230 DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 50 50 {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 122 122 {ECO:0000255|HAMAP-Rule:MF_00104}. FT METAL 46 46 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 119 119 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 122 122 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. SQ SEQUENCE 239 AA; 26853 MW; 54D0F0473049607C CRC64; MKDDVLKQQA HAAIQKKLGY AFRDISLLRQ ALTHRSHHAK HNERFEFVGD SILNYTVARM LFDAFPKLTE GELSRLRASL VNEGVLAEMA AEMNVGDGLY LGAGELKSGG FRRPSILADA MEAMFAAVSF DADFNTAEKV VRHLFADRVR RADFQNQAKD GKTALQEALQ ARRFALPKYR IEEQIGYAND SMFVISCDLG ELGFVCRAKG TSRKAAEQEA AKEALKWLEE KLPLKRKKK // ID RNPH_NEIMB Reviewed; 242 AA. AC Q9JYN5; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564}; DE Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564}; DE EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564}; DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564}; GN Name=rph {ECO:0000255|HAMAP-Rule:MF_00564}; OrderedLocusNames=NMB1499; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide CC residues following the -CCA terminus of tRNA and adds nucleotides CC to the ends of RNA molecules by using nucleoside diphosphates as CC substrates. {ECO:0000255|HAMAP-Rule:MF_00564}. CC -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_00564}. CC -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP- CC Rule:MF_00564}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41855.1; -; Genomic_DNA. DR PIR; G81076; G81076. DR RefSeq; NP_274507.1; NC_003112.2. DR RefSeq; WP_002225077.1; NC_003112.2. DR ProteinModelPortal; Q9JYN5; -. DR SMR; Q9JYN5; 9-240. DR STRING; 122586.NMB1499; -. DR PaxDb; Q9JYN5; -. DR EnsemblBacteria; AAF41855; AAF41855; NMB1499. DR GeneID; 903925; -. DR KEGG; nme:NMB1499; -. DR PATRIC; 20358780; VBINeiMen85645_1900. DR eggNOG; ENOG4105ED0; Bacteria. DR eggNOG; COG0689; LUCA. DR HOGENOM; HOG000229516; -. DR KO; K00989; -. DR OMA; KGKGQGW; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NMEN122586:GHGG-1539-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.70; -; 1. DR HAMAP; MF_00564; RNase_PH; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR002381; RNase_PH_bac-type. DR InterPro; IPR018336; RNase_PH_CS. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55666; SSF55666; 1. DR TIGRFAMs; TIGR01966; RNasePH; 1. DR PROSITE; PS01277; RIBONUCLEASE_PH; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Reference proteome; KW Transferase; tRNA processing. FT CHAIN 1 242 Ribonuclease PH. FT /FTId=PRO_0000139914. SQ SEQUENCE 242 AA; 25697 MW; 59B379F7554EDE0C CRC64; MPDYIRISRA ADSLRDIKIT PHFLPHTDGS CLIECGNTKV ICTASIDENV PPFLRGKNQG WVTAEYGMLP ASTASRMLRE ASAGKQSGRT QEIQRLIGRS LRAVVDMEKL GERQILIDCD VIQADGGTRT ASITGAFVAL QIAVGKLVSD GILSENPIRE AVAAVSVGVV NGVPLLDLDY PEDSGCDSDV NIVMTASGKI IEIQGTAEDA PFSLDELGKL VALAQKGIGE LLQHQQNALS AA // ID RNPA_NEIMB Reviewed; 121 AA. AC Q9JXS6; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227}; DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227}; GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; GN OrderedLocusNames=NMB1905; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence CC from pre-tRNA to produce the mature 5'-terminus. It can also CC cleave other RNA substrates such as 4.5S RNA. The protein CC component plays an auxiliary but essential role in vivo by binding CC to the 5'-leader sequence and broadening the substrate specificity CC of the ribozyme. {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00227}. CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP- CC Rule:MF_00227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42235.1; -; Genomic_DNA. DR PIR; H81027; H81027. DR RefSeq; NP_274899.1; NC_003112.2. DR RefSeq; WP_002223062.1; NC_003112.2. DR ProteinModelPortal; Q9JXS6; -. DR STRING; 122586.NMB1905; -. DR PaxDb; Q9JXS6; -. DR EnsemblBacteria; AAF42235; AAF42235; NMB1905. DR GeneID; 904262; -. DR KEGG; nme:NMB1905; -. DR PATRIC; 20359853; VBINeiMen85645_2431. DR eggNOG; ENOG4105NVJ; Bacteria. DR eggNOG; COG0594; LUCA. DR HOGENOM; HOG000266301; -. DR KO; K03536; -. DR OMA; SVFNFRK; -. DR OrthoDB; EOG6S52QN; -. DR BioCyc; NMEN122586:GHGG-1962-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00227; RNase_P; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000100; RNase_P. DR InterPro; IPR020539; RNase_P_CS. DR Pfam; PF00825; Ribonuclease_P; 1. DR ProDom; PD003629; Ribonuclease_P; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00188; rnpA; 1. DR PROSITE; PS00648; RIBONUCLEASE_P; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding; tRNA processing. FT CHAIN 1 121 Ribonuclease P protein component. FT /FTId=PRO_0000198498. SQ SEQUENCE 121 AA; 14211 MW; D4DE8C0EA865E325 CRC64; MDYRFGRQYR LLKTDDFSSV FAFRNRRSRD LLQVSRSNGN GLGHPRIGLV VGKKTAKRAN ERNYMKRVIR DWFRLNKNRL PPQDFVVRVH RKFDRATAKQ ARAELAQLMF GNPATGCRKQ A // ID RPIA_NEIMB Reviewed; 223 AA. AC Q9JYM6; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170}; DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170}; GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; GN OrderedLocusNames=NMB1511; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5- CC phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00170}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative CC stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41867.1; -; Genomic_DNA. DR PIR; C81076; C81076. DR RefSeq; NP_274519.1; NC_003112.2. DR RefSeq; WP_002225069.1; NC_003112.2. DR ProteinModelPortal; Q9JYM6; -. DR SMR; Q9JYM6; 3-218. DR STRING; 122586.NMB1511; -. DR PaxDb; Q9JYM6; -. DR EnsemblBacteria; AAF41867; AAF41867; NMB1511. DR GeneID; 903979; -. DR KEGG; nme:NMB1511; -. DR PATRIC; 20358810; VBINeiMen85645_1915. DR eggNOG; ENOG4105E66; Bacteria. DR eggNOG; COG0120; LUCA. DR HOGENOM; HOG000276368; -. DR KO; K01807; -. DR OMA; DHGLFNG; -. DR OrthoDB; EOG67MF61; -. DR BioCyc; NMEN122586:GHGG-1551-MONOMER; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00170; Rib_5P_isom_A; 1. DR InterPro; IPR004788; Ribose5P_isomerase_typA. DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr. DR PANTHER; PTHR11934; PTHR11934; 1. DR Pfam; PF06026; Rib_5-P_isom_A; 1. DR TIGRFAMs; TIGR00021; rpiA; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 223 Ribose-5-phosphate isomerase A. FT /FTId=PRO_0000158439. FT REGION 29 32 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT REGION 82 85 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT REGION 95 98 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT ACT_SITE 104 104 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00170}. SQ SEQUENCE 223 AA; 23904 MW; 7BE9482230763FF2 CRC64; MTTQDELKRI AAEKAVEFVP ENEYIGIGTG STINFFIEAL GKSGKKIKGA VSTSKKSGEL LAQYDIPVVS LNEVSGLAVY IDGADEVNHA LQMIKGGGGA HLNEKIVASA SEKFICIADE SKYVSRLGKF PLPVEVVESA RSLVSRKLLA MGGQPELRIG YTTFYGNQIV DVHGLNIDQP LTMEDEINKI TGVLENGIFA RDAADVLILG TEEGAKVIYP CQG // ID RPOC_NEIMB Reviewed; 1391 AA. AC Q9K1J1; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; GN OrderedLocusNames=NMB0133; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000255|HAMAP-Rule:MF_01322}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01322}. CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000255|HAMAP-Rule:MF_01322}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000255|HAMAP-Rule:MF_01322}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40592.1; -; Genomic_DNA. DR PIR; F81233; F81233. DR RefSeq; NP_273191.1; NC_003112.2. DR RefSeq; WP_002218564.1; NC_003112.2. DR ProteinModelPortal; Q9K1J1; -. DR STRING; 122586.NMB0133; -. DR PaxDb; Q9K1J1; -. DR PRIDE; Q9K1J1; -. DR EnsemblBacteria; AAF40592; AAF40592; NMB0133. DR GeneID; 902241; -. DR KEGG; nme:NMB0133; -. DR PATRIC; 20355287; VBINeiMen85645_0173. DR eggNOG; ENOG4107QR0; Bacteria. DR eggNOG; COG0086; LUCA. DR HOGENOM; HOG000218386; -. DR KO; K03046; -. DR OMA; YDLVNQN; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; NMEN122586:GHGG-143-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01322; RNApol_bact_RpoC; 1. DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR006592; RNA_pol_N. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SMART; SM00663; RPOLA_N; 1. DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 1391 DNA-directed RNA polymerase subunit FT beta'. FT /FTId=PRO_0000067768. SQ SEQUENCE 1391 AA; 153762 MW; 18FCEAE6CAC5D50E CRC64; MNLLNLFNPL QTAGMEEEFD AIKIGIASPE TIRSWSYGEV KKPETINYRT FKPERDGLFC AKIFGPVKDY ECLCGKYKRL KFKGVTCEKC GVEVTLSKVR RERMGHIELA APVAHIWFLK SLPSRLGMVL DMTLRDIERV LYFEAFVVTD PGMTPLQRRQ LLTEDDYYNK LDEYGDDFDA KMGAEGIREL LRTLNVAGEI EILRQELEST GSDTKIKKIA KRLKVLEAFH RSGMKLEWMI MDVLPVLPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLLELHAP DIIVRNEKRM LQEAVDSLLD NGRRGKAMTG ANKRPLKSLA DMIKGKGGRF RQNLLGKRVD YSGRSVITVG PYLRLHQCGL PKKMALELFK PFIFHKLEKQ GLASTVKAAK KLVEQEVPEV WDILEEVIRE HPIMLNRAPT LHRLGIQAFE PILIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLSLEAQM EARTLMLASN NVLSPANGEP IIVPSQDIVL GLYYMTRDRI NAKGEGSLFA DVKEVHRAYH TKQVELGTKI TVRLREWVKN EAGEFEPVVN RYETTVGRAL LSEILPKGLP FEYVNKALKK KEISKLINAS FRLCGLRDTV IFADHLMYTG FGFAAKGGIS IAVDDMEIPK EKAALLAEAN AEVKEIEDQY RQGLVTNGER YNKVVDIWGR AGDKIAKAMM DNLSKQKVID RAGNEVDQES FNSIYMMADS GARGSAAQIK QLSGMRGLMA KPDGSIIETP ITSNFREGLT VLQYFIATHG ARKGLADTAL KTANSGYLTR RLVDVTQDLV VVEDDCGTSD GFVMKAVVQG GDVIEALRDR ILGRVTASDV VDPSSGETLV EAGTLLTEKL VDMIDQSGVD EVKVRTPITC KTRHGLCAHC YGRDLARGKL VNAGEAVGVI AAQSIGEPGT QLTMRTFHIG GAASRAAAAS QVEAKSNGTA RFSSQMRYVA NNKGELVVIG RSCEVVIHDD IGRERERHKV PYGAILLVQD GMAIKAGQTL ATWDPHTRPM ITEHAGMVKF ENVEEGVTVA KQTDDVTGLS TLVVIDGKRR SSSASKLLRP TVKLLDENGV EICIPGTSTP VSMAFPVGAV ITVREGQEIG KGDVLARIPQ ASSKTRDITG GLPRVAELFE ARVPKDAGML AEITGTVSFG KETKGKQRLI VTDVDGVAYE TLISKEKQIL VHDGQVVNRG ETIVDGAVDP HDILRLQGIE ALARYIVQEV QEVYRLQGVK ISDKHIEVII RQMLRRVNIA DAGETGFITG EQVERGDVMA ANEKALEEGK EPARYENVLL GITKASLSTD SFISAASFQE TTRVLTEAAI MGKQDELRGL KENVIVGRLI PAGTGLTYHR SRHQQWQEVE QETAETQVTD E // ID RPOZ_NEIMB Reviewed; 68 AA. AC P66724; Q9JQS9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 69. DE RecName: Full=DNA-directed RNA polymerase subunit omega; DE Short=RNAP omega subunit; DE EC=2.7.7.6; DE AltName: Full=RNA polymerase omega subunit; DE AltName: Full=Transcriptase subunit omega; GN Name=rpoZ; OrderedLocusNames=NMB1660; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- CC terminal regions of the beta' subunit thereby facilitating its CC interaction with the beta and alpha subunits (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42009.1; -; Genomic_DNA. DR PIR; F81055; F81055. DR RefSeq; NP_274665.1; NC_003112.2. DR RefSeq; WP_002212665.1; NC_003112.2. DR STRING; 122586.NMB1660; -. DR PaxDb; P66724; -. DR EnsemblBacteria; AAF42009; AAF42009; NMB1660. DR GeneID; 903451; -. DR KEGG; nme:NMB1660; -. DR PATRIC; 20359258; VBINeiMen85645_2137. DR eggNOG; ENOG4105VFG; Bacteria. DR eggNOG; COG1758; LUCA. DR HOGENOM; HOG000245721; -. DR KO; K03060; -. DR OMA; CLKRIPN; -. DR OrthoDB; EOG6Q5NV5; -. DR BioCyc; NMEN122586:GHGG-1714-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.940.10; -; 1. DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1. DR InterPro; IPR003716; DNA-dir_RNA_pol_omega. DR InterPro; IPR006110; Pol_omega/K/RPB6. DR InterPro; IPR012293; RNAP_RPB6_omega. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR SMART; SM01409; RNA_pol_Rpb6; 1. DR SUPFAM; SSF63562; SSF63562; 1. DR TIGRFAMs; TIGR00690; rpoZ; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 68 DNA-directed RNA polymerase subunit FT omega. FT /FTId=PRO_0000128955. SQ SEQUENCE 68 AA; 7500 MW; D317176466D0D1D9 CRC64; MARITTEDCT GKISNHFDLT LVAARRARQL ENGNTPLVDD VRNNKPTVTA LREIAAGHIG TELLTRNK // ID RS11_NEIMB Reviewed; 131 AA. AC P66355; Q9JQR2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=NMB0166; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Located on the platform of the 30S subunit, it bridges CC several disparate RNA helices of the 16S rRNA. Forms part of the CC Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01310}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with CC proteins S7 and S18. Binds to IF-3. {ECO:0000255|HAMAP- CC Rule:MF_01310}. CC -!- SIMILARITY: Belongs to the ribosomal protein S11P family. CC {ECO:0000255|HAMAP-Rule:MF_01310}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40623.1; -; Genomic_DNA. DR PIR; F81229; F81229. DR RefSeq; NP_273224.1; NC_003112.2. DR RefSeq; WP_002216249.1; NC_003112.2. DR ProteinModelPortal; P66355; -. DR SMR; P66355; 15-131. DR STRING; 122586.NMB0166; -. DR PaxDb; P66355; -. DR EnsemblBacteria; AAF40623; AAF40623; NMB0166. DR GeneID; 25048807; -. DR GeneID; 902273; -. DR KEGG; nme:NMB0166; -. DR PATRIC; 20355355; VBINeiMen85645_0207. DR eggNOG; ENOG4108UHH; Bacteria. DR eggNOG; COG0100; LUCA. DR HOGENOM; HOG000111597; -. DR KO; K02948; -. DR OMA; NTPYASQ; -. DR OrthoDB; EOG6ZSPF3; -. DR BioCyc; NMEN122586:GHGG-176-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.80; -; 1. DR HAMAP; MF_01310; Ribosomal_S11; 1. DR InterPro; IPR001971; Ribosomal_S11. DR InterPro; IPR019981; Ribosomal_S11_bac-type. DR InterPro; IPR018102; Ribosomal_S11_CS. DR PANTHER; PTHR11759; PTHR11759; 1. DR Pfam; PF00411; Ribosomal_S11; 1. DR PIRSF; PIRSF002131; Ribosomal_S11; 1. DR TIGRFAMs; TIGR03632; uS11_bact; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 131 30S ribosomal protein S11. FT /FTId=PRO_0000123187. SQ SEQUENCE 131 AA; 13919 MW; DE7BDB80F3A9CFE9 CRC64; MAKANTASRV RKKVRKTVSE GIVHVHASFN NTIITITDRQ GNALSWATSG GAGFKGSRKS TPFAAQVAAE AAGKVAQEYG VKNLEVRIKG PGPGRESSVR ALNALGFKIT SITDVTPLPH NGCRPPKKRR I // ID RS12_NEIMB Reviewed; 123 AA. AC P66375; Q9JQR6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=NMB0136; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that CC are involved in tRNA selection in the A site and with the mRNA CC backbone. Located at the interface of the 30S and 50S subunits, it CC traverses the body of the 30S subunit contacting proteins on the CC other side and probably holding the rRNA structure together. The CC combined cluster of proteins S8, S12 and S17 appears to hold CC together the shoulder and platform of the 30S subunit. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 CC and S17. May interact with IF1 in the 30S initiation complex. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SIMILARITY: Belongs to the ribosomal protein S12P family. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- CAUTION: Because the enzyme that would modify Asp-89 to 3- CC methylthioaspartic acid has not been found in the proteome of this CC organism, that modification is not predicted. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40595.1; -; Genomic_DNA. DR PIR; A81234; A81234. DR RefSeq; NP_273194.1; NC_003112.2. DR RefSeq; WP_002218431.1; NC_003112.2. DR ProteinModelPortal; P66375; -. DR SMR; P66375; 3-123. DR STRING; 122586.NMB0136; -. DR PaxDb; P66375; -. DR EnsemblBacteria; AAF40595; AAF40595; NMB0136. DR GeneID; 25048857; -. DR GeneID; 902244; -. DR KEGG; nme:NMB0136; -. DR PATRIC; 20355293; VBINeiMen85645_0176. DR eggNOG; ENOG4108UKE; Bacteria. DR eggNOG; COG0048; LUCA. DR HOGENOM; HOG000040063; -. DR KO; K02950; -. DR OMA; LKSCPER; -. DR OrthoDB; EOG61ZTNF; -. DR BioCyc; NMEN122586:GHGG-146-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00403_B; Ribosomal_S12_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_S12/S23. DR InterPro; IPR005679; Ribosomal_S12_bac. DR PANTHER; PTHR11652; PTHR11652; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 123 30S ribosomal protein S12. FT /FTId=PRO_0000146275. SQ SEQUENCE 123 AA; 13708 MW; DB6D91737E918949 CRC64; MPTINQLVRK GRQKPVYVNK VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCKVRLTNG FEVISYIGGE GHNLQEHSVV LIRGGRVKDL PGVRYHTVRG SLDTAGVKDR KQARSKYGAK RPK // ID RS14_NEIMB Reviewed; 101 AA. AC P66408; Q9JQR3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=30S ribosomal protein S14 {ECO:0000255|HAMAP-Rule:MF_00537}; GN Name=rpsN {ECO:0000255|HAMAP-Rule:MF_00537}; GN OrderedLocusNames=NMB0155; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds 16S rRNA, required for the assembly of 30S CC particles and may also be responsible for determining the CC conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP- CC Rule:MF_00537}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 CC and S10. {ECO:0000255|HAMAP-Rule:MF_00537}. CC -!- SIMILARITY: Belongs to the ribosomal protein S14P family. CC {ECO:0000255|HAMAP-Rule:MF_00537}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40613.1; -; Genomic_DNA. DR PIR; E81232; E81232. DR RefSeq; NP_273213.1; NC_003112.2. DR RefSeq; WP_002216244.1; NC_003112.2. DR ProteinModelPortal; P66408; -. DR SMR; P66408; 41-101. DR STRING; 122586.NMB0155; -. DR PaxDb; P66408; -. DR EnsemblBacteria; AAF40613; AAF40613; NMB0155. DR GeneID; 902262; -. DR KEGG; nme:NMB0155; -. DR PATRIC; 20355333; VBINeiMen85645_0196. DR eggNOG; ENOG4105VBI; Bacteria. DR eggNOG; COG0199; LUCA. DR HOGENOM; HOG000039864; -. DR KO; K02954; -. DR OMA; NRCVLTS; -. DR OrthoDB; EOG6BCT0K; -. DR BioCyc; NMEN122586:GHGG-165-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00537; Ribosomal_S14_1; 1. DR InterPro; IPR001209; Ribosomal_S14. DR InterPro; IPR023036; Ribosomal_S14_bac/plaastid. DR PANTHER; PTHR19836; PTHR19836; 1. DR Pfam; PF00253; Ribosomal_S14; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 101 30S ribosomal protein S14. FT /FTId=PRO_0000130915. SQ SEQUENCE 101 AA; 11518 MW; DDC3585439E26E9C CRC64; MAKKALINRD LKRQALAKKY AAKRAAIKAV INDSNATEEE RFEARLRFQS IPRNAAPVRQ RRRCALTGRP RGTFRKFGLG RIKIREIAMR GEIPGVVKAS W // ID RS16_NEIMB Reviewed; 81 AA. AC P66438; Q9JQP8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=30S ribosomal protein S16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN Name=rpsP {ECO:0000255|HAMAP-Rule:MF_00385}; GN OrderedLocusNames=NMB0592; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein S16P family. CC {ECO:0000255|HAMAP-Rule:MF_00385}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41020.1; -; Genomic_DNA. DR PIR; E81180; E81180. DR RefSeq; NP_273636.1; NC_003112.2. DR RefSeq; WP_002214315.1; NC_003112.2. DR ProteinModelPortal; P66438; -. DR SMR; P66438; 1-77. DR STRING; 122586.NMB0592; -. DR PaxDb; P66438; -. DR EnsemblBacteria; AAF41020; AAF41020; NMB0592. DR GeneID; 902707; -. DR KEGG; nme:NMB0592; -. DR PATRIC; 20356469; VBINeiMen85645_0754. DR eggNOG; ENOG4105K5M; Bacteria. DR eggNOG; COG0228; LUCA. DR HOGENOM; HOG000246720; -. DR KO; K02959; -. DR OMA; SAHNPHY; -. DR OrthoDB; EOG6CVVKH; -. DR BioCyc; NMEN122586:GHGG-618-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1320.10; -; 1. DR HAMAP; MF_00385; Ribosomal_S16; 1. DR InterPro; IPR000307; Ribosomal_S16. DR InterPro; IPR023803; Ribosomal_S16_dom. DR PANTHER; PTHR12919; PTHR12919; 1. DR Pfam; PF00886; Ribosomal_S16; 1. DR SUPFAM; SSF54565; SSF54565; 1. DR TIGRFAMs; TIGR00002; S16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 81 30S ribosomal protein S16. FT /FTId=PRO_0000167216. SQ SEQUENCE 81 AA; 9292 MW; E7519DA9D9BFA23A CRC64; MVVIRLARGG SKHRPFYNVI VTDSRSRRDG RFIERVGFYN PVANEKQERV RLNADRLNHW IAQGAQVSDS VAKLIKEQKA A // ID RPOA_NEIMB Reviewed; 328 AA. AC P66704; Q9JR06; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; GN OrderedLocusNames=NMB0168; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 CC beta, 1 beta' and 1 omega subunit. When a sigma factor is CC associated with the core the holoenzyme is formed, which can CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000255|HAMAP-Rule:MF_00059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40625.1; -; Genomic_DNA. DR PIR; H81229; H81229. DR RefSeq; NP_273226.1; NC_003112.2. DR RefSeq; WP_002215457.1; NC_003112.2. DR ProteinModelPortal; P66704; -. DR SMR; P66704; 2-230, 249-325. DR STRING; 122586.NMB0168; -. DR PaxDb; P66704; -. DR PRIDE; P66704; -. DR EnsemblBacteria; AAF40625; AAF40625; NMB0168. DR GeneID; 902275; -. DR KEGG; nme:NMB0168; -. DR PATRIC; 20355359; VBINeiMen85645_0209. DR eggNOG; ENOG4105CTF; Bacteria. DR eggNOG; COG0202; LUCA. DR HOGENOM; HOG000218481; -. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR BioCyc; NMEN122586:GHGG-178-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.170.120.12; -; 1. DR HAMAP; MF_00059; RNApol_bact_RpoA; 1. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR011773; DNA-dir_RpoA. DR InterPro; IPR009025; RBP11-like_dimer. DR InterPro; IPR011260; RNAP_asu_C. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR ProDom; PD001179; RNAP_asu_C; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF55257; SSF55257; 2. DR SUPFAM; SSF56553; SSF56553; 1. DR TIGRFAMs; TIGR02027; rpoA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 328 DNA-directed RNA polymerase subunit FT alpha. FT /FTId=PRO_0000175347. FT REGION 1 234 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. FT REGION 248 328 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. SQ SEQUENCE 328 AA; 36076 MW; 893A4C39571DD34D CRC64; MQNSTTEFLK PRQIDVNTFS ATRAKVSMQP FERGFGHTLG NALRRILLSS MNGFAPTEVA IAGVLHEYST VDGIQEDVVD ILLNIKGIVF KLHGRSQVQL VLKKSGSGVV SAGDIELPHD VEILNPGHVI CHLADNGQIE MEIKVEQGRG YQSVSGRQVV RDENRQIGAI QLDASFSPIS RVSFEVEPAR VEQRTDLDKL VLDIETDGSI DPEEAVRSAA RILIDQMSIF ADLQGTPVEE VEEKAPPIDP VLLRPVDDLE LTVRSANCLK AEDIYYIGDL IQRTETELLK TPNLGRKSLN EIKEVLASKG LTLGSKLEAW PPVGLEKP // ID RS19_NEIMB Reviewed; 92 AA. AC P66487; Q9JR96; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=30S ribosomal protein S19 {ECO:0000255|HAMAP-Rule:MF_00531}; GN Name=rpsS {ECO:0000255|HAMAP-Rule:MF_00531}; GN OrderedLocusNames=NMB0146; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly CC to the 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00531}. CC -!- SIMILARITY: Belongs to the ribosomal protein S19P family. CC {ECO:0000255|HAMAP-Rule:MF_00531}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40604.1; -; Genomic_DNA. DR PIR; D81231; D81231. DR RefSeq; NP_273204.1; NC_003112.2. DR RefSeq; WP_002215422.1; NC_003112.2. DR ProteinModelPortal; P66487; -. DR SMR; P66487; 3-88. DR STRING; 122586.NMB0146; -. DR PaxDb; P66487; -. DR PRIDE; P66487; -. DR EnsemblBacteria; AAF40604; AAF40604; NMB0146. DR GeneID; 25048744; -. DR GeneID; 902253; -. DR KEGG; nme:NMB0146; -. DR PATRIC; 20355315; VBINeiMen85645_0187. DR eggNOG; ENOG4105K7S; Bacteria. DR eggNOG; COG0185; LUCA. DR HOGENOM; HOG000111560; -. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR BioCyc; NMEN122586:GHGG-156-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.860.10; -; 1. DR HAMAP; MF_00531; Ribosomal_S19; 1. DR InterPro; IPR002222; Ribosomal_S19. DR InterPro; IPR005732; Ribosomal_S19_bac-type. DR InterPro; IPR020934; Ribosomal_S19_CS. DR InterPro; IPR023575; Ribosomal_S19_SF. DR PANTHER; PTHR11880; PTHR11880; 1. DR Pfam; PF00203; Ribosomal_S19; 1. DR PIRSF; PIRSF002144; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR SUPFAM; SSF54570; SSF54570; 1. DR TIGRFAMs; TIGR01050; rpsS_bact; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 92 30S ribosomal protein S19. FT /FTId=PRO_0000129865. SQ SEQUENCE 92 AA; 10362 MW; 482B972C59C401AA CRC64; MARSLKKGPY VDLHLLKKVD AARASNDKRP IKTWSRRSTI LPDFIGLTIA VHNGRTHVPV FISDNMVGHK LGEFSLTRTF KGHLADKKAK KK // ID RPPH_NEIMB Reviewed; 174 AA. AC Q9JY96; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=RNA pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00298}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00298}; DE AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00298}; GN Name=rppH {ECO:0000255|HAMAP-Rule:MF_00298}; GN Synonyms=nudH {ECO:0000255|HAMAP-Rule:MF_00298}; GN OrderedLocusNames=NMB1683; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Accelerates the degradation of transcripts by removing CC pyrophosphate from the 5'-end of triphosphorylated RNA, leading to CC a more labile monophosphorylated state that can stimulate CC subsequent ribonuclease cleavage. {ECO:0000255|HAMAP- CC Rule:MF_00298}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00298}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00298}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. {ECO:0000255|HAMAP- CC Rule:MF_00298}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42031.1; -; Genomic_DNA. DR PIR; E81055; E81055. DR RefSeq; NP_274687.1; NC_003112.2. DR RefSeq; WP_002244258.1; NC_003112.2. DR ProteinModelPortal; Q9JY96; -. DR STRING; 122586.NMB1683; -. DR PaxDb; Q9JY96; -. DR EnsemblBacteria; AAF42031; AAF42031; NMB1683. DR GeneID; 903424; -. DR KEGG; nme:NMB1683; -. DR PATRIC; 20359317; VBINeiMen85645_2165. DR eggNOG; ENOG4105EJF; Bacteria. DR eggNOG; COG0494; LUCA. DR HOGENOM; HOG000066723; -. DR KO; K08311; -. DR OMA; ERNEVFW; -. DR OrthoDB; EOG6Q2SKR; -. DR BioCyc; NMEN122586:GHGG-1738-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.79.10; -; 1. DR HAMAP; MF_00298; Nudix_RppH; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022927; RppH. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 174 RNA pyrophosphohydrolase. FT /FTId=PRO_0000057013. FT DOMAIN 6 149 Nudix hydrolase. {ECO:0000255|HAMAP- FT Rule:MF_00298}. FT MOTIF 38 59 Nudix box. SQ SEQUENCE 174 AA; 21019 MW; 5211F082E1C93B85 CRC64; MLDREGYRPN VGIILINNRN EVFWGKRVRE HSWQFPQGGI KPGESPETAM YRELYEEVGL LPQHVKIIGR TRDWLRYDVP NNWVRREWRG SYRGQKQIWY LLRLTGRDCD VNLRATRHPE FDGWRWHQYW APVDEVIDFK RDVYLGALKE LSSRFLRGME SYEDFAARQS SDNR // ID RRF_NEIMB Reviewed; 185 AA. AC P66737; Q9JR52; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Ribosome-recycling factor {ECO:0000255|HAMAP-Rule:MF_00040}; DE Short=RRF {ECO:0000255|HAMAP-Rule:MF_00040}; DE AltName: Full=Ribosome-releasing factor {ECO:0000255|HAMAP-Rule:MF_00040}; GN Name=frr {ECO:0000255|HAMAP-Rule:MF_00040}; OrderedLocusNames=NMB0187; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Responsible for the release of ribosomes from messenger CC RNA at the termination of protein biosynthesis. May increase the CC efficiency of translation by recycling ribosomes from one round of CC translation to another. {ECO:0000255|HAMAP-Rule:MF_00040}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00040}. CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP- CC Rule:MF_00040}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40644.1; -; Genomic_DNA. DR PIR; D81229; D81229. DR RefSeq; NP_273245.1; NC_003112.2. DR RefSeq; WP_002216270.1; NC_003112.2. DR ProteinModelPortal; P66737; -. DR SMR; P66737; 1-185. DR STRING; 122586.NMB0187; -. DR PaxDb; P66737; -. DR EnsemblBacteria; AAF40644; AAF40644; NMB0187. DR GeneID; 902294; -. DR KEGG; nme:NMB0187; -. DR PATRIC; 20355399; VBINeiMen85645_0229. DR eggNOG; ENOG4108VCV; Bacteria. DR eggNOG; COG0233; LUCA. DR HOGENOM; HOG000040143; -. DR KO; K02838; -. DR OMA; VQPWEKK; -. DR OrthoDB; EOG6SV5F9; -. DR BioCyc; NMEN122586:GHGG-197-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006415; P:translational termination; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.132.20; -; 1. DR HAMAP; MF_00040; RRF; 1. DR InterPro; IPR002661; Ribosome_recyc_fac. DR InterPro; IPR023584; Ribosome_recyc_fac_dom. DR PANTHER; PTHR20982; PTHR20982; 1. DR Pfam; PF01765; RRF; 1. DR SUPFAM; SSF55194; SSF55194; 1. DR TIGRFAMs; TIGR00496; frr; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 185 Ribosome-recycling factor. FT /FTId=PRO_0000167503. SQ SEQUENCE 185 AA; 20731 MW; 668D1C347B846603 CRC64; MINDIQKTAE GKMQRSVEVL KENLAKVRTG RAHTGLLDQV EVEYWGSMVP VSQVANVTLL DARTIGVKPF EGNMAAKVEK AIRDSNLGLN PAAVGDLIRV PMPMLTEERR KDLIKVVRGE AEEGRVSIRN VRRDANDHIK KLLKDKEISE DEARRGEEAV QKLTDKYITE ADKLLTAKEE DLMAI // ID RS13_NEIMB Reviewed; 120 AA. AC P66386; Q9JRI3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=NMB0165; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Located at the top of the head of the 30S subunit, it CC contacts several helices of the 16S rRNA. In the 70S ribosome it CC contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S CC subunit (bridge B1b), connecting the 2 subunits; these bridges are CC implicated in subunit movement. Contacts the tRNAs in the A and P- CC sites. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose CC heterodimer with protein S19. Forms two bridges to the 50S subunit CC in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SIMILARITY: Belongs to the ribosomal protein S13P family. CC {ECO:0000255|HAMAP-Rule:MF_01315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40622.1; -; Genomic_DNA. DR PIR; E81229; E81229. DR RefSeq; NP_273223.1; NC_003112.2. DR RefSeq; WP_002215453.1; NC_003112.2. DR ProteinModelPortal; P66386; -. DR SMR; P66386; 2-116. DR STRING; 122586.NMB0165; -. DR PaxDb; P66386; -. DR EnsemblBacteria; AAF40622; AAF40622; NMB0165. DR GeneID; 902272; -. DR KEGG; nme:NMB0165; -. DR PATRIC; 20355353; VBINeiMen85645_0206. DR eggNOG; ENOG4108Z04; Bacteria. DR eggNOG; COG0099; LUCA. DR HOGENOM; HOG000039879; -. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR BioCyc; NMEN122586:GHGG-175-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.910.10; -; 1. DR HAMAP; MF_01315; Ribosomal_S13_S18; 1. DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C. DR InterPro; IPR001892; Ribosomal_S13. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR019980; Ribosomal_S13_bac-type. DR InterPro; IPR018269; Ribosomal_S13_CS. DR Pfam; PF00416; Ribosomal_S13; 1. DR PIRSF; PIRSF002134; Ribosomal_S13; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR TIGRFAMs; TIGR03631; uS13_bact; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 120 30S ribosomal protein S13. FT /FTId=PRO_0000132116. SQ SEQUENCE 120 AA; 13360 MW; 0CA46DB81385B657 CRC64; MARIAGVNIP NNAHIVIGLQ AIYGIGATRA KLICEAANIA PDTKAKDLDE TQLDALRDQV AKYEVEGDLR REVTMSIKRL MDMGCYRGFR HRRGLPCRGQ RTRTNARTRK GPRKAIAGKK // ID RS1_NEIMB Reviewed; 561 AA. AC Q9JZ44; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=30S ribosomal protein S1; GN Name=rpsA; OrderedLocusNames=NMB1301; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Binds mRNA; thus facilitating recognition of the CC initiation point. It is needed to translate mRNA with a short CC Shine-Dalgarno (SD) purine-rich sequence (By similarity). CC {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein S1P family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 6 S1 motif domains. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41676.1; -; Genomic_DNA. DR PIR; G81099; G81099. DR RefSeq; NP_274320.1; NC_003112.2. DR RefSeq; WP_002237993.1; NC_003112.2. DR ProteinModelPortal; Q9JZ44; -. DR SMR; Q9JZ44; 360-402. DR STRING; 122586.NMB1301; -. DR PaxDb; Q9JZ44; -. DR PRIDE; Q9JZ44; -. DR EnsemblBacteria; AAF41676; AAF41676; NMB1301. DR GeneID; 903723; -. DR KEGG; nme:NMB1301; -. DR PATRIC; 20358243; VBINeiMen85645_1633. DR eggNOG; ENOG4105CAV; Bacteria. DR eggNOG; COG0539; LUCA. DR HOGENOM; HOG000044052; -. DR KO; K02945; -. DR OMA; SRRYPQG; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NMEN122586:GHGG-1339-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 6. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000110; Ribosomal_S1. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF00575; S1; 6. DR PIRSF; PIRSF002111; RpsA; 1. DR PRINTS; PR00681; RIBOSOMALS1. DR SMART; SM00316; S1; 6. DR SUPFAM; SSF50249; SSF50249; 6. DR TIGRFAMs; TIGR00717; rpsA; 1. DR PROSITE; PS50126; S1; 6. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Repeat; Ribonucleoprotein; KW Ribosomal protein; RNA-binding. FT CHAIN 1 561 30S ribosomal protein S1. FT /FTId=PRO_0000320264. FT DOMAIN 22 88 S1 motif 1. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 106 172 S1 motif 2. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 193 261 S1 motif 3. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 278 348 S1 motif 4. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 365 435 S1 motif 5. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 452 521 S1 motif 6. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. SQ SEQUENCE 561 AA; 61177 MW; 2CF6FD8DD99D1615 CRC64; MSMENFAQLL EESFTLQEMN PGEVITAEVV AIDQNFVTVN AGLKSESLID VAEFKNAQGE IEVKVGDFVT VTIESVENGF GETKLSREKA KRAADWIALE EAMENGDILS GIINGKVKGG LTVMISSIRA FLPGSLVDVR PVKDTSHFEG KEIEFKVIKL DKKRNNVVVS RRAVLEATLG EERKALLENL QEGSVIKGIV KNITDYGAFV DLGGIDGLLH ITDLAWRRVK HPSEVLEVGQ EVEAKVLKFD QEKQRVSLGM KQLGEDPWSG LTRRYPQGTR LFGKVSNLTD YGAFVEIEQG IEGLVHVSEM DWTNKNVHPS KVVQLGDEVE VMILEIDEGR RRISLGMKQC QANPWEEFAA NHNKGDKISG AVKSITDFGV FVGLPGGIDG LVHLSDLSWT ESGEEAVRKY KKGEEVEAVV LAIDVEKERI SLGIKQLEGD PFGNFISVND KGSLVKGSVK SVDAKGAVIA LSDEVEGYLP ASEFAADRVE DLTTKLKEGD EVEAVIVTVD RKNRSIKLSV KAKDAKESRE ALNSVNAAAN ANAGTTSLGD LLKAKLSGEQ E // ID RS4_NEIMB Reviewed; 206 AA. AC P66561; Q9JRD0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 66. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; GN OrderedLocusNames=NMB0167; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the body of CC the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. CC The interaction surface between S4 and S5 is involved in control CC of translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family. CC {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40624.1; -; Genomic_DNA. DR PIR; G81229; G81229. DR RefSeq; NP_273225.1; NC_003112.2. DR RefSeq; WP_002215455.1; NC_003112.2. DR ProteinModelPortal; P66561; -. DR SMR; P66561; 2-206. DR STRING; 122586.NMB0167; -. DR PaxDb; P66561; -. DR PRIDE; P66561; -. DR EnsemblBacteria; AAF40624; AAF40624; NMB0167. DR GeneID; 902274; -. DR KEGG; nme:NMB0167; -. DR PATRIC; 20355357; VBINeiMen85645_0208. DR eggNOG; ENOG4105G6W; Bacteria. DR eggNOG; COG0522; LUCA. DR HOGENOM; HOG000221003; -. DR KO; K02986; -. DR OMA; VYEWITW; -. DR OrthoDB; EOG6N3CXM; -. DR BioCyc; NMEN122586:GHGG-177-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1050.10; -; 1. DR Gene3D; 3.10.290.10; -; 1. DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1. DR InterPro; IPR022801; Ribosomal_S4/S9. DR InterPro; IPR001912; Ribosomal_S4/S9_N. DR InterPro; IPR005709; Ribosomal_S4_bac-type. DR InterPro; IPR018079; Ribosomal_S4_CS. DR InterPro; IPR002942; S4_RNA-bd. DR PANTHER; PTHR11831; PTHR11831; 1. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM01390; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR01017; rpsD_bact; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 206 30S ribosomal protein S4. FT /FTId=PRO_0000132424. FT DOMAIN 96 157 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_01306}. SQ SEQUENCE 206 AA; 23250 MW; 363AFD6C703669E9 CRC64; MARYIGPKCK LARREGTDLF LKSARRSLDS KCKIDSAPGQ HGAKKPRLSD YGLQLREKQK IRRIYGVLER QFRRYFAEAD RRKGSTGELL LQLLESRLDN VVYRMGFGST RAEARQLVSH KAIVVNGQVV NIPSFQVKAG DVVSVREKAK KQVRIQEALG LATQIGLPGW VSVDADKLEG VFKNMPDRSE LTGDINEQLV VEFYSK // ID RS5_NEIMB Reviewed; 172 AA. AC P66577; Q9JQP3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; GN OrderedLocusNames=NMB0159; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: With S4 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- FUNCTION: Located at the back of the 30S subunit body where it CC stabilizes the conformation of the head with respect to the body. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 CC and S8. {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S CC subunit; the C-terminal domain interacts with the body and CC contacts protein S4. The interaction surface between S4 and S5 is CC involved in control of translational fidelity. CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SIMILARITY: Contains 1 S5 DRBM domain. {ECO:0000255|HAMAP- CC Rule:MF_01307}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40617.1; -; Genomic_DNA. DR PIR; A81233; A81233. DR RefSeq; NP_273217.1; NC_003112.2. DR RefSeq; WP_002215445.1; NC_003112.2. DR ProteinModelPortal; P66577; -. DR SMR; P66577; 13-160. DR STRING; 122586.NMB0159; -. DR PaxDb; P66577; -. DR PRIDE; P66577; -. DR EnsemblBacteria; AAF40617; AAF40617; NMB0159. DR GeneID; 902266; -. DR KEGG; nme:NMB0159; -. DR PATRIC; 20355341; VBINeiMen85645_0200. DR eggNOG; ENOG4108RA9; Bacteria. DR eggNOG; COG0098; LUCA. DR HOGENOM; HOG000072595; -. DR KO; K02988; -. DR OMA; PHEQKGK; -. DR OrthoDB; EOG6FJNM5; -. DR BioCyc; NMEN122586:GHGG-169-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000851; Ribosomal_S5. DR InterPro; IPR005712; Ribosomal_S5_bac-type. DR InterPro; IPR005324; Ribosomal_S5_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR013810; Ribosomal_S5_N. DR InterPro; IPR018192; Ribosomal_S5_N_CS. DR PANTHER; PTHR13718; PTHR13718; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR01021; rpsE_bact; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 172 30S ribosomal protein S5. FT /FTId=PRO_0000131560. FT DOMAIN 13 76 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 172 AA; 18246 MW; EDB791DB33D5FB07 CRC64; MAKHEIEERG DGLIEKMVAV NRVTKVVKGG RIMAFSALTV VGDGDGRIGM GKGKSKEVPV AVQKAMDQAR RSMIKVPLKN GTIHHEVIGR HGATKVFMQP AKEGSGVKAG GPMRLVFDAM GIHNISAKVH GSTNPYNIVR ATLDGLSKLH TPADIAAKRG LTVEDILGVN HG // ID RS10_NEIMB Reviewed; 103 AA. AC P66333; Q9JR21; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 65. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rpsJ {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=NMB0140; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the binding of tRNA to the ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC -!- SIMILARITY: Belongs to the ribosomal protein S10P family. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40599.1; -; Genomic_DNA. DR PIR; E81234; E81234. DR RefSeq; NP_273198.1; NC_003112.2. DR RefSeq; WP_002215394.1; NC_003112.2. DR ProteinModelPortal; P66333; -. DR SMR; P66333; 5-102. DR STRING; 122586.NMB0140; -. DR PaxDb; P66333; -. DR PRIDE; P66333; -. DR EnsemblBacteria; AAF40599; AAF40599; NMB0140. DR GeneID; 902248; -. DR KEGG; nme:NMB0140; -. DR PATRIC; 20355301; VBINeiMen85645_0180. DR eggNOG; ENOG4108Z10; Bacteria. DR eggNOG; COG0051; LUCA. DR HOGENOM; HOG000270246; -. DR KO; K02946; -. DR OMA; QQKIRIK; -. DR OrthoDB; EOG6VXFHB; -. DR BioCyc; NMEN122586:GHGG-150-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.600; -; 1. DR HAMAP; MF_00508; Ribosomal_S10; 1. DR InterPro; IPR001848; Ribosomal_S10. DR InterPro; IPR018268; Ribosomal_S10_CS. DR InterPro; IPR027486; Ribosomal_S10_dom. DR PANTHER; PTHR11700; PTHR11700; 1. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR SMART; SM01403; Ribosomal_S10; 1. DR SUPFAM; SSF54999; SSF54999; 1. DR TIGRFAMs; TIGR01049; rpsJ_bact; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 103 30S ribosomal protein S10. FT /FTId=PRO_0000146564. SQ SEQUENCE 103 AA; 11807 MW; 7A112084E44867EF CRC64; MANQKIRIRL KAYDYALIDR SAQEIVETAK RTGAVVKGPI PLPTKIERFN ILRSPHVNKT SREQLEIRTH LRLMDIVDWT DKTTDALMKL DLPAGVDVEI KVQ // ID RS17_NEIMB Reviewed; 87 AA. AC Q7DDT3; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=NMB0151; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC specifically to the 5'-end of 16S ribosomal RNA. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01345}. CC -!- SIMILARITY: Belongs to the ribosomal protein S17P family. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40609.1; -; Genomic_DNA. DR RefSeq; NP_273209.1; NC_003112.2. DR RefSeq; WP_002215433.1; NC_003112.2. DR ProteinModelPortal; Q7DDT3; -. DR SMR; Q7DDT3; 7-84. DR STRING; 122586.NMB0151; -. DR PaxDb; Q7DDT3; -. DR EnsemblBacteria; AAF40609; AAF40609; NMB0151. DR GeneID; 902258; -. DR KEGG; nme:NMB0151; -. DR PATRIC; 20355325; VBINeiMen85645_0192. DR eggNOG; ENOG4105K87; Bacteria. DR eggNOG; COG0186; LUCA. DR HOGENOM; HOG000231339; -. DR KO; K02961; -. DR OMA; LKAHDEQ; -. DR OrthoDB; EOG63JRH2; -. DR BioCyc; NMEN122586:GHGG-161-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000266; Ribosomal_S17/S11. DR InterPro; IPR019984; Ribosomal_S17_bac-type. DR InterPro; IPR019979; Ribosomal_S17_CS. DR PANTHER; PTHR10744; PTHR10744; 1. DR Pfam; PF00366; Ribosomal_S17; 1. DR PRINTS; PR00973; RIBOSOMALS17. DR ProDom; PD001295; Ribosomal_S17; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR03635; uS17_bact; 1. DR PROSITE; PS00056; RIBOSOMAL_S17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 87 30S ribosomal protein S17. FT /FTId=PRO_0000233518. SQ SEQUENCE 87 AA; 9830 MW; FE93FDD2F3B5D72B CRC64; MSETKNVRTL QGKVVSDKMD KTVTVLVERK VKHPLYGKII RLSTKIHAHD ENNQYGIGDV VVISESRPLS KTKSWVVSEL VEKARSI // ID RS15_NEIMB Reviewed; 89 AA. AC Q7DDM4; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=NMB0609; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it helps nucleate assembly of the CC platform of the 30S subunit by binding and bridging several RNA CC helices of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01343}. CC -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S CC rRNA of the 50S subunit in the ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01343}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the CC 50S subunit in the 70S ribosome, contacting the 23S rRNA. CC {ECO:0000255|HAMAP-Rule:MF_01343}. CC -!- SIMILARITY: Belongs to the ribosomal protein S15P family. CC {ECO:0000255|HAMAP-Rule:MF_01343}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41036.1; -; Genomic_DNA. DR RefSeq; NP_273653.1; NC_003112.2. DR RefSeq; WP_002217790.1; NC_003112.2. DR ProteinModelPortal; Q7DDM4; -. DR SMR; Q7DDM4; 2-89. DR STRING; 122586.NMB0609; -. DR PaxDb; Q7DDM4; -. DR EnsemblBacteria; AAF41036; AAF41036; NMB0609. DR GeneID; 902723; -. DR KEGG; nme:NMB0609; -. DR PATRIC; 20356505; VBINeiMen85645_0772. DR eggNOG; ENOG4105K77; Bacteria. DR eggNOG; COG0184; LUCA. DR HOGENOM; HOG000040097; -. DR KO; K02956; -. DR OMA; TEHFKSH; -. DR OrthoDB; EOG6B368J; -. DR BioCyc; NMEN122586:GHGG-635-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.10; -; 1. DR HAMAP; MF_01343_B; Ribosomal_S15_B; 1. DR InterPro; IPR000589; Ribosomal_S15. DR InterPro; IPR005290; Ribosomal_S15_bac-type. DR InterPro; IPR009068; S15_NS1_RNA-bd. DR Pfam; PF00312; Ribosomal_S15; 1. DR SMART; SM01387; Ribosomal_S15; 1. DR SUPFAM; SSF47060; SSF47060; 1. DR TIGRFAMs; TIGR00952; S15_bact; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 89 30S ribosomal protein S15. FT /FTId=PRO_0000115489. SQ SEQUENCE 89 AA; 10386 MW; CF29ABE602503B01 CRC64; MALTVEQKAQ IVKDFQRKEG DTGSSEVQVA LLTFRINDLT PHFKANPKDH HSRRGLLKMV SQRRRLLAYL RRTQPDTYRA LITRLGLRK // ID RS20_NEIMB Reviewed; 87 AA. AC P66508; Q9JQM6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=NMB0463; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP- CC Rule:MF_00500}. CC -!- SIMILARITY: Belongs to the ribosomal protein S20P family. CC {ECO:0000255|HAMAP-Rule:MF_00500}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40900.1; -; Genomic_DNA. DR PIR; D81195; D81195. DR RefSeq; NP_273510.1; NC_003112.2. DR RefSeq; WP_002212556.1; NC_003112.2. DR ProteinModelPortal; P66508; -. DR SMR; P66508; 3-87. DR STRING; 122586.NMB0463; -. DR PaxDb; P66508; -. DR EnsemblBacteria; AAF40900; AAF40900; NMB0463. DR GeneID; 25048215; -. DR GeneID; 902579; -. DR KEGG; nme:NMB0463; -. DR PATRIC; 20356168; VBINeiMen85645_0605. DR eggNOG; ENOG41082GY; Bacteria. DR eggNOG; COG0268; LUCA. DR HOGENOM; HOG000097048; -. DR KO; K02968; -. DR OMA; ARRAHNI; -. DR OrthoDB; EOG6HMXNQ; -. DR BioCyc; NMEN122586:GHGG-487-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.58.110; -; 1. DR HAMAP; MF_00500; Ribosomal_S20; 1. DR InterPro; IPR002583; Ribosomal_S20. DR Pfam; PF01649; Ribosomal_S20p; 1. DR ProDom; PD004231; Ribosomal_S20; 1. DR SUPFAM; SSF46992; SSF46992; 1. DR TIGRFAMs; TIGR00029; S20; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 87 30S ribosomal protein S20. FT /FTId=PRO_0000167999. SQ SEQUENCE 87 AA; 9508 MW; F7C297D93537B4F0 CRC64; MANSAQARKR ARQSVKQRAH NASLRTAFRT AVKKVLKAVE AGDKAAAQAV YQESVKVIDR IADKGVFHKN KAARHKSRLS AKVKALA // ID RS8_NEIMB Reviewed; 130 AA. AC P66628; Q9JR58; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; GN OrderedLocusNames=NMB0156; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA central domain where it helps coordinate CC assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP- CC Rule:MF_01302}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 CC and S12. {ECO:0000255|HAMAP-Rule:MF_01302}. CC -!- SIMILARITY: Belongs to the ribosomal protein S8P family. CC {ECO:0000255|HAMAP-Rule:MF_01302}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40614.1; -; Genomic_DNA. DR PIR; F81232; F81232. DR RefSeq; NP_273214.1; NC_003112.2. DR RefSeq; WP_002215438.1; NC_003112.2. DR ProteinModelPortal; P66628; -. DR SMR; P66628; 2-130. DR STRING; 122586.NMB0156; -. DR PaxDb; P66628; -. DR EnsemblBacteria; AAF40614; AAF40614; NMB0156. DR GeneID; 902263; -. DR KEGG; nme:NMB0156; -. DR PATRIC; 20355335; VBINeiMen85645_0197. DR eggNOG; ENOG4108UJY; Bacteria. DR eggNOG; COG0096; LUCA. DR HOGENOM; HOG000204095; -. DR KO; K02994; -. DR OMA; KYKGNQS; -. DR OrthoDB; EOG6Z0QH1; -. DR BioCyc; NMEN122586:GHGG-166-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01302_B; Ribosomal_S8_B; 1. DR InterPro; IPR000630; Ribosomal_S8. DR PANTHER; PTHR11758; PTHR11758; 1. DR Pfam; PF00410; Ribosomal_S8; 1. DR SUPFAM; SSF56047; SSF56047; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 130 30S ribosomal protein S8. FT /FTId=PRO_0000126452. SQ SEQUENCE 130 AA; 14124 MW; 6420D912297511E6 CRC64; MSMHDPISDM LTRIRNAQRA NKAAVAMPSS KLKCAIAKVL KEEGYIEDFA VSSDVKSILE IQLKYYAGRP VIEQIKRVSR PGLRIYKASS EIPSVMNGLG IAIVSTSKGV MTDRKARSQG VGGELLCIVA // ID RSGA_NEIMB Reviewed; 307 AA. AC Q9K1A4; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative ribosome biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820}; GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820}; GN OrderedLocusNames=NMB0263; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May play a role in 30S ribosomal subunit biogenesis. CC Unusual circulary permuted GTPase that catalyzes rapid hydrolysis CC of GTP with a slow catalytic turnover. {ECO:0000255|HAMAP- CC Rule:MF_01820}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01820}; CC -!- SUBUNIT: Monomer. Associates with ribosomes. {ECO:0000255|HAMAP- CC Rule:MF_01820}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC RsgA subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}. CC -!- SIMILARITY: Contains 1 CP-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40717.1; -; Genomic_DNA. DR PIR; H81217; H81217. DR RefSeq; NP_273319.1; NC_003112.2. DR RefSeq; WP_002221919.1; NC_003112.2. DR ProteinModelPortal; Q9K1A4; -. DR STRING; 122586.NMB0263; -. DR PaxDb; Q9K1A4; -. DR EnsemblBacteria; AAF40717; AAF40717; NMB0263. DR GeneID; 902374; -. DR KEGG; nme:NMB0263; -. DR PATRIC; 20355606; VBINeiMen85645_0327. DR eggNOG; ENOG4105E06; Bacteria. DR eggNOG; COG1162; LUCA. DR HOGENOM; HOG000006957; -. DR KO; K06949; -. DR OMA; TARLFHF; -. DR OrthoDB; EOG69SKDD; -. DR BioCyc; NMEN122586:GHGG-278-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA. DR InterPro; IPR010914; RsgA_GTPase_dom. DR Pfam; PF03193; DUF258; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00157; TIGR00157; 1. DR PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1 307 Putative ribosome biogenesis GTPase RsgA. FT /FTId=PRO_0000171499. FT DOMAIN 85 242 CP-type G. FT NP_BIND 135 138 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT NP_BIND 184 192 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT MOTIF 266 279 Knuckle-like cysteine cluster. FT METAL 266 266 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 271 271 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 273 273 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 279 279 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. SQ SEQUENCE 307 AA; 33482 MW; D3E44FD50609F76C CRC64; MPSEHPFSDG IPTPNPKETM NDTAQITASY GRRYIVRTPD GTTYEASTRK KRVDFACGDR VRISPVNAEQ VVIEDFLPRQ SLLYRQDAWK TKLIAANVTQ LLIVTAAVPS PSVRLLQRAL LAAEAAGIEA VIVLNKADLP ETALWREKLK FYETLGYPVI ETRALENAGS LRPALQGHSN ILLGQSGMGK STLTNALLGS QTARTGDISA ALDSGKHTTT HARLYDLNGE TQLIDSPGLQ EFGLHHLQAA DLPRYFPDFR HLVGQCRFHN CTHRAEPGCA FKAAAQTGAA SPERLAFLQG ITDELPG // ID RSMH_NEIMB Reviewed; 328 AA. AC Q9K0Z0; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_01007}; DE EC=2.1.1.199 {ECO:0000255|HAMAP-Rule:MF_01007}; DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01007}; DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000255|HAMAP-Rule:MF_01007}; GN Name=rsmH {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW; GN OrderedLocusNames=NMB0411; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in CC position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01007}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(1402) in CC 16S rRNA = S-adenosyl-L-homocysteine + N(4)-methylcytosine(1402) CC in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH CC family. {ECO:0000255|HAMAP-Rule:MF_01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40850.1; -; Genomic_DNA. DR PIR; H81201; H81201. DR RefSeq; NP_273460.1; NC_003112.2. DR RefSeq; WP_002224919.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z0; -. DR STRING; 122586.NMB0411; -. DR PaxDb; Q9K0Z0; -. DR EnsemblBacteria; AAF40850; AAF40850; NMB0411. DR GeneID; 902527; -. DR KEGG; nme:NMB0411; -. DR PATRIC; 20356011; VBINeiMen85645_0521. DR eggNOG; ENOG4105CGJ; Bacteria. DR eggNOG; COG0275; LUCA. DR HOGENOM; HOG000049778; -. DR KO; K03438; -. DR OMA; HVPVMLQ; -. DR OrthoDB; EOG6X9MQ1; -. DR BioCyc; NMEN122586:GHGG-435-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.170; -; 1. DR Gene3D; 3.40.50.150; -; 2. DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1. DR InterPro; IPR002903; RsmH. DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11265; PTHR11265; 1. DR Pfam; PF01795; Methyltransf_5; 1. DR PIRSF; PIRSF004486; MraW; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR SUPFAM; SSF81799; SSF81799; 1. DR TIGRFAMs; TIGR00006; TIGR00006; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 328 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108671. FT REGION 37 39 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 57 57 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 83 83 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01007}. FT BINDING 104 104 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 111 111 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. SQ SEQUENCE 328 AA; 36115 MW; 6D535DAA63BE2B6A CRC64; MSGAESYRHI TVLLNEAVDA LAVREDGVYV DGTFGRGGHS RLILSRLGDA GRLIVFDKDP QAIAVAEELA RSDKRVGVVH GGFASFQTAL DGLGIGKVDG ALFDLGISSP QIDDGSRGFS FRFDAPLDMR MDTTRGMSAA EWIAVASEQD LHEVIKNYGE ERFSRRIARA IVAQRAESPI DTTRKLAQIV AQNVRTRERG QDPATRTFQA VRIFINRELE EVGAVLPQVM CRLKEGGRLA VIAFHSLEDR IVKQFVKKYS QHAPLPRWAA VREADLPELP LKIVGRALKP GEAEIAANPR ARSAVLRVAE RTAGPIPEQS QRKTSEWQ // ID RS18_NEIMB Reviewed; 76 AA. AC P0A0X7; O07815; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; GN OrderedLocusNames=NMB1321; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds as a heterodimer with protein S6 to the central CC domain of the 16S rRNA, where it helps stabilize the platform of CC the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_00270}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight CC heterodimer with protein S6. {ECO:0000255|HAMAP-Rule:MF_00270}. CC -!- SIMILARITY: Belongs to the ribosomal protein S18P family. CC {ECO:0000255|HAMAP-Rule:MF_00270}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41696.1; -; Genomic_DNA. DR PIR; H81096; H81096. DR RefSeq; NP_274340.1; NC_003112.2. DR RefSeq; WP_002213306.1; NC_003112.2. DR ProteinModelPortal; P0A0X7; -. DR SMR; P0A0X7; 8-76. DR STRING; 122586.NMB1321; -. DR PaxDb; P0A0X7; -. DR EnsemblBacteria; AAF41696; AAF41696; NMB1321. DR GeneID; 903743; -. DR KEGG; nme:NMB1321; -. DR PATRIC; 20358291; VBINeiMen85645_1657. DR eggNOG; ENOG4105VH8; Bacteria. DR eggNOG; COG0238; LUCA. DR HOGENOM; HOG000218466; -. DR KO; K02963; -. DR OMA; YKRPDIL; -. DR OrthoDB; EOG6PCQ4R; -. DR BioCyc; NMEN122586:GHGG-1359-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.640.10; -; 1. DR HAMAP; MF_00270; Ribosomal_S18; 1. DR InterPro; IPR001648; Ribosomal_S18. DR InterPro; IPR018275; Ribosomal_S18_CS. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR SUPFAM; SSF46911; SSF46911; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 76 30S ribosomal protein S18. FT /FTId=PRO_0000111194. SQ SEQUENCE 76 AA; 8993 MW; 0842C771DC9CAD5A CRC64; MARQSFKRRK FCRFTAEKIQ EVDYKQVDLL KDFISENGKI IPARITGTKA FYQRQLAVAV KRARFLALLP YTDQHK // ID RS3_NEIMB Reviewed; 230 AA. AC P66551; Q9JQX2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; GN OrderedLocusNames=NMB0148; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA CC in the 70S ribosome, positioning it for translation. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex CC with proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SIMILARITY: Belongs to the ribosomal protein S3P family. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_01309}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40606.1; -; Genomic_DNA. DR PIR; F81231; F81231. DR RefSeq; NP_273206.1; NC_003112.2. DR RefSeq; WP_002215427.1; NC_003112.2. DR ProteinModelPortal; P66551; -. DR SMR; P66551; 2-203. DR STRING; 122586.NMB0148; -. DR PaxDb; P66551; -. DR PRIDE; P66551; -. DR EnsemblBacteria; AAF40606; AAF40606; NMB0148. DR GeneID; 902255; -. DR KEGG; nme:NMB0148; -. DR PATRIC; 20355319; VBINeiMen85645_0189. DR eggNOG; ENOG4105CKE; Bacteria. DR eggNOG; COG0092; LUCA. DR HOGENOM; HOG000210610; -. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR BioCyc; NMEN122586:GHGG-158-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1140.32; -; 1. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR005704; Ribosomal_S3_bac. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR018280; Ribosomal_S3_CS. DR Pfam; PF07650; KH_2; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR SUPFAM; SSF54821; SSF54821; 1. DR TIGRFAMs; TIGR01009; rpsC_bact; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 230 30S ribosomal protein S3. FT /FTId=PRO_0000130161. FT DOMAIN 39 107 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 230 AA; 25798 MW; A82CFF1A4D155A30 CRC64; MGQKINPTGF RLAVTKDWAS KWFAKSTDFS TVLKQDIDVR NYLRQKLANA SVGRVVIERP AKSARITIHS ARPGVVIGKK GEDIEVLKRD LQVLMGVPVH VNIEEIRRPE LDAQIIADGI AQQLEKRVQF RRAMKRAMQN AMRSGAKGIK IMTSGRLNGA DIARSEWYRE GRVPLHTLRA NVDYATSEAH TTYGVLGLKV WVYTEGNIKS SKPEHESKQR KAGRRNAAAN // ID RS21_NEIMB Reviewed; 70 AA. AC P66519; Q9JRG3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 16-MAR-2016, entry version 57. DE RecName: Full=30S ribosomal protein S21; GN Name=rpsU; OrderedLocusNames=NMB1950; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein S21P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42279.1; -; Genomic_DNA. DR PIR; G81023; G81023. DR RefSeq; NP_274944.1; NC_003112.2. DR RefSeq; WP_002214819.1; NC_003112.2. DR ProteinModelPortal; P66519; -. DR SMR; P66519; 4-54. DR STRING; 122586.NMB1950; -. DR PaxDb; P66519; -. DR EnsemblBacteria; AAF42279; AAF42279; NMB1950. DR GeneID; 23784015; -. DR GeneID; 904200; -. DR KEGG; nme:NMB1950; -. DR PATRIC; 20359957; VBINeiMen85645_2483. DR eggNOG; ENOG4105VCC; Bacteria. DR eggNOG; COG0828; LUCA. DR HOGENOM; HOG000157460; -. DR KO; K02970; -. DR OMA; KRHFKRL; -. DR OrthoDB; EOG6FBX3Z; -. DR BioCyc; NMEN122586:GHGG-2007-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00358; Ribosomal_S21; 1. DR InterPro; IPR001911; Ribosomal_S21. DR Pfam; PF01165; Ribosomal_S21; 1. DR PRINTS; PR00976; RIBOSOMALS21. DR ProDom; PD005521; Ribosomal_S21; 1. DR TIGRFAMs; TIGR00030; S21p; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 70 30S ribosomal protein S21. FT /FTId=PRO_0000178356. SQ SEQUENCE 70 AA; 8355 MW; 1A80F0A6CEC081D6 CRC64; MPAIRVKENE PFEVAMRRFK RAVEKTGLLT ELRAREAYEK PTTERKRKKA AAVKRLQKRL RSQQLPPKMY // ID RS2_NEIMB Reviewed; 242 AA. AC P66540; Q9JRG7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=30S ribosomal protein S2 {ECO:0000255|HAMAP-Rule:MF_00291}; GN Name=rpsB {ECO:0000255|HAMAP-Rule:MF_00291}; GN OrderedLocusNames=NMB2101; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the ribosomal protein S2P family. CC {ECO:0000255|HAMAP-Rule:MF_00291}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42418.1; -; Genomic_DNA. DR PIR; F81006; F81006. DR RefSeq; NP_275089.1; NC_003112.2. DR RefSeq; WP_002218221.1; NC_003112.2. DR ProteinModelPortal; P66540; -. DR SMR; P66540; 9-226. DR STRING; 122586.NMB2101; -. DR PaxDb; P66540; -. DR PRIDE; P66540; -. DR EnsemblBacteria; AAF42418; AAF42418; NMB2101. DR GeneID; 903940; -. DR KEGG; nme:NMB2101; -. DR PATRIC; 20360372; VBINeiMen85645_2683. DR eggNOG; ENOG4105CE9; Bacteria. DR eggNOG; COG0052; LUCA. DR HOGENOM; HOG000071892; -. DR KO; K02967; -. DR OMA; RIPDILY; -. DR OrthoDB; EOG6XWV6P; -. DR BioCyc; NMEN122586:GHGG-2166-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid. DR InterPro; IPR018130; Ribosomal_S2_CS. DR InterPro; IPR023591; Ribosomal_S2_flav_dom. DR PANTHER; PTHR12534; PTHR12534; 1. DR Pfam; PF00318; Ribosomal_S2; 1. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; SSF52313; 1. DR TIGRFAMs; TIGR01011; rpsB_bact; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 242 30S ribosomal protein S2. FT /FTId=PRO_0000134205. SQ SEQUENCE 242 AA; 26899 MW; 1812C11824C4FB39 CRC64; MSQITMRQMI EAGVHFGHQT RFWNPKMAQY IFGARNKIHI VNLEKTLPMF QDAQEAVRRL VANKGTVLFV GTKRQARDII REEATRAGMP FVDYRWLGGM LTNYKTVKQS IKRLEEKTAA LENAAESGFS KKEILEMQRD VEKLERSLGG IKNMKGLPDA IFVIDTGYQK GTLVEAEKLG IPVIAVVDTN NSPDGVKYVI PGNDDSAKAI RLYCRGIADA VLEGKNQALQ ETVAAAQEAA AE // ID RS6_NEIMB Reviewed; 122 AA. AC Q9JZ29; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=30S ribosomal protein S6; GN Name=rpsF; OrderedLocusNames=NMB1323; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S6P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41698.1; -; Genomic_DNA. DR PIR; B81097; B81097. DR RefSeq; NP_274342.1; NC_003112.2. DR RefSeq; WP_010980921.1; NC_003112.2. DR ProteinModelPortal; Q9JZ29; -. DR SMR; Q9JZ29; 1-100. DR STRING; 122586.NMB1323; -. DR PaxDb; Q9JZ29; -. DR PRIDE; Q9JZ29; -. DR EnsemblBacteria; AAF41698; AAF41698; NMB1323. DR GeneID; 903745; -. DR KEGG; nme:NMB1323; -. DR PATRIC; 20358295; VBINeiMen85645_1659. DR eggNOG; ENOG4108ZDX; Bacteria. DR eggNOG; COG0360; LUCA. DR HOGENOM; HOG000040438; -. DR KO; K02990; -. DR OMA; ITEASPM; -. DR OrthoDB; EOG6P33DH; -. DR BioCyc; NMEN122586:GHGG-1361-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.60; -; 1. DR HAMAP; MF_00360; Ribosomal_S6; 1. DR InterPro; IPR000529; Ribosomal_S6. DR InterPro; IPR020815; Ribosomal_S6_CS. DR InterPro; IPR020814; Ribosomal_S6_plastid/chlpt. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. DR Pfam; PF01250; Ribosomal_S6; 1. DR SUPFAM; SSF54995; SSF54995; 1. DR TIGRFAMs; TIGR00166; S6; 1. DR PROSITE; PS01048; RIBOSOMAL_S6; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 122 30S ribosomal protein S6. FT /FTId=PRO_0000176805. SQ SEQUENCE 122 AA; 13949 MW; E7D74DCFABA4D05B CRC64; MRHYEIVFIV HPDQSEQVPA MVERYKTMIA EANGKIHRLE DWGRRQLAYP INKIHKAHYV LMNIETTPEV VEELETAFRF NDAILRHLTI KTKHAVTEAS PMLGGEKAKN LLSGASEEAV AQ // ID RS7_NEIMB Reviewed; 156 AA. AC P66614; Q9JR15; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; GN OrderedLocusNames=NMB0137; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the head CC domain of the 30S subunit. Is located at the subunit interface CC close to the decoding center, probably blocks exit of the E-site CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 CC and S11. {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- SIMILARITY: Belongs to the ribosomal protein S7P family. CC {ECO:0000255|HAMAP-Rule:MF_00480}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40596.1; -; Genomic_DNA. DR PIR; B81234; B81234. DR RefSeq; NP_273195.1; NC_003112.2. DR RefSeq; WP_002215391.1; NC_003112.2. DR ProteinModelPortal; P66614; -. DR SMR; P66614; 3-154. DR STRING; 122586.NMB0137; -. DR PaxDb; P66614; -. DR EnsemblBacteria; AAF40596; AAF40596; NMB0137. DR GeneID; 902245; -. DR KEGG; nme:NMB0137; -. DR PATRIC; 20355295; VBINeiMen85645_0177. DR eggNOG; ENOG4108UHY; Bacteria. DR eggNOG; COG0049; LUCA. DR HOGENOM; HOG000039067; -. DR KO; K02992; -. DR OMA; EVHRMAD; -. DR OrthoDB; EOG6P5ZKW; -. DR BioCyc; NMEN122586:GHGG-147-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.455.10; -; 1. DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1. DR InterPro; IPR000235; Ribosomal_S5/S7. DR InterPro; IPR005717; Ribosomal_S7_bac/org-type. DR InterPro; IPR020606; Ribosomal_S7_CS. DR InterPro; IPR023798; Ribosomal_S7_dom. DR PANTHER; PTHR11205; PTHR11205; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; SSF47973; 1. DR TIGRFAMs; TIGR01029; rpsG_bact; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 156 30S ribosomal protein S7. FT /FTId=PRO_0000124308. SQ SEQUENCE 156 AA; 17657 MW; 7D8A802971BCC53F CRC64; MPRRREVPKR DVLPDPKFGS VELTKFMNVL MIDGKKSVAE RIVYGALEQI EKKTGKVAIE VFNEAIANAK PIVEVKSRRV GGANYQVPVE VRPSRRLALA MRWVRDAARK RGEKSMDLRL AGELIDASEG RGGALKKREE VHRMAEANKA FSHFRF // ID RSMJ_NEIMB Reviewed; 250 AA. AC Q9JYF4; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523}; DE EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523}; DE AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523}; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523}; GN Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; GN OrderedLocusNames=NMB1608; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the guanosine in position 1516 CC of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(1516) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1516) in 16S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ CC family. {ECO:0000255|HAMAP-Rule:MF_01523}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41960.1; -; Genomic_DNA. DR PIR; F81062; F81062. DR RefSeq; NP_274614.1; NC_003112.2. DR RefSeq; WP_002225014.1; NC_003112.2. DR ProteinModelPortal; Q9JYF4; -. DR SMR; Q9JYF4; 2-250. DR STRING; 122586.NMB1608; -. DR PaxDb; Q9JYF4; -. DR DNASU; 904305; -. DR EnsemblBacteria; AAF41960; AAF41960; NMB1608. DR GeneID; 904305; -. DR KEGG; nme:NMB1608; -. DR PATRIC; 20359096; VBINeiMen85645_2060. DR eggNOG; ENOG4105FFN; Bacteria. DR eggNOG; ENOG410XPRJ; LUCA. DR HOGENOM; HOG000218236; -. DR KO; K15984; -. DR OMA; SSRYDIY; -. DR OrthoDB; EOG657J92; -. DR BioCyc; NMEN122586:GHGG-1656-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01523; 16SrRNA_methyltr_J; 1. DR InterPro; IPR007536; 16SrRNA_methylTrfase_J. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04445; SAM_MT; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 250 Ribosomal RNA small subunit FT methyltransferase J. FT /FTId=PRO_0000212079. FT REGION 96 97 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01523}. FT BINDING 168 168 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01523}. SQ SEQUENCE 250 AA; 27286 MW; 8212639CE4838C3E CRC64; MTDILIDNTA TETVRTLIRA FPLVPVSQPP EQGSYLLAEH DTVSLRLVGE KSSVIVDFAS GAAQYRRTKG GGELIAKAVN HTAHPTVWDA TAGLGRDSFV LASLGLAVTA FEQHPAVACL LSDGIRRALL NPETQNTAAH INLHFGNAAE QMPALVQTQG KPDIVYLDPM YPERRKSAAV KKEMTYFHRL VGEAQDEAAL LHTARQTAKK RVVVKRPRLG EHLAGQDPAY QYTGKSTRFD VYLPYGTDKG // ID RUVC_NEIMB Reviewed; 178 AA. AC Q9JYV1; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034}; DE EC=3.1.22.4 {ECO:0000255|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction nuclease RuvC {ECO:0000255|HAMAP-Rule:MF_00034}; DE AltName: Full=Holliday junction resolvase RuvC {ECO:0000255|HAMAP-Rule:MF_00034}; GN Name=ruvC {ECO:0000255|HAMAP-Rule:MF_00034}; GN OrderedLocusNames=NMB1419; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Nuclease that resolves Holliday junction intermediates CC in genetic recombination. Cleaves the cruciform structure in CC supercoiled DNA by nicking to strands with the same polarity at CC sites symmetrically opposed at the junction in the homologous arms CC and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl CC group. {ECO:0000255|HAMAP-Rule:MF_00034}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at a junction such as CC a reciprocal single-stranded crossover between two homologous DNA CC duplexes (Holliday junction). {ECO:0000255|HAMAP-Rule:MF_00034}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00034}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00034}; CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000255|HAMAP- CC Rule:MF_00034}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41780.1; -; Genomic_DNA. DR PIR; E81085; E81085. DR RefSeq; NP_274431.1; NC_003112.2. DR RefSeq; WP_002222304.1; NC_003112.2. DR ProteinModelPortal; Q9JYV1; -. DR SMR; Q9JYV1; 6-158. DR STRING; 122586.NMB1419; -. DR PaxDb; Q9JYV1; -. DR EnsemblBacteria; AAF41780; AAF41780; NMB1419. DR GeneID; 903841; -. DR KEGG; nme:NMB1419; -. DR PATRIC; 20358525; VBINeiMen85645_1774. DR eggNOG; ENOG4105NHU; Bacteria. DR eggNOG; COG0817; LUCA. DR HOGENOM; HOG000012181; -. DR KO; K01159; -. DR OMA; ILHMIKL; -. DR OrthoDB; EOG6RG044; -. DR BioCyc; NMEN122586:GHGG-1457-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00034; RuvC; 1. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR020563; X-over_junc_endoDNase_Mg_BS. DR InterPro; IPR002176; X-over_junc_endoDNase_RuvC. DR Pfam; PF02075; RuvC; 1. DR PRINTS; PR00696; RSOLVASERUVC. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00228; ruvC; 1. DR PROSITE; PS01321; RUVC; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 178 Crossover junction endodeoxyribonuclease FT RuvC. FT /FTId=PRO_0000183113. FT METAL 11 11 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00034}. FT METAL 71 71 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00034}. FT METAL 143 143 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00034}. FT METAL 146 146 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00034}. SQ SEQUENCE 178 AA; 18675 MW; 1A21D86BAC8D3F48 CRC64; MAASVRILGI DPGSRVTGFG VIDVRGRDHF YVASGCIKTP ADAPLADRIA VIVRHIGEVV TVYKPQQAAV EQVFVNVNPA STLMLGQARG AALAALVSHK LPVSEYTALQ VKQAVVGKGK AAKEQVQHMV VQMLGLSGTP QPDAADGLAV ALTHALRNHG LAAKLNPSGM QVKRGRFQ // ID RS9_NEIMB Reviewed; 130 AA. AC P66642; Q9JQZ9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=30S ribosomal protein S9 {ECO:0000255|HAMAP-Rule:MF_00532}; GN Name=rpsI {ECO:0000255|HAMAP-Rule:MF_00532}; GN OrderedLocusNames=NMB2056; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein S9P family. CC {ECO:0000255|HAMAP-Rule:MF_00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42376.1; -; Genomic_DNA. DR PIR; A81012; A81012. DR RefSeq; NP_275046.1; NC_003112.2. DR RefSeq; WP_002215008.1; NC_003112.2. DR ProteinModelPortal; P66642; -. DR SMR; P66642; 6-130. DR STRING; 122586.NMB2056; -. DR PaxDb; P66642; -. DR PRIDE; P66642; -. DR EnsemblBacteria; AAF42376; AAF42376; NMB2056. DR GeneID; 904024; -. DR KEGG; nme:NMB2056; -. DR PATRIC; 20360268; VBINeiMen85645_2634. DR eggNOG; ENOG4108UJD; Bacteria. DR eggNOG; COG0103; LUCA. DR HOGENOM; HOG000019802; -. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR BioCyc; NMEN122586:GHGG-2119-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000754; Ribosomal_S9. DR InterPro; IPR023035; Ribosomal_S9_bac/plastid. DR InterPro; IPR020574; Ribosomal_S9_CS. DR PANTHER; PTHR21569; PTHR21569; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 130 30S ribosomal protein S9. FT /FTId=PRO_0000111382. SQ SEQUENCE 130 AA; 14426 MW; 8DAEA439DBC491E1 CRC64; MNGKYYYGTG RRKSSVARVF LIKGTGQIIV NGRPVDEFFA RETSRMVVRQ PLVLTENAES FDIKVNVVGG GETGQSGAIR HGITRALIDF DAALKPALSQ AGFVTRDARE VERKKPGLRK ARRAKQFSKR // ID RUVA_NEIMB Reviewed; 194 AA. AC Q9K1A2; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031}; GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; GN OrderedLocusNames=NMB0265; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures CC cruciform structure in supercoiled DNA with palindromic sequence, CC indicating that it may promote strand exchange reactions in CC homologous recombination. RuvAB is a helicase that mediates the CC Holliday junction migration by localized denaturation and CC reannealing. RuvA stimulates, in the presence of DNA, the weak CC ATPase activity of RuvB. {ECO:0000255|HAMAP-Rule:MF_00031}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00031}. CC -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000255|HAMAP- CC Rule:MF_00031}. CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP- CC Rule:MF_00031}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40719.1; -; Genomic_DNA. DR PIR; B81218; B81218. DR RefSeq; NP_273321.1; NC_003112.2. DR RefSeq; WP_002223336.1; NC_003112.2. DR ProteinModelPortal; Q9K1A2; -. DR STRING; 122586.NMB0265; -. DR PaxDb; Q9K1A2; -. DR EnsemblBacteria; AAF40719; AAF40719; NMB0265. DR GeneID; 902376; -. DR KEGG; nme:NMB0265; -. DR PATRIC; 20355612; VBINeiMen85645_0330. DR eggNOG; ENOG4105KA4; Bacteria. DR eggNOG; COG0632; LUCA. DR HOGENOM; HOG000057116; -. DR KO; K03550; -. DR OMA; VGYQVHC; -. DR OrthoDB; EOG679THG; -. DR BioCyc; NMEN122586:GHGG-280-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00031; DNA_helic_RuvA; 1. DR InterPro; IPR011114; DNA_helicas_Holl-junc_RuvA_C. DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000085; RuvA. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF07499; RuvA_C; 1. DR Pfam; PF01330; RuvA_N; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF46929; SSF46929; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00084; ruvA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 194 Holliday junction ATP-dependent DNA FT helicase RuvA. FT /FTId=PRO_0000094656. SQ SEQUENCE 194 AA; 20688 MW; AA16321D725AD933 CRC64; MISRLTGKLV EKNPPQIVID VNGVGYEADV SMQTFYNLPP VGESVQLFTQ LIIREDAHLL FGFATAEERK TFRQLIKVGG IGAKTALGIL SAMTADELAR AVAEEDVKRL SSAPGIGKKT AERMVLELRG KLVAHTVTDG LFAAAPAADE TEDIVSTLLA LGYSEREAKA AVKGVPEGTD VGEGVRLALK NLLK // ID RSMA_NEIMB Reviewed; 259 AA. AC Q9K0B7; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607}; DE EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607}; GN OrderedLocusNames=NMB0697; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 CC and A1519) in the loop of a conserved hairpin near the 3'-end of CC 16S rRNA in the 30S particle. May play a critical role in CC biogenesis of 30S subunits. {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- CATALYTIC ACTIVITY: 4 S-adenosyl-L-methionine + CC adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L- CC homocysteine + N(6)-dimethyladenine(1518)/N(6)- CC dimethyladenine(1519) in 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00607}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. rRNA adenine N(6)-methyltransferase CC family. RsmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41114.1; -; Genomic_DNA. DR PIR; H81168; H81168. DR RefSeq; NP_273739.1; NC_003112.2. DR RefSeq; WP_002225484.1; NC_003112.2. DR ProteinModelPortal; Q9K0B7; -. DR STRING; 122586.NMB0697; -. DR PaxDb; Q9K0B7; -. DR EnsemblBacteria; AAF41114; AAF41114; NMB0697. DR GeneID; 902809; -. DR KEGG; nme:NMB0697; -. DR PATRIC; 20356725; VBINeiMen85645_0884. DR eggNOG; ENOG4105D1X; Bacteria. DR eggNOG; COG0030; LUCA. DR HOGENOM; HOG000227962; -. DR KO; K02528; -. DR OMA; HYPGRLE; -. DR OrthoDB; EOG66F08Z; -. DR BioCyc; NMEN122586:GHGG-725-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro. DR Gene3D; 1.10.8.100; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11727; PTHR11727; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00755; ksgA; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 259 Ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101572. FT BINDING 13 13 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 15 15 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 40 40 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 61 61 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 85 85 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 103 103 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. SQ SEQUENCE 259 AA; 29216 MW; 08B2DA47C1A0884E CRC64; MKEHKARKRF GQNFLQDTRI ISDIVNAVRP QADDVVIEIG PGLAAITEPL AKKLNRLHVV EIDRDIVCRL KTLPFADKLV IHEGDVLQFD FNGIAGKKKI VGNLPYNIST PLLFKLAEVA DDVVDMHFML QKEVVERMVA APKSNDYGRL GVMLQYFFDM EMLIDVPPES FDPAPKVDSA VVRMIPVKHR IGKADDFEHF AKLVKLAFHQ RRKTIRNNLK ELAGDDDLQA VGINPQDRAE HIAPEKYVAL SNYLAGKVV // ID RSMG_NEIMB Reviewed; 207 AA. AC Q9K1G3; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074}; DE EC=2.1.1.170 {ECO:0000255|HAMAP-Rule:MF_00074}; DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; GN OrderedLocusNames=NMB0190; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the N7 position of guanine in CC position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(527) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(527) in 16S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40647.1; -; Genomic_DNA. DR PIR; C81227; C81227. DR RefSeq; NP_273248.1; NC_003112.2. DR RefSeq; WP_002226919.1; NC_003112.2. DR ProteinModelPortal; Q9K1G3; -. DR STRING; 122586.NMB0190; -. DR PaxDb; Q9K1G3; -. DR EnsemblBacteria; AAF40647; AAF40647; NMB0190. DR GeneID; 902298; -. DR KEGG; nme:NMB0190; -. DR PATRIC; 20355407; VBINeiMen85645_0232. DR eggNOG; ENOG4105D28; Bacteria. DR eggNOG; COG0357; LUCA. DR HOGENOM; HOG000221012; -. DR KO; K03501; -. DR OMA; NTRWLAM; -. DR OrthoDB; EOG6HF639; -. DR BioCyc; NMEN122586:GHGG-201-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1. DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02527; GidB; 1. DR PIRSF; PIRSF003078; GidB; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00138; rsmG_gidB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 207 Ribosomal RNA small subunit FT methyltransferase G. FT /FTId=PRO_0000184293. FT REGION 127 128 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00074}. FT BINDING 76 76 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 81 81 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 141 141 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00074}. SQ SEQUENCE 207 AA; 22920 MW; 6BD896134132E4B2 CRC64; MERKERLRAG IAAMGLDISE TAQDRLLVYV DLLKKWNKTY NLTALRDEEK MIVHHLLDSL TLLPHIEGVQ TMLDVGSGGG QPGIPAAVCR PDVQITLLDA NTKKTAFLQQ AVIELGLDNV RVVSGRVEAV SDVRADVVTS RAFAELADFV SWTVHLLKDG GYWAAMKGVY PQEEIGRLPQ DVCVEKVQRL DVPGLDAERH IVILSKR // ID RUVB_NEIMB Reviewed; 343 AA. AC Q9JZ86; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016}; GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; GN OrderedLocusNames=NMB1243; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures CC cruciform structure in supercoiled DNA with palindromic sequence, CC indicating that it may promote strand exchange reactions in CC homologous recombination. RuvAB is a helicase that mediates the CC Holliday junction migration by localized denaturation and CC reannealing. {ECO:0000255|HAMAP-Rule:MF_00016}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00016}. CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP- CC Rule:MF_00016}. CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP- CC Rule:MF_00016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41624.1; -; Genomic_DNA. DR PIR; H81105; H81105. DR RefSeq; NP_274267.1; NC_003112.2. DR RefSeq; WP_002220958.1; NC_003112.2. DR ProteinModelPortal; Q9JZ86; -. DR SMR; Q9JZ86; 31-341. DR STRING; 122586.NMB1243; -. DR PaxDb; Q9JZ86; -. DR EnsemblBacteria; AAF41624; AAF41624; NMB1243. DR GeneID; 903665; -. DR KEGG; nme:NMB1243; -. DR PATRIC; 20358083; VBINeiMen85645_1554. DR eggNOG; ENOG4105CKJ; Bacteria. DR eggNOG; COG2255; LUCA. DR HOGENOM; HOG000218623; -. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR BioCyc; NMEN122586:GHGG-1280-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00016; DNA_helic_RuvB; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB. DR InterPro; IPR008823; DNA_helicase_Holl-junc_RuvB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008824; RuvB_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF05491; RuvB_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR ProDom; PD005323; DNA_helicase_Holl-junc_RuvB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00635; ruvB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 343 Holliday junction ATP-dependent DNA FT helicase RuvB. FT /FTId=PRO_0000165565. FT NP_BIND 71 78 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. SQ SEQUENCE 343 AA; 37660 MW; CADBD72C77DAEEE4 CRC64; MLQTDNLTAA QPQRIVAAQT ASAQEELLER ALRPKTLDDY IGQDKAKEQL AIFIQAAKKR GEALDHVLLF GPPGLGKTTL AHIIAKELGV NLRQTSGPVL ERAGDLAALL TNLDPHDVLF IDEIHRLSPV VEEILYPALE DYRLDIMIGE GPAARSVKID LPPFTLIGAT TRAGMLTNPL RDRFGIVSRL EFYENRDLTT IVSRSAQLLQ LDMSEEGAEE IAKRSRGTPR IANRLLRRVR DFADVKNNGT IDGGIADAAL SMLDVDAQGL DVMDRKFLEA VLHKFGGGPV GLDNVAAAIG ESTDTIEDVI EPYLIQQGFL QRTPRGRMAT ERAYLHFGLP VEK // ID RSMI_NEIMB Reviewed; 291 AA. AC Q9JXE3; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877}; DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN OrderedLocusNames=NMB2088; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine CC 1402 (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(1402) in CC 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(1402) CC in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI CC family. {ECO:0000255|HAMAP-Rule:MF_01877}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42405.1; -; Genomic_DNA. DR PIR; F81007; F81007. DR RefSeq; NP_275076.1; NC_003112.2. DR RefSeq; WP_002225719.1; NC_003112.2. DR ProteinModelPortal; Q9JXE3; -. DR STRING; 122586.NMB2088; -. DR PaxDb; Q9JXE3; -. DR EnsemblBacteria; AAF42405; AAF42405; NMB2088. DR GeneID; 903963; -. DR KEGG; nme:NMB2088; -. DR PATRIC; 20360346; VBINeiMen85645_2670. DR eggNOG; ENOG4105CU0; Bacteria. DR eggNOG; COG0313; LUCA. DR HOGENOM; HOG000195941; -. DR KO; K07056; -. DR OMA; IALHDHN; -. DR OrthoDB; EOG6677TH; -. DR BioCyc; NMEN122586:GHGG-2153-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I. DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR00096; TIGR00096; 1. DR PROSITE; PS01296; RSMI; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 291 Ribosomal RNA small subunit FT methyltransferase I. FT /FTId=PRO_0000211949. SQ SEQUENCE 291 AA; 31353 MW; D98782330E05F15C CRC64; MFQKHLQKAS DSVVGGTLYV VATPIGNLAD ITLRALAVLQ KADIICAEDT RVTAQLLSAY GIQGKLVSVR EHNERQMADK IVGYLSDGMV VAQVSDAGTP AVCDPGAKLA RRVREAGFKV VPVVGASAVM AALSVAGVEG SDFYFNGFVP PKSGERRKLF AKWVRAAFPI VMFETPHRIG ATLADMAELF PERRLMLARE ITKTFETFLS GTVGEIQTAL SADGNQSRGE MVLVLYPAQD EKHEGLSESA QNIMKILTAE LPTKQAAELA AKITGEGKKA LYDLALSWKN K // ID SECA_NEIMB Reviewed; 916 AA. AC Q9JYK8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=NMB1536; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. Has a central role CC in coupling the hydrolysis of ATP to the transfer of proteins into CC and across the cell membrane, serving both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across CC the membrane. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382}; CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01382}; CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. CC Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP- CC Rule:MF_01382}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41891.1; -; Genomic_DNA. DR PIR; D81072; D81072. DR RefSeq; NP_274543.1; NC_003112.2. DR RefSeq; WP_002225053.1; NC_003112.2. DR ProteinModelPortal; Q9JYK8; -. DR SMR; Q9JYK8; 9-833. DR STRING; 122586.NMB1536; -. DR PaxDb; Q9JYK8; -. DR EnsemblBacteria; AAF41891; AAF41891; NMB1536. DR GeneID; 904068; -. DR KEGG; nme:NMB1536; -. DR PATRIC; 20358876; VBINeiMen85645_1947. DR eggNOG; ENOG4105CI6; Bacteria. DR eggNOG; COG0653; LUCA. DR HOGENOM; HOG000218168; -. DR KO; K03070; -. DR OMA; IATERHE; -. DR OrthoDB; EOG654P48; -. DR BioCyc; NMEN122586:GHGG-1577-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0017038; P:protein import; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3060.10; -; 1. DR Gene3D; 3.40.50.300; -; 3. DR Gene3D; 3.90.1440.10; -; 1. DR HAMAP; MF_01382; SecA; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004027; SEC_C_motif. DR InterPro; IPR000185; SecA. DR InterPro; IPR020937; SecA_CS. DR InterPro; IPR011115; SecA_DEAD. DR InterPro; IPR014018; SecA_motor_DEAD. DR InterPro; IPR011130; SecA_preprotein_X-link_dom. DR InterPro; IPR011116; SecA_Wing/Scaffold. DR Pfam; PF02810; SEC-C; 1. DR Pfam; PF07517; SecA_DEAD; 1. DR Pfam; PF01043; SecA_PP_bind; 1. DR Pfam; PF07516; SecA_SW; 1. DR PRINTS; PR00906; SECA. DR SMART; SM00957; SecA_DEAD; 1. DR SMART; SM00958; SecA_PP_bind; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 2. DR TIGRFAMs; TIGR00963; secA; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Cytoplasm; Membrane; Metal-binding; Nucleotide-binding; KW Protein transport; Reference proteome; Translocation; Transport; Zinc. FT CHAIN 1 916 Protein translocase subunit SecA. FT /FTId=PRO_0000320863. FT NP_BIND 102 109 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. FT METAL 900 900 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}. FT METAL 902 902 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}. FT METAL 911 911 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}. FT METAL 912 912 Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}. SQ SEQUENCE 916 AA; 103294 MW; 8A37D163E9BC3784 CRC64; MLTNIAKKIF GSRNDRLLKQ YRKSVARINA LEEQMQALSD ADLQAKTAEF KQRLADGQTL DGILPEAFAV CREASRRTLG MRHFDVQLIG GMVLHDGKIA EMRTGEGKTL VATLAVYLNA LAGKGVHVVT VNDYLASRDA GIMEPLYNFL GLTVGVIISD MQPFDRQNAY AADITYGTNN EFGFDYLRDN MVTDQYDKVQ RELNFAVVDE VDSILIDEAR TPLIISGQAD DNIQLYQIMN TVPPHLVRQE TEEGEGDYWV DEKAHQVILS EAGHEHAEQI LTQMGLLAEN DSLYSAANIA LMHHLMAALR AHSLFHKDQH YVIQDGEIVI VDEFTGRLMS GRRWSEGLHQ AVEAKEGVEI KRENQTLASI TFQNYFRLYT KLSGMTGTAD TEAFEFQSIY NLETVIIPTN RPVQRKDFND QIFRSAEEKF EAVVKDIEEC HKRGQPVLVG TTSIENSELV SKLLTQAGLP HNVLNAKEHE REALIVAQAG KVGAITVATN MAGRGTDIVL GGNLKHQTDA IRADETLSDE EKQAQIAALE DGWQAEHDKV MEAGGLHIIG TERHESRRID NQLRGRSGRQ GDPGSSRFYL SFEDPLLRLF ALDRAAAILN RLAPERGVAI EHNLLTRQIE GAQRKVEGRN FDMRKQVLEY DDVANEQRKV IYSQRNEILT SKDISDLMQE IRSDVVSDLV DTYMPPDSME EQWDIPTLEN RLAAEFRLHE DIQSWLKADN AIDGQDIKER LIERIENEYA AKTELVGKQA MADFERNVML QVIDNQWREH LAAMDYLRQG IHLRSYAQKN PKQEYKREAF TMFQDLWNGI KFHIASLLTS VQIEQNPVAV VEEQPIGNIQ SIHSESPDME ELLGQSQTDL VTEAFNPDGT DFSPEALEAR GQIVHRNDPC PCGSGLKYKQ CHGKLA // ID SIAA_NEIMB Reviewed; 377 AA. AC H2VFI5; DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 1. DT 20-JAN-2016, entry version 23. DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase; DE EC=3.2.1.183; GN Name=siaA; Synonyms=synX; OrderedLocusNames=NMB0070; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP AND MUTAGENESIS OF ASP-100; GLU-122 AND ASP-131. RC STRAIN=MC58; RX PubMed=15518580; DOI=10.1021/bi048606d; RA Murkin A.S., Chou W.K., Wakarchuk W.W., Tanner M.E.; RT "Identification and mechanism of a bacterial hydrolyzing UDP-N- RT acetylglucosamine 2-epimerase."; RL Biochemistry 43:14290-14298(2004). CC -!- FUNCTION: Catalyzes the conversion of UDP-N-acetylglucosamine CC (UDP-GlcNAc) to UDP and N-acetyl-D-mannosamine (ManNAc). CC {ECO:0000269|PubMed:15518580}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + H(2)O = N- CC acetyl-D-mannosamine + UDP. {ECO:0000269|PubMed:15518580}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.49 mM for UDP-N-acetyl-alpha-D-glucosamine CC {ECO:0000269|PubMed:15518580}; CC Note=kcat is 4.7 sec(-1).; CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15518580}. CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40537.1; -; Genomic_DNA. DR PIR; A53384; A53384. DR PIR; S60758; S60758. DR RefSeq; NP_273134.1; NC_003112.2. DR RefSeq; WP_002226892.1; NC_003112.2. DR ProteinModelPortal; H2VFI5; -. DR STRING; 122586.NMB0070; -. DR PaxDb; H2VFI5; -. DR EnsemblBacteria; AAF40537; AAF40537; NMB0070. DR GeneID; 902176; -. DR KEGG; nme:NMB0070; -. DR eggNOG; ENOG4107SE4; Bacteria. DR eggNOG; COG0381; LUCA. DR KO; K08068; -. DR OMA; CKEVTRE; -. DR OrthoDB; EOG6K13T4; -. DR BioCyc; NMEN122586:GHGG-76-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro. DR InterPro; IPR020004; UDP-GlcNAc_Epase. DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom. DR Pfam; PF02350; Epimerase_2; 1. DR TIGRFAMs; TIGR03568; NeuC_NnaA; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Isomerase; Reference proteome. FT CHAIN 1 377 UDP-N-acetylglucosamine 2-epimerase. FT /FTId=PRO_0000421996. FT ACT_SITE 212 212 {ECO:0000250}. FT MUTAGEN 100 100 D->N: Strongly decreased activity. FT {ECO:0000269|PubMed:15518580}. FT MUTAGEN 122 122 E->Q: Strongly decreased activity. FT {ECO:0000269|PubMed:15518580}. FT MUTAGEN 131 131 D->Q: Strongly decreased activity. FT {ECO:0000269|PubMed:15518580}. SQ SEQUENCE 377 AA; 42308 MW; D4289B3FA04EBB2B CRC64; MKRILCITGT RADFGKLKPL LAYIENHPDL ELHLIVTGMH MMKTYGRTYK EVTRENYQHT YLFSNQIQGE PMGAVLGNTI TFISRLSDEI EPDMVMIHGD RLEALAGAAV GALSSRLVCH IEGGELSGTV DDSIRHSISK LSHIHLVANE QAVTRLVQMG EKRKHIHIIG SPDLDVMASS TLPSLEEVKE YYGLPYENYG ISMFHPVTTE AHLMPQYAAQ YFKALELSGQ NIISIYPNND TGTESILQEL LKYQSDKFIA FPSIRFEYFL VLLKHAKFMV GNSSAGIREA PLYGVPSIDV GTRQSNRHMG KSIIHTDYET KNIFDAIQQA CSLGKFEADD TFNGGDTRTS TERFAEVINN PETWNVSAQK RFIDLNL // ID SECB_NEIMB Reviewed; 147 AA. AC Q9JY16; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821}; GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; GN OrderedLocusNames=NMB1789; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: One of the proteins required for the normal export of CC preproteins out of the cell cytoplasm. It is a molecular chaperone CC that binds to a subset of precursor proteins, maintaining them in CC a translocation-competent state. It also specifically binds to its CC receptor SecA. {ECO:0000255|HAMAP-Rule:MF_00821}. CC -!- SUBUNIT: Homotetramer, a dimer of dimers. One homotetramer CC interacts with 1 SecA dimer. {ECO:0000255|HAMAP-Rule:MF_00821}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00821}. CC -!- SIMILARITY: Belongs to the SecB family. {ECO:0000255|HAMAP- CC Rule:MF_00821}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42128.1; -; Genomic_DNA. DR PIR; D81041; D81041. DR RefSeq; NP_274788.1; NC_003112.2. DR RefSeq; WP_002225639.1; NC_003112.2. DR ProteinModelPortal; Q9JY16; -. DR STRING; 122586.NMB1789; -. DR PaxDb; Q9JY16; -. DR PRIDE; Q9JY16; -. DR EnsemblBacteria; AAF42128; AAF42128; NMB1789. DR GeneID; 903310; -. DR KEGG; nme:NMB1789; -. DR PATRIC; 20359543; VBINeiMen85645_2277. DR eggNOG; ENOG4105IX2; Bacteria. DR eggNOG; COG1952; LUCA. DR HOGENOM; HOG000218192; -. DR KO; K03071; -. DR OMA; CPNVLFP; -. DR OrthoDB; EOG6DVJZZ; -. DR BioCyc; NMEN122586:GHGG-1844-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.420.10; -; 1. DR HAMAP; MF_00821; SecB; 1. DR InterPro; IPR003708; SecB. DR Pfam; PF02556; SecB; 1. DR PRINTS; PR01594; SECBCHAPRONE. DR SUPFAM; SSF54611; SSF54611; 1. DR TIGRFAMs; TIGR00809; secB; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Protein transport; KW Reference proteome; Translocation; Transport. FT CHAIN 1 147 Protein-export protein SecB. FT /FTId=PRO_0000055388. SQ SEQUENCE 147 AA; 16319 MW; 835046016E5CE588 CRC64; MSEELQPVFS IERLYVKDLS LEVPHAPQIF LEQGEPEVEM RVSTGSQKLE DGYYNVDVTV TVTAKLDNER TMFLNEVTQS GIFRLENIPE EDADLLLGVA CPNILFPYAR EAVSGTVTRA GFPPVLLAPI NFEAIYQQQQ EAEAAGA // ID SERC_NEIMB Reviewed; 368 AA. AC P57007; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160}; DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160}; GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; GN OrderedLocusNames=NMB1640; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the reversible conversion of 3- CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- CC phosphonooxybutanoate to phosphohydroxythreonine. CC {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3- CC phosphonooxypyruvate + L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00160}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 2/3. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41989.1; -; Genomic_DNA. DR PIR; H81059; H81059. DR RefSeq; NP_274645.1; NC_003112.2. DR RefSeq; WP_002244251.1; NC_003112.2. DR ProteinModelPortal; P57007; -. DR STRING; 122586.NMB1640; -. DR PaxDb; P57007; -. DR EnsemblBacteria; AAF41989; AAF41989; NMB1640. DR GeneID; 903939; -. DR KEGG; nme:NMB1640; -. DR PATRIC; 20359198; VBINeiMen85645_2111. DR eggNOG; ENOG4105DXJ; Bacteria. DR eggNOG; COG1932; LUCA. DR HOGENOM; HOG000088965; -. DR KO; K00831; -. DR OMA; GAQKNMG; -. DR OrthoDB; EOG60CWP3; -. DR BioCyc; NMEN122586:GHGG-1689-MONOMER; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00160; SerC_aminotrans_5; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR022278; Pser_aminoTfrase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01364; serC_1; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis; KW Reference proteome; Serine biosynthesis; Transferase. FT CHAIN 1 368 Phosphoserine aminotransferase. FT /FTId=PRO_0000150192. FT REGION 78 79 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00160}. FT REGION 244 245 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00160}. FT BINDING 44 44 L-glutamate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 104 104 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 157 157 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 179 179 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 202 202 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT MOD_RES 203 203 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00160}. SQ SEQUENCE 368 AA; 41393 MW; 97DFCE52BBE5E021 CRC64; MSLYPIYNFS AGPAVLPEAV LETARQEMLD YNGTGFPVMA MSHRSEMFLS ILHHAEQDLR QLLKVPDNYK ILFLQGGATT QFNMAAMNLA HGFRTADAVV TGNWSRIAYE QMSRLTDTEI RLAAHGGEQF DYLDLPPVET WDVAPDSAFV HFAVNETVNG LQYREVPCLS EGMPPLVCDM SSEILSREFD VADYGLIYAG AQKNIGPAGV TVVIVREDLL ERCPNDIPDV FNYRSHINRD GMYNTPSTYA IYMSGLVFRW LQAQGGVKKI EAVNRLKAQT LYETIDGSDG FYINRIRPNA RSKMNVVFQT GDEELDRRFV LEAELQGLCL LKGYKTVGGM RASIYNAMPL EGVRALADFM RDFQRRYG // ID SLYX_NEIMB Reviewed; 74 AA. AC Q9JXG3; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Protein SlyX homolog {ECO:0000255|HAMAP-Rule:MF_00715}; GN Name=slyX {ECO:0000255|HAMAP-Rule:MF_00715}; GN OrderedLocusNames=NMB2063; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the SlyX family. {ECO:0000255|HAMAP- CC Rule:MF_00715}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42382.1; -; Genomic_DNA. DR PIR; C81010; C81010. DR RefSeq; NP_275053.1; NC_003112.2. DR RefSeq; WP_002219958.1; NC_003112.2. DR STRING; 122586.NMB2063; -. DR PaxDb; Q9JXG3; -. DR EnsemblBacteria; AAF42382; AAF42382; NMB2063. DR GeneID; 904015; -. DR KEGG; nme:NMB2063; -. DR PATRIC; 20360286; VBINeiMen85645_2643. DR eggNOG; COG2900; LUCA. DR HOGENOM; HOG000273046; -. DR KO; K03745; -. DR OMA; EGLECRI; -. DR OrthoDB; EOG6WT8KM; -. DR BioCyc; NMEN122586:GHGG-2126-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_00715; SlyX; 1. DR InterPro; IPR007236; SlyX. DR Pfam; PF04102; SlyX; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 74 Protein SlyX homolog. FT /FTId=PRO_0000209205. SQ SEQUENCE 74 AA; 8649 MW; 69A6CFFD4A724F5A CRC64; MDAVQELERR IVELEIQSAL QEDVIAGLNA MVAELRQTLD LQQAQLRLLY QKMQDRNPDA QEPYSLRDEI PPHY // ID SPEE_NEIMB Reviewed; 263 AA. AC P60594; Q9JQL8; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198}; DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198}; DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198}; DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198}; GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; GN OrderedLocusNames=NMB0869; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine CC group from the amino donor S-adenosylmethioninamine (decarboxy- CC AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine CC biosynthesis; spermidine from putrescine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP- CC Rule:MF_00198}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41280.1; -; Genomic_DNA. DR RefSeq; NP_273910.1; NC_003112.2. DR RefSeq; WP_002225376.1; NC_003112.2. DR ProteinModelPortal; P60594; -. DR STRING; 122586.NMB0869; -. DR PaxDb; P60594; -. DR EnsemblBacteria; AAF41280; AAF41280; NMB0869. DR GeneID; 902983; -. DR KEGG; nme:NMB0869; -. DR PATRIC; 20357127; VBINeiMen85645_1082. DR eggNOG; ENOG4105I7M; Bacteria. DR eggNOG; COG0421; LUCA. DR HOGENOM; HOG000263005; -. DR KO; K00797; -. DR OMA; YHRHYWE; -. DR OrthoDB; EOG6ZPT03; -. DR BioCyc; NMEN122586:GHGG-900-MONOMER; -. DR UniPathway; UPA00248; UER00314. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00198; Spermidine_synth; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001045; Spermi_synthase. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51006; PABS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Polyamine biosynthesis; KW Reference proteome; Spermidine biosynthesis; Transferase. FT CHAIN 1 263 Polyamine aminopropyltransferase. FT /FTId=PRO_0000156490. FT DOMAIN 1 221 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}. FT REGION 37 38 Polyamine binding. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT REGION 126 127 S-adenosylmethioninamine binding. FT {ECO:0000255|HAMAP-Rule:MF_00198}. FT ACT_SITE 144 144 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 98 98 S-adenosylmethioninamine. FT {ECO:0000255|HAMAP-Rule:MF_00198}. SQ SEQUENCE 263 AA; 29734 MW; FDCB5F0F72BAE472 CRC64; MARHPYRRLR PAKSGFPEVG ISEEGNIRSL HLGSDTVQSS MNLDHPSELV LSYSRAMMGW LLFTDALPQH ITQIGLGGGS FARWIDTYLP DTRQTAVDIN PQVIAIARNL FELPFEGEKF EIIEADGAEY IKVFRHNTDV ILVDGFDGEQ IIDALVEEPF FRDCRNALSS DGIFVTNWWS GDKRYQRFIE RLLSVFEGRV LELPAESHGN VAVMAFQSSP KEQNIDKLKK RADKLSNAYG LDFHRMLAGL KASNPNNGKH FHL // ID SPEA_NEIMB Reviewed; 630 AA. AC Q9K0U3; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417}; DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417}; DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417}; GN Name=speA {ECO:0000255|HAMAP-Rule:MF_01417}; GN OrderedLocusNames=NMB0468; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. CC {ECO:0000255|HAMAP-Rule:MF_01417}. CC -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01417}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417}; CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; CC agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01417}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40905.1; -; Genomic_DNA. DR PIR; A81196; A81196. DR RefSeq; NP_273515.1; NC_003112.2. DR RefSeq; WP_002224949.1; NC_003112.2. DR ProteinModelPortal; Q9K0U3; -. DR STRING; 122586.NMB0468; -. DR PaxDb; Q9K0U3; -. DR EnsemblBacteria; AAF40905; AAF40905; NMB0468. DR GeneID; 902584; -. DR KEGG; nme:NMB0468; -. DR PATRIC; 20356184; VBINeiMen85645_0613. DR eggNOG; ENOG4105DP5; Bacteria. DR eggNOG; COG1166; LUCA. DR HOGENOM; HOG000029191; -. DR KO; K01585; -. DR OMA; DQLFPIM; -. DR OrthoDB; EOG676Z0R; -. DR BioCyc; NMEN122586:GHGG-492-MONOMER; -. DR UniPathway; UPA00186; UER00284. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.37.10; -; 2. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_01417; SpeA; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR002985; Arg_decrbxlase. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR PANTHER; PTHR11482:SF36; PTHR11482:SF36; 2. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PIRSF; PIRSF001336; Arg_decrbxlase; 1. DR PRINTS; PR01180; ARGDCRBXLASE. DR PRINTS; PR01179; ODADCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR01273; speA; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding; KW Polyamine biosynthesis; Putrescine biosynthesis; Pyridoxal phosphate; KW Reference proteome; Spermidine biosynthesis. FT CHAIN 1 630 Biosynthetic arginine decarboxylase. FT /FTId=PRO_0000149965. FT REGION 279 289 Substrate-binding. {ECO:0000255|HAMAP- FT Rule:MF_01417}. FT MOD_RES 99 99 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01417}. SQ SEQUENCE 630 AA; 70902 MW; CB8A9ACBC61EDE02 CRC64; MPILTIREVC NINHWGIGYY DVDDSGEIIV RPNPSQHNQT VSLQKLTEAV QQKHQARLPV LFCFPQILEH RLRDINRAFQ TAREECGYKG GYCLVYPIKV NQHRRVIESL MSSGQPHGLE AGSKAELMAV LAHAGNRQTL IVCNGYKDRE YIRFALMGEK LGHQVYLVIE KLSEIQMVLE EAEKLGIKPR LGVRARLASQ GSGKWQSSGG EKSKFGLSAS QVLQLVDILK QKNRLDCLQL LHFHLGSQLG NIRDVATGVH ESARFYVELH KLGVNIRCFD VGGGLGVDYE GNRTQSDCSV NYSLNEYAAT VVWGISQACL EHGLPHPTII TESGRGITAH HAVLVANVIG VERYKPRRLD APSPEAPRVL HSMWETWTDI SASREKRSLR SWIHEGQFDL ADVHNQYNVG LLSLAQRAWA EQLYLNICHE VGELFNEKHR SHRTIIDELQ ERFADKLYVN FSLFQSLPDA WGIDQLFPVC PITGLNEPIA RRAVLLDITC DSDGTIDHYI DGDGIAGTMP MPDYPEEEPP LLGFFMVGAY QEILGNMHNL FGDTATADVV VGEDGQFTVI DYDEGNTVAD MLEYVYQDPK ELMKRYREQI EHSDLPASQA MSFLKELEAG LNGYTYLEDE // ID SODC_NEIMB Reviewed; 186 AA. AC Q59623; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 11-NOV-2015, entry version 117. DE RecName: Full=Superoxide dismutase [Cu-Zn]; DE EC=1.15.1.1; DE Flags: Precursor; GN Name=sodC; OrderedLocusNames=NMB1398; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=9423860; RA Wilks K.E., Dunn K.L., Farrant J.L., Reddin K.M., Gorringe A.R., RA Langford P.R., Kroll J.S.; RT "Periplasmic superoxide dismutase in meningococcal pathogenicity."; RL Infect. Immun. 66:213-217(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-173. RC STRAIN=MC58; RX PubMed=7496539; RA Kroll J.S., Langford P.R., Wilks K.E., Keil A.D.; RT "Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct RT from the eukaryotic enzyme, and not so rare after all!"; RL Microbiology 141:2271-2279(1995). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001313; CAA04674.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41762.1; -; Genomic_DNA. DR EMBL; X83126; CAA58207.1; -; Genomic_DNA. DR PIR; F81088; F81088. DR RefSeq; NP_274412.1; NC_003112.2. DR RefSeq; WP_002216968.1; NC_003112.2. DR PDB; 2AQR; X-ray; 1.75 A; A/B/C=23-186. DR PDB; 2AQS; X-ray; 1.70 A; A/B=23-186. DR PDBsum; 2AQR; -. DR PDBsum; 2AQS; -. DR ProteinModelPortal; Q59623; -. DR SMR; Q59623; 32-186. DR STRING; 122586.NMB1398; -. DR PaxDb; Q59623; -. DR EnsemblBacteria; AAF41762; AAF41762; NMB1398. DR GeneID; 903820; -. DR KEGG; nme:NMB1398; -. DR PATRIC; 20358483; VBINeiMen85645_1753. DR eggNOG; ENOG4108Z7T; Bacteria. DR eggNOG; COG2032; LUCA. DR HOGENOM; HOG000263449; -. DR KO; K04565; -. DR OMA; GARYACG; -. DR OrthoDB; EOG6K13RS; -. DR BioCyc; NMEN122586:GHGG-1436-MONOMER; -. DR EvolutionaryTrace; Q59623; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR Gene3D; 2.60.40.200; -; 1. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003; PTHR10003; 1. DR Pfam; PF00080; Sod_Cu; 1. DR SUPFAM; SSF49329; SSF49329; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Complete proteome; Copper; Disulfide bond; KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal; KW Zinc. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 186 Superoxide dismutase [Cu-Zn]. FT /FTId=PRO_0000032834. FT METAL 79 79 Copper; catalytic. {ECO:0000250}. FT METAL 81 81 Copper; catalytic. {ECO:0000250}. FT METAL 104 104 Copper; catalytic. {ECO:0000250}. FT METAL 104 104 Zinc; structural. {ECO:0000250}. FT METAL 113 113 Zinc; structural. {ECO:0000250}. FT METAL 122 122 Zinc; structural. {ECO:0000250}. FT METAL 125 125 Zinc; structural. {ECO:0000250}. FT METAL 160 160 Copper; catalytic. {ECO:0000250}. FT DISULFID 86 182 {ECO:0000250}. FT STRAND 30 40 {ECO:0000244|PDB:2AQS}. FT TURN 43 45 {ECO:0000244|PDB:2AQS}. FT STRAND 48 58 {ECO:0000244|PDB:2AQS}. FT STRAND 61 68 {ECO:0000244|PDB:2AQS}. FT STRAND 73 76 {ECO:0000244|PDB:2AQS}. FT STRAND 78 84 {ECO:0000244|PDB:2AQS}. FT STRAND 89 91 {ECO:0000244|PDB:2AQS}. FT STRAND 94 96 {ECO:0000244|PDB:2AQS}. FT HELIX 99 101 {ECO:0000244|PDB:2AQS}. FT STRAND 129 131 {ECO:0000244|PDB:2AQS}. FT STRAND 141 143 {ECO:0000244|PDB:2AQS}. FT HELIX 149 152 {ECO:0000244|PDB:2AQS}. FT STRAND 155 162 {ECO:0000244|PDB:2AQS}. FT STRAND 166 171 {ECO:0000244|PDB:2AQS}. FT HELIX 172 175 {ECO:0000244|PDB:2AQS}. FT STRAND 178 185 {ECO:0000244|PDB:2AQS}. SQ SEQUENCE 186 AA; 19520 MW; 6499049BFAC3427C CRC64; MNMKTLLALA VSAVCSVGVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV GTVTITESNY GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG AGGHWDPKGA KQHGYPWQDD AHLGDLPALT VLHDGTATNP VLAPRLKHLD DVRGHSIMIH TGGDNHSDHP APLGGGGPRM ACGVIK // ID SMG_NEIMB Reviewed; 153 AA. AC P66821; Q9JR28; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 51. DE RecName: Full=Protein Smg homolog {ECO:0000255|HAMAP-Rule:MF_00598}; GN Name=smg {ECO:0000255|HAMAP-Rule:MF_00598}; OrderedLocusNames=NMB0117; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the Smg family. {ECO:0000255|HAMAP- CC Rule:MF_00598}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40576.1; -; Genomic_DNA. DR PIR; G81236; G81236. DR RefSeq; NP_273175.1; NC_003112.2. DR RefSeq; WP_002215351.1; NC_003112.2. DR STRING; 122586.NMB0117; -. DR PaxDb; P66821; -. DR EnsemblBacteria; AAF40576; AAF40576; NMB0117. DR GeneID; 902221; -. DR KEGG; nme:NMB0117; -. DR PATRIC; 20355247; VBINeiMen85645_0157. DR eggNOG; COG2922; LUCA. DR HOGENOM; HOG000137865; -. DR KO; K03747; -. DR OMA; HWSTGIE; -. DR OrthoDB; EOG6X6RDW; -. DR BioCyc; NMEN122586:GHGG-123-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_00598; Smg; 1. DR InterPro; IPR007456; Smg. DR Pfam; PF04361; DUF494; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 153 Protein Smg homolog. FT /FTId=PRO_0000209175. SQ SEQUENCE 153 AA; 17105 MW; 73C0F790DFE4FB15 CRC64; MTEVIAYLIE HFQDFDTCPP PEDLGMLLEE AGFDTMEIGN TLMMMEVLLN SSEFSAEPAD SGALRVYSKE ETDNLPQEVM GLMQYLIEEK AVSCEQREII IHALMHIPGD EITVDTAKVL TLLLLWANKS ELPVLVGDEL MSALLLDNKP TMN // ID SPEB_NEIMB Reviewed; 307 AA. AC P60654; Q9JRG2; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Agmatinase {ECO:0000255|HAMAP-Rule:MF_01418}; DE EC=3.5.3.11 {ECO:0000255|HAMAP-Rule:MF_01418}; DE AltName: Full=Agmatine ureohydrolase {ECO:0000255|HAMAP-Rule:MF_01418}; DE Short=AUH {ECO:0000255|HAMAP-Rule:MF_01418}; GN Name=speB {ECO:0000255|HAMAP-Rule:MF_01418}; GN OrderedLocusNames=NMB0469; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC -!- CATALYTIC ACTIVITY: Agmatine + H(2)O = putrescine + urea. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01418}; CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis CC via agmatine pathway; putrescine from agmatine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40906.1; -; Genomic_DNA. DR PIR; B81196; B81196. DR RefSeq; NP_273516.1; NC_003112.2. DR RefSeq; WP_002222073.1; NC_003112.2. DR ProteinModelPortal; P60654; -. DR STRING; 122586.NMB0469; -. DR PaxDb; P60654; -. DR EnsemblBacteria; AAF40906; AAF40906; NMB0469. DR GeneID; 902585; -. DR KEGG; nme:NMB0469; -. DR PATRIC; 20356186; VBINeiMen85645_0614. DR eggNOG; ENOG4105CYW; Bacteria. DR eggNOG; COG0010; LUCA. DR HOGENOM; HOG000204320; -. DR KO; K01480; -. DR OMA; YELTTIM; -. DR OrthoDB; EOG6R2GW5; -. DR BioCyc; NMEN122586:GHGG-493-MONOMER; -. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IEA:UniProtKB-UniPathway. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.800.10; -; 1. DR HAMAP; MF_01418; SpeB; 1. DR InterPro; IPR023694; Agmatinase. DR InterPro; IPR005925; Agmatinase-rel. DR InterPro; IPR006035; Ureohydrolase. DR InterPro; IPR023696; Ureohydrolase_domain. DR InterPro; IPR020855; Ureohydrolase_Mn_BS. DR PANTHER; PTHR11358; PTHR11358; 1. DR Pfam; PF00491; Arginase; 1. DR PIRSF; PIRSF036979; Arginase; 1. DR TIGRFAMs; TIGR01230; agmatinase; 1. DR PROSITE; PS01053; ARGINASE_1; 1. DR PROSITE; PS51409; ARGINASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Metal-binding; KW Polyamine biosynthesis; Putrescine biosynthesis; Reference proteome; KW Spermidine biosynthesis. FT CHAIN 1 307 Agmatinase. FT /FTId=PRO_0000173736. FT METAL 128 128 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. FT METAL 151 151 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. FT METAL 153 153 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. FT METAL 155 155 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. FT METAL 232 232 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. FT METAL 234 234 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01418}. SQ SEQUENCE 307 AA; 33905 MW; 1B5013800B47E4BF CRC64; MQYSTLAGQT DNSLVSNNFG FLRLPLNFMP YESHADWVIT GVPYDMAVSG RSGARFGPEA IRRASVNLAW EHRRFPWTFD VRERLNIIDC GDLVFSFGDS RDFVEKMEAH AGKLLSSGKR CLSLGGDHFI TLPLLRAHAR YFGKLALIHF DAHTDTYDNG SEYDHGTMFY TAPKEGLIDP SRSVQIGIRT EHSKKLPFTV LSAPKVNEDS VEETVRKIKE TVGNMPVYLT FDIDCLDPSF APGTGTPVCG GLSSDRALKI LRGLTDLDIV GMDVVEVAPS YDQSDITALA GATIALEMLY LQGAKKD // ID SSB_NEIMB Reviewed; 174 AA. AC P66849; Q9JRF8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984}; DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984}; GN Name=ssb; OrderedLocusNames=NMB1460; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Plays an important role in DNA replication, CC recombination and repair. Binds to ssDNA and to an array of CC partner proteins to recruit them to their sites of action during CC DNA metabolism. {ECO:0000255|HAMAP-Rule:MF_00984}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|HAMAP- CC Rule:MF_00984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41819.1; -; Genomic_DNA. DR PIR; A81080; A81080. DR RefSeq; NP_274471.1; NC_003112.2. DR RefSeq; WP_002212976.1; NC_003112.2. DR ProteinModelPortal; P66849; -. DR STRING; 122586.NMB1460; -. DR PaxDb; P66849; -. DR EnsemblBacteria; AAF41819; AAF41819; NMB1460. DR GeneID; 903882; -. DR KEGG; nme:NMB1460; -. DR PATRIC; 20358667; VBINeiMen85645_1843. DR eggNOG; ENOG4108UUM; Bacteria. DR eggNOG; COG0629; LUCA. DR HOGENOM; HOG000106483; -. DR KO; K03111; -. DR OMA; QQYNEPP; -. DR OrthoDB; EOG6M9F32; -. DR BioCyc; NMEN122586:GHGG-1500-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00984; SSB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR PANTHER; PTHR10302; PTHR10302; 1. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF002070; SSB; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00621; ssb; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW DNA replication; DNA-binding; Reference proteome. FT CHAIN 1 174 Single-stranded DNA-binding protein. FT /FTId=PRO_0000096071. FT DOMAIN 3 107 SSB. {ECO:0000255|HAMAP-Rule:MF_00984}. FT MOTIF 169 174 Important for interaction with partner FT proteins. {ECO:0000255|HAMAP- FT Rule:MF_00984}. SQ SEQUENCE 174 AA; 19453 MW; 2276BC639B3B6F9B CRC64; MSLNKVILIG RLGRDPEVRY MPNGEAVCNF SVATSETWND RNGQRVERTE WHNITMYRKL AEIAGQYLKK GGLVYLEGRI QSRKYQGKDG IERTAYDIVA NEMKMLGGRN ENSGGAPYEE GYGQSQEAYQ RPAQQSRQPA SDAPSHPQEA PAAPRRQPVP AAAPVEDIDD DIPF // ID SSTT_NEIMB Reviewed; 409 AA. AC Q9JXB8; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Serine/threonine transporter SstT {ECO:0000255|HAMAP-Rule:MF_01582}; DE AltName: Full=Na(+)/serine-threonine symporter {ECO:0000255|HAMAP-Rule:MF_01582}; GN Name=sstT {ECO:0000255|HAMAP-Rule:MF_01582}; GN OrderedLocusNames=NMB2133; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the import of serine and threonine into the CC cell, with the concomitant import of sodium (symport system). CC {ECO:0000255|HAMAP-Rule:MF_01582}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01582}. CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter CC (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42441.1; -; Genomic_DNA. DR PIR; F81003; F81003. DR RefSeq; NP_275118.1; NC_003112.2. DR RefSeq; WP_002225733.1; NC_003112.2. DR ProteinModelPortal; Q9JXB8; -. DR STRING; 122586.NMB2133; -. DR PaxDb; Q9JXB8; -. DR EnsemblBacteria; AAF42441; AAF42441; NMB2133. DR GeneID; 903354; -. DR KEGG; nme:NMB2133; -. DR PATRIC; 20360444; VBINeiMen85645_2718. DR eggNOG; ENOG4107QV7; Bacteria. DR eggNOG; COG3633; LUCA. DR HOGENOM; HOG000218252; -. DR KO; K07862; -. DR OMA; WIINVAP; -. DR OrthoDB; EOG63Z78S; -. DR BioCyc; NMEN122586:GHGG-2198-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022889; F:serine transmembrane transporter activity; IEA:InterPro. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR GO; GO:0015565; F:threonine efflux transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.10.3860.10; -; 1. DR HAMAP; MF_01582; Ser_Thr_transp_SstT; 1. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR023025; Ser_Thr_transp_SstT. DR PANTHER; PTHR11958; PTHR11958; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; SSF118215; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 409 Serine/threonine transporter SstT. FT /FTId=PRO_0000309101. FT TRANSMEM 24 44 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 48 68 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 82 102 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 142 162 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 194 214 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 218 238 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 247 269 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 292 312 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 319 339 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. SQ SEQUENCE 409 AA; 41942 MW; 1A7BB589E9A5B58F CRC64; MAFGKSLFHA IGRVSLVRQI AAGLALGIVI GSVSPQLGLA AGLFGSLFVG ALKAVAPVLV FILVAATIAQ HQKGNKAHIR PIIVLYLIGT FSAALTAVIA GMVFPTHIVL AGAGDVSAAP PSGIVEVLKS LLMNLVANPI NAIANANYIG ILAWALVLGA ALRNHGSDVT RQVVADLAEA VSTVVKWIIR FAPLGIFGLV SSTIAETGFG ALAGYAKLLA VLLGCMAFIA LAVNPAIVWW KIRRNPFPLV FTCLRESGVY AFFTRSSAAN IPVNMALAKK LGLHEDTYSI SIPLGATINM AGAAITITVL AMAAAHTQGI TVDFATALLL SLVATVSACG ASGVAGGSLL LIPLACSLFG IDNDVAMQVV AVGFIIGVIQ DSAETALNSS TDVLFTAAAD LGRQRNRAE // ID SUCC_NEIMB Reviewed; 388 AA. AC Q9JZP4; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558}; DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558}; GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; GN OrderedLocusNames=NMB0959; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC succinate from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00558}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41365.1; -; Genomic_DNA. DR PIR; F81137; F81137. DR RefSeq; NP_273997.1; NC_003112.2. DR RefSeq; WP_002225315.1; NC_003112.2. DR ProteinModelPortal; Q9JZP4; -. DR SMR; Q9JZP4; 1-386. DR STRING; 122586.NMB0959; -. DR PaxDb; Q9JZP4; -. DR PRIDE; Q9JZP4; -. DR EnsemblBacteria; AAF41365; AAF41365; NMB0959. DR GeneID; 903079; -. DR KEGG; nme:NMB0959; -. DR PATRIC; 20357399; VBINeiMen85645_1214. DR eggNOG; ENOG4105CMV; Bacteria. DR eggNOG; COG0045; LUCA. DR HOGENOM; HOG000007059; -. DR KO; K01903; -. DR OMA; YIESGCD; -. DR OrthoDB; EOG644ZT0; -. DR BioCyc; NMEN122586:GHGG-996-MONOMER; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.261; -; 1. DR HAMAP; MF_00558; Succ_CoA_beta; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS. DR InterPro; IPR005809; Succ_CoA_synthase_bsu. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR PANTHER; PTHR11815; PTHR11815; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01016; sucCoAbeta; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 388 Succinyl-CoA ligase [ADP-forming] subunit FT beta. FT /FTId=PRO_0000102842. FT DOMAIN 9 245 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00558}. FT NP_BIND 35 109 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 198 198 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 200 200 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. SQ SEQUENCE 388 AA; 41336 MW; 361E70FBF49ADEF9 CRC64; MNLHEYQAKE LLASYGLPVQ GGILAHNGEE AAAAYDKLGG KFAVVKAQVH AGGRGKAGGV KVVKSREEAK EVAESLIGTN LVTYQTDANG QPVNSVLVCE DMYPVQTELY LGAVVDRSTR RITFMASTEG GVEIEKVAAE TPEKIFKVTV DPLVGLQPCQ AREVAFQLGL KDKQINEFVK LMTGAYKAFV ENDFALFEVN PLAVRENGAL ACVDGKIGID SNALYRLPKI AELRDKSQEN ERELKASEFD LNYVALEGNI GCMVNGAGLA MATMDIIKLK GGQPANFLDV GGGATKDRVV EAFKLILEDK SVQGVLINIF GGIVRCDMIA EAIVAAVKEI NVNVPVVVRL EGNNAELGAK ILNESGLKLT SADGLNDAAE KIVAAVNA // ID SSRP_NEIMB Reviewed; 148 AA. AC P0A0Y8; Q51111; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=SsrA-binding protein {ECO:0000255|HAMAP-Rule:MF_00023}; DE AltName: Full=Small protein B {ECO:0000255|HAMAP-Rule:MF_00023}; GN Name=smpB {ECO:0000255|HAMAP-Rule:MF_00023}; GN OrderedLocusNames=NMB1526; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=8852280; DOI=10.1006/mpat.1995.0074; RA Jennings M.P., Bisercic M., Dunn K.L.R., Martin A., Wilkes K.E., RA Virji M., Richards J.C., Moxon E.R.; RT "Cloning and molecular analysis of the Isi1 (rfaF) gene of Neisseria RT meningitidis which encodes a heptosyl-2-transferase involved in LPS RT biosynthesis: evaluation of surface exposed carbohydrates in LPS RT mediated toxicity for human endothelial cells."; RL Microb. Pathog. 19:391-407(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by CC trans-translation. Binds to transfer-messenger RNA (tmRNA), CC required for stable association of tmRNA with ribosomes. tmRNA and CC SmpB together mimic tRNA shape, replacing the anticodon stem-loop CC with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold CC to resemble tRNA(Ala) and it encodes a 'tag peptide', a short CC internal open reading frame. During trans-translation Ala- CC aminoacylated tmRNA acts like a tRNA, entering the A-site of CC stalled ribosomes, displacing the stalled mRNA. The ribosome then CC switches to translate the ORF on the tmRNA; the nascent peptide is CC terminated with the 'tag peptide' encoded by the tmRNA and CC targeted for degradation. The ribosome is freed to recommence CC translation, which seems to be the essential function of trans- CC translation. {ECO:0000255|HAMAP-Rule:MF_00023}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00023}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP- CC Rule:MF_00023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U23782; AAC44080.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41881.1; -; Genomic_DNA. DR PIR; B81073; B81073. DR RefSeq; NP_274533.1; NC_003112.2. DR RefSeq; WP_002229688.1; NC_003112.2. DR ProteinModelPortal; P0A0Y8; -. DR STRING; 122586.NMB1526; -. DR PaxDb; P0A0Y8; -. DR EnsemblBacteria; AAF41881; AAF41881; NMB1526. DR GeneID; 904025; -. DR KEGG; nme:NMB1526; -. DR PATRIC; 20358850; VBINeiMen85645_1935. DR eggNOG; ENOG4108UH4; Bacteria. DR eggNOG; COG0691; LUCA. DR HOGENOM; HOG000009628; -. DR KO; K03664; -. DR OMA; FLLNAHI; -. DR OrthoDB; EOG6HXJ9P; -. DR BioCyc; NMEN122586:GHGG-1566-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070929; P:trans-translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.280.10; -; 1. DR HAMAP; MF_00023; SmpB; 1. DR InterPro; IPR023620; SmpB. DR InterPro; IPR000037; SsrA-bd_prot. DR InterPro; IPR020081; SsrA-bd_prot_CS. DR Pfam; PF01668; SmpB; 1. DR ProDom; PD004488; SmpB; 1. DR SUPFAM; SSF74982; SSF74982; 1. DR TIGRFAMs; TIGR00086; smpB; 1. DR PROSITE; PS01317; SSRP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; RNA-binding. FT CHAIN 1 148 SsrA-binding protein. FT /FTId=PRO_0000102994. FT CONFLICT 37 39 RVQ -> LSM (in Ref. 1; AAC44080). FT {ECO:0000305}. FT CONFLICT 45 45 I -> M (in Ref. 1; AAC44080). FT {ECO:0000305}. FT CONFLICT 76 79 PRKL -> RASF (in Ref. 1; AAC44080). FT {ECO:0000305}. FT CONFLICT 90 90 I -> N (in Ref. 1; AAC44080). FT {ECO:0000305}. FT CONFLICT 100 100 I -> T (in Ref. 1; AAC44080). FT {ECO:0000305}. FT CONFLICT 104 106 DLH -> GFA (in Ref. 1; AAC44080). FT {ECO:0000305}. SQ SEQUENCE 148 AA; 17179 MW; B80FDB82161C1D6C CRC64; MAIANNKKAF HDFFIEDRIE AGLVLEGWEV KAIRAARVQL KESYIYWKKD AFYLVGCHIT ALPTASTHIK PDAVRPRKLL LNQSEINKLI GKTERAGYTI VPLDLHFSRG KIKMEIGLAK GKKQHDKRQS MKEADWKREK QRLIKHTR // ID SUHB_NEIMB Reviewed; 261 AA. AC Q9JZ07; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Inositol-1-monophosphatase; DE Short=I-1-Pase; DE Short=IMPase; DE Short=Inositol-1-phosphatase; DE EC=3.1.3.25; GN Name=suhB; OrderedLocusNames=NMB1347; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the inositol monophosphatase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41721.1; -; Genomic_DNA. DR PIR; F81092; F81092. DR RefSeq; NP_274365.1; NC_003112.2. DR RefSeq; WP_002222348.1; NC_003112.2. DR ProteinModelPortal; Q9JZ07; -. DR STRING; 122586.NMB1347; -. DR PaxDb; Q9JZ07; -. DR EnsemblBacteria; AAF41721; AAF41721; NMB1347. DR GeneID; 903769; -. DR KEGG; nme:NMB1347; -. DR PATRIC; 20358349; VBINeiMen85645_1686. DR eggNOG; ENOG4105ECY; Bacteria. DR eggNOG; COG0483; LUCA. DR HOGENOM; HOG000282238; -. DR KO; K01092; -. DR OMA; YILATNG; -. DR OrthoDB; EOG6QK4W4; -. DR BioCyc; NMEN122586:GHGG-1385-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR InterPro; IPR022337; Inositol_monophosphatase_SuhB. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PRINTS; PR01959; SBIMPHPHTASE. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 261 Inositol-1-monophosphatase. FT /FTId=PRO_0000142567. FT REGION 86 89 Substrate binding. {ECO:0000250}. FT METAL 67 67 Magnesium 1. {ECO:0000250}. FT METAL 84 84 Magnesium 1. {ECO:0000250}. FT METAL 84 84 Magnesium 2. {ECO:0000250}. FT METAL 86 86 Magnesium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 87 87 Magnesium 2. {ECO:0000250}. FT METAL 212 212 Magnesium 2. {ECO:0000250}. FT BINDING 67 67 Substrate. {ECO:0000250}. FT BINDING 183 183 Substrate. {ECO:0000250}. FT BINDING 212 212 Substrate. {ECO:0000250}. SQ SEQUENCE 261 AA; 28469 MW; 3D22B2295AC04653 CRC64; MNPFLNTAFK AARRAGQMMI RAAGNLDAVK TDSKAFNDFV SDVDRNSEII LVEALKEAYP HHKITCEESG SHGKAAAEYE WIIDPLDGTT NFLHGHPQYA ISMALLHKGV LQEALVYAPE RNDVYMASRG KGALLNDRRI RVSNRIELNR CLIGTGFPVV DQSMMDKYLA ILKDFLAKTA GGRREGAASL DLCAVATGRF DGFFEFNLKP WDIAAGALIV QEAGGIVTDM SGEDGWLESG DIVAANPKVL AQMLKIISAH V // ID SURE_NEIMB Reviewed; 248 AA. AC Q9JYP8; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060}; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060}; GN Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; GN OrderedLocusNames=NMB1484; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on CC nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00060}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. CC {ECO:0000255|HAMAP-Rule:MF_00060}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41840.1; -; Genomic_DNA. DR PIR; B81077; B81077. DR RefSeq; NP_274492.1; NC_003112.2. DR RefSeq; WP_002225086.1; NC_003112.2. DR ProteinModelPortal; Q9JYP8; -. DR STRING; 122586.NMB1484; -. DR PaxDb; Q9JYP8; -. DR EnsemblBacteria; AAF41840; AAF41840; NMB1484. DR GeneID; 903906; -. DR KEGG; nme:NMB1484; -. DR PATRIC; 20358734; VBINeiMen85645_1876. DR eggNOG; ENOG4105CV2; Bacteria. DR eggNOG; COG0496; LUCA. DR HOGENOM; HOG000122500; -. DR KO; K03787; -. DR OMA; NLNIPPC; -. DR OrthoDB; EOG68WR45; -. DR BioCyc; NMEN122586:GHGG-1524-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1210.10; -; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SSF64167; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 248 5'-nucleotidase SurE. FT /FTId=PRO_0000111823. FT METAL 8 8 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 9 9 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 39 39 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 91 91 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. SQ SEQUENCE 248 AA; 27034 MW; DDE344D9B4E22989 CRC64; MNVLISNDDG YLSEGIAVLA RVTAEFANVR VVAPERDRSG VSNSLTLERP LQLKQAQNGF YYVNGTPTDC IHIGQSVFSD FQADFVFSGI NRGANMGDDT LYSGTVAAAT EAYLMGIPAV AFSLNDASGR YWATAEQALW TLLAHFFKNP PQSPILWNIN IPAVAPEDVR GIKIARLGRR HHGQNVIPAR NPRGEQIYWI GPVGEVSDRE EGTDFGECGA GFITVTPLQI DLTAYPDMAE TAAFWHAD // ID SYE_NEIMB Reviewed; 464 AA. AC Q9K1R6; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=NMB0003; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a CC two-step reaction: glutamate is first activated by ATP to form CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu). CC {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + CC diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000255|HAMAP- CC Rule:MF_00022}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00022}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40482.1; -; Genomic_DNA. DR PIR; A81247; A81247. DR RefSeq; NP_273069.1; NC_003112.2. DR RefSeq; WP_002225749.1; NC_003112.2. DR ProteinModelPortal; Q9K1R6; -. DR STRING; 122586.NMB0003; -. DR PaxDb; Q9K1R6; -. DR EnsemblBacteria; AAF40482; AAF40482; NMB0003. DR GeneID; 902105; -. DR KEGG; nme:NMB0003; -. DR PATRIC; 20354933; VBINeiMen85645_0003. DR eggNOG; ENOG4105C20; Bacteria. DR eggNOG; COG0008; LUCA. DR HOGENOM; HOG000252722; -. DR KO; K01885; -. DR OMA; AMIYRAM; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NMEN122586:GHGG-3-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00464; gltX_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 464 Glutamate--tRNA ligase. FT /FTId=PRO_0000119613. FT MOTIF 9 19 "HIGH" region. FT MOTIF 242 246 "KMSKS" region. FT BINDING 245 245 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}. SQ SEQUENCE 464 AA; 52717 MW; B722585FAAAC0295 CRC64; MTVKTRFAPS PTGYLHIGGV RTALFSWAFA RHHKGEFLLR IEDTDLARST AESVNIILDG MKWVGLNYDN ADNVVYQTRR FDRYKEVIAE LLEKGHAYYC YCSKEELEAM REKAEKEGSA TYDRRWRPEV GKTLPEIPSD VQPVVRFKTP LDGVTKWTDL VKGEISIPNE ALDDLIIARA DGTPTYNFCV VVDDYDMGVT HVIRGDDHVN NTPKQINILK AIDANLPEYG HLPMILNEQG KKISKRSGDT VAITDFGAMG ILPEAMLNYL ARLGWAHGDD EFFTMEQFIE WFDLKDVSPS PSRMDLKKLY WINGEHIKIT PNGKLAELVK PRLALRDIHE TEKPALEDVL ELVKDRPQDL NTLADECFYF YVKQTPAEAD VQKHWDDEAA ARMLRFAERL EGLEDWNAEA IHDLFKPFCD EEGIKMGKLG MPLRLAVCGT AKTPSVDAVL ALIGKEEVLK RIRA // ID SYH_NEIMB Reviewed; 431 AA. AC Q9JZX9; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127}; DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127}; DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127}; DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127}; GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; GN OrderedLocusNames=NMB0854; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + CC diphosphate + L-histidyl-tRNA(His). {ECO:0000255|HAMAP- CC Rule:MF_00127}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00127}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41265.1; -; Genomic_DNA. DR PIR; A81150; A81150. DR RefSeq; NP_273895.1; NC_003112.2. DR RefSeq; WP_002225391.1; NC_003112.2. DR ProteinModelPortal; Q9JZX9; -. DR STRING; 122586.NMB0854; -. DR PaxDb; Q9JZX9; -. DR EnsemblBacteria; AAF41265; AAF41265; NMB0854. DR GeneID; 902968; -. DR KEGG; nme:NMB0854; -. DR PATRIC; 20357099; VBINeiMen85645_1068. DR eggNOG; ENOG4105CUT; Bacteria. DR eggNOG; COG0124; LUCA. DR HOGENOM; HOG000018072; -. DR KO; K01892; -. DR OMA; CGGGNFK; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; NMEN122586:GHGG-885-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00127; His_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR015807; His-tRNA-ligase. DR InterPro; IPR004516; HisRS/HisZ. DR PANTHER; PTHR11476; PTHR11476; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00442; hisS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 431 Histidine--tRNA ligase. FT /FTId=PRO_0000136210. SQ SEQUENCE 431 AA; 48465 MW; 63602E583A27DF12 CRC64; MAQKIQSVKG MNDLLPVKQK DFKLTAAFWQ AFEDTVGRWT RAYGYQQIRT PIVEQTGLFV RSIGEETDVV GKEMYTFSDS NDSLSLSLRP EGTASCLRAV VEHNLLYNSP QKLWYMGPMF RRERPQKGRY RQFHQVGIEA LGFEGPDIDA EIIAMSADLW EKLGIREYLT LEINSLGNRE ERAAHRAALV EYLTRYEDKL DEDSKRRLKT NPLRVLDTKN PDLQEICNAA PRLVDYLGED SQNHYVRFKA MLDGLGIQYI ENPRLVRGLD YYNQTVFEWT TDKLGAQATV CGGGRYDGLI EELGGKPAPS IGFAMGIERL LLLVSEYGSL EVNAAPDVYA MHQGEGADLQ VMKYAQALRA QGFNVMQHSG YQSLKAQMKK ADNSGARFAL IVAQDELANG TVTLKDMNGA HGQQTVAAED LTPTLQQWKN A // ID SYP_NEIMB Reviewed; 570 AA. AC Q9JZ14; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569}; DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569}; DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569}; GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; GN OrderedLocusNames=NMB1339; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a CC two-step reaction: proline is first activated by ATP to form Pro- CC AMP and then transferred to the acceptor end of tRNA(Pro). As CC ProRS can inadvertently accommodate and process non-cognate amino CC acids such as alanine and cysteine, to avoid such errors it has CC two additional distinct editing activities against alanine. One CC activity is designated as 'pretransfer' editing and involves the CC tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other CC activity is designated 'posttransfer' editing and involves CC deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- CC tRNA(Pro) is not edited by ProRS. {ECO:0000255|HAMAP- CC Rule:MF_01569}. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP- CC Rule:MF_01569}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the editing domain and the C-terminal anticodon-binding CC domain. {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41714.1; -; Genomic_DNA. DR PIR; C81094; C81094. DR RefSeq; NP_274358.1; NC_003112.2. DR RefSeq; WP_002222353.1; NC_003112.2. DR ProteinModelPortal; Q9JZ14; -. DR STRING; 122586.NMB1339; -. DR PaxDb; Q9JZ14; -. DR EnsemblBacteria; AAF41714; AAF41714; NMB1339. DR GeneID; 903761; -. DR KEGG; nme:NMB1339; -. DR PATRIC; 20358333; VBINeiMen85645_1678. DR eggNOG; ENOG4105C90; Bacteria. DR eggNOG; COG0442; LUCA. DR HOGENOM; HOG000076893; -. DR KO; K01881; -. DR OMA; IQPAELW; -. DR OrthoDB; EOG6TTVMR; -. DR BioCyc; NMEN122586:GHGG-1377-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR Gene3D; 3.90.960.10; -; 1. DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR002316; Pro-tRNA-ligase_IIa. DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type. DR InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1. DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom. DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 2. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF04073; tRNA_edit; 1. DR PIRSF; PIRSF001535; ProRS_1; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55826; SSF55826; 1. DR TIGRFAMs; TIGR00409; proS_fam_II; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 570 Proline--tRNA ligase. FT /FTId=PRO_0000248728. SQ SEQUENCE 570 AA; 62992 MW; B2A9EC450893F818 CRC64; MKASQFFIST LKEAPAEAAL ASHKLMIRAG LIKANASGLY TWMPMGLRVL RKVENVVREE MARAGSVELL MPVVQPAELW QESGRWEFYG KELLRLKDRH DRDFCMGPTC EEVIADIVRK EINSYKQLPK NFYHIQTKFR DEVRPRFGVM RAREFVMKDA YSFHADYASL QTTYQDMYDA YCRIFTRLGL AFRPVAADTG SIGGTGSHEF QVLAESGEDV IAYSDTSDYA ANIELAPTLP LKGERAAAQA ELVKVHTPNV KTIDSLVDFL SIPIEKTLKS IVVEGENEGE LILLLLRGDH EFNDIKAEKL AGVKSPLTMA SPAAIVEQFG ANGGSLGPVG FAGKVYADFA TEKGADWVIG ANEDDYHYTG FNFGRDAAEP EFVDLRNVVE GDESPDGQGR LKLARGIEVG HVFQLRDKYT QAMNVSFLDN NGKSQIMEMG CYGIGITRVV AAAIEQNNDE KGIIWTKAMA PFEVVIVPMN YKKSDTVREA ADKIYAELLA AGADVLLDDR DERAGVLLND SELLGIPHRI VIGDRALKEG NVEYAERRDN EAQAVAIGEI VARVTASLNA // ID SYC_NEIMB Reviewed; 473 AA. AC Q9JXE6; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 95. DE RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041}; DE EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041}; DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041}; DE Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041}; GN Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041}; GN OrderedLocusNames=NMB2083; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). {ECO:0000255|HAMAP- CC Rule:MF_00041}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00041}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00041}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42401.1; -; Genomic_DNA. DR PIR; B81007; B81007. DR RefSeq; NP_275072.1; NC_003112.2. DR RefSeq; WP_002225718.1; NC_003112.2. DR ProteinModelPortal; Q9JXE6; -. DR SMR; Q9JXE6; 1-414. DR STRING; 122586.NMB2083; -. DR PaxDb; Q9JXE6; -. DR EnsemblBacteria; AAF42401; AAF42401; NMB2083. DR GeneID; 903970; -. DR KEGG; nme:NMB2083; -. DR PATRIC; 20360334; VBINeiMen85645_2664. DR eggNOG; ENOG4105C8N; Bacteria. DR eggNOG; COG0215; LUCA. DR HOGENOM; HOG000245250; -. DR KO; K01883; -. DR OMA; HENEACQ; -. DR OrthoDB; EOG6RVFXC; -. DR BioCyc; NMEN122586:GHGG-2149-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00041; Cys_tRNA_synth; 1. DR InterPro; IPR015803; Cys-tRNA-ligase. DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR. DR InterPro; IPR024909; Cys-tRNA/MSH_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR032678; tRNA-synt_1_cat_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR10890; PTHR10890; 2. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR SMART; SM00840; DALR_2; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00435; cysS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 473 Cysteine--tRNA ligase. FT /FTId=PRO_0000159444. FT MOTIF 30 40 "HIGH" region. FT MOTIF 282 286 "KMSKS" region. FT METAL 28 28 Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}. FT METAL 209 209 Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}. FT METAL 234 234 Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}. FT METAL 238 238 Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}. FT BINDING 285 285 ATP. {ECO:0000255|HAMAP-Rule:MF_00041}. SQ SEQUENCE 473 AA; 52954 MW; F4BC85BD50268BA4 CRC64; MTTIYNTLTR QKEPFSPIDP ENVRMYVCGM TVYDYCHLGH ARVMVVFDMI ARWLRECGYP LTYVRNITDI DDKIIARAAE NGETIGKLTA RFIQAMHEDA DALGVLRPDI EPKATENIPQ MIAMIETLIQ NGKAYPAANG DVYYAVREFA AYGQLSGKSL DDLRAGERVE VDGFKRDPLD FVLWKAAKAG EPAWESPWGN GRPGWHIECS AMSENLFGDT FDIHGGGADL QFPHHENEIA QSVGATGHTC GHHHAQTHHG QSIASHVKYW LHNGFIRVDG EKMSKSLGNF FTIREVLKQY DPEVVRFFIL RAHYRSPLNY SDAHLDDAKG ALTRLYTTLK NTPPADPMPS EAGDDYTRRF YVAMNDDFDT VKAVAVLFEL AGEVNKTNDA QLAGRLKALG GIIGLLQRDP TEFLQGGAAS DGLSNEEIED LIARRKQARA DKNWAESDRI RDLLNEHKII LEDNAGGTTW RRG // ID SYFA_NEIMB Reviewed; 330 AA. AC Q9K092; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit; DE Short=PheRS; GN Name=pheS; OrderedLocusNames=NMB0724; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41137.1; -; Genomic_DNA. DR PIR; G81165; G81165. DR RefSeq; NP_273766.1; NC_003112.2. DR RefSeq; WP_002244061.1; NC_003112.2. DR ProteinModelPortal; Q9K092; -. DR STRING; 122586.NMB0724; -. DR PaxDb; Q9K092; -. DR EnsemblBacteria; AAF41137; AAF41137; NMB0724. DR GeneID; 902837; -. DR KEGG; nme:NMB0724; -. DR PATRIC; 20356805; VBINeiMen85645_0923. DR eggNOG; ENOG4105CSS; Bacteria. DR eggNOG; COG0016; LUCA. DR HOGENOM; HOG000242675; -. DR KO; K01889; -. DR OMA; KGTGWLE; -. DR OrthoDB; EOG6WX4QN; -. DR BioCyc; NMEN122586:GHGG-753-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR004188; Phe-tRNA_ligase_II_N. DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR010978; tRNA-bd_arm. DR Pfam; PF02912; Phe_tRNA-synt_N; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00468; pheS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 330 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126735. FT METAL 254 254 Magnesium. {ECO:0000250}. SQ SEQUENCE 330 AA; 37333 MW; F350FADF4F9DE202 CRC64; MENVNRIVAE GIAAVEAAQD FNALEQIKAR YLGKTGELTG LLKTLGQMSP EERKTIGAHI NECKNRFQTA FNAKREALNE VKLQARLAAE ALDITLPGRA QEGGSLHPVT LTLQRVVELF HGMGFEVADG PEIEDDFHNF QALNIPANHP ARAMQDTFYV ENGDVLRTHT SPIQIRYMLD KKEPPIRIIA PGRVYRVDSD ATHSPMFHQA EGLWVEEGVT FADLKAVFTD FIRRFFERDD LQVRFRPSFF PFTEPSAEID IMGENGKWLE VGGCGMVHPN VLKNVNIDPE KYTGFAFGIG LDRFAMLRYN VNDLRLFFDN DLNFLKQFAK // ID SYL_NEIMB Reviewed; 876 AA. AC Q9JXT2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=NMB1897; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP + CC diphosphate + L-leucyl-tRNA(Leu). {ECO:0000255|HAMAP- CC Rule:MF_00049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00049}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42228.1; -; Genomic_DNA. DR PIR; G81029; G81029. DR RefSeq; NP_274892.1; NC_003112.2. DR RefSeq; WP_002225801.1; NC_003112.2. DR ProteinModelPortal; Q9JXT2; -. DR STRING; 122586.NMB1897; -. DR PaxDb; Q9JXT2; -. DR EnsemblBacteria; AAF42228; AAF42228; NMB1897. DR GeneID; 904274; -. DR KEGG; nme:NMB1897; -. DR PATRIC; 20359831; VBINeiMen85645_2420. DR eggNOG; ENOG4105C8T; Bacteria. DR eggNOG; COG0495; LUCA. DR HOGENOM; HOG000200747; -. DR KO; K01869; -. DR OMA; EGAHRFI; -. DR OrthoDB; EOG63Z74X; -. DR BioCyc; NMEN122586:GHGG-1954-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 3. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR PANTHER; PTHR11946:SF7; PTHR11946:SF7; 3. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00396; leuS_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 876 Leucine--tRNA ligase. FT /FTId=PRO_0000152054. FT MOTIF 42 52 "HIGH" region. FT MOTIF 634 638 "KMSKS" region. FT BINDING 637 637 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. SQ SEQUENCE 876 AA; 98097 MW; 7A53210ED4A823AA CRC64; MQEQYRPAAI EPAAQKKWDD ARIFNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID WARETATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS KQGLEGDYAK FLQVYTTRPD TLMGATYVAV AAEHPLAAAA AADKPELQAF IAECKAGSVA EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFATK YNLPKKQVIA VGDNAFDENQ WQEWYGDKEN GVLVNSGDLD GLDFQTAFDA VAAKLQSQGA GEPKTQYRLR DWGISRQRYW GCPIPIVHCE QCGDVPVPAD QLPVVLPENV VPDGMGSPLA KMPEFYETAC PCCGGAAKRE TDTMDTFMES SWYFFRYMSP KFSDGMVDPA AAKYWGAVDQ YIGGIEHAIL HLLYARFFTK LMRDEGLVNV DEPFERLLTQ GMVVCETYYR ENDKGGKDWI NPADVELTFD DKGRPISAVL KADGLPVVIS GTEKMSKSKN NGVDPQELIN AYGADTARLF MMFAAPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYLKQGE AVKAFAGSQD GLSKELKDLR HKLHATTAKV SDDYGRRQQF NTAIAAVMEL LNQYDKTDTG GEQGRAVAQE VLETAVRLLW PIVPHICETL WSELNGAKLW EAGWPTVDEA ALVKSEIEVM VQVNGKLRGK ITVAADASKA DLEAAALATE GAVKFMEGKP AKKIIVVPGR LVNIVV // ID SYQ_NEIMB Reviewed; 562 AA. AC P56927; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Glutamine--tRNA ligase; DE EC=6.1.1.18; DE AltName: Full=Glutaminyl-tRNA synthetase; DE Short=GlnRS; GN Name=glnS; OrderedLocusNames=NMB1560; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamine + tRNA(Gln) = AMP + CC diphosphate + L-glutaminyl-tRNA(Gln). CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41914.1; -; Genomic_DNA. DR PIR; E81069; E81069. DR RefSeq; NP_274567.2; NC_003112.2. DR ProteinModelPortal; P56927; -. DR SMR; P56927; 11-557. DR STRING; 122586.NMB1560; -. DR PaxDb; P56927; -. DR EnsemblBacteria; AAF41914; AAF41914; NMB1560. DR GeneID; 904126; -. DR KEGG; nme:NMB1560; -. DR PATRIC; 20358976; VBINeiMen85645_2007. DR eggNOG; ENOG4105CX6; Bacteria. DR eggNOG; COG0008; LUCA. DR HOGENOM; HOG000259232; -. DR KO; K01886; -. DR OMA; KWLGFEW; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NMEN122586:GHGG-1601-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 2.40.240.10; -; 2. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00126; Gln_tRNA_synth; 1. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR022861; Gln_tRNA_ligase_bac. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF50715; SSF50715; 1. DR TIGRFAMs; TIGR00440; glnS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 562 Glutamine--tRNA ligase. FT /FTId=PRO_0000195839. FT MOTIF 35 45 "HIGH" region. FT MOTIF 271 275 "KMSKS" region. FT BINDING 274 274 ATP. {ECO:0000250}. SQ SEQUENCE 562 AA; 64650 MW; 52F3C71FA22DE36D CRC64; MLNKDQFADN HFIRTIIEED LESGKHTAVQ TRFPPEPNGY LHIGHAKSIC LNFGLAYIYD GLCNLRFDDT NPEKENDEYV NAIKEDVEWL GFHWAGEPRF ASNYFDQLYD YAVGLIKDGK AYVDDLTPEE MREYRGTLTE AGKNSPYRDR SVEENLDLFT RMKNGEFPDG SKTLRLKIDM ASGNINMRDP VIYRIRRAHH HNTGDKWCIY PMYDYTHCIS DAIEGITHSL CTLEFEAHRP LYDCVLDNIP APHATRPRQY EFSRLELLYT ITSKRKLNQL VVEKHVSGWD DPRMPTISGM RRRGYTPEGL RLFAKRAGIS KSENIVDMSV LEGAIREELE NSAPRLMAVL NPLKVTLTNF ETGRTQSRRA AFHPNHEEMG EREVPISQTI YIEADDFAEN PPKGFKRLIP GGEVRLRHGY VIKCDEVVKD EAGNVVELKC SIDHDTLGKN PEGRKVKGVI HWVSAEHAAE IKVRLYDRLF TVERPDAVRG EDGEYLPFTD FLNPESVKEI TAYAEPAAKD LPAESRWQFE RIGYFVTDRK DHGKDTPVFN RTVTLKDSWQ PK // ID SYA_NEIMB Reviewed; 874 AA. AC Q9JYG6; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036}; DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036}; DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036}; GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; GN OrderedLocusNames=NMB1595; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a CC two-step reaction: alanine is first activated by ATP to form Ala- CC AMP and then transferred to the acceptor end of tRNA(Ala). Also CC edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its CC editing domain. {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP- CC Rule:MF_00036}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00036}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic CC domain, the editing domain and the C-terminal C-Ala domain. The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00036}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41948.1; -; Genomic_DNA. DR PIR; F81063; F81063. DR RefSeq; NP_274601.1; NC_003112.2. DR RefSeq; WP_010980961.1; NC_003112.2. DR ProteinModelPortal; Q9JYG6; -. DR SMR; Q9JYG6; 1-460. DR STRING; 122586.NMB1595; -. DR PaxDb; Q9JYG6; -. DR EnsemblBacteria; AAF41948; AAF41948; NMB1595. DR GeneID; 904276; -. DR KEGG; nme:NMB1595; -. DR PATRIC; 20359074; VBINeiMen85645_2049. DR eggNOG; ENOG4105CIM; Bacteria. DR eggNOG; COG0013; LUCA. DR HOGENOM; HOG000156964; -. DR KO; K01872; -. DR OMA; FSITDGQ; -. DR OrthoDB; EOG6Q2SQ2; -. DR BioCyc; NMEN122586:GHGG-1643-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF01411; tRNA-synt_2c; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR00980; TRNASYNTHALA. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF101353; SSF101353; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 874 Alanine--tRNA ligase. FT /FTId=PRO_0000075161. FT METAL 562 562 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 566 566 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 664 664 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 668 668 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. SQ SEQUENCE 874 AA; 96038 MW; 4BC2D6AAEDEE4BF5 CRC64; MKTSELRQKF LKFFETKGHT VVRSSSLVPH DDPTLLFTNA GMNQFKDVFL GFDKRPYSRA TTAQKCVRAG GKHNDLENVG YTARHHTFFE MMGNFSFGDY FKRDAIHFAW EFLTSPEWLN IPKDKLLATV YAEDDEAYNI WLNEIGMPSE RIVRIGDNKG AKYASDNFWQ MGDTGPCGPC SEIFYDHGEE IWGGIPGSPE EDGDRWIEIW NCVFMQFNRD EQGNMNPLPK PSVDTGMGLE RIAAVMQHVH SNYEIDLFQD LLKAVARETG APFRMEEPSL KVIADHIRSC SFLIADGVLP SNEGRGYVLR RIIRRAVRHG YKLGQSKPFF HKLVADLVKE MGGAYPELKE KQAQIEEALK NEESRFAQTL ETGMALLENA LVKGGKTLGG EIIFKLYDTY GFPYDLTADI CRERNIEPDE AGFEREMEAQ RARARAAQSF KANAQLPYDG QDTEFKGYSE RQTESKVLAL YKDGEQVNEL NEGDSGAVVI DFTPFYAESG GQVGDVGYIF SGENRFEVRD TQKIKAAVFG QFGVQTSGRL KVGDSVTAKV DDEIRNANMR NHSATHLMHK ALRDVLGRHV EQKGSLVTAE STRFDISHPQ AVTAEEIAEV ERRVNEAILA NVAVNAAIMS MEDAQKTGAM MLFGEKYGEE VRVLQMGGFS TELCGGTHVS RTGDIGLFKI ISEGGIAAGV RRIEAITGLN ALKWAQEQER LVKDIIAETK AQTEKDVLAK IQAGAAHAKA LEKELARAKA ELAVHAGAKL LDDAKDLGAA KLVAAQIEAD AAALREIVTD LTGKSDNAVI LLAAVNDGKV SLCAGVSKPL TGKVKAGDLV KFAAEQVGGK GGGRPDLAQA GGTDADKLPA VLDSVKDWVG AKLV // ID SYDND_NEIMB Reviewed; 602 AA. AC Q9K0U5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; GN OrderedLocusNames=NMB0466; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity CC since it is able to aspartylate not only its cognate tRNA(Asp) but CC also tRNA(Asn). Reaction proceeds in two steps: aspartate is first CC activated by ATP to form Asp-AMP and then transferred to the CC acceptor end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP + CC diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000255|HAMAP- CC Rule:MF_00044}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40903.1; -; Genomic_DNA. DR PIR; G81195; G81195. DR RefSeq; NP_273513.1; NC_003112.2. DR RefSeq; WP_002224947.1; NC_003112.2. DR ProteinModelPortal; Q9K0U5; -. DR SMR; Q9K0U5; 1-593. DR STRING; 122586.NMB0466; -. DR PaxDb; Q9K0U5; -. DR EnsemblBacteria; AAF40903; AAF40903; NMB0466. DR GeneID; 902582; -. DR KEGG; nme:NMB0466; -. DR PATRIC; 20356180; VBINeiMen85645_0611. DR eggNOG; ENOG4105C9M; Bacteria. DR eggNOG; COG0173; LUCA. DR HOGENOM; HOG000275160; -. DR KO; K01876; -. DR OMA; YQLDVEM; -. DR OrthoDB; EOG68Q0NX; -. DR BioCyc; NMEN122586:GHGG-490-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1360.30; -; 1. DR HAMAP; MF_00044; Asp_tRNA_synth; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004524; Asp-tRNA-ligase_bac/mit. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR004115; GAD-like. DR InterPro; IPR029351; GAD_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 2. DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 2. DR Pfam; PF02938; GAD; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF55261; SSF55261; 1. DR TIGRFAMs; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 602 Aspartate--tRNA(Asp/Asn) ligase. FT /FTId=PRO_0000110910. FT NP_BIND 218 220 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 543 546 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 196 199 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 172 172 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 218 218 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 227 227 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 457 457 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 491 491 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 498 498 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT SITE 30 30 Important for tRNA non-discrimination. FT {ECO:0000255|HAMAP-Rule:MF_00044}. FT SITE 81 81 Important for tRNA non-discrimination. FT {ECO:0000255|HAMAP-Rule:MF_00044}. SQ SEQUENCE 602 AA; 68124 MW; 5DC8A016B0C13E3C CRC64; MRTNYCGLIS EQYLDQTVTV KGWVHRRRDH GGVIFIDLRD REGIVQVVID PDTPEAFAAA DSSRNEYVLS ITGRVRNRPE GTTNDKMISG KIEILAKEIE VLNAAATPPF QIDDENISEN VRLTNRVIDL RRPVMQRNLR LRYQVAMGVR RYLDAQGFID IETPMLTRST PEGARDYLVP SRVHPGEFFA LPQSPQLFKQ LLMVAGFDRY YQITKCFRDE DLRADRQPEF TQIDLETSFL NEDEIMDITE GMAKQVFKDA LNVDLGDFPR MPYSEAMFYY GSDKPDMRIN LKFTELTDLM KTEEFKVFRG AADMKGGRVV ALRVPNGAEF SRKEIDEYTK FVGIYGAKGL AYIKVNDVSN LSNGEDSGLQ SPIVKYLSEN ALKEIIARTG AQNGDIIFFG ADKAKVVNEA IGALRIKVGL EHGKDNGYFT DEWKPLWVVD FPMFEYDEEA DRYVAVHHPF TAPKEGHEDL MVSDPANCLA RAYDMVLNGW EIGGGSIRIH RADVQEKVFA ALKISPEEQQ EKFGFLLDNL KFGAPPHGGL AFGLDRLVTL MTGAESIRDV IAFPKTQRAQ CLLTNAPNSV DDKQLRELSL RLRQKATETK EV // ID SYI_NEIMB Reviewed; 929 AA. AC Q9JXY7; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; GN OrderedLocusNames=NMB1833; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As CC IleRS can inadvertently accommodate and process structurally CC similar amino acids such as valine, to avoid such errors it has CC two additional distinct tRNA(Ile)-dependent editing activities. CC One activity is designated as 'pretransfer' editing and involves CC the hydrolysis of activated Val-AMP. The other activity is CC designated 'posttransfer' editing and involves deacylation of CC mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP + CC diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- DOMAIN: IleRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated valine is CC translocated from the active site to the editing site, which CC sterically excludes the correctly activated isoleucine. The single CC editing site contains two valyl binding pockets, one specific for CC each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42168.1; -; Genomic_DNA. DR PIR; G81036; G81036. DR RefSeq; NP_274830.1; NC_003112.2. DR RefSeq; WP_002225664.1; NC_003112.2. DR ProteinModelPortal; Q9JXY7; -. DR STRING; 122586.NMB1833; -. DR PaxDb; Q9JXY7; -. DR EnsemblBacteria; AAF42168; AAF42168; NMB1833. DR GeneID; 903267; -. DR KEGG; nme:NMB1833; -. DR PATRIC; 20359667; VBINeiMen85645_2339. DR eggNOG; ENOG4105C07; Bacteria. DR eggNOG; COG0060; LUCA. DR HOGENOM; HOG000246402; -. DR KO; K01870; -. DR OMA; PIPFFLH; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; NMEN122586:GHGG-1888-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00392; ileS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 929 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098429. FT MOTIF 58 68 "HIGH" region. FT MOTIF 605 609 "KMSKS" region. FT METAL 892 892 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 895 895 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 912 912 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 915 915 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT BINDING 563 563 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 608 608 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. SQ SEQUENCE 929 AA; 104199 MW; 5D942C44EEA516B6 CRC64; MTDYSKTVNL LESPFPMRGN LAKREPAWLK SWYEQKRYQK LREIAKGRPK FILHDGPPYA NGDIHIGHAV NKILKDIIIR SKTQAGFDAP YVPGWDCHGL PIEVMVEKLH GKDMPKARFR ELCREYAAEQ IARQKKDFIR LGVLGDWDHP YLTMDFKTEA DTVRMLGEIY KSGYLYRGAK PVQFCLDCGS SLAEAEVEYK DKISPAIDVA YLFKDTAALA AAFGLAGFEG KAFAVIWTTT PWTLPASQAV SAGADVVYQL IDTPKGKLVL AKDLAEDALK RYGFSDGIAI LAETTGDKLE NLHMNHPFLE RDIPMLNGEH VTTDAGTGLV HTAPAHGLED YAVCNKYGIE LYNPVNAEGR YIGETPRVAG MRVWEANPVI LQWLEETGNL LASSKIEHSY AHCWRHKTPL IYRATGQWFV GMDKAGADGK TLRDKAIKAV DDTEFFPSWG RARLEAMIEG RPDWVVSRQR YWGTPMTFFV HKETGELHPN SAELLEKVAL KIEEKGIEAW FSLDKSELLS AEDCENYDKL SDTMDVWFDS GSTHYSVVKQ REELEWPADL YLEGSDQHRG WFQSSMLTGC ASSMGRAPYK QLLTHGFVVD GEGKKMSKSI GNVVAPQEVY NEFGADILRL WAASTDYSGE LAISKEILKR VTESYRRIRN TLSFLFANLS DFNPIEDAVQ QADMVEIDRY AVVLARQLQE CLAGDYYPRY AFHFAVKDIV SFCSEDLGAF YLDILKDRLY TTKADSHARR SAQTALYHIT RSLVLLIAPI LCFTGEEAWD IIGGGEEDSV LFHTWHEFPT INEKTEAELV KKWTAIREAR EAVTAAIEPL RADKTVGSSL QAEAEITAPE EMAGYLNALG EELRFALLVS KAEVKVGSEL AVAAKASDGE KCERCWHYTR DVGAVAGYET VCKRCAENVG GEGETRHYA // ID SYFB_NEIMB Reviewed; 787 AA. AC Q9K089; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit; DE Short=PheRS; GN Name=pheT; OrderedLocusNames=NMB0728; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41141.1; -; Genomic_DNA. DR PIR; C81166; C81166. DR RefSeq; NP_273770.1; NC_003112.2. DR RefSeq; WP_002225459.1; NC_003112.2. DR ProteinModelPortal; Q9K089; -. DR STRING; 122586.NMB0728; -. DR PaxDb; Q9K089; -. DR EnsemblBacteria; AAF41141; AAF41141; NMB0728. DR GeneID; 902841; -. DR KEGG; nme:NMB0728; -. DR PATRIC; 20356811; VBINeiMen85645_0926. DR eggNOG; ENOG4105C6A; Bacteria. DR eggNOG; COG0072; LUCA. DR eggNOG; COG0073; LUCA. DR HOGENOM; HOG000292085; -. DR KO; K01890; -. DR OMA; MKFSEQW; -. DR OrthoDB; EOG6CCH1J; -. DR BioCyc; NMEN122586:GHGG-757-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.56.20; -; 1. DR Gene3D; 3.30.70.380; -; 1. DR Gene3D; 3.50.40.10; -; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54991; SSF54991; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1 787 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000126919. FT DOMAIN 39 149 tRNA-binding. FT DOMAIN 400 475 B5. FT DOMAIN 694 786 FDX-ACB. FT METAL 453 453 Magnesium. {ECO:0000250}. FT METAL 459 459 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 462 462 Magnesium. {ECO:0000250}. FT METAL 463 463 Magnesium. {ECO:0000250}. SQ SEQUENCE 787 AA; 86049 MW; 79CD0310861A366F CRC64; MQFSYSWLKT QADTELSSDK LEHLLTMSGL EVEEAETAAP AFAGVVIAEV KSVEKHPDAD RLNVTRVDAG TGGLVQIVCG APNVKAGIKV PCSLPGAVLP GNFKIKPTKM RGEVSDGMLC STDELGLPDD GVNGLHILPE DAPVGTNIRE YLDLDDTLFT LKITPNRADC LSIKGIAREV SALTGCAFRQ PEIHTAPITG SRKQPVQINA PADCGRFISR VIENVNARAT TPDWMKQRLE RSGIRSISAL VDIGNYVMLE IGQPMHVFDA DKLSGSLHIR RAREGETLEC LNEKTVSLSE NTLVVADEKG VLSLAGLMGG AASAVSDGTQ NIVLEAAWFA PEIIAGKSRQ YGFGSDSSFR FERGVDYRLQ ADAIERATEL VLQICGGAAG EMVEAQGELP EAKQVGLRLD RLKTVLGVDI PAEQVETILQ HLGLQPEKTA EGFRVTAPSF RFDIEIEADL IEEIGRVYGY ENIPDDYTSG RLKMLELPET RRPRFAVYNE MAARGYREVV SYAFVDEQWE QDFAANADPI RLQNPLAAQY AVMRSTLIGG LVEILQNNLN RKQNRVCVFE IARVFSKGSD GQFVQNERIG GLWYGAVMPE QWGGKTRNAD FYDIKADVEN LLKNKAVEFV KTGHPALHPG RAANIVSDGK VIGFVGELHP KWLQKYDLPQ APLVFEIDMA AVLECGKTRY RVVSKFQPVR RDLAFVMPEA MSHDDLLLVL KGAANKLVQE ISVFDVYRGT GLPEGMKSVA VKVILQDMEN TLTDEAVEPL IGKLIGAATA AGARLRS // ID SYV_NEIMB Reviewed; 945 AA. AC Q9K1H7; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004}; DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004}; DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004}; DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004}; GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; GN OrderedLocusNames=NMB0174; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As CC ValRS can inadvertently accommodate and process structurally CC similar amino acids such as threonine, to avoid such errors, it CC has a "posttransfer" editing activity that hydrolyzes mischarged CC Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_02004}. CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- DOMAIN: ValRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated threonine is CC translocated from the active site to the editing site. CC {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for CC aminoacylation activity. {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40631.1; -; Genomic_DNA. DR PIR; F81230; F81230. DR RefSeq; NP_273232.1; NC_003112.2. DR RefSeq; WP_002224777.1; NC_003112.2. DR ProteinModelPortal; Q9K1H7; -. DR STRING; 122586.NMB0174; -. DR PaxDb; Q9K1H7; -. DR EnsemblBacteria; AAF40631; AAF40631; NMB0174. DR GeneID; 902281; -. DR KEGG; nme:NMB0174; -. DR PATRIC; 20355373; VBINeiMen85645_0216. DR eggNOG; ENOG4105CA4; Bacteria. DR eggNOG; COG0525; LUCA. DR HOGENOM; HOG000020094; -. DR KO; K01873; -. DR OMA; SQYRFDL; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; NMEN122586:GHGG-184-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.380; -; 1. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 3. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR010978; tRNA-bd_arm. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR002303; Valyl-tRNA_ligase. DR PANTHER; PTHR11946:SF5; PTHR11946:SF5; 4. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF10458; Val_tRNA-synt_C; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR SUPFAM; SSF46589; SSF46589; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00422; valS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 945 Valine--tRNA ligase. FT /FTId=PRO_0000106235. FT COILED 879 945 {ECO:0000255|HAMAP-Rule:MF_02004}. FT MOTIF 42 52 "HIGH" region. FT MOTIF 552 556 "KMSKS" region. FT BINDING 555 555 ATP. {ECO:0000255|HAMAP-Rule:MF_02004}. SQ SEQUENCE 945 AA; 106685 MW; B29FB68AE37DC38F CRC64; MLDKYNPAEI ESKHYQNWEE QGYFQPDMDL TKPSFSIQLP PPNVTGTLHM GHAFNQTIMD GLTRYYRMKG CNTAWIPGTD HAGIATQIVV ERQLAAQNVS RHDLGREKFL EKVWEWKEVS GGTITQQMRR VGCSADWTRE YFTMDDVRAE TVTEVFVRLY EQGLIYRGKR LVNWDPVLGT AVSDLEVESV EEQGSMWHIR YPLADNPAEA VIVATTRPET LLGDVAVAVN PEDERYTHLI GKELILPLTG RTIPVIADEY VEKDFGTGCV KITPAHDFND YEVGKRHDTR LINVFNLEAK VLANAEVFNF KGEAQLGFAL PEKYAGLDRF AARKQMVADL QEQGFLVEIK PHTLMTPKGD RTGSVIEPML TSQWFVAMSA TPNGGEPDSE FKGLSLADKA KKAVDSGAVR FIPENWVNTY NQWMNNIQDW CISRQLWWGH QIPAWYDNEG NVYVARNQEE AEKQAGKTGL TREEDVLDTW FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKDVY IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI GLEKLLVKRT TGLRKPETAP KVEEATKKLF PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG YGATAAEPRG YSFPDMWIVG RLNQTIEQVT QAYETYRFDL AAETLYSFVW NDYCDWYLEL AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML ARFPEADSGE IVQTAFEQMT VLQDLIGAVR NLRGEMGIQP NVKAPLFVES TDDLADYLKY LPMMTRLTEA QQVAALPESE DAPVAVCNGA RLMLKVEIDK AAETARLSKE AEKLQKALDK LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQNQL AKLKD // ID SYGA_NEIMB Reviewed; 301 AA. AC P67029; Q9JRC6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254}; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254}; GN Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254}; GN OrderedLocusNames=NMB1932; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00254}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00254}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00254}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42261.1; -; Genomic_DNA. DR PIR; E81024; E81024. DR RefSeq; NP_274926.1; NC_003112.2. DR RefSeq; WP_002218046.1; NC_003112.2. DR ProteinModelPortal; P67029; -. DR SMR; P67029; 2-286. DR STRING; 122586.NMB1932; -. DR PaxDb; P67029; -. DR EnsemblBacteria; AAF42261; AAF42261; NMB1932. DR GeneID; 904222; -. DR KEGG; nme:NMB1932; -. DR PATRIC; 20359911; VBINeiMen85645_2460. DR eggNOG; ENOG4107QIB; Bacteria. DR eggNOG; COG0752; LUCA. DR HOGENOM; HOG000264291; -. DR KO; K01878; -. DR OMA; LGSYYQF; -. DR OrthoDB; EOG661H9S; -. DR BioCyc; NMEN122586:GHGG-1989-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR002310; Gly-tRNA_ligase_asu. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR TIGRFAMs; TIGR00388; glyQ; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 301 Glycine--tRNA ligase alpha subunit. FT /FTId=PRO_0000072851. SQ SEQUENCE 301 AA; 34210 MW; 38A5A86552B3197F CRC64; MLTFQQIIFK LQTFWADKGC TVIQPFDMEV GAGTSHPATC LRALGPEPWF AAYVQPSRRP KDGRYGDNPN RLQHYYQFQV ALKPAPANIQ DLYLDSLREL GIDPKVHDIR FVEDDWENPT LGAWGLGWEV WLNGMEVTQF TYFQQVGGID CTPVLGEITY GIERLAMYLQ GVENVYDLVW AKTLDGNTVT YGDVYHQNEV EQSTYNFEYS DADWLLRQFN DYEAQAKRLL AEENAALALP AYELVLKAGH TFNLLDARGA ISVTERATYI GRIRALSRAV AQKYVESREK LGFPLMKANA A // ID SYR_NEIMB Reviewed; 572 AA. AC Q9JYM8; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; GN OrderedLocusNames=NMB1506; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + CC diphosphate + L-arginyl-tRNA(Arg). {ECO:0000255|HAMAP- CC Rule:MF_00123}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00123}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41862.1; -; Genomic_DNA. DR PIR; F81075; F81075. DR RefSeq; NP_274514.1; NC_003112.2. DR RefSeq; WP_002225071.1; NC_003112.2. DR ProteinModelPortal; Q9JYM8; -. DR STRING; 122586.NMB1506; -. DR PaxDb; Q9JYM8; -. DR DNASU; 903953; -. DR EnsemblBacteria; AAF41862; AAF41862; NMB1506. DR GeneID; 903953; -. DR KEGG; nme:NMB1506; -. DR PATRIC; 20358794; VBINeiMen85645_1907. DR eggNOG; ENOG4105C75; Bacteria. DR eggNOG; COG0018; LUCA. DR HOGENOM; HOG000247212; -. DR KO; K01887; -. DR OMA; KLVGNYY; -. DR OrthoDB; EOG6JB13C; -. DR BioCyc; NMEN122586:GHGG-1546-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.30.1360.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR11956; PTHR11956; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF55190; SSF55190; 1. DR TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 572 Arginine--tRNA ligase. FT /FTId=PRO_0000151583. FT MOTIF 122 132 "HIGH" region. SQ SEQUENCE 572 AA; 62802 MW; DA53F495CBB69EA7 CRC64; MNLHQTVEHE AAAAFAAAGI ADSPIVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK VAEALADNAV IESAEVAGPG FINLRLRPEF LAQNIQTALN DARFGVAKTD KPQTVVIDYS SPNLAKEMHV GHLRSSIIGD SISRVLAFMG NTVIRQNHVG DWGTQFGMLV AYLVEQQKDN AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA VYDTLGLKLR PEDVAGESKY NDDLQPVVDD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA FIVQKQGGGF LYASTDLACL RYRIGRLKAD RLLYVVDHRQ ALHFEQLFTT SRKAGYLPEN VGAAFIGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA TALVKEKNPE LGADEAAKIG KTVGIGAVKY ADLSKNRTSD YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDANA PTVLTEPLEK QLAAELLKFE DVLQSVADTA YPHYLAAYLY QIATLFSRFY EACPILKAEG ASRNSRLQLA KLTGDTLKQG LDLLGIDVLD VM // ID SYGB_NEIMB Reviewed; 687 AA. AC Q9JXQ5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255}; DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255}; GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; GN OrderedLocusNames=NMB1930; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00255}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00255}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42259.1; -; Genomic_DNA. DR PIR; E81027; E81027. DR RefSeq; NP_274924.1; NC_003112.2. DR RefSeq; WP_002244319.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ5; -. DR STRING; 122586.NMB1930; -. DR PaxDb; Q9JXQ5; -. DR EnsemblBacteria; AAF42259; AAF42259; NMB1930. DR GeneID; 904225; -. DR KEGG; nme:NMB1930; -. DR PATRIC; 20359907; VBINeiMen85645_2458. DR eggNOG; ENOG4105C38; Bacteria. DR eggNOG; COG0751; LUCA. DR HOGENOM; HOG000264302; -. DR KO; K01879; -. DR OMA; LPIPKRM; -. DR OrthoDB; EOG661H9S; -. DR BioCyc; NMEN122586:GHGG-1987-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR015944; Gly-tRNA-synth_bsu. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR006674; HD_domain. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF02092; tRNA_synt_2f; 1. DR PRINTS; PR01045; TRNASYNTHGB. DR TIGRFAMs; TIGR00211; glyS; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 687 Glycine--tRNA ligase beta subunit. FT /FTId=PRO_0000072916. SQ SEQUENCE 687 AA; 74573 MW; 616BCBDD76A3D4FB CRC64; MMTQTLLIEL LTEELPPKAL NNLGNHFAAS VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV KNVKAVQADQ KIVKKGPAVA NAMKDGAPTK ALEGFARGAG AKIEDLTIVH DGKQDVYAYE YVQIGKPLGG LLEDIINQAV KKLPIPKVMR WGSSTFTFVR PVHGLVVLHG GDIVNVSVLG LQSGNKTLGH RFLSDGEITI ENADSYAAQM REQGKVVASF AERKAAIQTV LEGQARRLNA TAAADEALLD EVTALVEWPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN RFLLVSNLQT EDPSHIIQGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL TNVVYHNKIG SQAERIERLQ SIAAHIAKAL GADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL DGETEEITEA VEQHYQPRFA GDNLPEGKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA LRRAALGILR MLMQYGLDVN ELIQTAFNSF PQGLLNEKTP SETADFMQAR LAVLLQNDYP QDIVAAVLAK QPRRLDDLTA KLQAVAAFKQ LPEAAALAAA NKRVQNLLKK ADAELGAVNE SLLQQDEEKA LFAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA VKQNRLNLLN RLAEQMNAVA DIALLGE // ID SYS_NEIMB Reviewed; 431 AA. AC Q9JY95; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=NMB1684; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also CC able to aminoacylate tRNA(Sec) with serine, to form the CC misacylated tRNA L-seryl-tRNA(Sec), which will be further CC converted into selenocysteinyl-tRNA(Sec). {ECO:0000255|HAMAP- CC Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate CC + L-seryl-tRNA(Ser). {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate CC + L-seryl-tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a CC N-terminal extension that is involved in tRNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Type-1 seryl-tRNA synthetase subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42032.1; -; Genomic_DNA. DR PIR; E81053; E81053. DR RefSeq; NP_274688.1; NC_003112.2. DR RefSeq; WP_002224981.1; NC_003112.2. DR ProteinModelPortal; Q9JY95; -. DR SMR; Q9JY95; 1-428. DR STRING; 122586.NMB1684; -. DR PaxDb; Q9JY95; -. DR EnsemblBacteria; AAF42032; AAF42032; NMB1684. DR GeneID; 903423; -. DR KEGG; nme:NMB1684; -. DR PATRIC; 20359319; VBINeiMen85645_2166. DR eggNOG; ENOG4105CGR; Bacteria. DR eggNOG; COG0172; LUCA. DR HOGENOM; HOG000035938; -. DR KO; K01875; -. DR OMA; YRPERHE; -. DR OrthoDB; EOG61KBH9; -. DR BioCyc; NMEN122586:GHGG-1739-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.40; -; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR11778; PTHR11778; 1. DR Pfam; PF02403; Seryl_tRNA_N; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1. DR PRINTS; PR00981; TRNASYNTHSER. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00414; serS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 431 Serine--tRNA ligase. FT /FTId=PRO_0000122090. FT NP_BIND 268 270 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT NP_BIND 355 358 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT REGION 237 239 Serine binding. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 291 291 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 390 390 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. SQ SEQUENCE 431 AA; 47883 MW; 043CE1BEAA67FB82 CRC64; MLDIQLLRSN TAAVAERLAR RGYDFDTARF DTLEERRKSV QVKTEELQAS RNSISKQIGA LKGQGKHEEA QAAMNQVAQI KTDLEQAAAD LDAVQKELDA WLLSIPNLPH ESVPAGKDET ENVEVRKVGT PREFDFEIKD HVDLGEPLGL DFEGGAKLSG ARFTVMRGQI ARLHRALAQF MLDTHTLQHG YTEHYTPYIV DDTTLQGTGQ LPKFAEDLFH VTRGGDETKT TQYLIPTAEV TLTNTVADSI IPSEQLPLKL TAHSPCFRSE AGSYGKDTRG LIRQHQFDKV EMVQIVHPEK SYETLEEMVG HAENILKALE LPYRVITLCT GDMGFGAAKT YDLEVWVPAQ NTYREISSCS NCEDFQARRL KARFKDENGK NRLVHTLNGS GLAVGRTLVA VLENHQNADG SINIPAALQP YMGGVAKLEV K // ID TAL_NEIMB Reviewed; 351 AA. AC Q9K139; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Transaldolase; DE EC=2.2.1.2; GN Name=tal; OrderedLocusNames=NMB0351; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D- CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative CC stage): step 2/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40794.1; -; Genomic_DNA. DR PIR; E81210; E81210. DR RefSeq; NP_273400.1; NC_003112.2. DR RefSeq; WP_002221981.1; NC_003112.2. DR ProteinModelPortal; Q9K139; -. DR SMR; Q9K139; 1-350. DR STRING; 122586.NMB0351; -. DR PaxDb; Q9K139; -. DR EnsemblBacteria; AAF40794; AAF40794; NMB0351. DR GeneID; 902466; -. DR KEGG; nme:NMB0351; -. DR PATRIC; 20355851; VBINeiMen85645_0444. DR eggNOG; ENOG4107V25; Bacteria. DR eggNOG; COG0176; LUCA. DR HOGENOM; HOG000226074; -. DR KO; K00616; -. DR OMA; GLTSNPT; -. DR OrthoDB; EOG6T1WSN; -. DR BioCyc; NMEN122586:GHGG-372-MONOMER; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00493; Transaldolase_2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR004732; Transaldolase_2. DR InterPro; IPR018225; Transaldolase_AS. DR PANTHER; PTHR10683; PTHR10683; 1. DR Pfam; PF00923; Transaldolase; 1. DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1. DR TIGRFAMs; TIGR00876; tal_mycobact; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Pentose shunt; Reference proteome; KW Schiff base; Transferase. FT CHAIN 1 351 Transaldolase. FT /FTId=PRO_0000173638. FT ACT_SITE 138 138 Schiff-base intermediate with substrate. FT {ECO:0000250}. SQ SEQUENCE 351 AA; 37317 MW; AEB10FDF8CBDDF8B CRC64; MTILSDVKAL GQQIWLDNLS RSLVQSGELA QMLKQGVCGV TSNPAIFQKA FAGDALYADE IAALKQQNLS PKQRYETMAV ADVRAACDVC LAEHESTGGK TGFVSLEVSP ELSKDAQGTV EEARRLYAAI GCKNAMIKVP ATDAGIDALE TLVSDGISVN LTLLFSRAQT LKAYAAYARG IAKRLAAGQS VAHIQVVASF FISRVDGALD TTLPDHLKGK IAIALAKAAY QDWAQYFGSP EFAALETKGA NRVQLLWAST GVKNPAYPDT LYVDSLIGAH TVNTVPDATL KAFIDHGTAK ATLTEGVEEA QAQLAETAAL GIDVETLATR LQEDGLKQFE EAFEKLLAPL A // ID TBPB_NEIMB Reviewed; 712 AA. AC Q9K0V0; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Transferrin-binding protein 2; DE Short=TBP-2; DE Flags: Precursor; GN Name=tbpB; Synonyms=tbp2; OrderedLocusNames=NMB0460; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Acts as a transferrin receptor and is required for CC transferrin utilization. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40897.1; -; Genomic_DNA. DR PIR; E81196; E81196. DR RefSeq; NP_273507.1; NC_003112.2. DR RefSeq; WP_010980796.1; NC_003112.2. DR PDB; 3V8U; X-ray; 2.40 A; A/B=22-711. DR PDBsum; 3V8U; -. DR ProteinModelPortal; Q9K0V0; -. DR DIP; DIP-59654N; -. DR STRING; 122586.NMB0460; -. DR PaxDb; Q9K0V0; -. DR EnsemblBacteria; AAF40897; AAF40897; NMB0460. DR GeneID; 902576; -. DR KEGG; nme:NMB0460; -. DR PATRIC; 20356158; VBINeiMen85645_0600. DR HOGENOM; HOG000220760; -. DR OMA; VNQAAMV; -. DR OrthoDB; EOG6XHC16; -. DR BioCyc; NMEN122586:GHGG-484-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR001677; Solute-bd_prot_TBP-like. DR Pfam; PF01298; Lipoprotein_5; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Receptor; Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 712 Transferrin-binding protein 2. FT /FTId=PRO_0000018193. FT LIPID 21 21 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 21 21 S-diacylglycerol cysteine. {ECO:0000305}. FT STRAND 61 66 {ECO:0000244|PDB:3V8U}. FT TURN 74 77 {ECO:0000244|PDB:3V8U}. FT HELIX 85 87 {ECO:0000244|PDB:3V8U}. FT HELIX 102 109 {ECO:0000244|PDB:3V8U}. FT STRAND 147 149 {ECO:0000244|PDB:3V8U}. FT STRAND 153 172 {ECO:0000244|PDB:3V8U}. FT STRAND 176 192 {ECO:0000244|PDB:3V8U}. FT STRAND 194 199 {ECO:0000244|PDB:3V8U}. FT STRAND 201 212 {ECO:0000244|PDB:3V8U}. FT STRAND 214 216 {ECO:0000244|PDB:3V8U}. FT TURN 220 222 {ECO:0000244|PDB:3V8U}. FT TURN 230 232 {ECO:0000244|PDB:3V8U}. FT STRAND 246 249 {ECO:0000244|PDB:3V8U}. FT STRAND 260 269 {ECO:0000244|PDB:3V8U}. FT TURN 270 273 {ECO:0000244|PDB:3V8U}. FT STRAND 274 284 {ECO:0000244|PDB:3V8U}. FT STRAND 297 304 {ECO:0000244|PDB:3V8U}. FT STRAND 307 314 {ECO:0000244|PDB:3V8U}. FT STRAND 321 323 {ECO:0000244|PDB:3V8U}. FT STRAND 326 328 {ECO:0000244|PDB:3V8U}. FT STRAND 333 342 {ECO:0000244|PDB:3V8U}. FT STRAND 347 353 {ECO:0000244|PDB:3V8U}. FT STRAND 359 365 {ECO:0000244|PDB:3V8U}. FT STRAND 401 403 {ECO:0000244|PDB:3V8U}. FT STRAND 405 411 {ECO:0000244|PDB:3V8U}. FT STRAND 415 419 {ECO:0000244|PDB:3V8U}. FT STRAND 428 431 {ECO:0000244|PDB:3V8U}. FT STRAND 434 438 {ECO:0000244|PDB:3V8U}. FT STRAND 461 466 {ECO:0000244|PDB:3V8U}. FT STRAND 501 506 {ECO:0000244|PDB:3V8U}. FT STRAND 511 520 {ECO:0000244|PDB:3V8U}. FT STRAND 544 553 {ECO:0000244|PDB:3V8U}. FT STRAND 565 580 {ECO:0000244|PDB:3V8U}. FT STRAND 582 585 {ECO:0000244|PDB:3V8U}. FT STRAND 590 601 {ECO:0000244|PDB:3V8U}. FT TURN 602 605 {ECO:0000244|PDB:3V8U}. FT STRAND 606 612 {ECO:0000244|PDB:3V8U}. FT STRAND 620 628 {ECO:0000244|PDB:3V8U}. FT STRAND 631 637 {ECO:0000244|PDB:3V8U}. FT STRAND 660 669 {ECO:0000244|PDB:3V8U}. FT TURN 670 672 {ECO:0000244|PDB:3V8U}. FT STRAND 674 682 {ECO:0000244|PDB:3V8U}. FT STRAND 697 707 {ECO:0000244|PDB:3V8U}. SQ SEQUENCE 712 AA; 77417 MW; 77EA248941E8EF0C CRC64; MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVFSE KPQAQKDQGG YGFAMRLKRR NWYPQAKEDE VKLDESDWEA TGLPDEPKEL PKRQKSVIEK VETDSDNNIY SSPYLKPSNH QNGNTGNGIN QPKNQAKDYE NFKYVYSGWF YKHAKREFNL KVEPKSAKNG DDGYIFYHGK EPSRQLPASG KITYKGVWHF ATDTKKGQKF REIIQPSKSQ GDRYSGFSGD DGEEYSNKNK STLTDGQEGY GFTSNLEVDF HNKKLTGKLI RNNANTDNNQ ATTTQYYSLE AQVTGNRFNG KATATDKPQQ NSETKEHPFV SDSSSLSGGF FGPQGEELGF RFLSDDQKVA VVGSAKTKDK PANGNTAAAS GGTDAAASNG AAGTSSENGK LTTVLDAVEL KLGDKEVQKL DNFSNAAQLV VDGIMIPLLP EASESGNNQA NQGTNGGTAF TRKFDHTPES DKKDAQAGTQ TNGAQTASNT AGDTNGKTKT YEVEVCCSNL NYLKYGMLTR KNSKSAMQAG ESSSQADAKT EQVEQSMFLQ GERTDEKEIP SEQNIVYRGS WYGYIANDKS TSWSGNASNA TSGNRAEFTV NFADKKITGT LTADNRQEAT FTIDGNIKDN GFEGTAKTAE SGFDLDQSNT TRTPKAYITD AKVQGGFYGP KAEELGGWFA YPGDKQTKNA TNASGNSSAT VVFGAKRQQP VR // ID SYK_NEIMB Reviewed; 503 AA. AC Q9JYU6; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00252}; DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252}; DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00252}; DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00252}; GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00252}; GN OrderedLocusNames=NMB1425; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). {ECO:0000255|HAMAP-Rule:MF_00252}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00252}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00252}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00252}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00252}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41786.1; -; Genomic_DNA. DR PIR; C81086; C81086. DR RefSeq; NP_274437.1; NC_003112.2. DR RefSeq; WP_002225120.1; NC_003112.2. DR ProteinModelPortal; Q9JYU6; -. DR SMR; Q9JYU6; 13-502. DR STRING; 122586.NMB1425; -. DR PaxDb; Q9JYU6; -. DR EnsemblBacteria; AAF41786; AAF41786; NMB1425. DR GeneID; 903847; -. DR KEGG; nme:NMB1425; -. DR PATRIC; 20358545; VBINeiMen85645_1784. DR eggNOG; ENOG4105CRK; Bacteria. DR eggNOG; COG1190; LUCA. DR HOGENOM; HOG000236578; -. DR KO; K04567; -. DR OMA; DMMNLTE; -. DR OrthoDB; EOG69PQ2M; -. DR BioCyc; NMEN122586:GHGG-1463-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002313; Lys-tRNA-ligase_II. DR InterPro; IPR018149; Lys-tRNA-synth_II_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR00982; TRNASYNTHLYS. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00499; lysS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 503 Lysine--tRNA ligase. FT /FTId=PRO_0000152659. FT METAL 414 414 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00252}. FT METAL 421 421 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00252}. FT METAL 421 421 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00252}. SQ SEQUENCE 503 AA; 57312 MW; 28CEC5BDA02B46C6 CRC64; MSEQNHPQTE PQLDENQIIA LRREKLHNIR QQRNAYPNDF KRDSFAADLH AQYGEIGKEE LDPQGIPVKV AGRMMLKRQM GKASFATIQD VSGQIQLYLN NKGVSQEVLD DFNHWDLGDI VGAEGTLFKT NHGELTVRVS GIRLLSKSLR PLPDKHKGLS DQETKYRQRY VDLIANEESR NTFIKRSQII QSVRNFMVGE HYLEVETPMM HPIPGGATAK PFVTHHNALD IPLYLRIAPE LYLKRLVVGG LERVFEINRS FRNEGMSVRH NPEFTMIEFY EAFSDYERMM QMAEDIIRNA SRTVNGTANI TYNGKEVDLE SPFERLTILE AIKKYNPHYT DEQLNDAEWL KKEIVKHGES LPPSPGIGSL QLALFEGCAE GKLWNPTFIV DYPVEVSPLA RASDTKQGLT ERFELFVVGR ELANGYSELN DPEDQAERFK AQVVQKDAGD DEAMHYDADY IRAMEFGLPP TGGCGIGIDR LVMLLTDSQT IRDVILFPQM RPE // ID SYM_NEIMB Reviewed; 685 AA. AC Q9K1Q0; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098}; DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098}; DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098}; GN Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; GN OrderedLocusNames=NMB0030; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Is required not only for elongation of protein synthesis CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00098}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40501.1; -; Genomic_DNA. DR PIR; A81246; A81246. DR RefSeq; NP_273096.1; NC_003112.2. DR RefSeq; WP_002225763.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q0; -. DR SMR; Q9K1Q0; 2-556. DR STRING; 122586.NMB0030; -. DR PaxDb; Q9K1Q0; -. DR EnsemblBacteria; AAF40501; AAF40501; NMB0030. DR GeneID; 902133; -. DR KEGG; nme:NMB0030; -. DR PATRIC; 20355009; VBINeiMen85645_0041. DR eggNOG; ENOG4105CKH; Bacteria. DR eggNOG; COG0073; LUCA. DR eggNOG; COG0143; LUCA. DR HOGENOM; HOG000200400; -. DR KO; K01874; -. DR OMA; CHEAARG; -. DR OrthoDB; EOG6CVV9B; -. DR BioCyc; NMEN122586:GHGG-31-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 2.20.28.20; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR023458; Met-tRNA_ligase_1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR029038; MetRS_Zn. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF57770; SSF57770; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 685 Methionine--tRNA ligase. FT /FTId=PRO_0000139146. FT DOMAIN 582 685 tRNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_00098}. FT MOTIF 12 22 "HIGH" region. FT MOTIF 339 343 "KMSKS" region. FT METAL 143 143 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 146 146 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 156 156 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 159 159 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT BINDING 342 342 ATP. {ECO:0000255|HAMAP-Rule:MF_00098}. SQ SEQUENCE 685 AA; 76852 MW; 9C0F39507B1FD50A CRC64; MTRKILVTSA LPYANGSIHL GHMVEHIQTD VWVRFQKLRG HACHYCCADD THGTPVMLAA QKQGIAPEDM IAKVREEHLA DFTGFFIGYD NYYSTHSPEN KQFSQDIYRA LKANGKIESR VIEQLFDPEK QMFLPDRFVK GECPKCHAQD QYGDNCEVCG TTYSPTELIN PYSAVSGTKP ELRESEHFFF KLGECADFLK AWTSGNNPHD GKPHLQAEAL NKMKEWLGEG EETTLSDWDI SRDAPYFGFE IPDAPGKYFY VWLDAPVGYM ASFKNLCDRI GVDFDEYFKA DSQTEMYHFI GKDILYFHAL FWPAMLHFSG HRAPTGVYAH GFLTVDGQKM SKSRGTFITA KSYLEQGLNP EWMRYYIAAK LNSKIEDIDL NLQDFISRVN SDLVGKYVNI AARASGFIAK RFEGRLKDVA DSELLAKLTA QSEAIAECYE SREYAKALRD IMALADIVNE YVDANKPWEL AKQEGQDERL HEVCSELINA FTMLTAYLAP VLPQTAANAA KFLNLEAITW ANTRDTLGKH AINKYEHLMQ RVEQKQVDDL IEANKQSIAA AAAPAAEEGK YEKVAEQASF DDFMKIDMRV AKVLNCEAVE GSTKLLKFDL DFGFEKRIIF SGIAASYPNP AELNGRMVIA VANFAPRKMA KFGVSEGMIL SAATADGKLK LLDVDTGAQP GDKVG // ID SYY_NEIMB Reviewed; 431 AA. AC Q9JXY5; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006}; DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006}; DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006}; GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; GN OrderedLocusNames=NMB1835; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000255|HAMAP- CC Rule:MF_02006}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_02006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42170.1; -; Genomic_DNA. DR PIR; A81037; A81037. DR RefSeq; NP_274832.1; NC_003112.2. DR RefSeq; WP_002225666.1; NC_003112.2. DR ProteinModelPortal; Q9JXY5; -. DR SMR; Q9JXY5; 2-318. DR STRING; 122586.NMB1835; -. DR PaxDb; Q9JXY5; -. DR EnsemblBacteria; AAF42170; AAF42170; NMB1835. DR GeneID; 903265; -. DR KEGG; nme:NMB1835; -. DR PATRIC; 20359675; VBINeiMen85645_2343. DR eggNOG; ENOG4105DA0; Bacteria. DR eggNOG; COG0162; LUCA. DR HOGENOM; HOG000242790; -. DR KO; K01866; -. DR OMA; GKHFPVN; -. DR OrthoDB; EOG6B09VR; -. DR BioCyc; NMEN122586:GHGG-1890-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.290.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type. DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1. DR PANTHER; PTHR11766; PTHR11766; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR TIGRFAMs; TIGR00234; tyrS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome; KW RNA-binding. FT CHAIN 1 431 Tyrosine--tRNA ligase. FT /FTId=PRO_0000234741. FT DOMAIN 353 422 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT MOTIF 39 48 "HIGH" region. FT MOTIF 231 235 "KMSKS" region. FT BINDING 34 34 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 171 171 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 175 175 Tyrosine. {ECO:0000255|HAMAP- FT Rule:MF_02006}. FT BINDING 234 234 ATP. {ECO:0000255|HAMAP-Rule:MF_02006}. SQ SEQUENCE 431 AA; 47254 MW; C4F970F48D51EAC3 CRC64; MSVIQDLQSR GLIAQTTDIE ALDALLNEQK IALYCGFDPT ADSLHIGHLL PVLALRRFQQ AGHTPIALVG GATGMIGDPS FKAAERSLNS AETVAGWVES IRNQLTPFLS FEGGNAAIMA NNADWFGSMN CLDFLRDIGK HFSVNAMLNK ESVKQRIDRD GAGISFTEFA YSLLQGYDFA ELNKRHGAVL EIGGSDQWGN ITAGIDLTRR LHQKQVFGLT LPLVTKSDGT KFGKTEGGAV WLNAKKTSPY QFYQFWLKVA DADVYKFLKY FTFLSIEEID AIEAKDKASG SKPEAQRILA EEMTRLIHGE EALAAAQRIS ESLFAEDQSS LTESDFEQLA LDGLPAFEVS DGINVVEALV KTGLASSNKE ARGFVNSKAV LLNGKPAEAN NPNHAAERPD DACLLNGEHK RFGKYTILRR GKRNHALLVW K // ID TATA_NEIMB Reviewed; 67 AA. AC P66892; P57049; Q4W576; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 61. DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236}; GN Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; GN OrderedLocusNames=NMB0601; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. TatA CC could form the protein-conducting channel of the Tat system. CC {ECO:0000255|HAMAP-Rule:MF_00236}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000255|HAMAP-Rule:MF_00236}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00236}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00236}. CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP- CC Rule:MF_00236}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52136.1; -; Genomic_DNA. DR RefSeq; NP_273645.1; NC_003112.2. DR RefSeq; WP_002214303.1; NC_003112.2. DR STRING; 122586.NMB0601; -. DR PaxDb; P66892; -. DR EnsemblBacteria; AAY52136; AAY52136; NMB0601. DR GeneID; 903198; -. DR KEGG; nme:NMB0601; -. DR PATRIC; 20356487; VBINeiMen85645_0763. DR eggNOG; COG1826; LUCA. DR HOGENOM; HOG000245363; -. DR KO; K03116; -. DR OMA; HKVIDAD; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NMEN122586:GHGG-627-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00236; TatA_E; 1. DR InterPro; IPR003369; TatA/B/E. DR InterPro; IPR006312; TatA/E. DR Pfam; PF02416; MttA_Hcf106; 1. DR TIGRFAMs; TIGR01411; tatAE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 67 Sec-independent protein translocase FT protein TatA. FT /FTId=PRO_0000097948. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00236}. SQ SEQUENCE 67 AA; 7405 MW; A9C9D4558B0FCF55 CRC64; MGSFSLTHWI IVLIIVVLIF GTKKLRNVGK DLGGAVHDFK QGLNEGTDGK EAQKDDVIEH KKDEDKA // ID SYW_NEIMB Reviewed; 336 AA. AC Q9JYQ9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140}; DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140}; DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140}; DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140}; GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; GN OrderedLocusNames=NMB1471; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + CC diphosphate + L-tryptophyl-tRNA(Trp). {ECO:0000255|HAMAP- CC Rule:MF_00140}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00140}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41828.1; -; Genomic_DNA. DR PIR; B81081; B81081. DR RefSeq; NP_274480.1; NC_003112.2. DR RefSeq; WP_002225097.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ9; -. DR STRING; 122586.NMB1471; -. DR PaxDb; Q9JYQ9; -. DR EnsemblBacteria; AAF41828; AAF41828; NMB1471. DR GeneID; 903893; -. DR KEGG; nme:NMB1471; -. DR PATRIC; 20358707; VBINeiMen85645_1863. DR eggNOG; ENOG4105C31; Bacteria. DR eggNOG; COG0180; LUCA. DR HOGENOM; HOG000059939; -. DR KO; K01867; -. DR OMA; WYLSCFF; -. DR OrthoDB; EOG686NJQ; -. DR BioCyc; NMEN122586:GHGG-1511-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type. DR PANTHER; PTHR10055; PTHR10055; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR TIGRFAMs; TIGR00233; trpS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 336 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136654. FT MOTIF 12 20 "HIGH" region. FT MOTIF 203 207 "KMSKS" region. FT BINDING 206 206 ATP. {ECO:0000255|HAMAP-Rule:MF_00140}. SQ SEQUENCE 336 AA; 37616 MW; 0AE32C8C00B621AA CRC64; MSKKRVLTGV TTTGIPHLGN YVGAIRPAVR AAQNLDTESF LFLADYHGII KCHEPEMIHQ STQAVAATWL ACGLDPERTT FYRQSDTPEV MELNWILTCI TAKGLMNRAH AYKAAVQANA ENGQEDPDFG VEMGLFSYPI LMTADILMFN ANEVPVGRDQ IQHVEMARDI AGRFNHRFRE LFTLPEVKID ENVELLVGLD GRKMSKSYGN TIPLWENDKK TQKSVNKIIT NMKEPGEPKQ PDESPLFEIY KAFSTPSETV EFTKMLADGL AWGEAKKLLA AKINAELAEP RERYNELTAD PSQIEEILQA GAAKARKEAR ELLDKVRDAV GIRPLK // ID TBP1_NEIMB Reviewed; 915 AA. AC Q9K0U9; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Transferrin-binding protein 1; DE Flags: Precursor; GN Name=tbp1; OrderedLocusNames=NMB0461; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Acts as a transferrin receptor and is required for CC transferrin utilization. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40898.1; -; Genomic_DNA. DR PIR; F81196; F81196. DR RefSeq; NP_273508.1; NC_003112.2. DR RefSeq; WP_010980797.1; NC_003112.2. DR PDB; 3V89; X-ray; 3.10 A; A=25-915. DR PDB; 3V8X; X-ray; 2.60 A; A=25-915. DR PDBsum; 3V89; -. DR PDBsum; 3V8X; -. DR ProteinModelPortal; Q9K0U9; -. DR DIP; DIP-59653N; -. DR STRING; 122586.NMB0461; -. DR PaxDb; Q9K0U9; -. DR EnsemblBacteria; AAF40898; AAF40898; NMB0461. DR GeneID; 902577; -. DR KEGG; nme:NMB0461; -. DR PATRIC; 20356160; VBINeiMen85645_0601. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000219090; -. DR KO; K16087; -. DR OMA; TFAYNRV; -. DR OrthoDB; EOG6HB9KP; -. DR BioCyc; NMEN122586:GHGG-485-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 4. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010916; TonB_box_CS. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010948; TonB_lacto/transferrin_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR TIGRFAMs; TIGR01776; TonB-tbp-lbp; 1. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Membrane; KW Receptor; Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1 24 {ECO:0000250}. FT CHAIN 25 915 Transferrin-binding protein 1. FT /FTId=PRO_0000349889. FT MOTIF 38 45 TonB box. FT MOTIF 898 915 TonB C-terminal box. FT TURN 56 59 {ECO:0000244|PDB:3V8X}. FT STRAND 60 64 {ECO:0000244|PDB:3V8X}. FT HELIX 65 71 {ECO:0000244|PDB:3V8X}. FT HELIX 76 79 {ECO:0000244|PDB:3V8X}. FT TURN 80 82 {ECO:0000244|PDB:3V8X}. FT STRAND 86 90 {ECO:0000244|PDB:3V8X}. FT STRAND 92 94 {ECO:0000244|PDB:3V8X}. FT STRAND 96 101 {ECO:0000244|PDB:3V8X}. FT HELIX 106 108 {ECO:0000244|PDB:3V8X}. FT STRAND 109 113 {ECO:0000244|PDB:3V8X}. FT HELIX 145 147 {ECO:0000244|PDB:3V8X}. FT STRAND 148 156 {ECO:0000244|PDB:3V8X}. FT HELIX 159 162 {ECO:0000244|PDB:3V8X}. FT STRAND 167 175 {ECO:0000244|PDB:3V8X}. FT HELIX 178 180 {ECO:0000244|PDB:3V8X}. FT STRAND 187 197 {ECO:0000244|PDB:3V8X}. FT HELIX 198 200 {ECO:0000244|PDB:3V8X}. FT STRAND 202 213 {ECO:0000244|PDB:3V8X}. FT STRAND 216 228 {ECO:0000244|PDB:3V8X}. FT HELIX 234 236 {ECO:0000244|PDB:3V89}. FT STRAND 239 243 {ECO:0000244|PDB:3V8X}. FT STRAND 246 250 {ECO:0000244|PDB:3V8X}. FT STRAND 257 260 {ECO:0000244|PDB:3V8X}. FT HELIX 261 263 {ECO:0000244|PDB:3V8X}. FT STRAND 266 268 {ECO:0000244|PDB:3V89}. FT HELIX 269 272 {ECO:0000244|PDB:3V8X}. FT STRAND 280 284 {ECO:0000244|PDB:3V8X}. FT STRAND 287 290 {ECO:0000244|PDB:3V8X}. FT TURN 291 293 {ECO:0000244|PDB:3V8X}. FT STRAND 296 298 {ECO:0000244|PDB:3V8X}. FT STRAND 305 314 {ECO:0000244|PDB:3V8X}. FT STRAND 317 319 {ECO:0000244|PDB:3V8X}. FT TURN 321 324 {ECO:0000244|PDB:3V89}. FT STRAND 325 341 {ECO:0000244|PDB:3V8X}. FT HELIX 351 361 {ECO:0000244|PDB:3V8X}. FT TURN 365 368 {ECO:0000244|PDB:3V8X}. FT HELIX 375 378 {ECO:0000244|PDB:3V89}. FT STRAND 380 382 {ECO:0000244|PDB:3V8X}. FT STRAND 384 386 {ECO:0000244|PDB:3V89}. FT STRAND 388 390 {ECO:0000244|PDB:3V8X}. FT STRAND 393 415 {ECO:0000244|PDB:3V8X}. FT STRAND 417 419 {ECO:0000244|PDB:3V89}. FT STRAND 424 450 {ECO:0000244|PDB:3V8X}. FT STRAND 465 488 {ECO:0000244|PDB:3V8X}. FT STRAND 494 527 {ECO:0000244|PDB:3V8X}. FT STRAND 533 535 {ECO:0000244|PDB:3V8X}. FT STRAND 547 560 {ECO:0000244|PDB:3V8X}. FT STRAND 563 566 {ECO:0000244|PDB:3V8X}. FT STRAND 575 592 {ECO:0000244|PDB:3V8X}. FT TURN 593 595 {ECO:0000244|PDB:3V8X}. FT STRAND 596 610 {ECO:0000244|PDB:3V8X}. FT STRAND 612 614 {ECO:0000244|PDB:3V89}. FT STRAND 620 632 {ECO:0000244|PDB:3V8X}. FT STRAND 635 649 {ECO:0000244|PDB:3V8X}. FT HELIX 653 657 {ECO:0000244|PDB:3V8X}. FT STRAND 673 686 {ECO:0000244|PDB:3V8X}. FT STRAND 689 742 {ECO:0000244|PDB:3V8X}. FT STRAND 756 771 {ECO:0000244|PDB:3V8X}. FT STRAND 775 779 {ECO:0000244|PDB:3V8X}. FT STRAND 790 798 {ECO:0000244|PDB:3V8X}. FT STRAND 802 813 {ECO:0000244|PDB:3V8X}. FT HELIX 818 821 {ECO:0000244|PDB:3V8X}. FT STRAND 822 826 {ECO:0000244|PDB:3V8X}. FT STRAND 828 830 {ECO:0000244|PDB:3V8X}. FT STRAND 832 837 {ECO:0000244|PDB:3V8X}. FT STRAND 845 856 {ECO:0000244|PDB:3V8X}. FT STRAND 859 870 {ECO:0000244|PDB:3V8X}. FT HELIX 877 880 {ECO:0000244|PDB:3V8X}. FT HELIX 881 883 {ECO:0000244|PDB:3V8X}. FT HELIX 897 900 {ECO:0000244|PDB:3V8X}. FT STRAND 905 915 {ECO:0000244|PDB:3V8X}. SQ SEQUENCE 915 AA; 102107 MW; 110A3F38A59287D5 CRC64; MQQQHLFRFN ILCLSLMTAL PAYAENVQAG QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK LVKSSDTLSK EQVLNIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVS LTVDGVSQIQ SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSV EQGSGALAGS VAFQTKTADD VIGEGRQWGI QSKTAYSGKN RGLTQSIALA GRIGGAEALL IHTGRRAGEI RAHEDAGRGV QSFNRLVPVE DSSNYAYFIV KEECKNGSYE TCKANPKKDV VGKDERQTVS TRDYTGPNRF LADPLSYESR SWLFRPGFRF ENKRHYIGGI LEHTQQTFDT RDMTVPAFLT KAVFDANKKQ AGSLPGNGKY AGNHKYGGLF TNGENGALVG AEYGTGVFYD ETHTKSRYGL EYVYTNADKD TWADYARLSY DRQGIGLDNH FQQTHCSADG SDKYCRPSAD KPFSYYKSDR VIYGESHRLL QAAFKKSFDT AKIRHNLSVN LGFDRFGSNL RHQDYYYQHA NRAYSSNTPP QNNGKKISPN GSETSPYWVT IGRGNVVTGQ ICRLGNNTYT DCTPRSINGK SYYAAVRDNV RLGRWADVGA GLRYDYRSTH SDDGSVSTGT HRTLSWNAGI VLKPTDWLDL TYRTSTGFRL PSFAEMYGWR AGVQSKAVKI DPEKSFNKEA GIVFKGDFGN LEASWFNNAY RDLIVRGYEA QIKDGKEEAK GDPAYLNAQS ARITGINILG KIDWNGVWDK LPEGWYSTFA YNRVRVRDIK KRADRTDIQS HLFDAIQPSR YVVGLGYDQP EGKWGVNGML TYSKAKEITE LLGSRALLNG NSRNTKATAR RTRPWYIVDV SGYYTVKKHF TLRAGVYNLL NYRYVTWENV RQTAGGAVNQ HKNVGVYNRY AAPGRNYTFS LEMKF // ID SYT_NEIMB Reviewed; 637 AA. AC Q9K095; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184}; DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184}; DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184}; DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184}; GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; GN OrderedLocusNames=NMB0720; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). {ECO:0000255|HAMAP- CC Rule:MF_00184}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00184}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00184}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41133.1; -; Genomic_DNA. DR PIR; E81167; E81167. DR RefSeq; NP_273762.1; NC_003112.2. DR RefSeq; WP_002225463.1; NC_003112.2. DR ProteinModelPortal; Q9K095; -. DR SMR; Q9K095; 4-630. DR STRING; 122586.NMB0720; -. DR PaxDb; Q9K095; -. DR EnsemblBacteria; AAF41133; AAF41133; NMB0720. DR GeneID; 902833; -. DR KEGG; nme:NMB0720; -. DR PATRIC; 20356795; VBINeiMen85645_0918. DR eggNOG; ENOG4105C22; Bacteria. DR eggNOG; COG0441; LUCA. DR HOGENOM; HOG000003880; -. DR KO; K01868; -. DR OMA; FYYDFAY; -. DR OrthoDB; EOG61KBFJ; -. DR BioCyc; NMEN122586:GHGG-749-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00184; Thr_tRNA_synth; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF02824; TGS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 637 Threonine--tRNA ligase. FT /FTId=PRO_0000101016. FT REGION 242 533 Catalytic. FT METAL 333 333 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00184}. FT METAL 384 384 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00184}. FT METAL 510 510 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00184}. SQ SEQUENCE 637 AA; 72691 MW; 7A6B45C2B7412CFA CRC64; MLNITLPDGS VRQYESPVTV AQIAASIGAG LAKATVAGRV NGKLVDACDP IVEDSAVQII TPKDQEGIEI IRHSCAHLVG HAVKQLYPNA KMVIGPVIEE GFYYDIATEK PFTPEDVAAI EARMKELIAQ DYDVVKIMTP RAEAIKIFQE RGEEYKLRLI DDMPEVEAMG MYHHQEYVDM CRGPHVPNTR FLKNFKLTKL AGAYWRGDSN NEMLQRIYGT AWATKDELKA YIQRIEEAEK RDHRKLGKQL DLFHLQDEAP GMVFWHPKGW ALWQVIEQHM RKELNAAGYK EVKTPQIMDK TFWEKSGHWD NYKDNMFVTS SEKREYAVKP MNCPGHVQIF NNGLRSYRDL PMRLAEFGSC HRNEPSGALH GLMRVRGFVQ DDAHIFCTED QIVSEARAFN ELLIRIYKQF GFHDVSVKLS LRPEKRAGSD DVWDKAEQGL REALTACGVE WGELPGEGAF YGPKIEYHVR DALGRSWQCG TLQLDFVLPE RLNAEYVTEN NDRARPVMLH RAILGSLERF IGILIENHAG SFPLWLAPVQ LVIMNITENQ ADYCREVAAK LQAAGFRAEL DLRNEKIGYK IRDNSQYRFP YQIVVGDKEK QENKVAVRRK AEDLGSLDLD DFIAQLQQEI TDALVNH // ID TATB_NEIMB Reviewed; 228 AA. AC Q9K0J6; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237}; GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; GN OrderedLocusNames=NMB0600; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. CC Together with TatC, TatB is part of a receptor directly CC interacting with Tat signal peptides. TatB may form an oligomeric CC binding site that transiently accommodates folded Tat precursor CC proteins before their translocation. {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000255|HAMAP-Rule:MF_00237}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00237}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41028.1; -; Genomic_DNA. DR PIR; E81181; E81181. DR RefSeq; NP_273644.1; NC_003112.2. DR RefSeq; WP_002222848.1; NC_003112.2. DR STRING; 122586.NMB0600; -. DR PaxDb; Q9K0J6; -. DR EnsemblBacteria; AAF41028; AAF41028; NMB0600. DR GeneID; 902715; -. DR KEGG; nme:NMB0600; -. DR PATRIC; 20356485; VBINeiMen85645_0762. DR eggNOG; ENOG4105X8U; Bacteria. DR eggNOG; COG1826; LUCA. DR HOGENOM; HOG000027889; -. DR KO; K03117; -. DR OMA; HAAGTHP; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NMEN122586:GHGG-626-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00237; TatB; 1. DR InterPro; IPR003369; TatA/B/E. DR InterPro; IPR018448; TatB. DR InterPro; IPR003998; TatB-like. DR Pfam; PF02416; MttA_Hcf106; 1. DR PRINTS; PR01506; TATBPROTEIN. DR TIGRFAMs; TIGR01410; tatB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 228 Sec-independent protein translocase FT protein TatB. FT /FTId=PRO_0000192663. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00237}. SQ SEQUENCE 228 AA; 25060 MW; C54BE0573B68EC63 CRC64; MFDFGLGELV FVGIIALIVL GPERLPEAAR TAGRLIGRLQ RFVGSVKQEF DTQIELEELR KAKQEFEAAA AQVRDSLKET GTDMEGNLHD ISDGLKPWEK LPEQRTPADF GVDENGNPLP DAANTLSDGI SDVMPSERSY ASAETLGDSG QTGSTAEPAE TDQDRAWREY LTASAAAPVV QTVEVSYIDT AVETPVPHTT SLRKQAISRK RDFRPKHRAK PKLRVRKS // ID THIC_NEIMB Reviewed; 633 AA. AC Q9JXI0; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089}; GN Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089}; GN OrderedLocusNames=NMB2040; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + CC formate + CO. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00089}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000255|HAMAP-Rule:MF_00089}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP- CC Rule:MF_00089}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42361.1; -; Genomic_DNA. DR PIR; E81012; E81012. DR RefSeq; NP_275031.1; NC_003112.2. DR RefSeq; WP_002244346.1; NC_003112.2. DR ProteinModelPortal; Q9JXI0; -. DR STRING; 122586.NMB2040; -. DR PaxDb; Q9JXI0; -. DR EnsemblBacteria; AAF42361; AAF42361; NMB2040. DR GeneID; 904053; -. DR KEGG; nme:NMB2040; -. DR PATRIC; 20360220; VBINeiMen85645_2611. DR eggNOG; ENOG4105CBF; Bacteria. DR eggNOG; COG0422; LUCA. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; TWELFRD; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; NMEN122586:GHGG-2102-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR002817; ThiC. DR InterPro; IPR025747; ThiC-associated_dom. DR Pfam; PF13667; ThiC-associated; 1. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis; KW Zinc. FT CHAIN 1 633 Phosphomethylpyrimidine synthase. FT /FTId=PRO_0000152818. FT REGION 359 361 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT REGION 400 403 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT METAL 443 443 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 507 507 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 587 587 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 590 590 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 595 595 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT BINDING 245 245 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 274 274 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 303 303 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 339 339 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 439 439 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 466 466 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. SQ SEQUENCE 633 AA; 71045 MW; 92BFC40C25EA41D6 CRC64; MTTPKKTAKT SGNEARELAD LSEDIGICFK YPNSERVYLQ GSRDDIRVPL REIRQDDTYT AQGTEANPPI PVYDTSGVYG DPAAHIDLKQ GLPHIRTAWL DERGDTEILP KLSSEYGIER AHDPKTAHLR FNQITRPRRA KSGSNVTQLH YARQGIITPE MEFVAIRERL KLDELSQKPE YAKLLEQHAG QSFGANIPTH PDQITPEFVR QEIAAGRAII PANINHPELE PMIIGRNFRV KINGNLGNSA VTSSLTEEVE KMVWSLRWGA DTIMDLSTGA HIHETREWII RNAPVPIGTV PIYQALEKTG GIAEDLTWDL FRDTLIEQAE QGVDYFTIHA GVLLRYVPMT ANRLTGIVSR GGSIMAKWCL AHHRENFLYT HFDEICEIMK AYDVSFSLGD GLRPGCIADA NDESQFAELH TLGELTDKAW KHDVQVMIEG PGHVPLQRVK ENMTEELQHC FEAPFYTLGP LVTDIAPGYD HITSGIGAAN IGWYGTAMLC YVTPKEHLGL PDKEDVRTGI ITYKLAAHAA DLAKGWPGAQ LRDNALSKAR FEFRWRDQFR LSLDPERAES FHDETLPAEG AKIAHFCSMC GPKFCSMKIT QEVRDYADKQ KAQRQGMEEK AVEFVKKGAK IYS // ID THIG_NEIMB Reviewed; 262 AA. AC Q9JXF5; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00443}; DE EC=2.8.1.10 {ECO:0000255|HAMAP-Rule:MF_00443}; GN Name=thiG {ECO:0000255|HAMAP-Rule:MF_00443}; GN OrderedLocusNames=NMB2071; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- CC phosphate (DXP) to produce the thiazole phosphate moiety of CC thiamine. Sulfur is provided by the thiocarboxylate moiety of the CC carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. CC {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 2- CC iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] CC = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl CC phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or CC ThiS. {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00443}. CC -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000255|HAMAP- CC Rule:MF_00443}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42390.1; -; Genomic_DNA. DR PIR; F81008; F81008. DR RefSeq; NP_275061.1; NC_003112.2. DR RefSeq; WP_002221723.1; NC_003112.2. DR ProteinModelPortal; Q9JXF5; -. DR STRING; 122586.NMB2071; -. DR PaxDb; Q9JXF5; -. DR EnsemblBacteria; AAF42390; AAF42390; NMB2071. DR GeneID; 903997; -. DR KEGG; nme:NMB2071; -. DR PATRIC; 20360302; VBINeiMen85645_2651. DR eggNOG; ENOG4105CA8; Bacteria. DR eggNOG; COG2022; LUCA. DR HOGENOM; HOG000248049; -. DR KO; K03149; -. DR OMA; AQYPSPA; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NMEN122586:GHGG-2134-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0036355; F:2-iminoacetate synthase activity; IEA:InterPro. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00443; ThiG; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR008867; ThiG. DR SUPFAM; SSF110399; SSF110399; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Schiff base; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 262 Thiazole synthase. FT /FTId=PRO_0000162835. FT REGION 185 186 DXP binding. {ECO:0000255|HAMAP- FT Rule:MF_00443}. FT REGION 207 208 DXP binding. {ECO:0000255|HAMAP- FT Rule:MF_00443}. FT ACT_SITE 97 97 Schiff-base intermediate with DXP. FT {ECO:0000255|HAMAP-Rule:MF_00443}. FT BINDING 158 158 DXP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00443}. SQ SEQUENCE 262 AA; 28067 MW; 15DD6603380324A9 CRC64; MLTLYGETFP SRLLLGTAAY PTPEILKQSI QTAQPAMITV SLRRAGSGGE AHGQGFWSLL QETGVPVLPN TAGCQSVQEA VTTAQMAREV FETDWIKLEL IGDDDTLQPD VFQLVEAAEI LIKDGFKVLP YCTEDLIACR RLLDAGCQAL MPWAAPIGTG LGAVHAYALN VLRERLPDTP LIIDAGLGLP SQAAQVMEWG FDGVLLNTAV SRSGDPVNMA RAFALAVESG RLAFEAGPVE ARDKAQASTP TVGQPFWHSA EY // ID TIG_NEIMB Reviewed; 437 AA. AC Q9JZ37; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=NMB1313; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by CC maintaining the newly synthesized protein in an open conformation. CC Functions as a peptidyl-prolyl cis-trans isomerase (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to CC the ribosome near the polypeptide exit tunnel while the other half CC is free in the cytoplasm. {ECO:0000250}. CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, CC the middle domain has PPIase activity, while the C-terminus has CC intrinsic chaperone activity on its own. {ECO:0000250}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41688.1; -; Genomic_DNA. DR PIR; G81098; G81098. DR RefSeq; NP_274332.1; NC_003112.2. DR RefSeq; WP_002225166.1; NC_003112.2. DR ProteinModelPortal; Q9JZ37; -. DR STRING; 122586.NMB1313; -. DR PaxDb; Q9JZ37; -. DR EnsemblBacteria; AAF41688; AAF41688; NMB1313. DR GeneID; 903735; -. DR KEGG; nme:NMB1313; -. DR PATRIC; 20358271; VBINeiMen85645_1647. DR eggNOG; ENOG4105DEA; Bacteria. DR eggNOG; COG0544; LUCA. DR HOGENOM; HOG000218239; -. DR KO; K03545; -. DR OMA; FRNDATK; -. DR OrthoDB; EOG63VBX3; -. DR BioCyc; NMEN122586:GHGG-1351-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3120.10; -; 1. DR Gene3D; 3.30.70.1050; -; 1. DR HAMAP; MF_00303; Trigger_factor_Tig; 1. DR InterPro; IPR001179; PPIase_FKBP_dom. DR InterPro; IPR005215; Trig_fac. DR InterPro; IPR008880; Trigger_fac_C. DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF00254; FKBP_C; 1. DR Pfam; PF05698; Trigger_C; 1. DR Pfam; PF05697; Trigger_N; 1. DR PIRSF; PIRSF003095; Trigger_factor; 1. DR SUPFAM; SSF102735; SSF102735; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR TIGRFAMs; TIGR00115; tig; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm; KW Isomerase; Reference proteome; Rotamase. FT CHAIN 1 437 Trigger factor. FT /FTId=PRO_0000179394. FT DOMAIN 163 248 PPIase FKBP-type. SQ SEQUENCE 437 AA; 48325 MW; C5AF247504A86CAF CRC64; MMSVTVETLE NLERKVVLSL PWSEINAETD KKLKQTQRRA KIDGFRPGKA PLKMIAQMYG ASAQNDVINE LVQRRFYDVA VAQELKVAGF PRFEGVEEQD DKESFKVAAI FEVFPEVVIG DLSAQEVEKV TASVGDAEVD QTVEILRKQR TRFNHVEREA RNGDRVIIDF EGKIDGEPFA GGASKNYAFV LGASQMLPEF EAGVVGMKAG ESKDVTVNFP EDYHGKDVAG KTAVFTITLN NVSEATLPEV DADFAKALGI ADGDVAKMRE EVQKNVSREV ERRVNEQTKE SVMNALLKAV ELKAPVALVN EEAARLANEM KQNFVNQGMA DAANLDLPLD MFKEQAERRV SLGLILAKLV DENKLEPTEE QIKAVVANFA ESYEDPQEVI DWYYADPSRL QAPTSLAVES NVVDFVLGKA KVNEKALSFD EVMGAQA // ID TGT_NEIMB Reviewed; 371 AA. AC Q9K096; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168}; DE EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168}; DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168}; DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168}; GN Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168}; OrderedLocusNames=NMB0719; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7- CC deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His CC and -Tyr). After this exchange, a cyclopentendiol moiety is CC attached to the 7-aminomethyl group of 7-deazaguanine, resulting CC in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). CC {ECO:0000255|HAMAP-Rule:MF_00168}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) CC in tRNA + guanine. {ECO:0000255|HAMAP-Rule:MF_00168}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7- CC carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. CC {ECO:0000255|HAMAP-Rule:MF_00168}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00168}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00168}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00168}. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_00168}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41132.1; -; Genomic_DNA. DR PIR; D81167; D81167. DR RefSeq; NP_273761.1; NC_003112.2. DR RefSeq; WP_002225464.1; NC_003112.2. DR ProteinModelPortal; Q9K096; -. DR SMR; Q9K096; 2-364. DR STRING; 122586.NMB0719; -. DR PaxDb; Q9K096; -. DR EnsemblBacteria; AAF41132; AAF41132; NMB0719. DR GeneID; 902831; -. DR KEGG; nme:NMB0719; -. DR PATRIC; 20356791; VBINeiMen85645_0917. DR eggNOG; ENOG4105C6U; Bacteria. DR eggNOG; COG0343; LUCA. DR HOGENOM; HOG000223473; -. DR KO; K00773; -. DR OMA; MGVGKPD; -. DR OrthoDB; EOG6SNDVG; -. DR BioCyc; NMEN122586:GHGG-747-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Metal-binding; KW Queuosine biosynthesis; Reference proteome; Transferase; KW tRNA processing; Zinc. FT CHAIN 1 371 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_0000135496. FT ACT_SITE 90 90 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00168}. FT METAL 303 303 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}. FT METAL 305 305 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}. FT METAL 308 308 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}. FT METAL 334 334 Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}. FT BINDING 91 91 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00168}. SQ SEQUENCE 371 AA; 41945 MW; 8492FEEBAE577D43 CRC64; MLKFTLHKKD GLARRGTLEL NHGKIETPVF MPVGTYGSVK AMNPQNLHDI KAQIILGNTY HLWLRPGLEV IGQFGGLHGF IGWDKPILTD SGGFQVFSLS DMRKLTEEGC TFKSPINGDK LFLSPEISMK IQTVLNSDIA MQLDECTPGE ATREQARKSL QMSLRWAERS KKAFEDLKNP NALFGIVQGA MYEDLREESL RGLEQFDFPG LAVGGLSVGE PKPEMYRMLR AVGPILPEHK PHYLMGVGTP EDLVYGVAHG IDMFDCVMPT RNARNGWLFT RFGDLKIKNA KHKLDKRPID ESCTCYACQN FSRAYLHHLH RTGEILGAQL NTIHNLHFYQ VIMAEMREAV EQGKFADWQA RFHENRARGT D // ID TILS_NEIMB Reviewed; 426 AA. AC Q4W568; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161}; DE EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161}; DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161}; DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161}; GN Name=tilS1 {ECO:0000255|HAMAP-Rule:MF_01161}; GN OrderedLocusNames=NMB1140; GN and GN Name=tilS2 {ECO:0000255|HAMAP-Rule:MF_01161}; GN OrderedLocusNames=NMB1178; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 CC of the AUA codon-specific tRNA(Ile) that contains the anticodon CC CAU, in an ATP-dependent manner. Cytidine is converted to CC lysidine, thus changing the amino acid specificity of the tRNA CC from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- CATALYTIC ACTIVITY: (tRNA(Ile2))-cytidine(34) + L-lysine + ATP = CC (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS CC motif, predicted to be a P-loop motif involved in ATP binding. CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52148.1; -; Genomic_DNA. DR EMBL; AE002098; AAY52164.1; -; Genomic_DNA. DR RefSeq; WP_002222469.1; NC_003112.2. DR RefSeq; YP_338291.1; NC_003112.2. DR RefSeq; YP_338292.1; NC_003112.2. DR ProteinModelPortal; Q4W568; -. DR STRING; 122586.NMB1178; -. DR PaxDb; Q4W568; -. DR EnsemblBacteria; AAY52148; AAY52148; NMB1178. DR EnsemblBacteria; AAY52164; AAY52164; NMB1140. DR GeneID; 903561; -. DR GeneID; 903598; -. DR KEGG; nme:NMB1140; -. DR KEGG; nme:NMB1178; -. DR PATRIC; 20357855; VBINeiMen85645_1443. DR eggNOG; ENOG4105D3U; Bacteria. DR eggNOG; COG0037; LUCA. DR HOGENOM; HOG000220745; -. DR KO; K04075; -. DR OMA; DAFEQCL; -. DR OrthoDB; EOG6NKR0V; -. DR BioCyc; NMEN122586:GHGG-1176-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1213-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1. DR InterPro; IPR012796; Lysidine-tRNA-synth_C. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR012094; tRNA_Ile_lys_synt. DR InterPro; IPR012795; tRNA_Ile_lys_synt_N. DR InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd. DR PANTHER; PTHR11807:SF2; PTHR11807:SF2; 1. DR Pfam; PF01171; ATP_bind_3; 1. DR Pfam; PF09179; TilS; 1. DR SMART; SM00977; TilS_C; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1. DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 426 tRNA(Ile)-lysidine synthase. FT /FTId=PRO_0000181734. FT NP_BIND 19 24 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 426 AA; 47732 MW; 623B51BCD8212A9E CRC64; MKDCFPQGLN GKKTAVALSG GLDSVVLLHL LVRAGKKGGF IPDALHIHHG LSPRADDWAD FCQNYCDMLG VGLETVKVCV EKNGLGIEAA ARQKRYAAFA EKGFDVLALA HHRDDQIETF MLAVARGGGL RALAAMPAVR PFGEKGIIWR PLLPFSRQDI WDYAQKHGLP NIEDESNTDT AYLRNRFRHR ILPELSAQIP HFGRHVLNNV RALQEDLALL DEVVVQDCRW VCGAGYFDTA RWLTFSPRRK THILRHFLKE NGIPVPNQNA LADIARVLTE AKTGRWNLQG FELHHYAGRL FVFRLEKTDK LRFLKDRQIS GNLREILTGQ GFVLKRHPFG LPEHLLEQDG ILRTVAASDT LAMGGIHKDV KKILQGKRVL PVLRPIWPLV ADSGNRPLAL ANCCADFQYS VSDGILPVHP DFPILF // ID THIE_NEIMB Reviewed; 205 AA. AC Q9JXF7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 89. DE RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TPS {ECO:0000255|HAMAP-Rule:MF_00097}; DE EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_00097}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_00097}; GN Name=thiE {ECO:0000255|HAMAP-Rule:MF_00097}; GN OrderedLocusNames=NMB2069; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate CC = diphosphate + thiamine phosphate + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + CC thiamine phosphate + CO(2). {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00097}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00097}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00097}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42388.1; -; Genomic_DNA. DR PIR; A81011; A81011. DR RefSeq; NP_275059.1; NC_003112.2. DR RefSeq; WP_002225708.1; NC_003112.2. DR ProteinModelPortal; Q9JXF7; -. DR STRING; 122586.NMB2069; -. DR PaxDb; Q9JXF7; -. DR EnsemblBacteria; AAF42388; AAF42388; NMB2069. DR GeneID; 904001; -. DR KEGG; nme:NMB2069; -. DR PATRIC; 20360298; VBINeiMen85645_2649. DR eggNOG; ENOG4108UV6; Bacteria. DR eggNOG; COG0352; LUCA. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; DSVEWIA; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN122586:GHGG-2132-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 205 Thiamine-phosphate synthase. FT /FTId=PRO_0000157030. FT REGION 34 38 HMP-PP binding. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT REGION 131 133 THZ-P binding. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT METAL 67 67 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT METAL 86 86 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 66 66 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 105 105 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 134 134 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 163 163 THZ-P; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00097}. SQ SEQUENCE 205 AA; 21605 MW; 7DAC8AFBD9AD2D26 CRC64; MTFPPLKSPL KFYAVVPTAD WVGRMVKAGA DTVQLRCKAL HGDELKREIA RCAAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALSVHP SYIASGAIFP TTTKQMPTAP QGLDKLREYV KQAGGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID TONB_NEIMB Reviewed; 280 AA. AC P57004; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Protein TonB; GN Name=tonB; OrderedLocusNames=NMB1730; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Interacts with outer membrane receptor proteins that CC carry out high-affinity binding and energy dependent uptake into CC the periplasmic space of specific substrates. It could act to CC transduce energy from the cytoplasmic membrane to specific energy- CC requiring processes in the outer membrane, resulting in the CC release into the periplasm of ligands bound by these outer CC membrane proteins. Required for heme utilization and virulence. CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a CC complex with TonB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}; Periplasmic side CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42075.1; -; Genomic_DNA. DR PIR; A81049; A81049. DR RefSeq; NP_274733.1; NC_003112.2. DR RefSeq; WP_002212590.1; NC_003112.2. DR ProteinModelPortal; P57004; -. DR STRING; 122586.NMB1730; -. DR PaxDb; P57004; -. DR EnsemblBacteria; AAF42075; AAF42075; NMB1730. DR GeneID; 903369; -. DR KEGG; nme:NMB1730; -. DR PATRIC; 20359423; VBINeiMen85645_2217. DR eggNOG; ENOG41080KD; Bacteria. DR eggNOG; COG0810; LUCA. DR HOGENOM; HOG000220758; -. DR OMA; MRHQGVV; -. DR OrthoDB; EOG6R2H0M; -. DR BioCyc; NMEN122586:GHGG-1785-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031992; F:energy transducer activity; IEA:InterPro. DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003538; TonB. DR InterPro; IPR006260; TonB_C. DR Pfam; PF03544; TonB_C; 1. DR PRINTS; PR01374; TONBPROTEIN. DR TIGRFAMs; TIGR01352; tonB_Cterm; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix; Transport; Virulence. FT CHAIN 1 280 Protein TonB. FT /FTId=PRO_0000196203. FT TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 6 27 Helical; Signal-anchor. {ECO:0000255}. FT TOPO_DOM 28 280 Periplasmic. {ECO:0000255}. SQ SEQUENCE 280 AA; 29199 MW; DF82E3A9C4A16A9A CRC64; MDKERILTPA VVFSVALLHL AMVALLWQAH KLPVIESGNV IEFVDLGDFG GGDGAPEGAG APAAPEPQPV PEPPKPVEPP KPVLKPVVTK KADADIQQPK EEPKPEEKPK PEEKPKPEPK PEAKPVPKPA EKPVEKPSEK PAEHPGNASA KADSEQGNGE DKGTGTKGDG TGRGEGSGKG SGGVKGEHGE GAGSSKGNPL RANGSIPRPA YPTLSMENDE QGTVVLSVLV SPGGHVESVK IVKSSGFSRL DNAARKAAQN GHFQANAWTE FKVPVKFELN // ID TRMD_NEIMB Reviewed; 249 AA. AC Q9K0K4; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase; DE EC=2.1.1.228; DE AltName: Full=M1G-methyltransferase; DE AltName: Full=tRNA [GM37] methyltransferase; GN Name=trmD; OrderedLocusNames=NMB0590; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA CC = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41018.1; -; Genomic_DNA. DR PIR; C81180; C81180. DR RefSeq; NP_273634.1; NC_003112.2. DR RefSeq; WP_002222855.1; NC_003112.2. DR ProteinModelPortal; Q9K0K4; -. DR SMR; Q9K0K4; 1-246. DR STRING; 122586.NMB0590; -. DR PaxDb; Q9K0K4; -. DR EnsemblBacteria; AAF41018; AAF41018; NMB0590. DR GeneID; 902705; -. DR KEGG; nme:NMB0590; -. DR PATRIC; 20356465; VBINeiMen85645_0752. DR eggNOG; ENOG4105D6X; Bacteria. DR eggNOG; COG0336; LUCA. DR HOGENOM; HOG000016242; -. DR KO; K00554; -. DR OMA; YKGVDQR; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NMEN122586:GHGG-616-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.1270.20; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00605; TrmD; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac. DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF000386; tRNA_mtase; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00088; trmD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 249 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060421. FT REGION 133 138 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 113 113 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 249 AA; 27887 MW; 313D90F21AB8C3AA CRC64; MLIQAVTIFP EMFDSITRYG VTGRANRQGI WQFEAVNPRK FADNRLGYID DRPFGGGPGM IMMAPPLHAA IEHAKTQSSQ AAKVIYLSPQ GKPLTHQKAV ELAELPHLIL LCGRYEGIDE RLLQSSVDEE ISIGDFVVSG GELPAMMLMD AVLRLVPGVL GDMQSAEQDS FSSGILDCPH YTKPLEFQGM AVPEVLRSGN HGLIAEWRLE QSLRRTLERR PDLLEKRVLI PKESRLLETI RQEQREIQS // ID TPIS_NEIMB Reviewed; 251 AA. AC Q9JXT8; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 16-MAR-2016, entry version 90. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; GN OrderedLocusNames=NMB1887; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42221.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42221.1; ALT_INIT; Genomic_DNA. DR PIR; E81031; E81031. DR RefSeq; NP_274883.1; NC_003112.2. DR ProteinModelPortal; Q9JXT8; -. DR STRING; 122586.NMB1887; -. DR PaxDb; Q9JXT8; -. DR EnsemblBacteria; AAF42221; AAF42221; NMB1887. DR GeneID; 904291; -. DR KEGG; nme:NMB1887; -. DR PATRIC; 20359809; VBINeiMen85645_2410. DR eggNOG; ENOG4105CP7; Bacteria. DR eggNOG; COG0149; LUCA. DR HOGENOM; HOG000226413; -. DR KO; K01803; -. DR OMA; TKIAMAN; -. DR OrthoDB; EOG66QM23; -. DR BioCyc; NMEN122586:GHGG-1943-MONOMER; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR PANTHER; PTHR21139; PTHR21139; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; SSF51351; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Pentose shunt; Reference proteome. FT CHAIN 1 251 Triosephosphate isomerase. FT /FTId=PRO_0000090259. FT REGION 10 12 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT REGION 232 233 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 99 99 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 167 167 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 173 173 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT BINDING 211 211 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00147}. SQ SEQUENCE 251 AA; 27538 MW; D1A026C315EED6C6 CRC64; MWDQKWVIGN WKMNGRLQNN NALMHRFRIH PTAERVLIGL AAPTVYLLQL HNAMQIVLNN RILTCAQDVS RFPNNGAYTG EVSAEMLADT GTDIVLIGHS ERSLYFGEKN EIQRRKMENV LNVGLIPLLC VGESLEEREA GKEHEVIAHQ LSILQGLDTK NIAVAYEPVW AIGTGKVATV EQIADMHAFI YKEILSLCGS DVKIRVLYGG SVKADNAADI FAVPYVDGAL VGGASLSYDS FTAIISAAQN A // ID TRMA_NEIMB Reviewed; 362 AA. AC Q9JYA0; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011}; DE EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; GN Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011}; GN OrderedLocusNames=NMB1679; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the CC formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, CC and that of position 341 (m5U341) in tmRNA (transfer-mRNA). CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(54) in tRNA = CC S-adenosyl-L-homocysteine + 5-methyluracil(54) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(341) in tmRNA CC = S-adenosyl-L-homocysteine + 5-methyluracil(341) in tmRNA. CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC TrmA subfamily. {ECO:0000255|HAMAP-Rule:MF_01011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42027.1; -; Genomic_DNA. DR PIR; A81055; A81055. DR RefSeq; NP_274683.1; NC_003112.2. DR RefSeq; WP_002224986.1; NC_003112.2. DR ProteinModelPortal; Q9JYA0; -. DR SMR; Q9JYA0; 1-360. DR STRING; 122586.NMB1679; -. DR PaxDb; Q9JYA0; -. DR DNASU; 903429; -. DR EnsemblBacteria; AAF42027; AAF42027; NMB1679. DR GeneID; 903429; -. DR KEGG; nme:NMB1679; -. DR PATRIC; 20359309; VBINeiMen85645_2161. DR eggNOG; ENOG4107R9T; Bacteria. DR eggNOG; COG2265; LUCA. DR HOGENOM; HOG000218626; -. DR KO; K00557; -. DR OMA; IKMLEWA; -. DR OrthoDB; EOG6V4GKM; -. DR BioCyc; NMEN122586:GHGG-1734-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01011; RNA_methyltr_TrmA; 1. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR011869; TrmA_MeTrfase. DR InterPro; IPR010280; U5_MeTrfase_fam. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02143; trmA_only; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS01230; TRMA_1; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 362 tRNA/tmRNA (uracil-C(5))- FT methyltransferase. FT /FTId=PRO_0000161868. FT ACT_SITE 318 318 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT ACT_SITE 352 352 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT BINDING 182 182 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 210 210 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT BINDING 215 215 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 231 231 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 293 293 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. SQ SEQUENCE 362 AA; 41309 MW; 4CF18AF93E72F8EB CRC64; MNDYTQQLQG KKDYLKTLFA GLDVPEWEVY ESPDKHYRMR AEFRIWHEGG EMFYAMFEKG QKASGASMIR CDRFEAASEA VNRLMPELIA AAAQSPELKK RWYAVEFLST LSGEMLVTMI YHKRLDAEWM QAAQALQQQL DISVIGRSRG QKIVLKQDYV TETLKVGNRD FRYRQIEGSF TQPNAAVCQK MLEWACRTAE GLGSDLLELY CGNGNFTLPL SRYFRQVLAT EISKTSVSAA QWNIEANRIG NIKIARLSAE EFTEAYTGKR EFKRLKDGGI ALTDYAFSTI FVDPPRAGID EETLKLVSQF DNIIYISCNP ETLRANLDTL AETHAVERAA LFDQFPFTHH IESGVLLKKK IL // ID TRPD_NEIMB Reviewed; 352 AA. AC P66995; Q9JQM3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211}; DE EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211}; GN Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; GN OrderedLocusNames=NMB0967; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield CC N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00211}; CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00211}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase CC family. {ECO:0000255|HAMAP-Rule:MF_00211}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41372.1; -; Genomic_DNA. DR PIR; A81136; A81136. DR RefSeq; NP_274005.1; NC_003112.2. DR RefSeq; WP_002217365.1; NC_003112.2. DR ProteinModelPortal; P66995; -. DR STRING; 122586.NMB0967; -. DR PaxDb; P66995; -. DR EnsemblBacteria; AAF41372; AAF41372; NMB0967. DR GeneID; 903087; -. DR KEGG; nme:NMB0967; -. DR PATRIC; 20357423; VBINeiMen85645_1226. DR eggNOG; ENOG4107QYG; Bacteria. DR eggNOG; COG0547; LUCA. DR HOGENOM; HOG000230451; -. DR KO; K00766; -. DR OMA; MIVLNAG; -. DR OrthoDB; EOG66XBMH; -. DR BioCyc; NMEN122586:GHGG-1004-MONOMER; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1030.10; -; 1. DR HAMAP; MF_00211; TrpD; 1. DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR TIGRFAMs; TIGR01245; trpD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glycosyltransferase; Magnesium; Metal-binding; KW Reference proteome; Transferase; Tryptophan biosynthesis. FT CHAIN 1 352 Anthranilate phosphoribosyltransferase. FT /FTId=PRO_0000154464. FT REGION 86 87 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 93 96 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 111 119 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT METAL 95 95 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 228 228 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 229 229 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 229 229 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 83 83 Anthranilate 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 83 83 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 91 91 Phosphoribosylpyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 123 123 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 169 169 Anthranilate 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. SQ SEQUENCE 352 AA; 37698 MW; F879D9CF8BD77563 CRC64; MITPQQAIER LISNNELFYD EMTDLMRQIM RGQVLPEQIA AILTGLRIKV ETVSEITAAA AVMREFATKV PLENAEGLVD IVGTGGDGAK TFNISTTSMF VAAAAGAKVA KHGGRSVSSS SGAADVVEQM GANLNLTPEQ VAQSIRQTGI GFMFAPNHHS AMRHVAPVRR SLGFRSIFNI LGPLTNPAGA PNQLLGVFHT DLCGILSRVL QQLGSKHVLV VCGEGGLDEI TLTGKTRVAE LKDGKISEYD IRPEDFGIET RRNLDEIKVA NTQESLLKMN EVLEGREGAA RDIVLLNTAA ALYAGNVAAS LSDGISAARE AIDSGRAKSK KEEFVGFQPQ QRCHFLGKME LG // ID TRPE_NEIMB Reviewed; 491 AA. AC P56995; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 20-JAN-2016, entry version 99. DE RecName: Full=Anthranilate synthase component 1; DE Short=AS; DE Short=ASI; DE EC=4.1.3.27; GN Name=trpE; OrderedLocusNames=NMB1021; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00897}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P00897}; CC -!- ENZYME REGULATION: Feedback inhibited by tryptophan. CC {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anthranilate synthase component I CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41421.1; -; Genomic_DNA. DR PIR; E81132; E81132. DR RefSeq; NP_274055.1; NC_003112.2. DR RefSeq; WP_002219345.1; NC_003112.2. DR ProteinModelPortal; P56995; -. DR STRING; 122586.NMB1021; -. DR PaxDb; P56995; -. DR EnsemblBacteria; AAF41421; AAF41421; NMB1021. DR GeneID; 903159; -. DR KEGG; nme:NMB1021; -. DR PATRIC; 20357577; VBINeiMen85645_1305. DR eggNOG; ENOG4105CRQ; Bacteria. DR eggNOG; COG0147; LUCA. DR HOGENOM; HOG000025142; -. DR KO; K01657; -. DR OMA; MYFYNFG; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NMEN122586:GHGG-1058-MONOMER; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR006805; Anth_synth_I_N. DR InterPro; IPR005256; Anth_synth_I_PabB. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF04715; Anth_synt_I_N; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. DR TIGRFAMs; TIGR00564; trpE_most; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Magnesium; Metal-binding; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 491 Anthranilate synthase component 1. FT /FTId=PRO_0000154104. FT REGION 271 273 Tryptophan binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 306 307 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 455 457 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 333 333 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 470 470 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 49 49 Tryptophan. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 421 421 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 441 441 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 457 457 Chorismate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P00897}. SQ SEQUENCE 491 AA; 54702 MW; 815236B1334D122C CRC64; MISKQEYQAQ AAQGYNRIPL VQELLADLDT PLSLYLKLAN RPYTYLLESV VGGERFGRYS FIGLPCSHYL KASGKHVDVY QNGEIVEQHD GNPLPFIEAF HNRFKTPEIP SLPRFTGGLV GYFGYETIYN FEHFAHRLKN TTKADPLGTP DILLMLSQEL AVIDNLSGKI HLVVYADPSQ PDGYERARER LEDIRTQLRQ SCAIPLSLGS KHTEAVSEFG EEPFKACVNK IKDYIFAGDC MQVVPSQRMS MEFTDSPLAL YRALRTLNPS PYLFYYDFGD FHIVGSSPEI LVRRERNDVI VRPIAGTRLR GKTPAEDLAN EQDLLSDAKE IAEHVMLIDL GRNDVGRISK TGEVKVTDKM VIEKYSHVMH IVSNVEGRLK DGMTNMDILA ATFPAGTLSG APKVRAMEII EEVEPSKRGI YGGAVGVWGF NNDMDLAIAI RTAVVKNNTL YVQSGAGVVA DSDPASEWQE TQNKARAVIH AAQMVQEGLD K // ID TRUA_NEIMB Reviewed; 265 AA. AC Q9JXI2; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171}; DE EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171}; GN Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; GN OrderedLocusNames=NMB2036; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in CC the anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_00171}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38- CC 40). {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA CC family. {ECO:0000255|HAMAP-Rule:MF_00171}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42357.1; -; Genomic_DNA. DR PIR; A81014; A81014. DR RefSeq; NP_275027.1; NC_003112.2. DR RefSeq; WP_002244344.1; NC_003112.2. DR ProteinModelPortal; Q9JXI2; -. DR STRING; 122586.NMB2036; -. DR PaxDb; Q9JXI2; -. DR EnsemblBacteria; AAF42357; AAF42357; NMB2036. DR GeneID; 904060; -. DR KEGG; nme:NMB2036; -. DR PATRIC; 20360202; VBINeiMen85645_2602. DR eggNOG; ENOG4105DI7; Bacteria. DR eggNOG; COG0101; LUCA. DR HOGENOM; HOG000248672; -. DR KO; K06173; -. DR OMA; PWRNVHH; -. DR OrthoDB; EOG6Z9B4R; -. DR BioCyc; NMEN122586:GHGG-2098-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.580; -; 1. DR Gene3D; 3.30.70.660; -; 1. DR HAMAP; MF_00171; TruA; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001406; PsdUridine_synth_TruA. DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom. DR InterPro; IPR020095; PsdUridine_synth_TruA_C. DR InterPro; IPR020094; PsdUridine_synth_TruA_N. DR PANTHER; PTHR11142; PTHR11142; 1. DR Pfam; PF01416; PseudoU_synth_1; 2. DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00071; hisT_truA; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 265 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057420. FT ACT_SITE 58 58 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00171}. FT BINDING 116 116 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00171}. SQ SEQUENCE 265 AA; 29205 MW; DBACE58B8BDB2280 CRC64; MDTAQKQRWA ITLSYDGSRF YGWQKQADGV PTVQAALETA LAQIAGEAVS TTVAGRTDTG VHATAQVVHF DTTAARPQQA WVRGVNAHLP EGIAVLHARQ VAPEFHARFD AYGRHYRYLL ESAPVRSPLL KNRAGWTHLK LDIGQMRQAA ALLVGEQDFS SFRAAECQAK SPVKTIYRAD LTQSSGLVRL DLHGNAFLHH MVRNIMGALV YVGSGRLSVE GFAALIQERS RLKAPPTFMP DGLYLTGVDY PEAYGIIRPQ IPEWL // ID TRPB_NEIMB Reviewed; 400 AA. AC Q9K0B5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133}; GN Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; GN OrderedLocusNames=NMB0699; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000255|HAMAP- CC Rule:MF_00133}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00133}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00133}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00133}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_00133}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP- CC Rule:MF_00133}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41116.1; -; Genomic_DNA. DR PIR; B81169; B81169. DR RefSeq; NP_273741.1; NC_003112.2. DR RefSeq; WP_002225482.1; NC_003112.2. DR ProteinModelPortal; Q9K0B5; -. DR SMR; Q9K0B5; 12-397. DR STRING; 122586.NMB0699; -. DR PaxDb; Q9K0B5; -. DR EnsemblBacteria; AAF41116; AAF41116; NMB0699. DR GeneID; 902811; -. DR KEGG; nme:NMB0699; -. DR PATRIC; 20356731; VBINeiMen85645_0887. DR eggNOG; ENOG4105CG0; Bacteria. DR eggNOG; COG0133; LUCA. DR HOGENOM; HOG000161710; -. DR KO; K01696; -. DR OMA; IPEMLYP; -. DR OrthoDB; EOG6GFGH7; -. DR BioCyc; NMEN122586:GHGG-727-MONOMER; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR006654; Trp_synth_beta. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR PANTHER; PTHR10314:SF3; PTHR10314:SF3; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 400 Tryptophan synthase beta chain. FT /FTId=PRO_0000098973. FT MOD_RES 92 92 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00133}. SQ SEQUENCE 400 AA; 43209 MW; 86FCC42EF6F64210 CRC64; MKNYHAPDEK GFFGEHGGLY VSETLIPALQ ELADAYKAAK NDPEFWEAFR HDLKHYVGRP SPVYHAARLS EHLGGAQIWL KREDLNHTGA HKVNNTIGQA LLAKRMGKKR VIAETGAGQH GVASATVAAR FGMTCDVYMG ADDIQRQMPN VFRMKLLGAN VVGVESGSRT LKDAMNEAMR EWVARVDDTF YIIGTAAGPA PYPEMVRDFQ CVIGNEAKAQ MQEAIGRQPD VAVACVGGGS NAIGLFHPYI GEENVRLVGV EAGGLGVNTP DHAAPITSGA PIGVLHGFRS YLMQDENGQV LGTHSVSAGL DYPGIGPEHS HLHDIKRVEY TVAKDDEALE AFDLLCRFEG IIPALESSHA VAWAVKNAPK MGKDQVILVN LSGRGDKDIN TVAKLKGIKL // ID TSAC_NEIMB Reviewed; 189 AA. AC Q9JXA4; DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852}; GN Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN; GN OrderedLocusNames=NMB2150; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Catalyzes the conversion of L-threonine, CC HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as CC the acyladenylate intermediate, with the release of diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|HAMAP- CC Rule:MF_01852}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42458.1; -; Genomic_DNA. DR PIR; D81000; D81000. DR RefSeq; NP_275135.1; NC_003112.2. DR RefSeq; WP_002231013.1; NC_003112.2. DR ProteinModelPortal; Q9JXA4; -. DR STRING; 122586.NMB2150; -. DR PaxDb; Q9JXA4; -. DR EnsemblBacteria; AAF42458; AAF42458; NMB2150. DR GeneID; 903222; -. DR KEGG; nme:NMB2150; -. DR PATRIC; 20360496; VBINeiMen85645_2744. DR eggNOG; ENOG4105EK0; Bacteria. DR eggNOG; COG0009; LUCA. DR HOGENOM; HOG000076163; -. DR KO; K07566; -. DR OMA; FGLGCNP; -. DR OrthoDB; EOG6C5RT4; -. DR BioCyc; NMEN122586:GHGG-2215-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_01852; TsaC; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR023535; TC-AMP_synthase. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase; KW tRNA processing. FT CHAIN 1 189 Threonylcarbamoyl-AMP synthase. FT /FTId=PRO_0000352939. FT DOMAIN 9 189 YrdC-like. {ECO:0000255|HAMAP- FT Rule:MF_01852}. SQ SEQUENCE 189 AA; 21106 MW; 6C042D63421B3D5A CRC64; MLFPRIIAAS AQRKLSVYLK KGGLVAYPTE SCYGLGCLPT LAKALGKLAH LKKRPQHKGM IVIGNQFEQL QPLLQMPSEN LQDMLRKEWP APKTFLLSAK SCVLPELRGK QRSKLAVRVP AHVGARRLCQ ALQTPLVSTS CNRAGKRACR TEREVRRQFG RDVWIVGGRI GRQKSPSQII DGETGKRLR // ID TRPC_NEIMB Reviewed; 260 AA. AC Q9K192; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00134}; DE Short=IGPS {ECO:0000255|HAMAP-Rule:MF_00134}; DE EC=4.1.1.48 {ECO:0000255|HAMAP-Rule:MF_00134}; GN Name=trpC {ECO:0000255|HAMAP-Rule:MF_00134}; GN OrderedLocusNames=NMB0275; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00134}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00134}. CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000255|HAMAP- CC Rule:MF_00134}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40729.1; -; Genomic_DNA. DR PIR; H81216; H81216. DR RefSeq; NP_273331.1; NC_003112.2. DR RefSeq; WP_002221930.1; NC_003112.2. DR ProteinModelPortal; Q9K192; -. DR STRING; 122586.NMB0275; -. DR PaxDb; Q9K192; -. DR EnsemblBacteria; AAF40729; AAF40729; NMB0275. DR GeneID; 902386; -. DR KEGG; nme:NMB0275; -. DR PATRIC; 20355636; VBINeiMen85645_0342. DR eggNOG; ENOG4105DK0; Bacteria. DR eggNOG; COG0134; LUCA. DR HOGENOM; HOG000230463; -. DR KO; K01609; -. DR OMA; MIDPYQI; -. DR OrthoDB; EOG6WT8JX; -. DR BioCyc; NMEN122586:GHGG-290-MONOMER; -. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00134_B; IGPS_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00218; IGPS; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Decarboxylase; Lyase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 260 Indole-3-glycerol phosphate synthase. FT /FTId=PRO_0000154237. SQ SEQUENCE 260 AA; 28744 MW; 52C287401C1235C9 CRC64; MTDILNKILA TKAQEVAAQK AAVNAEHIRT LAAEAAPVRS FIDSIRGKHR LNLPAVIAEI KKASPSKGLI RPDFRPAEIA RAYENAGAAC LSVLTDEPYF QGSPEYLKQA REAVSLPVLR KDFIIDEYQV YQARAWGADA VLLIAAALEQ EQLERFEAVA HELGMTVLLE LHDETELEKC RNLTTPLWGV NNRNLRTFEV SLDQTLSLLP ALEGKTVVTE SGITGKADVE FMQSRGVHTF LIGETFMRAD DIEAEVGKLF // ID TRMB_NEIMB Reviewed; 238 AA. AC Q9JZ24; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; GN OrderedLocusNames=NMB1328; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at CC position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(46) in tRNA CC = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TrmB family. {ECO:0000255|HAMAP- CC Rule:MF_01057}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41703.1; -; Genomic_DNA. DR PIR; C81095; C81095. DR RefSeq; NP_274347.1; NC_003112.2. DR RefSeq; WP_002222361.1; NC_003112.2. DR ProteinModelPortal; Q9JZ24; -. DR STRING; 122586.NMB1328; -. DR PaxDb; Q9JZ24; -. DR EnsemblBacteria; AAF41703; AAF41703; NMB1328. DR GeneID; 903750; -. DR KEGG; nme:NMB1328; -. DR PATRIC; 20358311; VBINeiMen85645_1667. DR eggNOG; ENOG4105CZ1; Bacteria. DR eggNOG; COG0220; LUCA. DR HOGENOM; HOG000073968; -. DR KO; K03439; -. DR OMA; IKLGHGV; -. DR OrthoDB; EOG6K6VBC; -. DR BioCyc; NMEN122586:GHGG-1366-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR Pfam; PF02390; Methyltransf_4; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00091; TIGR00091; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 238 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171363. FT REGION 216 219 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT ACT_SITE 145 145 {ECO:0000250}. FT BINDING 70 70 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 95 95 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 122 122 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 145 145 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 149 149 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 181 181 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. SQ SEQUENCE 238 AA; 27038 MW; DC804A3FA1C8C201 CRC64; MTDTAENQTQ NNWQAGHPRS IRSFVLRQSH MTAAQQRAID TLWDSFGIDY QATPADLDAR FGSSRPKILE IGFGMGTATA EIARRLPETD FLAIDVHGPG VGNLLKLIDE NHLENIRVMR HDAVEVVENM LQDGSLDGIH IFFPDPWHKK RHHKRRLIQA PFIAKLLPKL KTGGYIHLAT DWEEYAQQML EVLSSFDSLQ NTAADYAPTP DYRPETKFEA RGKRLGHGVW DLVFKRIG // ID TRUB_NEIMB Reviewed; 307 AA. AC Q9JYY1; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 91. DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080}; DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080}; GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01080}; GN OrderedLocusNames=NMB1374; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_01080}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(55) = tRNA pseudouridine(55). CC {ECO:0000255|HAMAP-Rule:MF_01080}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41748.1; -; Genomic_DNA. DR PIR; C81091; C81091. DR RefSeq; NP_274392.1; NC_003112.2. DR RefSeq; WP_002222326.1; NC_003112.2. DR ProteinModelPortal; Q9JYY1; -. DR STRING; 122586.NMB1374; -. DR PaxDb; Q9JYY1; -. DR EnsemblBacteria; AAF41748; AAF41748; NMB1374. DR GeneID; 903796; -. DR KEGG; nme:NMB1374; -. DR PATRIC; 20358421; VBINeiMen85645_1722. DR eggNOG; ENOG4105D0T; Bacteria. DR eggNOG; COG0130; LUCA. DR HOGENOM; HOG000231223; -. DR KO; K03177; -. DR OMA; YELQFIR; -. DR OrthoDB; EOG6358D3; -. DR BioCyc; NMEN122586:GHGG-1412-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.130.10; -; 1. DR HAMAP; MF_01080; TruB_bact; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB. DR InterPro; IPR015240; tRNA_sdUridine_synth_fam1_C. DR InterPro; IPR032819; TruB_C. DR PANTHER; PTHR13767; PTHR13767; 1. DR Pfam; PF09157; TruB-C_2; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00431; TruB; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 307 tRNA pseudouridine synthase B. FT /FTId=PRO_0000121875. FT ACT_SITE 48 48 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01080}. SQ SEQUENCE 307 AA; 33632 MW; 4B0FBADACEB99E79 CRC64; MNTGKPQKRA VNGVLLLDKP EGLSSNTALQ KARRLFHAEK AGHTGVLDPL ATGLLPVCFG EATKFAQYLL DADKAYTATL KLGEASSTGD AEGEIIATAR ADISLAEFQT ACQALTGNIR QVPPMFSALK HEGKPLYEYA RKGIVIERKA RYITVYAIDI AEFDAPKAVI DVRCSKGTYI RTLSEDIAKH IGTFAHLTAL RRTETAGFTI AQSHTLEALA NLNETERDSL LLPCDVLVSH FPQTVLNDYA VHMLHCGQRP RFEEDLPSDT PVRVYTENGR FVGLAEYQKE ICRLKALRLM NTAASAA // ID TRPA_NEIMB Reviewed; 261 AA. AC Q9K0D4; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; GN OrderedLocusNames=NMB0678; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage CC of indoleglycerol phosphate to indole and glyceraldehyde 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41096.1; -; Genomic_DNA. DR PIR; D81171; D81171. DR RefSeq; NP_273720.1; NC_003112.2. DR RefSeq; WP_010980825.1; NC_003112.2. DR ProteinModelPortal; Q9K0D4; -. DR STRING; 122586.NMB0678; -. DR PaxDb; Q9K0D4; -. DR EnsemblBacteria; AAF41096; AAF41096; NMB0678. DR GeneID; 902790; -. DR KEGG; nme:NMB0678; -. DR PATRIC; 20356665; VBINeiMen85645_0850. DR eggNOG; ENOG4105F6H; Bacteria. DR eggNOG; COG0159; LUCA. DR HOGENOM; HOG000223815; -. DR KO; K01695; -. DR OMA; PVFICPP; -. DR OrthoDB; EOG6RVG0K; -. DR BioCyc; NMEN122586:GHGG-706-MONOMER; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00131; Trp_synth_alpha; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR018204; Trp_synthase_alpha_AS. DR InterPro; IPR002028; Trp_synthase_suA. DR Pfam; PF00290; Trp_syntA; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00262; trpA; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 261 Tryptophan synthase alpha chain. FT /FTId=PRO_0000098815. FT ACT_SITE 47 47 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. FT ACT_SITE 58 58 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. SQ SEQUENCE 261 AA; 27974 MW; DAEFDA4A10563206 CRC64; MSRIRQAFAA LDGGKALIAY ITVGDPDIRT TLALMHGMVA NGADILELGV PFSDPMADGP VIQRAAERAL ANGISLRDVL DVVRKFRETD TQTPVVLMGY LNPVHKMGYR EFAQEAAKAG VDGVLTVDSP VETIDPLYRE LKDNGVDCIF LIAPTTTEDR IKTIAELAGG FVYYVSLKGV TGAASLDTDE VSRKIEYLHQ YIDIPIGVGF GISNAESARK IGRVADAVIV GSRIVKEIEN NTGNEAAAVG ALVKELKDAV R // ID UBIX_NEIMB Reviewed; 189 AA. AC Q9JXP4; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 11-MAY-2016, entry version 83. DE RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984}; DE EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984}; GN Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984}; GN OrderedLocusNames=NMB1945; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of CC the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3- CC polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase CC is metal-independent and links a dimethylallyl moiety from CC dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms CC of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl phosphate + FMNH(2) = prenylated CC FMNH(2) + phosphate. {ECO:0000255|HAMAP-Rule:MF_01984}. CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP- CC Rule:MF_01984}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42274.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42274.1; ALT_INIT; Genomic_DNA. DR PIR; B81023; B81023. DR RefSeq; NP_274939.1; NC_003112.2. DR RefSeq; WP_010981011.1; NC_003112.2. DR ProteinModelPortal; Q9JXP4; -. DR SMR; Q9JXP4; 4-187. DR STRING; 122586.NMB1945; -. DR PaxDb; Q9JXP4; -. DR EnsemblBacteria; AAF42274; AAF42274; NMB1945. DR GeneID; 904206; -. DR KEGG; nme:NMB1945; -. DR PATRIC; 20359941; VBINeiMen85645_2475. DR eggNOG; ENOG4108UMA; Bacteria. DR eggNOG; COG0163; LUCA. DR HOGENOM; HOG000225437; -. DR KO; K03186; -. DR OMA; IIMPREM; -. DR OrthoDB; EOG6C8MXR; -. DR BioCyc; NMEN122586:GHGG-2002-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051188; P:cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1950; -; 1. DR HAMAP; MF_01984; ubiX_pad; 1. DR InterPro; IPR003382; Flavoprotein. DR InterPro; IPR004507; UbiX_Pad1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00421; ubiX_pad; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Prenyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 189 Flavin prenyltransferase UbiX. FT /FTId=PRO_0000134969. FT NP_BIND 11 13 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT NP_BIND 88 91 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 37 37 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 123 123 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 153 153 DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}. SQ SEQUENCE 189 AA; 20379 MW; 3CD8A363EF51A15D CRC64; MVRRLIIGIS GASGFQYGVK ALELLRAQDV ETHLVVSKGA EMARASETAY ARDEVYALAD FVHPIGNIGA CIASGTFKTD GMLVAPCSMR TLASVAHGFG DNLLTRAADV VLKERRRLVL MVRETPLNLA HLDNMKRVTE MGGVVFPPVP AMYRKPQTAD DIVAHSVAHA LSLFGIDTPD SAEWQGMAD // ID TRPF_NEIMB Reviewed; 208 AA. AC Q9K0C6; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135}; DE Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135}; DE EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135}; GN Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; GN OrderedLocusNames=NMB0688; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00135}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_00135}. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP- CC Rule:MF_00135}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41106.1; -; Genomic_DNA. DR PIR; G81169; G81169. DR RefSeq; NP_273730.1; NC_003112.2. DR RefSeq; WP_002225494.1; NC_003112.2. DR ProteinModelPortal; Q9K0C6; -. DR STRING; 122586.NMB0688; -. DR PaxDb; Q9K0C6; -. DR EnsemblBacteria; AAF41106; AAF41106; NMB0688. DR GeneID; 902800; -. DR KEGG; nme:NMB0688; -. DR PATRIC; 20356703; VBINeiMen85645_0873. DR eggNOG; ENOG4108ZGB; Bacteria. DR eggNOG; COG0135; LUCA. DR HOGENOM; HOG000161598; -. DR KO; K01817; -. DR OMA; FVNASRC; -. DR OrthoDB; EOG6N94DF; -. DR BioCyc; NMEN122586:GHGG-716-MONOMER; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001240; PRAI. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Isomerase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 208 N-(5'-phosphoribosyl)anthranilate FT isomerase. FT /FTId=PRO_0000154367. SQ SEQUENCE 208 AA; 22242 MW; 8B0532A226FE607D CRC64; MRKIRTKICG ITTPEDAAAA AAAGADAVGL VFFQGSSRAV DIARAKKITA ALPPFVSVVA LFVNESAQNI RRILAEVPIH IIQFHGDEDD AFCRQFHRPY IKAIRVQTAS DIRNAATRFP DAQALLFDAY HPSEYGGTGN RFDWTLLAEY SGKPWVLAGG LTPENVGEAV RITGAESVDV SGGVEASKGK KDAAKVAAFI ATANRLSR // ID TSAD_NEIMB Reviewed; 354 AA. AC Q9JY06; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445}; DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; GN Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp; GN OrderedLocusNames=NMB1802; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaE and TsaB. TsaD likely plays a CC direct catalytic role in this reaction. {ECO:0000255|HAMAP- CC Rule:MF_01445}. CC -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in CC tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01445}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP- CC Rule:MF_01445}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42139.1; -; Genomic_DNA. DR PIR; C81040; C81040. DR RefSeq; NP_274799.1; NC_003112.2. DR RefSeq; WP_002225646.1; NC_003112.2. DR ProteinModelPortal; Q9JY06; -. DR STRING; 122586.NMB1802; -. DR PaxDb; Q9JY06; -. DR DNASU; 903296; -. DR EnsemblBacteria; AAF42139; AAF42139; NMB1802. DR GeneID; 903296; -. DR KEGG; nme:NMB1802; -. DR PATRIC; 20359571; VBINeiMen85645_2291. DR eggNOG; ENOG4105CPM; Bacteria. DR eggNOG; COG0533; LUCA. DR HOGENOM; HOG000109568; -. DR KO; K01409; -. DR OMA; RDHVKRM; -. DR OrthoDB; EOG6K402S; -. DR BioCyc; NMEN122586:GHGG-1857-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR022450; TsaD. DR Pfam; PF00814; Peptidase_M22; 1. DR PRINTS; PR00789; OSIALOPTASE. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 354 tRNA N6-adenosine FT threonylcarbamoyltransferase. FT /FTId=PRO_0000303450. FT REGION 134 138 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT METAL 111 111 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 115 115 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 319 319 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 167 167 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 180 180 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 279 279 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. SQ SEQUENCE 354 AA; 37596 MW; 06AB4AD7A68E5D69 CRC64; MLVLGIESSC DETGVALYDT ERGLRAHCLH TQMAMHAEYG GVVPELASRD HIRRLVPLTE GCLAQAGASY GDIDAVAFTQ GPGLGGALLA GSSYANALAL ALDKPVIPVH HLEGHLLSPL LAEEKPDFPF VALLVSGGHT QIMAVRGIGD YALLGESVDD AAGEAFDKTA KLLGLLYPGG AKLSELAESG RFEAFVFPRP MIHSDDLQMS FSGLKTAVLT AVEKVRAENG ADDIPEQTRN DICRAFQDAV VDVLAAKVKK ALLQTGFRTV VVAGGVGANR KLRETFGNMT VQIPTPKGKP KHPSEKVSVF FPPTAYCTDN GAMIAFAGAM HLGKGREVGA FNVRPRWPLS EIVR // ID UBIB_NEIMB Reviewed; 503 AA. AC Q9K0N0; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Probable protein kinase UbiB {ECO:0000255|HAMAP-Rule:MF_00414}; DE EC=2.7.-.- {ECO:0000255|HAMAP-Rule:MF_00414}; DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000255|HAMAP-Rule:MF_00414}; GN Name=ubiB {ECO:0000255|HAMAP-Rule:MF_00414}; GN OrderedLocusNames=NMB0559; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity CC which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00414}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis CC [regulation]. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00414}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00414}. CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00414}. CC -!- SIMILARITY: Contains 1 protein kinase domain. {ECO:0000255|HAMAP- CC Rule:MF_00414}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40987.1; -; Genomic_DNA. DR PIR; B81184; B81184. DR RefSeq; NP_273603.1; NC_003112.2. DR RefSeq; WP_002225567.1; NC_003112.2. DR ProteinModelPortal; Q9K0N0; -. DR STRING; 122586.NMB0559; -. DR PaxDb; Q9K0N0; -. DR EnsemblBacteria; AAF40987; AAF40987; NMB0559. DR GeneID; 902674; -. DR KEGG; nme:NMB0559; -. DR PATRIC; 20356391; VBINeiMen85645_0715. DR eggNOG; ENOG4105CNK; Bacteria. DR eggNOG; COG0661; LUCA. DR HOGENOM; HOG000264440; -. DR KO; K03688; -. DR OMA; AKTEKFH; -. DR OrthoDB; EOG61P6SS; -. DR BioCyc; NMEN122586:GHGG-585-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00414; UbiB; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR010232; UbiB. DR InterPro; IPR004147; UbiB_dom. DR Pfam; PF03109; ABC1; 1. DR SUPFAM; SSF56112; SSF56112; 2. DR TIGRFAMs; TIGR01982; UbiB; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Membrane; Nucleotide-binding; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis. FT CHAIN 1 503 Probable protein kinase UbiB. FT /FTId=PRO_0000200709. FT TRANSMEM 13 35 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00414}. FT TRANSMEM 485 502 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00414}. FT DOMAIN 120 491 Protein kinase. {ECO:0000255|HAMAP- FT Rule:MF_00414}. FT NP_BIND 126 134 ATP. {ECO:0000255|HAMAP-Rule:MF_00414}. FT ACT_SITE 283 283 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00414}. FT BINDING 148 148 ATP. {ECO:0000255|HAMAP-Rule:MF_00414}. SQ SEQUENCE 503 AA; 57296 MW; 1015AB6C9004BD47 CRC64; MKWLKRLTVI VGTFYRYRLA GLCASLMGSG WICALLKMMP QSSKLKNEPP AVRLRLALES LGPIFIKFGQ VLSTRPDLIP HDYAVELAKL QDKVPPFDAR LSREQIEKSL GQSIEKLYAE FETEPIASAS IAQVHKARLH SGEQVAVKVL RPNLLPVIEQ DLSLMRFGAG WVERLFADGK RLKPREVVAE FDKYLHDELD LMREAANASQ LGRNFQNSDM LIVPKVFYDY CTSDVLTIEW MDGTPVSDIA KLKADGIDLH KLADYGVEIF FTQVFRDGFF HADMHPGNIL VAADNRYIAL DFGIVGTLTD YDKRYLAINF LAFFNRDYRR VATAHIESGW VPADTRAEEL EAAVRAVCEP VFNKPISQIS FGLVLMRLFE VSRRFNVEIQ PQLVLLQKTL LNIEGLGRQL DPDLDLWKTA KPFLVKWMNG QVGPKALWRN LKNEAPDWAQ IIPSLPRKIS ALIDENRQQE MRDAYIHLVK VQQRQSLWLA VIAVVLLLIL LLK // ID UBIG_NEIMB Reviewed; 238 AA. AC Q9JXI7; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 11-MAY-2016, entry version 87. DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472}; DE AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000255|HAMAP-Rule:MF_00472}; DE EC=2.1.1.222 {ECO:0000255|HAMAP-Rule:MF_00472}; DE AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472}; DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_00472}; GN Name=ubiG {ECO:0000255|HAMAP-Rule:MF_00472}; GN OrderedLocusNames=NMB2030; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation CC steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP- CC Rule:MF_00472}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3- CC demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n. CC {ECO:0000255|HAMAP-Rule:MF_00472}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3-(all-trans- CC polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2- CC methoxy-6-(all-trans-polyprenyl)phenol. {ECO:0000255|HAMAP- CC Rule:MF_00472}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00472}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_00472}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42352.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42352.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_275022.1; NC_003112.2. DR ProteinModelPortal; Q9JXI7; -. DR STRING; 122586.NMB2030; -. DR PaxDb; Q9JXI7; -. DR DNASU; 904071; -. DR EnsemblBacteria; AAF42352; AAF42352; NMB2030. DR GeneID; 904071; -. DR KEGG; nme:NMB2030; -. DR PATRIC; 20360175; VBINeiMen85645_2587. DR eggNOG; ENOG4107RFD; Bacteria. DR eggNOG; COG2227; LUCA. DR HOGENOM; HOG000278065; -. DR KO; K00568; -. DR OMA; HDWEKFV; -. DR OrthoDB; EOG6D5G4H; -. DR BioCyc; NMEN122586:GHGG-2092-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0102004; F:2-octaprenyl-6-hydroxyphenol methylase activity; IEA:UniProtKB-EC. DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro. DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00472; UbiG; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR010233; UbiG_MeTrfase. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR01983; UbiG; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis. FT CHAIN 1 238 Ubiquinone biosynthesis O- FT methyltransferase. FT /FTId=PRO_0000193386. FT BINDING 40 40 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00472}. FT BINDING 59 59 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00472}. FT BINDING 81 81 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00472}. FT BINDING 126 126 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00472}. SQ SEQUENCE 238 AA; 26529 MW; 7CA7305A824BADFF CRC64; MSDKKYNVDE GEIAKFSRIA DKWWDKSGEF KTLHDINPLR LDYIDGHADL CGKRVLDVGC GGGILAESMA RRGAAFVKGI DMAEQSLETA RLHAALNNVA DIEYECIRVE DLAEAEPHSF DVVTCMEMME HVPDPAAIVR ACANLVKPDG MVFFSTINKN PKSYLHLIVA AEYLLKFVPK GTHDWKKFIA PAELARMCRQ AGLDVADTKG MTYHVLSQTY ALCDSTDVNY MFACRPAF // ID UPPP_NEIMB Reviewed; 273 AA. AC Q9K0Z3; Q84BX2; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; GN Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA, upk; GN OrderedLocusNames=NMB0408; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NMB / Serogroup B; RA Post D.M.B., Zaleski A., Gibson B.W., Apicella M.A.; RT "BacA is involved in the assembly of the alpha-chain oligosaccharide RT in Neisseria meningitidis serogroup B."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl CC diphosphate (UPP). Confers resistance to bacitracin. CC {ECO:0000255|HAMAP-Rule:MF_01006}. CC -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate + CC H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01006}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01006}. CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the CC inhibition of peptidoglycan synthesis by sequestering undecaprenyl CC diphosphate, thereby reducing the pool of lipid carrier available. CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP- CC Rule:MF_01006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF469607; AAO85431.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40847.1; -; Genomic_DNA. DR PIR; E81203; E81203. DR RefSeq; NP_273457.1; NC_003112.2. DR RefSeq; WP_002222025.1; NC_003112.2. DR STRING; 122586.NMB0408; -. DR PaxDb; Q9K0Z3; -. DR EnsemblBacteria; AAF40847; AAF40847; NMB0408. DR GeneID; 902522; -. DR KEGG; nme:NMB0408; -. DR PATRIC; 20355999; VBINeiMen85645_0517. DR eggNOG; ENOG4105DWR; Bacteria. DR eggNOG; COG1968; LUCA. DR HOGENOM; HOG000218356; -. DR KO; K06153; -. DR OMA; KVFDIAI; -. DR OrthoDB; EOG6QP13M; -. DR BioCyc; NMEN122586:GHGG-430-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01006; Undec_diphosphatase; 1. DR InterPro; IPR003824; UppP. DR Pfam; PF02673; BacA; 1. DR TIGRFAMs; TIGR00753; undec_PP_bacA; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Hydrolase; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 273 Undecaprenyl-diphosphatase. FT /FTId=PRO_0000151169. FT TRANSMEM 13 35 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 45 62 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 82 102 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 108 128 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 186 206 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 219 239 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 250 270 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT CONFLICT 38 38 G -> D (in Ref. 1; AAO85431). FT {ECO:0000305}. FT CONFLICT 73 73 L -> V (in Ref. 1; AAO85431). FT {ECO:0000305}. FT CONFLICT 107 107 Y -> H (in Ref. 1; AAO85431). FT {ECO:0000305}. FT CONFLICT 240 240 R -> K (in Ref. 1; AAO85431). FT {ECO:0000305}. FT CONFLICT 260 260 A -> V (in Ref. 1; AAO85431). FT {ECO:0000305}. SQ SEQUENCE 273 AA; 30371 MW; 0976868A46AF8FAA CRC64; MDFLIVLKAL MMGLVEGFTE FLPISSTGHL IVFGNLIGFH SNHKVFEIAI QLGAVLAVVF EYRQRFSNVL HGLGKDRKAN RFVLNLAIAF IPAAVMGLLF GKQIKEYLFN PLSVAVMLVL GGFFILWVEK RQSRAEPKIA DVDALRPIDA LMIGVAQVFA LVPGTSRSGS TIMGGMLWGI ERKTATEFSF FLAVPMMVAA TAYDVLKHYR FFTLHDVGLI LIGFIAAFVS GLVAVKALLR FVSKKNYIPF AYYRIVFGIA IIILWLSGWI SWE // ID UBIA_NEIMB Reviewed; 296 AA. AC Q9K083; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635}; DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01635}; DE AltName: Full=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635}; GN Name=ubiA {ECO:0000255|HAMAP-Rule:MF_01635}; GN OrderedLocusNames=NMB0735; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) CC with an all-trans polyprenyl group. Mediates the second step in CC the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, CC which is the condensation of the polyisoprenoid side chain with CC PHB, generating the first membrane-bound Q intermediate 3- CC octaprenyl-4-hydroxybenzoate. {ECO:0000255|HAMAP-Rule:MF_01635}. CC -!- CATALYTIC ACTIVITY: 4-hydroxybenzoate + farnesylfarnesylgeraniol = CC 3-octaprenyl-4-hydroxybenzoate. {ECO:0000255|HAMAP-Rule:MF_01635}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01635}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01635}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01635}. CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01635}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41148.1; -; Genomic_DNA. DR PIR; G81164; G81164. DR RefSeq; NP_273777.1; NC_003112.2. DR RefSeq; WP_002214069.1; NC_003112.2. DR STRING; 122586.NMB0735; -. DR PaxDb; Q9K083; -. DR EnsemblBacteria; AAF41148; AAF41148; NMB0735. DR GeneID; 902848; -. DR KEGG; nme:NMB0735; -. DR PATRIC; 20356829; VBINeiMen85645_0935. DR eggNOG; ENOG4105C4G; Bacteria. DR eggNOG; COG0382; LUCA. DR HOGENOM; HOG000003696; -. DR KO; K03179; -. DR OMA; KSTAIYF; -. DR OrthoDB; EOG680X3B; -. DR BioCyc; NMEN122586:GHGG-764-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01635; UbiA; 1. DR InterPro; IPR031103; HB_octoprenylTrfase. DR InterPro; IPR006370; HB_polyprenyltransferase. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR030470; UbiA_prenylTrfase_CS. DR Pfam; PF01040; UbiA; 1. DR TIGRFAMs; TIGR01474; ubiA_proteo; 1. DR PROSITE; PS00943; UBIA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Magnesium; KW Membrane; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix; Ubiquinone biosynthesis. FT CHAIN 1 296 4-hydroxybenzoate octaprenyltransferase. FT /FTId=PRO_0000262810. FT TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 51 71 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 102 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 143 163 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 174 194 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 212 232 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 233 253 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. FT TRANSMEM 274 294 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01635}. SQ SEQUENCE 296 AA; 33150 MW; A9B961CB2A0FC2FA CRC64; MNPKSPLFLR LSDRLDVYLR LMRADKPIGT LLLLWPTYWA LWLASDGIPD LAVLAAFTIG TFLMRSAGCV INDFADRDFD GAVERTKNRP FAQGRVKKKE ALLLTAFLCL LAALCLIPLN HLTWLMSLPA LFLALTYPFT KRFFPIPQLY LGLAFSFGIP MAFAAVAGNV PPQAWILFAA NVLWTLAYDT VYAMADKEDD LKIGIKTSAV TFGRYDIAAV MLCHGGFTLL MAVLGAVIGA AWAYWTAIPI VLLLQYRQYA AIKSRVRQIC FETFLANNRI GWVWFTAIFA HTFFAK // ID UNG_NEIMB Reviewed; 219 AA. AC Q9JZA1; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148}; DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148}; DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148}; GN Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=NMB1222; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as CC a result of misincorporation of dUMP residues by DNA polymerase or CC due to deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched CC double-stranded DNA and polynucleotides, releasing free uracil. CC {ECO:0000255|HAMAP-Rule:MF_00148}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}. CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family. CC {ECO:0000255|HAMAP-Rule:MF_00148}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41604.1; -; Genomic_DNA. DR PIR; H81107; H81107. DR RefSeq; NP_274247.1; NC_003112.2. DR RefSeq; WP_002224520.1; NC_003112.2. DR ProteinModelPortal; Q9JZA1; -. DR SMR; Q9JZA1; 3-217. DR STRING; 122586.NMB1222; -. DR PaxDb; Q9JZA1; -. DR EnsemblBacteria; AAF41604; AAF41604; NMB1222. DR GeneID; 903644; -. DR KEGG; nme:NMB1222; -. DR PATRIC; 20358027; VBINeiMen85645_1526. DR eggNOG; ENOG4105D5S; Bacteria. DR eggNOG; COG0692; LUCA. DR HOGENOM; HOG000229528; -. DR KO; K03648; -. DR OMA; IALIPKN; -. DR OrthoDB; EOG6MSS63; -. DR BioCyc; NMEN122586:GHGG-1259-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.470.10; -; 1. DR HAMAP; MF_00148; UDG; 1. DR InterPro; IPR018085; Ura-DNA_Glyclase_AS. DR InterPro; IPR002043; Ura_DNA_glycsylse. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR PANTHER; PTHR11264; PTHR11264; 1. DR Pfam; PF03167; UDG; 1. DR SMART; SM00986; UDG; 1. DR SUPFAM; SSF52141; SSF52141; 1. DR TIGRFAMs; TIGR00628; ung; 1. DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Reference proteome. FT CHAIN 1 219 Uracil-DNA glycosylase. FT /FTId=PRO_0000176122. FT ACT_SITE 61 61 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00148}. SQ SEQUENCE 219 AA; 24588 MW; 46D6E58FA283B3F2 CRC64; MDTWHDALGG EKQQPYFQEI LNAVRQERLS GQIIYPPAAD VFNAFRLTAF DRVKAVILGQ DPYHGAGQAH GLAFSVRQGI RIPPSLLNIY KELETDIEGF SIPAHGCLTA WAEQGVLLLN TVLTVRAGQA HSHALLGWER FTDTVIRQLA THRKHLVFML WGGYAQQKGR LIDSQNHLIL TAPHPSPLSA YRGFFGCRHF SQANSYLSRH GIDPINWKL // ID TTCA_NEIMB Reviewed; 319 AA. AC Q9JZJ6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000255|HAMAP-Rule:MF_01850}; GN Name=ttcA {ECO:0000255|HAMAP-Rule:MF_01850}; GN OrderedLocusNames=NMB1023; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Required for the thiolation of cytidine in position 32 CC of tRNA, to form 2-thiocytidine (s(2)C32). {ECO:0000255|HAMAP- CC Rule:MF_01850}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01850}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP- CC Rule:MF_01850}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41423.1; -; Genomic_DNA. DR PIR; F81129; F81129. DR RefSeq; NP_274057.1; NC_003112.2. DR RefSeq; WP_002222563.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ6; -. DR STRING; 122586.NMB1023; -. DR PaxDb; Q9JZJ6; -. DR EnsemblBacteria; AAF41423; AAF41423; NMB1023. DR GeneID; 903161; -. DR KEGG; nme:NMB1023; -. DR PATRIC; 20357581; VBINeiMen85645_1307. DR eggNOG; ENOG4105CB3; Bacteria. DR eggNOG; COG0037; LUCA. DR HOGENOM; HOG000013323; -. DR KO; K14058; -. DR OMA; IVQENTY; -. DR OrthoDB; EOG60KN2F; -. DR BioCyc; NMEN122586:GHGG-1060-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01850; TtcA; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 319 tRNA 2-thiocytidine biosynthesis protein FT TtcA. FT /FTId=PRO_0000320327. FT NP_BIND 43 48 ATP. {ECO:0000255|HAMAP-Rule:MF_01850}. FT MOTIF 118 121 CXXC. FT MOTIF 206 209 CXXC. SQ SEQUENCE 319 AA; 35941 MW; 0826D832A1B014D4 CRC64; MSKKTKQELE NNKLSKRLRH AVGDAINDFN MIEPDDKIMV CLSGGKDSYA LLDILRQLQA SAPIDFQLVA VNLDQKQPGF PEEVLPTYLE SIGVPYKIVE EDTYSTVKRV LDEGKTTCSL CSRLRRGILY RTAKELGCTK IALGHHRDDI LATLFLNMFY GGKLKAMPPK LVSDNGEHIV IRPLAYVKEK DLIKYAELKQ FPIIPCNLCG SQPNLQRQVI GDMLRDWDKR FPGRIESMFS ALQNVVPSHL ADTELFDFVG LERGQSLKHG GDLAFDSEKM PERFSDGSEE DESEIKIEPQ KAERKVINIL ANKPKTCGS // ID TYSY_NEIMB Reviewed; 264 AA. AC Q9JY72; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_00008}; DE Short=TS {ECO:0000255|HAMAP-Rule:MF_00008}; DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_00008}; DE EC=2.1.1.45 {ECO:0000255|HAMAP-Rule:MF_00008}; GN Name=thyA {ECO:0000255|HAMAP-Rule:MF_00008}; GN OrderedLocusNames=NMB1709; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Provides the sole de novo source of dTMP for DNA CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = CC dihydrofolate + dTMP. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}. CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial- CC type ThyA subfamily. {ECO:0000255|HAMAP-Rule:MF_00008}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42056.1; -; Genomic_DNA. DR PIR; G81050; G81050. DR RefSeq; NP_274712.1; NC_003112.2. DR RefSeq; WP_002212612.1; NC_003112.2. DR ProteinModelPortal; Q9JY72; -. DR SMR; Q9JY72; 1-264. DR STRING; 122586.NMB1709; -. DR PaxDb; Q9JY72; -. DR EnsemblBacteria; AAF42056; AAF42056; NMB1709. DR GeneID; 903393; -. DR KEGG; nme:NMB1709; -. DR PATRIC; 20359377; VBINeiMen85645_2194. DR eggNOG; ENOG4105C0V; Bacteria. DR eggNOG; COG0207; LUCA. DR HOGENOM; HOG000257899; -. DR KO; K00560; -. DR OMA; IVYELLW; -. DR OrthoDB; EOG6K6V53; -. DR BioCyc; NMEN122586:GHGG-1764-MONOMER; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.572.10; -; 1. DR HAMAP; MF_00008; Thymidy_synth_bact; 1. DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease. DR InterPro; IPR000398; Thymidylate_synthase. DR InterPro; IPR020940; Thymidylate_synthase_AS. DR Pfam; PF00303; Thymidylat_synt; 1. DR PRINTS; PR00108; THYMDSNTHASE. DR SUPFAM; SSF55831; SSF55831; 1. DR TIGRFAMs; TIGR03284; thym_sym; 2. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW Nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 264 Thymidylate synthase. FT /FTId=PRO_0000140994. FT ACT_SITE 146 146 {ECO:0000255|HAMAP-Rule:MF_00008}. SQ SEQUENCE 264 AA; 30277 MW; 012C15B55FE16BE2 CRC64; MKAYLDLMRH VLDNGTDKSD RTGTGTRSVF GYQMRFDLGK GFPLLTTKKL HLRSIIHELL WFLKGDTNIK YLKDNNVSIW DEWADENGDL GPVYGYQWRN WPAPDGRHID QIANVLEQIK KNPDSRRLIV SAWNPALVDE MALPPCHALF QFYVADGKLS CQLYQRSADI FLGVPFNIAS YALLTMMMAQ VCGLEAGEFV HTFGDAHLYR NHFEQAALQL EREPRALPVM KINPEVKDLF SFKFEDFELE GYDPHPHIKA AVSV // ID UBID_NEIMB Reviewed; 492 AA. AC Q9JY86; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 11-MAY-2016, entry version 97. DE RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase {ECO:0000255|HAMAP-Rule:MF_01636}; DE EC=4.1.1.98 {ECO:0000255|HAMAP-Rule:MF_01636}; DE AltName: Full=Polyprenyl p-hydroxybenzoate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01636}; GN Name=ubiD {ECO:0000255|HAMAP-Rule:MF_01636}; GN OrderedLocusNames=NMB1694; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy CC benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636}. CC -!- CATALYTIC ACTIVITY: A 4-hydroxy-3-polyprenylbenzoate = a 2- CC polyprenylphenol + CO(2). {ECO:0000255|HAMAP-Rule:MF_01636}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01636}; CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01636}; CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01636}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01636}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01636}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01636}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01636}. CC -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000255|HAMAP- CC Rule:MF_01636}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42042.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42042.1; ALT_INIT; Genomic_DNA. DR PIR; H81051; H81051. DR RefSeq; NP_274698.1; NC_003112.2. DR RefSeq; WP_002224977.1; NC_003112.2. DR ProteinModelPortal; Q9JY86; -. DR SMR; Q9JY86; 3-492. DR STRING; 122586.NMB1694; -. DR PaxDb; Q9JY86; -. DR EnsemblBacteria; AAF42042; AAF42042; NMB1694. DR GeneID; 903410; -. DR KEGG; nme:NMB1694; -. DR PATRIC; 20359341; VBINeiMen85645_2177. DR eggNOG; ENOG4105D3H; Bacteria. DR eggNOG; COG0043; LUCA. DR HOGENOM; HOG000227663; -. DR KO; K03182; -. DR OMA; DFQEWCQ; -. DR OrthoDB; EOG6QZMM7; -. DR BioCyc; NMEN122586:GHGG-1749-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01636; UbiD; 1. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR InterPro; IPR002830; UbiD. DR InterPro; IPR023677; UbiD_bacteria. DR Pfam; PF01977; UbiD; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR00148; TIGR00148; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Decarboxylase; Lyase; Manganese; KW Membrane; Metal-binding; Reference proteome; Ubiquinone biosynthesis. FT CHAIN 1 492 3-octaprenyl-4-hydroxybenzoate carboxy- FT lyase. FT /FTId=PRO_0000157362. FT REGION 177 182 prenyl-FMN binding. {ECO:0000255|HAMAP- FT Rule:MF_01636}. FT REGION 199 200 prenyl-FMN binding. {ECO:0000255|HAMAP- FT Rule:MF_01636}. FT ACT_SITE 292 292 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01636}. FT METAL 177 177 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01636}. FT METAL 243 243 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01636}. SQ SEQUENCE 492 AA; 55525 MW; CFCA201F2EB370E5 CRC64; MKYKDLRDFI AMLEQQGKLK RVAHPISPYL EMTEIADRVL RAEGPALLFE NPIKPDGTRY GYPVLANLFG TPERVAMGMG ADSVSKLREI GQTLAYLKEP EPPKGIKDAF SKLPLLKDIW SMAPNVVKNA PCQEIVWEGE DVDLYQLPIQ HCWPEDVAPL VTWGLTVTRG PHKKRQNLGI YRQQLIGKNK LIMRWLSHRG GALDYQEFRK LNPDTPYPVA VVLGCDPATI LGAVTPVPDT LSEYQFAGLL RGSRTELVKC IGNDLQVPAR AEIVLEGVIH PNETALEGPY GDHTGYYNEQ DYFPVFTVER ITMRENPIYH STYTGKPPDE PAVLGVALNE VFVPLLQKQF PEITDFYLPP EGCSYRMAVV SMKKQYAGHA KRVMMGCWSF LRQFMYTKFI IVVDDDVNVR DWKEVIWAVT TRMDPVRDTV LVENTPIDYL DFASPVSGLG GKMGLDATNK WPGETDREWG RVIKKDPAVT AKIDGIWEEL GL // ID UBIE_NEIMB Reviewed; 245 AA. AC Q9K075; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000255|HAMAP-Rule:MF_01813}; DE EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813}; DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_01813}; DE AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000255|HAMAP-Rule:MF_01813}; DE AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813}; GN Name=ubiE {ECO:0000255|HAMAP-Rule:MF_01813}; GN OrderedLocusNames=NMB0743; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Methyltransferase required for the conversion of CC demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion CC of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2- CC polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- CATALYTIC ACTIVITY: A demethylmenaquinol + S-adenosyl-L-methionine CC = a menaquinol + S-adenosyl-L-homocysteine. {ECO:0000255|HAMAP- CC Rule:MF_01813}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 2-methoxy-6-all- CC trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6- CC methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. MenG/UbiE family. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41156.1; -; Genomic_DNA. DR PIR; F81162; F81162. DR RefSeq; NP_273785.1; NC_003112.2. DR RefSeq; WP_002217627.1; NC_003112.2. DR ProteinModelPortal; Q9K075; -. DR STRING; 122586.NMB0743; -. DR PaxDb; Q9K075; -. DR EnsemblBacteria; AAF41156; AAF41156; NMB0743. DR GeneID; 902858; -. DR KEGG; nme:NMB0743; -. DR PATRIC; 20356857; VBINeiMen85645_0947. DR eggNOG; ENOG4105DDZ; Bacteria. DR eggNOG; COG2226; LUCA. DR HOGENOM; HOG000249463; -. DR KO; K03183; -. DR OMA; GGLHRAW; -. DR OrthoDB; EOG6M6JSB; -. DR BioCyc; NMEN122586:GHGG-774-MONOMER; -. DR UniPathway; UPA00079; UER00169. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0102005; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC. DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009060; P:aerobic respiration; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004033; UbiE/COQ5_MeTrFase. DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS. DR Pfam; PF01209; Ubie_methyltran; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1. DR PROSITE; PS51608; SAM_MT_UBIE; 1. DR PROSITE; PS01183; UBIE_1; 1. DR PROSITE; PS01184; UBIE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Menaquinone biosynthesis; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW Ubiquinone biosynthesis. FT CHAIN 1 245 Ubiquinone/menaquinone biosynthesis C- FT methyltransferase UbiE. FT /FTId=PRO_0000193301. FT REGION 118 119 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01813}. FT BINDING 71 71 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01813}. FT BINDING 92 92 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01813}. SQ SEQUENCE 245 AA; 27366 MW; 256E82361E6246C7 CRC64; MGGQKTHFGF STVNEDEKAG KVAEVFHSVA KNYDIMNDVM SAGLHRVWKH FTINTAHLKK GDKVLDIAGG TGDLSRGWAK RVGKEGEVWL TDINSSMLTV GRDRLLNEGM ILPVSLADAE KLPFPDNYFN LVSVAFGLRN MTHKDAALKE MYRVLKPGGT LLVLEFSKIY KPLEGAYDFY SFKLLPVMGR LIAKDAESYQ YLAESIRMHP DQETLKQMML DAGFDSVDYH NMSAGIVALH KGVKF // ID UVRC_NEIMB Reviewed; 617 AA. AC Q9JZ26; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203}; DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203}; DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203}; GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; GN OrderedLocusNames=NMB1326; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrC both incises the 5' and 3' sides CC of the lesion. The N-terminal half is responsible for the 3' CC incision and the C-terminal half is responsible for the 5' CC incision. {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBUNIT: Interacts with UvrB in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41701.1; -; Genomic_DNA. DR PIR; A81095; A81095. DR RefSeq; NP_274345.1; NC_003112.2. DR RefSeq; WP_010980922.1; NC_003112.2. DR ProteinModelPortal; Q9JZ26; -. DR SMR; Q9JZ26; 563-617. DR STRING; 122586.NMB1326; -. DR PaxDb; Q9JZ26; -. DR EnsemblBacteria; AAF41701; AAF41701; NMB1326. DR GeneID; 903748; -. DR KEGG; nme:NMB1326; -. DR PATRIC; 20358303; VBINeiMen85645_1663. DR eggNOG; ENOG4105CII; Bacteria. DR eggNOG; COG0322; LUCA. DR HOGENOM; HOG000279961; -. DR KO; K03703; -. DR OMA; LFPIRQC; -. DR OrthoDB; EOG6K13R9; -. DR BioCyc; NMEN122586:GHGG-1364-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1440.10; -; 1. DR Gene3D; 4.10.860.10; -; 1. DR HAMAP; MF_00203; UvrC; 1. DR InterPro; IPR027299; GIY-YIG_dom. DR InterPro; IPR000305; GIY-YIG_SF. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004791; UvrC. DR InterPro; IPR001162; UvrC_homol_region. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF08459; UvrC_HhH_N; 1. DR SMART; SM00465; GIYc; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF46600; SSF46600; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR TIGRFAMs; TIGR00194; uvrC; 1. DR PROSITE; PS50164; GIY_YIG; 1. DR PROSITE; PS50151; UVR; 1. DR PROSITE; PS50165; UVRC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA excision; DNA repair; KW Excision nuclease; Reference proteome; SOS response. FT CHAIN 1 617 UvrABC system protein C. FT /FTId=PRO_0000138323. FT DOMAIN 22 100 GIY-YIG. {ECO:0000255|HAMAP- FT Rule:MF_00203}. FT DOMAIN 209 244 UVR. {ECO:0000255|HAMAP-Rule:MF_00203}. SQ SEQUENCE 617 AA; 69822 MW; D2C4B27DF44113AF CRC64; MNKETRFPEH FDIPLFLKNL PNLPGVYRFF NESGNVLYVG KAVNLKRRVS GYFQKNDHSP RIALMVKQVH HIETTITRSE SEALILENNF IKALSPKYNI LFRDDKSYPY LMLSGHQYPQ MAYYRGTLKK PNQYFGPYPN SNAVRDSIQV LQKVFMLRTC EDSVFEHRDR PCLLYQIKRC TAPCVGHISE EDYRDSVREA ATFLNGKTDE LTRTLQHKMQ TAAANLQFEE AARYRDQIQA LGIMQSNQFI DSKNPNNPND IDLLALAVSD GLVCVHWVSI RGGRHVGDKS FFPDTKNDPE PNGQDYAEAF VAQHYLGKSK PDIIISNFPV PDALKEALEG EHGKQMQFVT KTIGERKVRL KMAEQNAQMA IAQRRLQQSS QQHRIDELAK ILGMDSDGLN RLECFDISHT QGEATIASCV VYDEQNIQPS QYRRYNITTA KPGDDYAAMR EVLTRRYGKM QEAEANGETV KWPDAVLIDG GKGQIGVAVS VWEELGLHIP LVGIAKGPER KAGMEELILP FTGEVFRLPP NSPALHLLQT VRDESHRFAI TGHRKKRDKA RVTSSLSDIP GVGSKRRQAL LTRFGGLRGV IAASREDLEK VEGISKALAE TIYNHLH // ID UPP_NEIMB Reviewed; 208 AA. AC Q9K048; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218}; DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218}; GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=NMB0774; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha- CC D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg- CC PRPP. {ECO:0000255|HAMAP-Rule:MF_01218}; CC -!- ENZYME REGULATION: Allosterically activated by GTP. CC {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uracil: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01218}. CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP- CC Rule:MF_01218}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41187.1; -; Genomic_DNA. DR PIR; C81160; C81160. DR RefSeq; NP_273816.1; NC_003112.2. DR RefSeq; WP_002225428.1; NC_003112.2. DR ProteinModelPortal; Q9K048; -. DR SMR; Q9K048; 6-208. DR STRING; 122586.NMB0774; -. DR PaxDb; Q9K048; -. DR PRIDE; Q9K048; -. DR EnsemblBacteria; AAF41187; AAF41187; NMB0774. DR GeneID; 902889; -. DR KEGG; nme:NMB0774; -. DR PATRIC; 20356923; VBINeiMen85645_0980. DR eggNOG; ENOG4105CZ5; Bacteria. DR eggNOG; COG0035; LUCA. DR HOGENOM; HOG000262754; -. DR KO; K00761; -. DR OMA; NTHLWIA; -. DR OrthoDB; EOG6HF5WX; -. DR BioCyc; NMEN122586:GHGG-805-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006223; P:uracil salvage; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01218_B; Upp_B; 1. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005765; Ura_phspho_trans. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01091; upp; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Glycosyltransferase; KW GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 208 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120861. FT REGION 130 138 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT REGION 198 200 Uracil binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT BINDING 78 78 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 103 103 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 193 193 Uracil; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 199 199 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. SQ SEQUENCE 208 AA; 22742 MW; F9DF2613C03F087B CRC64; MNVNVINHPL VRHKLTLMRE ADCSTYKFRT LATELARLMA YEASRDFEIE KYLIDGWCGQ IEGDRIKGKT LTVVPILRAG LGMLDGVLDL IPTAKISVVG LQRDEETLKP ISYFEKFVDS MDERPALIID PMLATGGSMV ATIDLLKAKG CKNIKALVLV AAPEGVKAVN DAHPDVTIYT AALDSHLNEN GYIIPGLGDA GDKIFGTR // ID UVRA_NEIMB Reviewed; 949 AA. AC Q9JZP1; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205}; DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; GN OrderedLocusNames=NMB0962; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding CC protein. A damage recognition complex composed of 2 UvrA and 2 CC UvrB subunits scans DNA for abnormalities. When the presence of a CC lesion has been verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41368.1; -; Genomic_DNA. DR PIR; A81138; A81138. DR RefSeq; NP_274000.1; NC_003112.2. DR RefSeq; WP_002244094.1; NC_003112.2. DR ProteinModelPortal; Q9JZP1; -. DR SMR; Q9JZP1; 13-948. DR STRING; 122586.NMB0962; -. DR PaxDb; Q9JZP1; -. DR EnsemblBacteria; AAF41368; AAF41368; NMB0962. DR GeneID; 903082; -. DR KEGG; nme:NMB0962; -. DR PATRIC; 20357407; VBINeiMen85645_1218. DR eggNOG; ENOG4105C5U; Bacteria. DR eggNOG; COG0178; LUCA. DR HOGENOM; HOG000050448; -. DR KO; K03701; -. DR OMA; GAIKGWD; -. DR OrthoDB; EOG6QK4PS; -. DR BioCyc; NMEN122586:GHGG-999-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.40.50.300; -; 4. DR HAMAP; MF_00205; UvrA; 1. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004602; UvrA. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; DNA-binding; Excision nuclease; Metal-binding; KW Nucleotide-binding; Reference proteome; Repeat; SOS response; Zinc; KW Zinc-finger. FT CHAIN 1 949 UvrABC system protein A. FT /FTId=PRO_0000093073. FT DOMAIN 319 596 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT DOMAIN 616 945 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 262 289 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 649 656 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 748 774 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. SQ SEQUENCE 949 AA; 105537 MW; 153F5AE2D48CDD35 CRC64; MCNHHPQHSH DNDTIRIRGA RTHNLKNIDL DIPRHKLVVV TGLSGSGKSS LAFDTLYAEG QRRYVESLSA YARQFLQMMD KPDVDLIEGL SPAISIEQKS TSHNPRSTVG TVTEIHDYLR LLYARVGTPY CPEHKLPLSS QTVSQMVDAV LKLPEDTRVM ILAPTVRERK GEFVDFFADL QAQGFARVRV DGEVYQLDEV PKLEKNIKHN IDVVIDRVKV KADIKQRLAE SFETALRHGN ERALAMEMDS GEEHWFSARF ACPVCSYSLP ELEPRLFSFN NPMGSCPTCD GLGNTNFFDP EKVVAHPELS LATGAIDGWD KRNQFYFQMI QSLARHYGFD VQAAWETLPE KVKKVVLHGS GKEVIDFTYL SERGTTFNRS HAFEGIIPNL ERRYRETDSE TVREKLREYQ NHRACPSCGG ARLRKEARYV YVSGEPLHEV SAWPLTKTHQ FFETLDLDGN KKQIAEKILK EITERLGFLI NVGLDYLNLS RSAETLSGGE AQRIRLASQI GSGLTGVMYV LDEPSIGLHQ RDNDRLLATL KRLRDLGNSV IVVEHDEDAI READFVVDMG PGAGEHGGNV LIADTPENVA QCENSVTGQY LSGKKSIAVP SERTPVNPDR MLVLKGARGN NLKNVTLELP LGLITCITGV SGSGKSTLIN DTLAKITARE LNRAQEEPAP FDDIHGLEHL DKVINVDQSP IGRTPRSNPA TYTGLFTPIR ELFAGVPLSR ERGYNVGRFS FNVKGGRCEA CQGDGVIKVE MHFLPDVYVP CEVCHGKRYN RETLEIQYKG KNISQVLDMT VEEAREFFDA VPTVSRKLQT LMDVGLGYIR LGQSATTLSG GEAQRVKLAL ELSKRDTGRT LYILDEPTTG LHFADIALLL EVIGRLKGKG NSIVIIEHNL DVIKTADWIV DLGPEGGDGG GRIIAKGSPE QVAKVKGSYT GKYLKVVLR // ID UVRB_NEIMB Reviewed; 675 AA. AC O33395; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 11-NOV-2015, entry version 104. DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204}; DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204}; DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204}; GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; GN OrderedLocusNames=NMB1331; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SD / Serogroup B / Serotype 15 / Subtype 16; RA Kizil G., Wilks K.E., Palmer H.M., Ala'Aldeen D.A.A.; RT "Detection and characterisation of meningococcal ultraviolet RT resistance gene (uvrB)."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. A damage recognition complex composed CC of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon CC binding of the UvrA(2)B(2) complex to a putative damaged site, the CC DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP CC binding by UvrB and probably causes local melting of the DNA CC helix, facilitating insertion of UvrB beta-hairpin between the DNA CC strands. Then UvrB probes one DNA strand for the presence of a CC lesion. If a lesion is found the UvrA subunits dissociate and the CC UvrB-DNA preincision complex is formed. This complex is CC subsequently bound by UvrC and the second UvrB is released. If no CC lesion is found, the DNA wraps around the other UvrB subunit that CC will check the other stand for damage. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y14299; CAA74675.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41706.1; -; Genomic_DNA. DR PIR; F81095; F81095. DR RefSeq; NP_274350.1; NC_003112.2. DR RefSeq; WP_002244151.1; NC_003112.2. DR ProteinModelPortal; O33395; -. DR SMR; O33395; 9-601. DR STRING; 122586.NMB1331; -. DR PaxDb; O33395; -. DR EnsemblBacteria; AAF41706; AAF41706; NMB1331. DR GeneID; 903753; -. DR KEGG; nme:NMB1331; -. DR PATRIC; 20358315; VBINeiMen85645_1669. DR eggNOG; ENOG4105CCW; Bacteria. DR eggNOG; COG0556; LUCA. DR HOGENOM; HOG000073580; -. DR KO; K03702; -. DR OMA; QEYVDRM; -. DR OrthoDB; EOG6B360R; -. DR BioCyc; NMEN122586:GHGG-1369-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 4. DR Gene3D; 4.10.860.10; -; 1. DR HAMAP; MF_00204; UvrB; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004807; UvrB. DR InterPro; IPR024759; UvrB_YAD/RRR_dom. DR PANTHER; PTHR24029; PTHR24029; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF04851; ResIII; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF12344; UvrB; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF46600; SSF46600; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00631; uvrb; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50151; UVR; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome; KW SOS response. FT CHAIN 1 675 UvrABC system protein B. FT /FTId=PRO_0000138416. FT DOMAIN 32 417 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 436 602 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 634 669 UVR. {ECO:0000255|HAMAP-Rule:MF_00204}. FT NP_BIND 45 52 ATP. {ECO:0000255|HAMAP-Rule:MF_00204}. FT MOTIF 98 121 Beta-hairpin. FT CONFLICT 449 449 E -> Q (in Ref. 1; CAA74675). FT {ECO:0000305}. FT CONFLICT 587 587 Q -> H (in Ref. 1; CAA74675). FT {ECO:0000305}. FT CONFLICT 611 612 GS -> SG (in Ref. 1; CAA74675). FT {ECO:0000305}. FT CONFLICT 616 617 LK -> RQ (in Ref. 1; CAA74675). FT {ECO:0000305}. FT CONFLICT 665 665 D -> N (in Ref. 1; CAA74675). FT {ECO:0000305}. SQ SEQUENCE 675 AA; 76914 MW; 6F2634F34EB77D43 CRC64; MEVIQYPNSP FKLHQPFPPA GDQPTAIAGL LEGLSDGLAY QTLLGVTGSG KTYTMANVIA QSGRPAIIMA HNKTLAAQLY AEMREFFPEN AVEYFVSYYD YYQPEAYVPS RDLFIEKDSA INEHIEQMRL SATKNLMTRN DVIIVATVSA IYGIGDPTEY QQMVLSVKEG DTIEQRDIIA TLVSMQYERG DLDFKRGSFR VRGDVIDVYP AESSENALRI SLFDDEIDRL DMFDPLSGSL IQRVGRYTVF PSSHYVTPRD TVLRACESIK EELRERIEFF AREQRPVEQQ RIEQRTRFDL EMLYEMGFCK GIENYSRHFS GKKEGEPPPT LMDYLPDNAI MFIDESHVTV TQIGGMYKGD ASRKQNLVDY GFRLPSARDN RPLKFHEFEK VMPQTIFVSA TPAKYEEEHA GQVVEQVVRP TGLVDPQIII RPVATQVDDL MSEINDRIEK GERVLVTTLT KRMAEQLTDY YSELGIKVRY LHSDIDTVER VEIIRDLRLG LFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSHRSL IQTIGRAARN VNGVAILYAD KITDSMKAAI DETERRREKQ IKFNEEQGIV PQQIKKQVKD IIDGVYHEED GSKGRLKGKN KVKVGEIHNE EDAIKEIAKL EKAMQQAARD LQFEEAAVLR DRIRDIKENL LFGAE // ID XERC_NEIMB Reviewed; 301 AA. AC Q9JXV6; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808}; GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; GN OrderedLocusNames=NMB1868; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by CC catalyzing the cutting and rejoining of the recombining DNA CC molecules. The XerC-XerD complex is essential to convert dimers of CC the bacterial chromosome into monomers to permit their segregation CC at cell division. It also contributes to the segregational CC stability of plasmids. {ECO:0000255|HAMAP-Rule:MF_01808}. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP- CC Rule:MF_01808}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01808}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42202.1; -; Genomic_DNA. DR PIR; B81032; B81032. DR RefSeq; NP_274864.1; NC_003112.2. DR RefSeq; WP_002225783.1; NC_003112.2. DR ProteinModelPortal; Q9JXV6; -. DR STRING; 122586.NMB1868; -. DR PaxDb; Q9JXV6; -. DR EnsemblBacteria; AAF42202; AAF42202; NMB1868. DR GeneID; 904320; -. DR KEGG; nme:NMB1868; -. DR PATRIC; 20359765; VBINeiMen85645_2388. DR eggNOG; ENOG4108IYS; Bacteria. DR eggNOG; COG4973; LUCA. DR HOGENOM; HOG000045294; -. DR KO; K03733; -. DR OMA; ERQVSPH; -. DR OrthoDB; EOG6PZXFP; -. DR BioCyc; NMEN122586:GHGG-1924-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR HAMAP; MF_01808; Recomb_XerC_XerD; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR InterPro; IPR004107; Integrase_SAM-like_N. DR InterPro; IPR011931; Recomb_XerC. DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD. DR Pfam; PF02899; Phage_int_SAM_1; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. DR TIGRFAMs; TIGR02224; recomb_XerC; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; DNA integration; DNA recombination; DNA-binding; KW Reference proteome. FT CHAIN 1 301 Tyrosine recombinase XerC. FT /FTId=PRO_0000095310. FT ACT_SITE 151 151 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 175 175 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 242 242 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 245 245 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 268 268 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 277 277 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01808}. SQ SEQUENCE 301 AA; 33993 MW; A75A3ED5B1E5A05A CRC64; MGLDGLAAYL DAYLENIVRE GKSEHTVAAY RRDLQELLAL LEEMPSANPS NCTRGDFVQA LRRLSGRGLG ERTLARKLSS WRQYCVWLVK RGLMHADPTA DIKPPKQPER VPKALPQEWL NRMLDLPVDG GDPLAVRDHA LFELMYGSGL RVSEIHGLNA DDVYLDEAWV HVIGKGRKQR QVPLVGKSVE ALKNYLPLRQ TASDGKALFT GRNGTRLSQR QIQKRLAQWA AQNGDGRHVS PHMMRHSYAG HLLQASRDIR AVQELLGHSS LSTTQIYTKL DFDHIARLYD EAHPRAKRQD E // ID Y1038_NEIMB Reviewed; 225 AA. AC Q9JZI3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=UPF0758 protein NMB1038; GN OrderedLocusNames=NMB1038; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41437.1; -; Genomic_DNA. DR PIR; A81129; A81129. DR RefSeq; NP_274072.1; NC_003112.2. DR RefSeq; WP_002213447.1; NC_003112.2. DR ProteinModelPortal; Q9JZI3; -. DR STRING; 122586.NMB1038; -. DR PaxDb; Q9JZI3; -. DR EnsemblBacteria; AAF41437; AAF41437; NMB1038. DR GeneID; 903175; -. DR KEGG; nme:NMB1038; -. DR PATRIC; 20357611; VBINeiMen85645_1322. DR eggNOG; ENOG4105W5Q; Bacteria. DR eggNOG; COG2003; LUCA. DR HOGENOM; HOG000273376; -. DR KO; K03630; -. DR OMA; PHEEFWV; -. DR OrthoDB; EOG6RRKTV; -. DR BioCyc; NMEN122586:GHGG-1075-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR001405; RadC. DR InterPro; IPR025657; RadC_JAB. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF04002; RadC; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00608; radc; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 225 UPF0758 protein NMB1038. FT /FTId=PRO_0000190712. SQ SEQUENCE 225 AA; 24940 MW; 8D4A2347776E0D6A CRC64; MSIKQWPEGE RPREKLLERG AAALSDAELL AILLRVGTRG MSAVDLARYL LQEFGSLGRL MSAEVGKLSA YKGMGTASFT QFAVVREIGR RILAEELQES IVLSDPDTVA DYLRFHLGQE KVEVSVALLL NRQNQLIAVR ELSRGTVAEN TIYIREIVKL ALDEYADSLI IAHNHPGGSP EPSQEDIMFT RRLAQAMSLV DVSLLDHFIV TSQSVCSFRQ LGLMP // ID Y1218_NEIMB Reviewed; 91 AA. AC P67536; Q9JRI4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=UPF0250 protein NMB1218 {ECO:0000255|HAMAP-Rule:MF_00659}; GN OrderedLocusNames=NMB1218; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0250 family. {ECO:0000255|HAMAP- CC Rule:MF_00659}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41600.1; -; Genomic_DNA. DR PIR; F81109; F81109. DR RefSeq; NP_274243.1; NC_003112.2. DR RefSeq; WP_002217171.1; NC_003112.2. DR ProteinModelPortal; P67536; -. DR STRING; 122586.NMB1218; -. DR PaxDb; P67536; -. DR EnsemblBacteria; AAF41600; AAF41600; NMB1218. DR GeneID; 903640; -. DR KEGG; nme:NMB1218; -. DR PATRIC; 20358017; VBINeiMen85645_1521. DR eggNOG; ENOG4108Z43; Bacteria. DR eggNOG; COG2921; LUCA. DR HOGENOM; HOG000265101; -. DR KO; K09158; -. DR OMA; KVMGLAK; -. DR OrthoDB; EOG6BGP43; -. DR BioCyc; NMEN122586:GHGG-1255-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.70.1460; -; 1. DR HAMAP; MF_00659; UPF0250; 1. DR InterPro; IPR007454; UPF0250. DR InterPro; IPR027471; YbeD-like. DR Pfam; PF04359; DUF493; 1. DR SUPFAM; SSF117991; SSF117991; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 91 UPF0250 protein NMB1218. FT /FTId=PRO_0000209302. SQ SEQUENCE 91 AA; 10228 MW; 0C8134C284B66288 CRC64; MTEQKNKTSL IEFPCTFPLK VMGAVHPEFE QAVLDTVRLH APDTQAHHIT TRPSSKGNYT GATVQVKVEN QEQLDNIYRA LTSHELVKVV L // ID Y1133_NEIMB Reviewed; 253 AA. AC Q9JRZ6; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative ankyrin repeat protein NMB1133/NMB1171; GN OrderedLocusNames=NMB1133; GN and GN OrderedLocusNames=NMB1171; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 2 ANK repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41521.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41556.1; -; Genomic_DNA. DR PIR; D81118; D81118. DR RefSeq; NP_274162.1; NC_003112.2. DR RefSeq; NP_274198.1; NC_003112.2. DR RefSeq; WP_002244131.1; NC_003112.2. DR ProteinModelPortal; Q9JRZ6; -. DR STRING; 122586.NMB1171; -. DR PaxDb; Q9JRZ6; -. DR EnsemblBacteria; AAF41521; AAF41521; NMB1133. DR EnsemblBacteria; AAF41556; AAF41556; NMB1171. DR GeneID; 903554; -. DR GeneID; 903591; -. DR KEGG; nme:NMB1133; -. DR KEGG; nme:NMB1171; -. DR PATRIC; 20357841; VBINeiMen85645_1436. DR eggNOG; ENOG4108NPY; Bacteria. DR eggNOG; COG0666; LUCA. DR eggNOG; COG3779; LUCA. DR HOGENOM; HOG000220744; -. DR KO; K06867; -. DR OMA; EHMWIND; -. DR OrthoDB; EOG6GXTRB; -. DR BioCyc; NMEN122586:GHGG-1169-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1206-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR018756; DUF2314. DR Pfam; PF10077; DUF2314; 1. DR SMART; SM00248; ANK; 1. DR SUPFAM; SSF48403; SSF48403; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. PE 3: Inferred from homology; KW ANK repeat; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 253 Putative ankyrin repeat protein FT NMB1133/NMB1171. FT /FTId=PRO_0000067239. FT REPEAT 196 225 ANK 1. FT REPEAT 229 252 ANK 2. SQ SEQUENCE 253 AA; 29197 MW; 989BAB1332CB9A44 CRC64; MMGDSVIYYV EQADEPVNRA DERARKTFKY FWRELFWERR RIISALDFAM VKVPFFQDGE DGEICEHMWI DDIYFDGLYI YGVLNNEPGE LTNVEQGESV CVPVDDISDW MFVCNGIPYG GFTIQAMRGQ MTEEERTEHD AAWGIDFGDP GQILLVYEEK EHPENLEEHP MCRNCIDDFR QQLSQNSDYL REQDEDGYTP LHHEAIAGNA LMVQAMLEYG ANPASTTSEG YTALDFACLT GWQNVADLLE PRH // ID Y1336_NEIMB Reviewed; 182 AA. AC Q9JZ17; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=UPF0301 protein NMB1336 {ECO:0000255|HAMAP-Rule:MF_00758}; GN OrderedLocusNames=NMB1336; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0301 (AlgH) family. CC {ECO:0000255|HAMAP-Rule:MF_00758}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41711.1; -; Genomic_DNA. DR PIR; H81093; H81093. DR RefSeq; NP_274355.1; NC_003112.2. DR RefSeq; WP_002222355.1; NC_003112.2. DR ProteinModelPortal; Q9JZ17; -. DR STRING; 122586.NMB1336; -. DR PaxDb; Q9JZ17; -. DR EnsemblBacteria; AAF41711; AAF41711; NMB1336. DR GeneID; 903758; -. DR KEGG; nme:NMB1336; -. DR PATRIC; 20358327; VBINeiMen85645_1675. DR eggNOG; ENOG4108UJU; Bacteria. DR eggNOG; COG1678; LUCA. DR HOGENOM; HOG000281193; -. DR KO; K07735; -. DR OMA; IYICAHS; -. DR OrthoDB; EOG6RVFX5; -. DR BioCyc; NMEN122586:GHGG-1374-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_00758; UPF0301; 1. DR InterPro; IPR003774; UPF0301. DR Pfam; PF02622; DUF179; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 182 UPF0301 protein NMB1336. FT /FTId=PRO_0000214332. SQ SEQUENCE 182 AA; 19895 MW; C44A47F8A6ECEF7A CRC64; MNLSNHFLIA MPDMEDAFFS QSVVYICKHD EDGALGIAIN KPSPITMDMI FSATGKNIPM RMQHDSVMMG GPVQVERGYV VHTPIGNWQS SIGVSDNIAL TSSRDVIENI SREGAVDKAL ISIGYSSWSK GQLERELADN AWLTVPADEH ILFDIPYEHR YAAAFAKLGI DPLALFSGAG HA // ID Y1444_NEIMB Reviewed; 111 AA. AC Q9JYT1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Nucleoid-associated protein NMB1444 {ECO:0000255|HAMAP-Rule:MF_00274}; GN OrderedLocusNames=NMB1444; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds to DNA and alters its conformation. May be CC involved in regulation of gene expression, nucleoid organization CC and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00274}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC -!- SIMILARITY: Belongs to the YbaB/EbfC family. {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41804.1; -; Genomic_DNA. DR PIR; E81082; E81082. DR RefSeq; NP_274456.1; NC_003112.2. DR RefSeq; WP_002219073.1; NC_003112.2. DR ProteinModelPortal; Q9JYT1; -. DR SMR; Q9JYT1; 7-101. DR STRING; 122586.NMB1444; -. DR PaxDb; Q9JYT1; -. DR EnsemblBacteria; AAF41804; AAF41804; NMB1444. DR GeneID; 903864; -. DR KEGG; nme:NMB1444; -. DR PATRIC; 20358603; VBINeiMen85645_1813. DR eggNOG; ENOG4105KDX; Bacteria. DR eggNOG; COG0718; LUCA. DR HOGENOM; HOG000293239; -. DR KO; K09747; -. DR OMA; EMGKLTG; -. DR OrthoDB; EOG6DVJWP; -. DR BioCyc; NMEN122586:GHGG-1482-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1310.10; -; 1. DR HAMAP; MF_00274; DNA_YbaB_EbfC; 1. DR InterPro; IPR004401; YbaB/EbfC. DR Pfam; PF02575; YbaB_DNA_bd; 1. DR PIRSF; PIRSF004555; UCP004555; 1. DR SUPFAM; SSF82607; SSF82607; 1. DR TIGRFAMs; TIGR00103; DNA_YbaB_EbfC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome. FT CHAIN 1 111 Nucleoid-associated protein NMB1444. FT /FTId=PRO_0000170415. SQ SEQUENCE 111 AA; 11925 MW; 09ECBA17E9930B1C CRC64; MFGKAGLGGL MKQAQQMQEN MKKAQAKLAE TEIEGEAGNG LVKITMTCAH EVRKIDISPD LIQEAADDKE MLEDLILAAL KSARGKAEET ANKTMGAFTQ GLPPGVGDFF R // ID Y1333_NEIMB Reviewed; 596 AA. AC Q9JZ20; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Uncharacterized protein NMB1333; DE Flags: Precursor; GN OrderedLocusNames=NMB1333; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41708.1; -; Genomic_DNA. DR PIR; H81095; H81095. DR RefSeq; NP_274352.1; NC_003112.2. DR RefSeq; WP_002222357.1; NC_003112.2. DR ProteinModelPortal; Q9JZ20; -. DR STRING; 122586.NMB1333; -. DR PaxDb; Q9JZ20; -. DR EnsemblBacteria; AAF41708; AAF41708; NMB1333. DR GeneID; 903755; -. DR KEGG; nme:NMB1333; -. DR PATRIC; 20358321; VBINeiMen85645_1672. DR eggNOG; COG4942; LUCA. DR HOGENOM; HOG000218993; -. DR OMA; HGNYLTV; -. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; NMEN122586:GHGG-1371-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01551; Peptidase_M23; 1. DR SUPFAM; SSF51261; SSF51261; 1. PE 1: Evidence at protein level; KW Coiled coil; Complete proteome; Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 596 Uncharacterized protein NMB1333. FT /FTId=PRO_0000320334. FT COILED 177 281 {ECO:0000255}. FT COILED 318 454 {ECO:0000255}. FT COMPBIAS 33 183 Lys-rich. SQ SEQUENCE 596 AA; 65741 MW; 5787ECC7FB6C42DB CRC64; MRYKPLLLAL MLVFSTPAVA AHDAAHNRSA EVKKQTKNKK EQPEAAEGKK EKGKNGAVKD KKTGGKEAAK EGKESKKTAK NRKEAEKEAT SRQSARKGRE GDKKSKAEHK KAHGKPVSGS KEKNAKTQPE NKQGKKEAKG QGNPRKGGKA EKDTVSANKK VRSDKNGKAV KQDKKYREEK NAKTDSDELK AAVAAATNDV ENKKALLKQS EGMLLHVSNS LKQLQEERIR QERIRQARGN LASVNRKQRE AWDKFQKLNT ELNRLKTEVA ATKAQISRFV SGNYKNSQPN AVALFLKNAE PGQKNRFLRY TRYVNASNRE VVKDLEKQQK ALAVQEQKIN NELARLKKIQ ANVQSLLKKQ GVTDAAEQTE SRRQNAKIAK DARKLLEQKG NEQQLNKLLS NLEKKKAEHR IQDAEAKRKL AEARLAAAEK ARKEAAQQKA EARRAEMSNL TAEDRNIQAP SVMGIGSADG FSRMQGRLKK PVDGVPTGLF GQNRSGGDIW KGVFYSTAPA TVESIAPGTV SYADELDGYG KVVVVDHGEN YISIYAGLSE ISVGKGYMVA AGSKIGSSGS LPDGEEGLYL QIRYQGQVLN PSSWIR // ID Y1648_NEIMB Reviewed; 242 AA. AC Q9JYC7; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Probable transcriptional regulatory protein NMB1648 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=NMB1648; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00693}. CC -!- SIMILARITY: Belongs to the TACO1 family. {ECO:0000255|HAMAP- CC Rule:MF_00693}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41997.1; -; Genomic_DNA. DR PIR; G81058; G81058. DR RefSeq; NP_274653.1; NC_003112.2. DR RefSeq; WP_002216723.1; NC_003112.2. DR ProteinModelPortal; Q9JYC7; -. DR SMR; Q9JYC7; 3-238. DR STRING; 122586.NMB1648; -. DR PaxDb; Q9JYC7; -. DR EnsemblBacteria; AAF41997; AAF41997; NMB1648. DR GeneID; 903468; -. DR KEGG; nme:NMB1648; -. DR PATRIC; 20359216; VBINeiMen85645_2120. DR eggNOG; ENOG4105CDY; Bacteria. DR eggNOG; COG0217; LUCA. DR HOGENOM; HOG000228371; -. DR OMA; MTRNGGS; -. DR OrthoDB; EOG6HJ29R; -. DR BioCyc; NMEN122586:GHGG-1697-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.200; -; 1. DR Gene3D; 3.30.1270.10; -; 2. DR Gene3D; 3.30.70.980; -; 1. DR HAMAP; MF_00693; Transcrip_reg_TACO1; 1. DR InterPro; IPR017856; Integrase_Zn-bd_dom-like_N. DR InterPro; IPR002876; Transcrip_reg_TACO1-like. DR InterPro; IPR026563; Transcrip_reg_TACO1-like_dom2. DR InterPro; IPR026564; Transcrip_reg_TACO1-like_dom3. DR InterPro; IPR029072; YebC-like. DR PANTHER; PTHR12532; PTHR12532; 1. DR Pfam; PF01709; Transcrip_reg; 1. DR SUPFAM; SSF75625; SSF75625; 1. DR TIGRFAMs; TIGR01033; TIGR01033; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 242 Probable transcriptional regulatory FT protein NMB1648. FT /FTId=PRO_0000175856. SQ SEQUENCE 242 AA; 26032 MW; 80188A12815869F9 CRC64; MAGHSKWANI QHKKARQDAK RGKIFTRLIK EITVAARMGG GDPGSNPRLR LALEKAAENN MPKDNVQRAI DKGTGNLEGV EYIELRYEGY GIGGAALMVD CLTDNKTRTV ADVRHAFTKN GGNLGTDGCV AFNFVHQGYL VFEPGVDEDA LMEAALEAGA EDVVTNDDGS IEVITAPNDW AGVKSALEAA GYKSVDGDVT MRAQNETELS GDDAVKMQKL IDALEDLDDV QDVYTSAVLN LD // ID Y1653_NEIMB Reviewed; 90 AA. AC Q9JYC2; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=UPF0237 protein NMB1653 {ECO:0000255|HAMAP-Rule:MF_01054}; GN OrderedLocusNames=NMB1653; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0237 family. {ECO:0000255|HAMAP- CC Rule:MF_01054}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|HAMAP- CC Rule:MF_01054}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42002.1; -; Genomic_DNA. DR PIR; D81059; D81059. DR RefSeq; NP_274658.1; NC_003112.2. DR RefSeq; WP_002218494.1; NC_003112.2. DR ProteinModelPortal; Q9JYC2; -. DR STRING; 122586.NMB1653; -. DR PaxDb; Q9JYC2; -. DR EnsemblBacteria; AAF42002; AAF42002; NMB1653. DR GeneID; 903463; -. DR KEGG; nme:NMB1653; -. DR PATRIC; 20359228; VBINeiMen85645_2126. DR eggNOG; ENOG4105VUC; Bacteria. DR eggNOG; COG3830; LUCA. DR HOGENOM; HOG000241054; -. DR KO; K07166; -. DR OMA; IFKYMHR; -. DR OrthoDB; EOG6ZPT4H; -. DR BioCyc; NMEN122586:GHGG-1702-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR HAMAP; MF_01054; UPF0237; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR022986; UPF0237_ACT. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 90 UPF0237 protein NMB1653. FT /FTId=PRO_0000219905. FT DOMAIN 5 83 ACT. {ECO:0000255|HAMAP-Rule:MF_01054}. SQ SEQUENCE 90 AA; 10362 MW; 534039E010370328 CRC64; MNNSVITVIG KDRVGIVYDV SKILAENQIN ILNISQQLMD DFFTMIILVD TSKCSKSRQE VLDLFAEESK KLALDIRMQN EEIFQAMHRI // ID Y1088_NEIMB Reviewed; 56 AA. AC Q7DDI1; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=UPF0339 protein NMB1088; GN OrderedLocusNames=NMB1088; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0339 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41480.1; -; Genomic_DNA. DR RefSeq; NP_274120.1; NC_003112.2. DR RefSeq; WP_002215844.1; NC_003112.2. DR PDB; 3BID; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-56. DR PDBsum; 3BID; -. DR ProteinModelPortal; Q7DDI1; -. DR SMR; Q7DDI1; 1-56. DR STRING; 122586.NMB1088; -. DR PaxDb; Q7DDI1; -. DR EnsemblBacteria; AAF41480; AAF41480; NMB1088. DR GeneID; 903505; -. DR KEGG; nme:NMB1088; -. DR PATRIC; 20357737; VBINeiMen85645_1385. DR eggNOG; ENOG4107EPN; Bacteria. DR eggNOG; COG3422; LUCA. DR HOGENOM; HOG000236178; -. DR OMA; RREDCEH; -. DR OrthoDB; EOG6FRD29; -. DR BioCyc; NMEN122586:GHGG-1124-MONOMER; -. DR EvolutionaryTrace; Q7DDI1; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.160.160; -; 1. DR InterPro; IPR010879; DUF1508. DR Pfam; PF07411; DUF1508; 1. DR SUPFAM; SSF160113; SSF160113; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 56 UPF0339 protein NMB1088. FT /FTId=PRO_0000218140. FT STRAND 2 7 {ECO:0000244|PDB:3BID}. FT STRAND 13 18 {ECO:0000244|PDB:3BID}. FT STRAND 24 27 {ECO:0000244|PDB:3BID}. FT HELIX 34 45 {ECO:0000244|PDB:3BID}. FT STRAND 53 55 {ECO:0000244|PDB:3BID}. SQ SEQUENCE 56 AA; 6403 MW; 2C7B82FDC9B5D925 CRC64; MYFEIYKDAK GEYRWRLKAA NHEIIAQGEG YTSKQNCQHA VDLLKSTTAA TPVKEV // ID Y1327_NEIMB Reviewed; 467 AA. AC Q9JZ25; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein NMB1327; GN OrderedLocusNames=NMB1327; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Contains 9 Sel1-like repeats. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41702.1; -; Genomic_DNA. DR PIR; B81095; B81095. DR RefSeq; NP_274346.1; NC_003112.2. DR RefSeq; WP_002225161.1; NC_003112.2. DR ProteinModelPortal; Q9JZ25; -. DR STRING; 122586.NMB1327; -. DR PaxDb; Q9JZ25; -. DR EnsemblBacteria; AAF41702; AAF41702; NMB1327. DR GeneID; 903749; -. DR KEGG; nme:NMB1327; -. DR PATRIC; 20358307; VBINeiMen85645_1665. DR eggNOG; ENOG410632Y; Bacteria. DR eggNOG; COG0790; LUCA. DR HOGENOM; HOG000218678; -. DR KO; K07126; -. DR OMA; GYGTAQD; -. DR OrthoDB; EOG6F81PD; -. DR BioCyc; NMEN122586:GHGG-1365-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF08238; Sel1; 9. DR SMART; SM00671; SEL1; 9. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Repeat. FT CHAIN 1 467 Uncharacterized protein NMB1327. FT /FTId=PRO_0000320333. FT REPEAT 38 73 Sel1-like 1. FT REPEAT 107 138 Sel1-like 2. FT REPEAT 139 172 Sel1-like 3. FT REPEAT 173 208 Sel1-like 4. FT REPEAT 240 275 Sel1-like 5. FT REPEAT 276 311 Sel1-like 6. FT REPEAT 343 378 Sel1-like 7. FT REPEAT 379 414 Sel1-like 8. FT REPEAT 415 450 Sel1-like 9. SQ SEQUENCE 467 AA; 52596 MW; E38F0D04F834DBC6 CRC64; MNNPDLPYRQ ALECLSQKQY NFTEVRRLLT EAFSAGHPAA AFELAKHLMD ADSPYQDREQ GMEMLRIAAE QGHPYARYNL AYIQELEGAP PETLIPLYRP LAEEGLPEAQ VRLMYLLYAS RHFEEALEWA KTSAKNNNPH GQYLLAQYCR YGTPPDFETA HLLYRKSAAQ GLPEAHWQLG LQYRFGQGTK VDTAQAVNHL RAAAQQGYIP AYTPLAELIL PTAPDEAVHW FQQAAQENDP DAHAALADIY LQGKHLERNH KLALHHAEAA AAERHPEGLR ILGDICRYGL GIAPDTEKAR HYYRQAAEAG SLSAYQKLIS DSALNHPDQY GGIKDSAIRR QRAERLYQKA QALHYGLQCA PEYAAALKLY TEAAELGHSK AQTNLGSMYY FGQGMTADYN EARKWFEKAA AKKDSMAFYN LACIHYSGHG VEPDKEKACR YLQEAINNGY GQKSVLQELL QQWQNAV // ID Y1497_NEIMB Reviewed; 921 AA. AC Q7DDB6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Probable TonB-dependent receptor NMB1497; DE Flags: Precursor; GN OrderedLocusNames=NMB1497; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- FUNCTION: Probable receptor, TonB-dependent. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41853.1; -; Genomic_DNA. DR RefSeq; NP_274505.1; NC_003112.2. DR RefSeq; WP_002244190.1; NC_003112.2. DR ProteinModelPortal; Q7DDB6; -. DR STRING; 122586.NMB1497; -. DR TCDB; 1.B.14.7.2; the outer membrane receptor (omr) family. DR PaxDb; Q7DDB6; -. DR EnsemblBacteria; AAF41853; AAF41853; NMB1497. DR GeneID; 903921; -. DR KEGG; nme:NMB1497; -. DR PATRIC; 20358768; VBINeiMen85645_1893. DR eggNOG; ENOG41063SR; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000219020; -. DR KO; K16087; -. DR OMA; NNQELQK; -. DR OrthoDB; EOG6T7N3H; -. DR BioCyc; NMEN122586:GHGG-1537-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 921 Probable TonB-dependent receptor NMB1497. FT /FTId=PRO_0000320273. FT MOTIF 904 921 TonB C-terminal box. SQ SEQUENCE 921 AA; 104222 MW; 67985B75EDF8819D CRC64; MRSSFRLKPI CFYLMGVTLY HYSYAEDAGR AGSEAQIQVL EDVHVKAKRV PKDKKVFTDA RAVSTRQDIF KSSENLDNIV RSIPGAFTQQ DKSSGIVSLN IRGDSGFGRV NTMVDGITQT FYSTSTDAGR AGGSSQFGAS VDSNFIAGLD VVKGSFSGSA GINSLAGSAN LRTLGVDDVV QGNNTYGLLL KGLTGTNSTK GNAMAAIGAR KWLESGASVG VLYGHSRRSV AQNYRVGGGG QHIGNFGAEY LERRKQRYFV QEGALKFNSD SGKWERDLQR QQWKYKPYKN YNNQELQKYI EEHDKSWREN LAPQYDITPI DPSSLKQQSA GNLFKLEYDG VFNKYTAQFR DLNTKIGSRK IINRNYQFNY GLSLNPYTNL NLTAAYNSGR QKYPKGSKFT GWGLLKDFET YNNAKILDLN NTATFRLPRE TELQTTLGFN YFHNEYGKNR FPEELGLFFD GPDQDNGLYS YLGRFKGDKG LLPQKSTIVQ PAGSQYFNTF YFDAALKKDI YRLNYSTNTV GYRFGGEYTG YYGSDDEFKR AFGENSPTYK KHCNRSCGIY EPVLKKYGKK RANNHSVSIS ADFGDYFMPF ASYSRTHRMP NIQEMYFSQI GDSGVHTALK PERANTWQFG FNTYKKGLLK QDDTLGLKLV GYRSRIDNYI HNVYGKWWDL NGDIPSWVSS TGLAYTIQHR NFKDKVHKHG FELELNYDYG RFFTNLSYAY QKSTQPTNFS DASESPNNAS KEDQLKQGYG LSRVSALPRD YGRLEVGTRW LGNKLTLGGA MRYFGKSIRA TAEERYIDGT NGGNTSNFRQ LGKRSIKQTE TLARQPLIFD FYAAYEPKKN LIFRAEVKNL FDRRYIDPLD AGNDAATQRY YSSFDPKDKD EDVTCNADKT LCNGKYGGTS KSVLTNFARG RTFLMTMSYK F // ID Y1652_NEIMB Reviewed; 451 AA. AC Q9JYC3; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=UPF0210 protein NMB1652 {ECO:0000255|HAMAP-Rule:MF_01221}; GN OrderedLocusNames=NMB1652; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01221}. CC -!- SIMILARITY: Belongs to the UPF0210 family. {ECO:0000255|HAMAP- CC Rule:MF_01221}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42001.1; -; Genomic_DNA. DR PIR; C81059; C81059. DR RefSeq; NP_274657.1; NC_003112.2. DR RefSeq; WP_002218495.1; NC_003112.2. DR ProteinModelPortal; Q9JYC3; -. DR SMR; Q9JYC3; 7-446. DR STRING; 122586.NMB1652; -. DR PaxDb; Q9JYC3; -. DR EnsemblBacteria; AAF42001; AAF42001; NMB1652. DR GeneID; 903464; -. DR KEGG; nme:NMB1652; -. DR PATRIC; 20359226; VBINeiMen85645_2125. DR eggNOG; ENOG4105CAG; Bacteria. DR eggNOG; COG2848; LUCA. DR HOGENOM; HOG000059201; -. DR KO; K09157; -. DR OMA; EAMTSVC; -. DR OrthoDB; EOG64BQ65; -. DR BioCyc; NMEN122586:GHGG-1701-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_01221; UPF0210; 1. DR InterPro; IPR007841; UPF0210. DR Pfam; PF05167; DUF711; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 451 UPF0210 protein NMB1652. FT /FTId=PRO_0000070560. SQ SEQUENCE 451 AA; 46429 MW; 88BA21DD8C000C04 CRC64; MSIQSGEILE TVKMVADQNF DVRTITIGID LHDCISSDIN VLNQNIYNKI TTVGKDLVTT AKYLSAKYGV PIVNQRISVT PIAQIAAATH ADSYVSVAQT LDKAAKAIGV SFIGGFSALV QKGMSPSDEV LIRSIPEAMK TTDIVCSSIN IGSTRAGINM DAVKLAGETV KRTAEITPEG FGCAKIVVFC NAVEDNPFMA GAFHGSGEAD AVINVGVSGP GVVKAALENS DATTLTEVAE VVKKTAFKIT RVGELIGREA SKMLNIPFGI LDLSLAPTPA VGDSVARILE EMGLSVCGTH GTTAALALLN DAVKKGGMMA SSAVGGLSGA FIPVSEDEGM IAAAEAGVLT LDKLEAMTAV CSVGLDMIAV PGDTPAHTIS GIIADEAAIG MINSKTTAVR IIPVTGKTVG DSVEFGGLLG YAPVMPVKEG SCEVFVNRGG RIPAPVQSMK N // ID Y2020_NEIMB Reviewed; 227 AA. AC P63702; Q9JRI0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Uncharacterized protein NMB2020; GN OrderedLocusNames=NMB2020; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42343.1; -; Genomic_DNA. DR PIR; G81014; G81014. DR RefSeq; NP_275012.1; NC_003112.2. DR RefSeq; WP_002225674.1; NC_003112.2. DR STRING; 122586.NMB2020; -. DR PaxDb; P63702; -. DR EnsemblBacteria; AAF42343; AAF42343; NMB2020. DR GeneID; 904090; -. DR KEGG; nme:NMB2020; -. DR PATRIC; 20360155; VBINeiMen85645_2577. DR eggNOG; ENOG4108XRP; Bacteria. DR eggNOG; COG0670; LUCA. DR HOGENOM; HOG000060391; -. DR KO; K19416; -. DR OMA; NIFLAIP; -. DR OrthoDB; EOG6PZXBH; -. DR BioCyc; NMEN122586:GHGG-2082-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR006214; Bax_inhibitor_1-related. DR PANTHER; PTHR23291; PTHR23291; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 227 Uncharacterized protein NMB2020. FT /FTId=PRO_0000179109. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. SQ SEQUENCE 227 AA; 24454 MW; 0E24A04F9676CDBD CRC64; MQHDVYDYTA HTVSKNTVLQ KTYRLLGFSF IPASAGAALA ANAGFNFYAA FGSRWIGFAV VLAFFYGMIH FIEKNRYSNT GVTLLMVFTF GMGVLIGPVL QYALHIADGA KIVGIAAAMT AAVFLTMSAL ARRTRLDMNA LGRFLTVGAV ILMVAVVANL FLGIPALALT ISAGFVLFSS LMIMWQVRTV IDGGEDSHIS AALTLFISLY NIFSSLLNIL LSLNGED // ID Y2089_NEIMB Reviewed; 115 AA. AC Q9JXE2; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=UPF0102 protein NMB2089 {ECO:0000255|HAMAP-Rule:MF_00048}; GN OrderedLocusNames=NMB2089; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0102 family. {ECO:0000255|HAMAP- CC Rule:MF_00048}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42406.1; -; Genomic_DNA. DR PIR; G81007; G81007. DR RefSeq; NP_275077.1; NC_003112.2. DR RefSeq; WP_002217775.1; NC_003112.2. DR STRING; 122586.NMB2089; -. DR PaxDb; Q9JXE2; -. DR EnsemblBacteria; AAF42406; AAF42406; NMB2089. DR GeneID; 903961; -. DR KEGG; nme:NMB2089; -. DR PATRIC; 20360348; VBINeiMen85645_2671. DR eggNOG; ENOG41082RQ; Bacteria. DR eggNOG; COG0792; LUCA. DR HOGENOM; HOG000016278; -. DR KO; K07460; -. DR OMA; KEDINWI; -. DR OrthoDB; EOG6PP9TH; -. DR BioCyc; NMEN122586:GHGG-2154-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_00048; UPF0102; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR InterPro; IPR003509; UPF0102. DR Pfam; PF02021; UPF0102; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00252; TIGR00252; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 115 UPF0102 protein NMB2089. FT /FTId=PRO_0000167366. SQ SEQUENCE 115 AA; 13009 MW; E089FDDC29DDD16B CRC64; MRLNHKQGEA GEDAALAFLQ SQGCTLLARN WHCAYGEIDL IVKNGGMILF VEVKYRKNRQ FGGVAYSISP SKLLKLQRSV EYYLQQNRLT NVPCRLDAVL IEGSRPPEWI QNITG // ID XERD_NEIMB Reviewed; 291 AA. AC Q9K068; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807}; GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; GN OrderedLocusNames=NMB0751; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by CC catalyzing the cutting and rejoining of the recombining DNA CC molecules. The XerC-XerD complex is essential to convert dimers of CC the bacterial chromosome into monomers to permit their segregation CC at cell division. It also contributes to the segregational CC stability of plasmids. {ECO:0000255|HAMAP-Rule:MF_01807}. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP- CC Rule:MF_01807}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01807}. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01807}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41164.1; -; Genomic_DNA. DR PIR; F81163; F81163. DR RefSeq; NP_273793.1; NC_003112.2. DR RefSeq; WP_002222739.1; NC_003112.2. DR ProteinModelPortal; Q9K068; -. DR STRING; 122586.NMB0751; -. DR PaxDb; Q9K068; -. DR EnsemblBacteria; AAF41164; AAF41164; NMB0751. DR GeneID; 902866; -. DR KEGG; nme:NMB0751; -. DR PATRIC; 20356873; VBINeiMen85645_0955. DR eggNOG; ENOG4105C13; Bacteria. DR eggNOG; COG4974; LUCA. DR HOGENOM; HOG000045296; -. DR KO; K04763; -. DR OMA; AIWQMIK; -. DR OrthoDB; EOG6PZXFP; -. DR BioCyc; NMEN122586:GHGG-782-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR HAMAP; MF_01807; Recomb_XerD; 1. DR HAMAP; MF_01808; Recomb_XerC_XerD; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR010998; Integrase_Lambda-type_N. DR InterPro; IPR023109; Integrase_recombinase_N. DR InterPro; IPR004107; Integrase_SAM-like_N. DR InterPro; IPR011932; Recomb_XerD. DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD. DR Pfam; PF02899; Phage_int_SAM_1; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF47823; SSF47823; 1. DR SUPFAM; SSF56349; SSF56349; 1. DR TIGRFAMs; TIGR02225; recomb_XerD; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; DNA integration; DNA recombination; DNA-binding; KW Reference proteome. FT CHAIN 1 291 Tyrosine recombinase XerD. FT /FTId=PRO_0000095401. FT ACT_SITE 143 143 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 167 167 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 237 237 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 240 240 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 263 263 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 272 272 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01807}. SQ SEQUENCE 291 AA; 32975 MW; 23BD423C470F0239 CRC64; MEEGLIDRLL ETLWLDRRLS QNTLNGYRRD LEKIARRLSQ SGRMLKDADE ADLAAAVYVD GEQRSSQARA LSACKRLYIW MEREGIRTDN PTRLLKPPKI DKNIPTLITE QQISRLLAAP DTDTPHGLRD KALLELMYAT GLRVSEAVGL NFGNVDLDRG CITALGKGDK QRMVPMGQES AYWVERYYTE ARPLLLKGRN CDALFVSQKK TGISRQLAWM IVKEYASQAG IGHISPHSLR HAFATHLVRH GLDLRVVQDM LGHADLNTTQ IYTHVANVWL QGVVKEHHSR N // ID Y0313_NEIMB Reviewed; 488 AA. AC Q9K165; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=TPR repeat-containing protein NMB0313; DE Flags: Precursor; GN OrderedLocusNames=NMB0313; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Contains 2 TPR repeats. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40758.1; -; Genomic_DNA. DR PIR; G81213; G81213. DR RefSeq; NP_273362.1; NC_003112.2. DR RefSeq; WP_010980777.1; NC_003112.2. DR STRING; 122586.NMB0313; -. DR PaxDb; Q9K165; -. DR EnsemblBacteria; AAF40758; AAF40758; NMB0313. DR GeneID; 902429; -. DR KEGG; nme:NMB0313; -. DR PATRIC; 20355753; VBINeiMen85645_0396. DR eggNOG; ENOG4108R0G; Bacteria. DR eggNOG; ENOG41116RD; LUCA. DR HOGENOM; HOG000219118; -. DR KO; K07280; -. DR OMA; FMPARNR; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NMEN122586:GHGG-333-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR007655; DUF560. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF04575; DUF560; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Repeat; Signal; TPR repeat. FT SIGNAL 1 31 {ECO:0000255}. FT CHAIN 32 488 TPR repeat-containing protein NMB0313. FT /FTId=PRO_0000320328. FT REPEAT 118 151 TPR 1. FT REPEAT 171 204 TPR 2. SQ SEQUENCE 488 AA; 56224 MW; 808FCE9C39A68AE9 CRC64; MVIFYFCGKT FMPARNRWML LLPLLASAAY AEETPREPDL RSRPEFRLHE AEVKPIDREK VPGQVREKGK VLQIDGETLL KNPELLSRAM YSAVVSNNIA GIRVILPIYL QQAQQDKMLA LYAQGILAQA DGRVKEAISH YRELIAAQPD APAVRMRLAA ALFENRQNEA AADQFDRLKA ENLPPQLMEQ VELYRKALRE RDAWKVNGGF SVTREHNINQ APKRQQYGKW TFPKQVDGTA VNYRLGAEKK WSLKNGWYTT AGGDVSGRVY PGNKKFNDMT AGVSGGIGFA DRRKDAGLAV FHERRTYGND AYSYTNGARL YFNRWQTPKW QTLSSAEWGR LKNTRRARSD NTHLQISNSL VFYRNARQYW MGGLDFYRER NPADRGDNFN RYGLRFAWGQ EWGGSGLSSL LRLGAAKRHY EKPGFFSGFK GERRRDKELN TSLSLWHRAL HFKGITPRLT LSHRETRSND VFNEYEKNRA FVEFNKTF // ID Y1437_NEIMB Reviewed; 233 AA. AC Q9JYT7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 79. DE RecName: Full=Uncharacterized protein NMB1437; GN OrderedLocusNames=NMB1437; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the LutC/YkgG family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41798.1; -; Genomic_DNA. DR PIR; E81083; E81083. DR RefSeq; NP_274449.1; NC_003112.2. DR RefSeq; WP_002216938.1; NC_003112.2. DR ProteinModelPortal; Q9JYT7; -. DR STRING; 122586.NMB1437; -. DR PaxDb; Q9JYT7; -. DR EnsemblBacteria; AAF41798; AAF41798; NMB1437. DR GeneID; 903858; -. DR KEGG; nme:NMB1437; -. DR PATRIC; 20358587; VBINeiMen85645_1805. DR eggNOG; ENOG4108ZZK; Bacteria. DR eggNOG; COG1556; LUCA. DR HOGENOM; HOG000257978; -. DR KO; K00782; -. DR OMA; VHTEIHL; -. DR OrthoDB; EOG6VB704; -. DR BioCyc; NMEN122586:GHGG-1475-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.10420; -; 1. DR InterPro; IPR024185; FTHF_cligase-like. DR InterPro; IPR003741; LUD_dom. DR Pfam; PF02589; DUF162; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 233 Uncharacterized protein NMB1437. FT /FTId=PRO_0000320335. SQ SEQUENCE 233 AA; 25898 MW; 2863D1D637C25F74 CRC64; MSARENILAK LKKADALPME EPAVFDYYRE MGVSWGSEVE RLKHWAAAMR AVKTEIYWVT KSNWMQVFRE AAEGKGLKNI LLPLATEHGQ IARAALADSN IEPIAFEREI DTWKTEFFTN IDAGFSGAQC GIARTGTLML FSSPEEPRTL SLVPPVHFCL FDTSKMYNEF HNAVEGEKLV ENGMPTNVFL ISGPSKTADI QLTLAYGAHG PRDLVILAIL PDHISPADLE ENA // ID Y1126_NEIMB Reviewed; 223 AA. AC Q7DDH4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE RecName: Full=Putative lipoprotein NMB1126/NMB1164; DE Flags: Precursor; GN OrderedLocusNames=NMB1126; GN and GN OrderedLocusNames=NMB1164; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41514.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41549.1; -; Genomic_DNA. DR PIR; F81120; F81120. DR RefSeq; NP_274155.1; NC_003112.2. DR RefSeq; NP_274191.1; NC_003112.2. DR RefSeq; WP_002217215.1; NC_003112.2. DR STRING; 122586.NMB1164; -. DR PaxDb; Q7DDH4; -. DR EnsemblBacteria; AAF41514; AAF41514; NMB1126. DR EnsemblBacteria; AAF41549; AAF41549; NMB1164. DR GeneID; 903547; -. DR GeneID; 903584; -. DR KEGG; nme:NMB1126; -. DR KEGG; nme:NMB1164; -. DR PATRIC; 20357825; VBINeiMen85645_1428. DR eggNOG; ENOG4106B0W; Bacteria. DR eggNOG; COG1462; LUCA. DR HOGENOM; HOG000265565; -. DR OMA; MNIQTRR; -. DR OrthoDB; EOG600DTR; -. DR BioCyc; NMEN122586:GHGG-1162-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1199-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR Gene3D; 3.40.50.10070; -; 1. DR InterPro; IPR005534; Curli_assmbl/transp-comp_CsgG. DR InterPro; IPR007195; TolB_N. DR Pfam; PF03783; CsgG; 1. DR SUPFAM; SSF52964; SSF52964; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 223 Putative lipoprotein NMB1126/NMB1164. FT /FTId=PRO_0000320332. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 223 AA; 23798 MW; 2AB27B742CAAB7F0 CRC64; MKTVSTAVVL AAAAVSLTGC ATESSRSLEV EKVASYNTQY HGVRTPISVG TFDNRSSFQK GIFSDGEDRL GSQAKTILVT HLQQTNRFNV LNRTNLNALK QESGISGKAH NLKGADYVVT GDVTEFGRRD VGDHQLFGIL GRGKSQIAYA KVALNIVNVN TSEIVYSAQG AGEYALSNRE IIGFGGTSGY DATLNGKVLD LAIREAVNSL VQAVDNGAWQ PNR // ID Y2142_NEIMB Reviewed; 280 AA. AC Q9JXB0; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 11-MAY-2016, entry version 74. DE RecName: Full=UPF0276 protein NMB2142 {ECO:0000255|HAMAP-Rule:MF_00697}; GN OrderedLocusNames=NMB2142; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0276 family. {ECO:0000255|HAMAP- CC Rule:MF_00697}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF42450.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42450.1; ALT_INIT; Genomic_DNA. DR PIR; D81002; D81002. DR RefSeq; NP_275127.1; NC_003112.2. DR RefSeq; WP_010981032.1; NC_003112.2. DR ProteinModelPortal; Q9JXB0; -. DR SMR; Q9JXB0; 1-273. DR STRING; 122586.NMB2142; -. DR PaxDb; Q9JXB0; -. DR EnsemblBacteria; AAF42450; AAF42450; NMB2142. DR GeneID; 903230; -. DR KEGG; nme:NMB2142; -. DR PATRIC; 20360478; VBINeiMen85645_2735. DR eggNOG; ENOG4105E18; Bacteria. DR eggNOG; COG3220; LUCA. DR HOGENOM; HOG000281002; -. DR KO; K09930; -. DR OMA; IYSEHLS; -. DR OrthoDB; EOG6X9MK9; -. DR BioCyc; NMEN122586:GHGG-2207-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00697; UPF0276; 1. DR InterPro; IPR007801; UPF0276. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF05114; DUF692; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 280 UPF0276 protein NMB2142. FT /FTId=PRO_0000192698. SQ SEQUENCE 280 AA; 31603 MW; D9359E1058318E1C CRC64; MIQHAGLGYR RDLAEDFLSL SENSPICFIE AAPENWLKMG GWARKQFDRV AERLPLALHG LSMSLGGQAP LDTDLIDGIK EMMRRYDCTF FSDHLSYCHD GGHLYDLLPL PFTEEMVHHT ARRIREVQDR LGCRIAVENT SYYLHSPLAE MNEVEFLNAV AREADCGIHL DVNNIYVNAV NHGLLSPEAF LENVDAERVC YIHIAGHDVE TPELLIDTHG AAVLPTVWDL LELAYAKLPT IPPTLLERDF NFPPFSELEA EVAKIADYQT RAGKECRRAA // ID Y088_NEIMB Reviewed; 466 AA. AC Q9K1M2; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE RecName: Full=Putative outer membrane protein NMB0088; DE Flags: Precursor; GN OrderedLocusNames=NMB0088; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the OmpP1/FadL family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40551.1; -; Genomic_DNA. DR PIR; A81239; A81239. DR RefSeq; NP_273150.1; NC_003112.2. DR RefSeq; WP_002221819.1; NC_003112.2. DR ProteinModelPortal; Q9K1M2; -. DR STRING; 122586.NMB0088; -. DR PaxDb; Q9K1M2; -. DR EnsemblBacteria; AAF40551; AAF40551; NMB0088. DR GeneID; 902192; -. DR KEGG; nme:NMB0088; -. DR PATRIC; 20355183; VBINeiMen85645_0125. DR eggNOG; ENOG4105ISI; Bacteria. DR eggNOG; COG2067; LUCA. DR HOGENOM; HOG000277334; -. DR KO; K06076; -. DR OMA; NRYGFTY; -. DR OrthoDB; EOG6Z0Q6D; -. DR BioCyc; NMEN122586:GHGG-94-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005017; OMPP1/FadL/TodX. DR Pfam; PF03349; Toluene_X; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 466 Putative outer membrane protein NMB0088. FT /FTId=PRO_0000349890. FT COMPBIAS 40 50 Poly-Ala. SQ SEQUENCE 466 AA; 50518 MW; 878A5B34A8646609 CRC64; MTPSALKKTV LLLGTAFAAA SVHASGYHFG TQSVNAQSTA NAAAAEAADA STIFYNPAGL TKLDSSQISV NANIVLPSIH YEADSATDFT GLPVQGSKSG KITKTTVAPH IYGAYKVNDN LTVGLGVYVP FGSATEYEKD SVLRHNINKL GLTSIAVEPV AAWKLNDRHS FGAGIIAQHT SAELRKYADW GIKSKAEILT AKPPKPNGVA EAAKIQADGH ADVKGSDWGF GYQLAWMWDI NDRARVGVNY RSKVSHTLKG DAEWAADGAA AKAMWSTMLA ANGYTANEKA RVKIVTPESL SVHGMYKVSD KADLFGDVTW TRHSRFDKAE LVFEKEKTVV KGKSDRTTIT PNWRNTYKVG FGGSYQISEP LQLRAGIAFD KSPVRNADYR MNSLPDGNRI WFSAGMKYHI GKNHVVDAAY THIHINDTSY RTAKASGNDV DSKGASSARF KNHADIIGLQ YTYKFK // ID Y1124_NEIMB Reviewed; 215 AA. AC Q7DDE8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Putative lipoprotein NMB1124/NMB1162; DE Flags: Precursor; GN OrderedLocusNames=NMB1124; GN and GN OrderedLocusNames=NMB1162; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41512.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41547.1; -; Genomic_DNA. DR RefSeq; NP_274153.1; NC_003112.2. DR RefSeq; NP_274189.1; NC_003112.2. DR RefSeq; WP_002217218.1; NC_003112.2. DR STRING; 122586.NMB1162; -. DR PaxDb; Q7DDE8; -. DR EnsemblBacteria; AAF41512; AAF41512; NMB1124. DR EnsemblBacteria; AAF41547; AAF41547; NMB1162. DR GeneID; 903545; -. DR GeneID; 903582; -. DR KEGG; nme:NMB1124; -. DR KEGG; nme:NMB1162; -. DR PATRIC; 20357821; VBINeiMen85645_1426. DR eggNOG; ENOG4107Y60; Bacteria. DR eggNOG; COG4380; LUCA. DR HOGENOM; HOG000265543; -. DR OMA; ILYGPRS; -. DR OrthoDB; EOG6X3W4X; -. DR BioCyc; NMEN122586:GHGG-1160-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1197-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR008517; DUF799. DR Pfam; PF05643; DUF799; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 16 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 17 215 Putative lipoprotein NMB1124/NMB1162. FT /FTId=PRO_0000320331. FT LIPID 17 17 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 17 17 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 215 AA; 22931 MW; B963F5F9ED8A53F2 CRC64; MKPLILGLAA VLALSACQVQ KAPDFDYTSF KESKPASILV VPPLNESPDV NGTWGVLAST AAPLSEAGYY VFPAAVVEET FKQNGLTNAA DIHAVRPEKL HQIFGNDAVL YITVTEYGTS YQILDSVTTV SAKARLVDSR NGKELWSGSA SIREGSNNSN SGLLGALVSA VVNQIANSLT DRGYQVSKTA AYNLLSPYSH NGILKGPRFV EEQPK // ID Y183_NEIMB Reviewed; 446 AA. AC Q9K1G9; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative zinc metalloprotease NMB0183; DE EC=3.4.24.-; GN OrderedLocusNames=NMB0183; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40640.1; -; Genomic_DNA. DR PIR; H81228; H81228. DR RefSeq; NP_273241.1; NC_003112.2. DR RefSeq; WP_002243948.1; NC_003112.2. DR ProteinModelPortal; Q9K1G9; -. DR STRING; 122586.NMB0183; -. DR MEROPS; M50.004; -. DR PaxDb; Q9K1G9; -. DR EnsemblBacteria; AAF40640; AAF40640; NMB0183. DR GeneID; 902290; -. DR KEGG; nme:NMB0183; -. DR PATRIC; 20355391; VBINeiMen85645_0225. DR eggNOG; ENOG4105DZP; Bacteria. DR eggNOG; COG0750; LUCA. DR HOGENOM; HOG000006281; -. DR KO; K11749; -. DR OMA; YVKMYGE; -. DR OrthoDB; EOG66F07W; -. DR BioCyc; NMEN122586:GHGG-193-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004387; Pept_M50_Zn. DR InterPro; IPR008915; Peptidase_M50. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF02163; Peptidase_M50; 1. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 2. DR TIGRFAMs; TIGR00054; TIGR00054; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 446 Putative zinc metalloprotease NMB0183. FT /FTId=PRO_0000088451. FT TRANSMEM 93 115 Helical. {ECO:0000255}. FT TRANSMEM 376 398 Helical. {ECO:0000255}. FT TRANSMEM 419 438 Helical. {ECO:0000255}. FT DOMAIN 100 181 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 19 19 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 18 18 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 22 22 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 446 AA; 48024 MW; A32AB9349C58752B CRC64; MHTLLAFIFA ILILVSLHEF GHYIVARLCG VKVVRFSVGF GKPFFTRKRG DTEWCLAPIP LGGYVKMVDT REGEVSEADL PYAFDKQHPA KRIAIVAAGP LTNLALAVLL YGLSFSFGVT ELRPYVGTVE PDTIAARAGF QSGDKIQSVN GTPVADWGSA QTEIVLNLEA GKVAVGVQTA SGAQTVRTID AAGTPEAGKI AKNQGYIGLM PFKITTVAGG VEKGSPAEKA GLKPGDRLTA ADGKPIASWQ EWANLTRQSP GKKITLNYER AGQTHTADIR PDTVEQSDHT LIGRVGLRPQ PDRAWDAQIR RSYRPSVVRA FGMGWEKTVS HSWTTLKFFG KLISGNASVS HISGPLTIAD IAGQSAELGL QSYLEFLALV SISLGVLNLL PVPVLDGGHL VFYTAEWIRG KPLGERVQNI GLRFGLALMM LMMAVAFFND VTRLLG // ID Y361_NEIMB Reviewed; 91 AA. AC Q9K132; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=UPF0213 protein NMB0361; GN OrderedLocusNames=NMB0361; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0213 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000255|PROSITE- CC ProRule:PRU00977}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40804.1; -; Genomic_DNA. DR PIR; H81208; H81208. DR RefSeq; NP_273410.1; NC_003112.2. DR RefSeq; WP_002218732.1; NC_003112.2. DR ProteinModelPortal; Q9K132; -. DR STRING; 122586.NMB0361; -. DR PaxDb; Q9K132; -. DR EnsemblBacteria; AAF40804; AAF40804; NMB0361. DR GeneID; 902477; -. DR KEGG; nme:NMB0361; -. DR PATRIC; 20355879; VBINeiMen85645_0457. DR eggNOG; ENOG41082IR; Bacteria. DR eggNOG; COG2827; LUCA. DR HOGENOM; HOG000285485; -. DR KO; K07461; -. DR OMA; VEQWPSK; -. DR OrthoDB; EOG6RC3X0; -. DR BioCyc; NMEN122586:GHGG-383-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR000305; GIY-YIG_SF. DR Pfam; PF01541; GIY-YIG; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR PROSITE; PS50164; GIY_YIG; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 91 UPF0213 protein NMB0361. FT /FTId=PRO_0000161371. FT DOMAIN 4 83 GIY-YIG. {ECO:0000255|PROSITE- FT ProRule:PRU00977}. SQ SEQUENCE 91 AA; 10088 MW; 3F1A998E84AF77C8 CRC64; MNASNWSVYL ILCENSAFYC GISPNPQQRL AAHTTGKGAK YTRVFKPVAM RIVAGGMDKG TALRQEIAVK KLTAAQKRQL WEQAEKMPSE T // ID Y1378_NEIMB Reviewed; 148 AA. AC P0A0Z0; Q51134; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Putative HTH-type transcriptional regulator NMB1378; GN OrderedLocusNames=NMB1378; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 37602 / M1080 / Serogroup B / Serotype 1; RX PubMed=8759842; RA Erwin A.L., Gotschlich E.C.; RT "Cloning of a Neisseria meningitidis gene for L-lactate dehydrogenase RT (L-LDH): evidence for a second meningococcal L-LDH with different RT regulation."; RL J. Bacteriol. 178:4807-4813(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH rrf2-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00540}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U58911; AAB09668.1; -; Genomic_DNA. DR EMBL; AE002098; AAF62328.1; -; Genomic_DNA. DR RefSeq; NP_274394.1; NC_003112.2. DR RefSeq; WP_002213178.1; NC_003112.2. DR ProteinModelPortal; P0A0Z0; -. DR STRING; 122586.NMB1378; -. DR PaxDb; P0A0Z0; -. DR EnsemblBacteria; AAF62328; AAF62328; NMB1378. DR GeneID; 903800; -. DR KEGG; nme:NMB1378; -. DR PATRIC; 20358433; VBINeiMen85645_1728. DR eggNOG; ENOG4108ZF1; Bacteria. DR eggNOG; COG1959; LUCA. DR HOGENOM; HOG000249812; -. DR KO; K13643; -. DR OMA; MTHDLWS; -. DR OrthoDB; EOG63FW56; -. DR BioCyc; NMEN122586:GHGG-1416-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR010242; TF_HTH_IscR. DR InterPro; IPR030489; TR_Rrf2-type_CS. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR02010; IscR; 1. DR TIGRFAMs; TIGR00738; rrf2_super; 1. DR PROSITE; PS01332; HTH_RRF2_1; 1. DR PROSITE; PS51197; HTH_RRF2_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 148 Putative HTH-type transcriptional FT regulator NMB1378. FT /FTId=PRO_0000036208. FT DOMAIN 2 131 HTH rrf2-type. {ECO:0000255|PROSITE- FT ProRule:PRU00540}. FT CONFLICT 8 9 RF -> LS (in Ref. 1; AAB09668). FT {ECO:0000305}. FT CONFLICT 132 148 QKNNGDGSRVVQFTHIH -> TEKQRRRQPRSSNLHTSIK FT (in Ref. 1; AAB09668). {ECO:0000305}. SQ SEQUENCE 148 AA; 15985 MW; E7CF370DE5D9BFBA CRC64; MRLTTKGRFA VTAMLDLAMN AQTGAVKLSA ISERQNISLS YLEQLFGKLR RAGLVESLRG PGGGYILAAP AARINIAQII AAAEDRLDAT QCGSKANCHH GAPCLTHDLW ENLNKTINDY LGSVTLQSII EQKNNGDGSR VVQFTHIH // ID Y524_NEIMB Reviewed; 406 AA. AC Q9K0R0; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=UPF0761 membrane protein NMB0524 {ECO:0000255|HAMAP-Rule:MF_00672}; GN OrderedLocusNames=NMB0524; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00672}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00672}. CC -!- SIMILARITY: Belongs to the UPF0761 family. {ECO:0000255|HAMAP- CC Rule:MF_00672}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40954.1; -; Genomic_DNA. DR PIR; D81189; D81189. DR RefSeq; NP_273569.1; NC_003112.2. DR RefSeq; WP_002237729.1; NC_003112.2. DR STRING; 122586.NMB0524; -. DR PaxDb; Q9K0R0; -. DR DNASU; 902639; -. DR EnsemblBacteria; AAF40954; AAF40954; NMB0524. DR GeneID; 902639; -. DR KEGG; nme:NMB0524; -. DR PATRIC; 20356291; VBINeiMen85645_0665. DR eggNOG; ENOG4107S2Z; Bacteria. DR eggNOG; COG1295; LUCA. DR HOGENOM; HOG000259417; -. DR KO; K07058; -. DR OMA; SVMTMMT; -. DR OrthoDB; EOG63NMKT; -. DR BioCyc; NMEN122586:GHGG-549-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00672; UPF0761; 1. DR InterPro; IPR023679; UPF0761_bac. DR InterPro; IPR017039; Virul_fac_BrkB. DR Pfam; PF03631; Virul_fac_BrkB; 1. DR TIGRFAMs; TIGR00765; yihY_not_rbn; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 406 UPF0761 membrane protein NMB0524. FT /FTId=PRO_0000200989. FT TRANSMEM 43 63 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 100 120 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 139 159 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 176 196 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 210 230 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 248 268 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. SQ SEQUENCE 406 AA; 45887 MW; 8A219088A89EE7D3 CRC64; MTFLQRLQGL ADNKICAFAW FVVRRFDEER VPQAAASMTF TTLLALVPVL TVMVAVASIF PVFDRWSDSF VSFVNQTIVP QGADMVFDYI NAFREQANRL TAIGSVMLVV TSLMLIRTID NTFNRIWRVN SQRPWMMQFL VYWALLTFGP LSLGVGISFM VGSVQDAALA SGAPQWSGAL RTAATLTFMT LLLWGLYRFV PNRFVPARQA FVGALATAFC LETARSLFTW YMGNFDGYRS IYGAFAAVPF FLLWLNLLWT LVLGGAVLTS SLSYWQGEAF RRGFDSRGRF DDVLKILLLL DAAQKEGKAL PVQEFRRHIN MGYDELGELL EKLARHGYIY SGRQGWVLKT GADSIELNEL FKLFVYRPLP VERDHVNQAV DAVMTPCLQT LNMTLAEFDA QAKKRQ // ID Y1645_NEIMB Reviewed; 446 AA. AC Q9JYD0; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE RecName: Full=Uncharacterized membrane protein NMB1645; GN OrderedLocusNames=NMB1645; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41994.1; -; Genomic_DNA. DR PIR; D81058; D81058. DR RefSeq; NP_274650.1; NC_003112.2. DR RefSeq; WP_002224998.1; NC_003112.2. DR STRING; 122586.NMB1645; -. DR PaxDb; Q9JYD0; -. DR EnsemblBacteria; AAF41994; AAF41994; NMB1645. DR GeneID; 903471; -. DR KEGG; nme:NMB1645; -. DR PATRIC; 20359210; VBINeiMen85645_2117. DR eggNOG; ENOG4105KD1; Bacteria. DR eggNOG; ENOG4111ZBE; LUCA. DR HOGENOM; HOG000219060; -. DR OMA; YGFVWET; -. DR OrthoDB; EOG6D8B6H; -. DR BioCyc; NMEN122586:GHGG-1694-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021296; DUF2868. DR Pfam; PF11067; DUF2868; 1. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 446 Uncharacterized membrane protein NMB1645. FT /FTId=PRO_0000320336. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. SQ SEQUENCE 446 AA; 50221 MW; 01FDCFEC98E04A6F CRC64; MLNPSRKLVE LVRILDEGGF IFSGDPVQAT EALRRVDGST EEKIIRRAEM IDRNRMLRET LERVRAGSFW LWVVAATFAF FTGFSVTYLL MDNQGLNFFL VLAGVLGMNT LMLAVWLAML FLRVKVGRFF SSPATWFRGK DPVNQAVLRL YADEWRQPSV RWKIGATSHS LWLCTLLGML VSVLLLLLVR QYTFNWESTL LSNAASVRAV EMLAWLPSKL GFPVPDARAV IEGRLNGNIA DARAWSGLLV GSIACYGILP RLLAWVVCKI LLKTSENGLD LEKPYYQAVI RRWQNKITDA DTRRETVSAV SPKIILNDAP KWAVMLETEW QDGEWFEGRL AQEWLDKGVA TNREQVAALE TELKQKPAQL LIGVRAQTVP DRGVLRQIVR LSEAAQGGAV VQLLAEQGLS DDLSEKLEHW RNALAECGAA WLEPDRAAQE GRLKDQ // ID Y1909_NEIMB Reviewed; 196 AA. AC Q9JXS2; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Maf-like protein NMB1909 {ECO:0000255|HAMAP-Rule:MF_00528}; GN OrderedLocusNames=NMB1909; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}. CC -!- SIMILARITY: Belongs to the maf family. {ECO:0000255|HAMAP- CC Rule:MF_00528}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42239.1; -; Genomic_DNA. DR PIR; D81028; D81028. DR RefSeq; NP_274903.1; NC_003112.2. DR RefSeq; WP_002221554.1; NC_003112.2. DR ProteinModelPortal; Q9JXS2; -. DR STRING; 122586.NMB1909; -. DR PaxDb; Q9JXS2; -. DR EnsemblBacteria; AAF42239; AAF42239; NMB1909. DR GeneID; 904255; -. DR KEGG; nme:NMB1909; -. DR PATRIC; 20359861; VBINeiMen85645_2435. DR eggNOG; ENOG4108UHJ; Bacteria. DR eggNOG; COG0424; LUCA. DR HOGENOM; HOG000241744; -. DR OMA; CAGSFKA; -. DR OrthoDB; EOG6SV5F0; -. DR BioCyc; NMEN122586:GHGG-1966-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_00528; Maf; 1. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR003697; Maf. DR Pfam; PF02545; Maf; 1. DR PIRSF; PIRSF006305; Maf; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00172; maf; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 196 Maf-like protein NMB1909. FT /FTId=PRO_0000123034. FT ACT_SITE 36 36 {ECO:0000255|HAMAP-Rule:MF_00528}. SQ SEQUENCE 196 AA; 21911 MW; C545A16B978561E9 CRC64; MGLELPLILG TSSVFRREQM ERLGIAFQAA SPDFDETPML GESAPQTALR LAEGKARSLT GRFPEALIVG ADQVAWCDGR QWGKPMNLAN AQKMLMHLSG REIEFYSAIV LLNTVTGRMR RHIDKTVVVM RQLDELHILR YLEREPDAVY CSCALKSEDL GALLIERIES TDPNALIGLP VFRLVDFLKN EGVEVL // ID Y228_NEIMB Reviewed; 245 AA. AC P0A0Z2; Q9JQN2; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=UPF0271 protein rni3 {ECO:0000255|HAMAP-Rule:MF_00691}; GN Name=rni3; OrderedLocusNames=NMB0228; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0271 (lamB) family. CC {ECO:0000255|HAMAP-Rule:MF_00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40684.1; -; Genomic_DNA. DR PIR; F81223; F81223. DR RefSeq; NP_273285.1; NC_003112.2. DR RefSeq; WP_002215593.1; NC_003112.2. DR ProteinModelPortal; P0A0Z2; -. DR STRING; 122586.NMB0228; -. DR PaxDb; P0A0Z2; -. DR EnsemblBacteria; AAF40684; AAF40684; NMB0228. DR GeneID; 902340; -. DR KEGG; nme:NMB0228; -. DR PATRIC; 20355532; VBINeiMen85645_0290. DR eggNOG; ENOG4105E7W; Bacteria. DR eggNOG; COG1540; LUCA. DR HOGENOM; HOG000237330; -. DR KO; K07160; -. DR OMA; AQVGYRD; -. DR OrthoDB; EOG6CZQJG; -. DR BioCyc; NMEN122586:GHGG-243-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR HAMAP; MF_00691; UPF0271; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR005501; UPF0271_LamB_YcsF. DR Pfam; PF03746; LamB_YcsF; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 245 UPF0271 protein rni3. FT /FTId=PRO_0000185020. SQ SEQUENCE 245 AA; 25983 MW; F3A5BB07B77DB5D6 CRC64; MKQVDLNADL AEGCGSDEAL LQLITSANIA CAQHAGSIAD IRAALAYAQQ NGVRIGAHPG YPDRENFGRT EMNLSEADLR ACLNYQLGAL QALCRDQGLE MAYVKPHGAM YNQAAKNRAL ADTVARIVAD FDPKLKLMAL SGSLLLEAGK AAGLGVISEV FADRRYMPDG TLVPRSRPDA QVDSDEEAIA QVLQMVRDGQ VKAVDGSLVA VQADSICLHG DGPHAVVFAE KIRQELLAAG IKVSA // ID Y598_NEIMB Reviewed; 202 AA. AC Q9K0J8; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Maf-like protein NMB0598 {ECO:0000255|HAMAP-Rule:MF_00528}; GN OrderedLocusNames=NMB0598; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}. CC -!- SIMILARITY: Belongs to the maf family. {ECO:0000255|HAMAP- CC Rule:MF_00528}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41026.1; -; Genomic_DNA. DR PIR; C81181; C81181. DR RefSeq; NP_273642.1; NC_003112.2. DR RefSeq; WP_002222850.1; NC_003112.2. DR ProteinModelPortal; Q9K0J8; -. DR STRING; 122586.NMB0598; -. DR PaxDb; Q9K0J8; -. DR EnsemblBacteria; AAF41026; AAF41026; NMB0598. DR GeneID; 902713; -. DR KEGG; nme:NMB0598; -. DR PATRIC; 20356481; VBINeiMen85645_0760. DR eggNOG; ENOG4108Z03; Bacteria. DR eggNOG; COG0424; LUCA. DR HOGENOM; HOG000241745; -. DR KO; K06287; -. DR OMA; EEEIAWY; -. DR OrthoDB; EOG6SV5F0; -. DR BioCyc; NMEN122586:GHGG-624-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_00528; Maf; 1. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR003697; Maf. DR Pfam; PF02545; Maf; 1. DR PIRSF; PIRSF006305; Maf; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00172; maf; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 202 Maf-like protein NMB0598. FT /FTId=PRO_0000123033. FT ACT_SITE 33 33 {ECO:0000255|HAMAP-Rule:MF_00528}. SQ SEQUENCE 202 AA; 22016 MW; 31A606823A5984F8 CRC64; MNTLYLGSNS PRRMEILTQL GYRVIQLPAG IDESVKAGET PFAYVQRMAE EKNRTALTLF CETNGTMPDF PLITADTCVV SDGIILGKPR SQAEAIEFLN RLSGKQHTVL TAVCIHYRGK TSSRVQTNRV VFKPLSSEEI SAYVQSGEPM DKAGAYAVQG IGGIFIQSIE GSFSGIMGLP VYETVSMLQD LGYRSPLSAL KP // ID Y681_NEIMB Reviewed; 74 AA. AC P67103; Q9JR98; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=UPF0033 protein NMB0681; GN OrderedLocusNames=NMB0681; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0033 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41099.1; -; Genomic_DNA. DR PIR; G81171; G81171. DR RefSeq; NP_273723.1; NC_003112.2. DR RefSeq; WP_002222784.1; NC_003112.2. DR ProteinModelPortal; P67103; -. DR STRING; 122586.NMB0681; -. DR PaxDb; P67103; -. DR EnsemblBacteria; AAF41099; AAF41099; NMB0681. DR GeneID; 902793; -. DR KEGG; nme:NMB0681; -. DR PATRIC; 20356671; VBINeiMen85645_0853. DR eggNOG; ENOG4105VFE; Bacteria. DR eggNOG; COG0425; LUCA. DR HOGENOM; HOG000259290; -. DR OMA; VRDFQAF; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-709-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.110.40; -; 1. DR InterPro; IPR001455; TusA-like. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS01148; UPF0033; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 74 UPF0033 protein NMB0681. FT /FTId=PRO_0000159074. SQ SEQUENCE 74 AA; 7896 MW; 478070A123B8F5D0 CRC64; MNSETLDVTG LKCPLPILRA KKALAQMQQG DVLTVLATDG GAPGDFEAFC RQTGHVLLDA SEQDGVFTLV VQHK // ID Y928_NEIMB Reviewed; 398 AA. AC Q9JZR5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein NMB0928; GN OrderedLocusNames=NMB0928; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41335.1; -; Genomic_DNA. DR PIR; C81141; C81141. DR RefSeq; NP_273967.1; NC_003112.2. DR RefSeq; WP_002225338.1; NC_003112.2. DR STRING; 122586.NMB0928; -. DR PaxDb; Q9JZR5; -. DR EnsemblBacteria; AAF41335; AAF41335; NMB0928. DR GeneID; 903049; -. DR KEGG; nme:NMB0928; -. DR PATRIC; 20357325; VBINeiMen85645_1177. DR eggNOG; COG3317; LUCA. DR HOGENOM; HOG000259527; -. DR KO; K07287; -. DR OMA; EVYISHR; -. DR OrthoDB; EOG6BCSRW; -. DR BioCyc; NMEN122586:GHGG-966-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010653; NlpB/DapX. DR Pfam; PF06804; Lipoprotein_18; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 398 Uncharacterized protein NMB0928. FT /FTId=PRO_0000320330. SQ SEQUENCE 398 AA; 43815 MW; 5EBDAB12FC734686 CRC64; MPSEPFGRHN ATNTLISITQ DDTMTHIKPV IAALALIGLA ACSGSKTEQP KLDYQSRSHR LIKLEVPPDL NNPDQGNLYR LPAGSGAVRA SDLEKRRTPA VQQPADAEVL KSVKGVRLER DGSQRWLVVD GKSPAEIWPL LKAFWQENGF DIKSEEPAIG QMETEWAENR AKIPQDSLRR LFDKVGLGGI YSTGERDKFI VRIEQGKNGV SDIFFAHKAM KEVYGGKDKD TTVWQPSPSD PNLEAAFLTR FMQYLGVDGQ QAENASAKKP TLPAANEMAR IEGKSLIVFG DYGRNWRRTV LALDRIGLTV VGQNTERHAF LVQKAPNESN AVTEQKPGLF KRLLGKGKAE KPAEQPELIV YAEPVANGSR IVLLNKDGSA YAGKDASALL GKLHSELR // ID Y1979_NEIMB Reviewed; 338 AA. AC Q9JXM0; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=UPF0324 membrane protein NMB1979; GN OrderedLocusNames=NMB1979; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0324 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42307.1; -; Genomic_DNA. DR PIR; D81020; D81020. DR RefSeq; NP_274972.1; NC_003112.2. DR RefSeq; WP_002225852.1; NC_003112.2. DR STRING; 122586.NMB1979; -. DR PaxDb; Q9JXM0; -. DR EnsemblBacteria; AAF42307; AAF42307; NMB1979. DR GeneID; 904160; -. DR KEGG; nme:NMB1979; -. DR PATRIC; 20360033; VBINeiMen85645_2521. DR eggNOG; ENOG4105HMI; Bacteria. DR eggNOG; COG2855; LUCA. DR HOGENOM; HOG000056253; -. DR KO; K19239; -. DR OMA; FTIFVVY; -. DR OrthoDB; EOG65QWM8; -. DR BioCyc; NMEN122586:GHGG-2036-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004630; UPF0324_bac. DR InterPro; IPR018383; UPF0324_pro. DR PANTHER; PTHR30106; PTHR30106; 1. DR Pfam; PF03601; Cons_hypoth698; 1. DR TIGRFAMs; TIGR00698; TIGR00698; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 338 UPF0324 membrane protein NMB1979. FT /FTId=PRO_0000157430. FT TRANSMEM 5 23 Helical. {ECO:0000255}. FT TRANSMEM 33 55 Helical. {ECO:0000255}. FT TRANSMEM 62 84 Helical. {ECO:0000255}. FT TRANSMEM 94 116 Helical. {ECO:0000255}. FT TRANSMEM 123 145 Helical. {ECO:0000255}. FT TRANSMEM 155 177 Helical. {ECO:0000255}. FT TRANSMEM 222 239 Helical. {ECO:0000255}. FT TRANSMEM 254 273 Helical. {ECO:0000255}. FT TRANSMEM 280 302 Helical. {ECO:0000255}. FT TRANSMEM 312 334 Helical. {ECO:0000255}. SQ SEQUENCE 338 AA; 36807 MW; BC160B75713BEEA5 CRC64; MNTRPFYFGL IFIAIIAILA NYLGNTDFSH HYHISALIIA ILLGMAIGNT IYPQFSTQVE KGVLFAKGAL LRTGIVLYGF RLTFGDIADV GLNAVVTDAI MLISTFFFTA LLGIRYLKMD KQLVYLTGAG CSICGAAAVM AAEPVTKAES HKVSVAIAVV VIFGTLAIFT YPLFYTWSQH LINAHQFGIY VGSSVHEVAQ VYAIGENIDP IVANTAVISK MIRVMMLAPF LLMLSWLLTR SNGVSENTSH KITIPWFAVL FIGVAIFNSF DLLPKELVKL FVEIDSFLLI SSMAALGLTT QASAIKKAGL KPFVLGILTY LWLVVGGFLV NYGISKLI // ID Y459_NEIMB Reviewed; 369 AA. AC Q9K0V1; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE RecName: Full=Uncharacterized protein NMB0459; GN OrderedLocusNames=NMB0459; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Contains 1 fido domain. {ECO:0000255|PROSITE- CC ProRule:PRU00791}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40896.1; -; Genomic_DNA. DR PIR; D81196; D81196. DR RefSeq; NP_273506.1; NC_003112.2. DR RefSeq; WP_002224940.1; NC_003112.2. DR ProteinModelPortal; Q9K0V1; -. DR STRING; 122586.NMB1423; -. DR PaxDb; Q9K0V1; -. DR EnsemblBacteria; AAF40896; AAF40896; NMB0459. DR GeneID; 902575; -. DR KEGG; nme:NMB0459; -. DR PATRIC; 20356138; VBINeiMen85645_0586. DR eggNOG; ENOG4107R3N; Bacteria. DR eggNOG; COG3177; LUCA. DR HOGENOM; HOG000295052; -. DR OrthoDB; EOG6SR92R; -. DR BioCyc; NMEN122586:GHGG-483-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR026287; AMPylator. DR InterPro; IPR025758; Fic/DOC_N. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR Pfam; PF13784; Fic_N; 1. DR PIRSF; PIRSF038925; AMP-prot_trans; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 369 Uncharacterized protein NMB0459. FT /FTId=PRO_0000320329. FT DOMAIN 111 261 Fido. {ECO:0000255|PROSITE- FT ProRule:PRU00791}. SQ SEQUENCE 369 AA; 41784 MW; E35B478AECDAB50F CRC64; MSNWKPNIPY NDLPPLPPKQ DIESKTILKR CIAARASLAR LKQAAELIPN QAMLINTLPV MEARASSEIE NIVTTTDKLF QSLQMDTERQ DPATKEALQY RTALFAGYES LTSRPLCTQT AIMVCNAIKH PYEMAIRKTG GTALKGGNSG NVVYTPPEGE ETIRGKLANW ERFIHESGDL DPLIIMAAAH YQFEAIHPFT DGNGRTGRIL NSLLLIEKGL LDLPILYLSR YIIENRADYY RLLLGVTERQ DWESWIIYIL DGVADTADWT VSKIDAIRRL FEQTRQHIRT HAQGIYTHEL VNLLFEQPYT RIANLEAAGI AKRQTASKYL KELSDIGVLQ EIVIGRDKLF IHPRLMELLR GEGNSFTSF // ID Y674_NEIMB Reviewed; 60 AA. AC Q7DDM0; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=UPF0434 protein NMB0674 {ECO:0000255|HAMAP-Rule:MF_01187}; GN OrderedLocusNames=NMB0674; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0434 family. {ECO:0000255|HAMAP- CC Rule:MF_01187}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41092.1; -; Genomic_DNA. DR PIR; H81170; H81170. DR RefSeq; NP_273716.1; NC_003112.2. DR RefSeq; WP_002221286.1; NC_003112.2. DR ProteinModelPortal; Q7DDM0; -. DR SMR; Q7DDM0; 1-60. DR STRING; 122586.NMB0674; -. DR PaxDb; Q7DDM0; -. DR EnsemblBacteria; AAF41092; AAF41092; NMB0674. DR GeneID; 23782006; -. DR GeneID; 902785; -. DR KEGG; nme:NMB0674; -. DR PATRIC; 20356651; VBINeiMen85645_0844. DR eggNOG; ENOG4105W49; Bacteria. DR eggNOG; COG2835; LUCA. DR HOGENOM; HOG000227338; -. DR KO; K09791; -. DR OMA; ELICHAD; -. DR OrthoDB; EOG6C8N1M; -. DR BioCyc; NMEN122586:GHGG-701-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_01187; UPF0434; 1. DR InterPro; IPR005651; UPF0434/Trm112. DR Pfam; PF03966; Trm112p; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 60 UPF0434 protein NMB0674. FT /FTId=PRO_0000291117. SQ SEQUENCE 60 AA; 7065 MW; C7E447A4281357A5 CRC64; MEKKFLDILV CPVTKGRLEY HQDKQELWSR QAKLAYPIKD GIPYMLENEA RALSEEELKA // ID Y738_NEIMB Reviewed; 284 AA. AC Q9K080; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Nucleotide-binding protein NMB0738 {ECO:0000255|HAMAP-Rule:MF_00636}; GN OrderedLocusNames=NMB0738; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Displays ATPase and GTPase activities. CC {ECO:0000255|HAMAP-Rule:MF_00636}. CC -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP- CC Rule:MF_00636}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41151.1; -; Genomic_DNA. DR PIR; B81165; B81165. DR RefSeq; NP_273780.1; NC_003112.2. DR RefSeq; WP_010980831.1; NC_003112.2. DR ProteinModelPortal; Q9K080; -. DR STRING; 122586.NMB0738; -. DR PaxDb; Q9K080; -. DR EnsemblBacteria; AAF41151; AAF41151; NMB0738. DR GeneID; 902851; -. DR KEGG; nme:NMB0738; -. DR PATRIC; 20356835; VBINeiMen85645_0938. DR eggNOG; ENOG4105C21; Bacteria. DR eggNOG; COG1660; LUCA. DR HOGENOM; HOG000244885; -. DR KO; K06958; -. DR OMA; VSFGYKY; -. DR OrthoDB; EOG6WHNW8; -. DR BioCyc; NMEN122586:GHGG-767-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00636; RapZ_like; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005337; RapZ-like. DR Pfam; PF03668; ATP_bind_2; 1. DR PIRSF; PIRSF005052; P-loopkin; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 284 Nucleotide-binding protein NMB0738. FT /FTId=PRO_0000107735. FT NP_BIND 8 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00636}. FT NP_BIND 58 61 GTP. {ECO:0000255|HAMAP-Rule:MF_00636}. SQ SEQUENCE 284 AA; 32831 MW; 967910AD437A5EBD CRC64; MKIVLISGLS GSGKSVALRQ MEDSGYFCVD NLPLEMLPAL VSYHIERADE TELAVSVDVR SGIDIGQARE QIASLRRLGH RVEVLFVEAE ESVLVRRFSE TRRGHPLSNQ DMTLLESLKK EREWLFPLKE IAYCIDTSKM NAQQLRHAVR QWLKVERTGL LVILESFGFK YGVPNNADFM FDMRSLPNPY YDPELRPYTG MDKPVWDYLD GQPLVQEMVD DIERFVTHWL PRLEDESRSY VTVAIGCTGG QHRSVYIVEK LARRLKGRYE LLIRHRQAQN LSDR // ID Y895_NEIMB Reviewed; 259 AA. AC Q9JZU5; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 17-FEB-2016, entry version 65. DE RecName: Full=UPF0246 protein NMB0895 {ECO:0000255|HAMAP-Rule:MF_00652}; GN OrderedLocusNames=NMB0895; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0246 family. {ECO:0000255|HAMAP- CC Rule:MF_00652}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41304.1; -; Genomic_DNA. DR PIR; E81146; E81146. DR RefSeq; NP_273936.1; NC_003112.2. DR RefSeq; WP_002225351.1; NC_003112.2. DR STRING; 122586.NMB0895; -. DR PaxDb; Q9JZU5; -. DR EnsemblBacteria; AAF41304; AAF41304; NMB0895. DR GeneID; 903014; -. DR KEGG; nme:NMB0895; -. DR PATRIC; 20357213; VBINeiMen85645_1122. DR eggNOG; ENOG4105D1Q; Bacteria. DR eggNOG; COG3022; LUCA. DR HOGENOM; HOG000218488; -. DR KO; K09861; -. DR OMA; GLMARYI; -. DR OrthoDB; EOG6423KT; -. DR BioCyc; NMEN122586:GHGG-931-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR HAMAP; MF_00652; UPF0246; 1. DR InterPro; IPR005583; YaaA. DR Pfam; PF03883; DUF328; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 259 UPF0246 protein NMB0895. FT /FTId=PRO_0000203991. SQ SEQUENCE 259 AA; 29696 MW; C2FCB5443047D54D CRC64; MFFVLSPAKN LNEKDPAPVS EFTQPDLLAE SDILMQQLRE LAPQQIAELM HVSDKIALLN AQRNAEWNTP FTPENAKQAV FMFNGDVYEG MDANTLDIGQ IRYLQNHVRL LSGLYGLLRP LDLIQPYRLE MGTAFANLRG KNLYEFWGDI ITNLLNDTLA QAGSNTLVNL ASQEYFKSVN TKKLRARLIT PIFKDEKNGK YKIISFYAKR ARGLMVRYAA EHHITDPEML KNFNYEGYAF NDAASNESEW VFMRSEQIK // ID Y840_NEIMB Reviewed; 168 AA. AC Q9JZZ2; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 11-MAY-2016, entry version 78. DE RecName: Full=UPF0307 protein NMB0840 {ECO:0000255|HAMAP-Rule:MF_00765}; GN OrderedLocusNames=NMB0840; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0307 family. {ECO:0000255|HAMAP- CC Rule:MF_00765}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF41251.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41251.1; ALT_INIT; Genomic_DNA. DR PIR; E81151; E81151. DR RefSeq; NP_273881.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ2; -. DR STRING; 122586.NMB0840; -. DR PaxDb; Q9JZZ2; -. DR DNASU; 902954; -. DR EnsemblBacteria; AAF41251; AAF41251; NMB0840. DR GeneID; 902954; -. DR KEGG; nme:NMB0840; -. DR PATRIC; 20357067; VBINeiMen85645_1052. DR eggNOG; ENOG4105N42; Bacteria. DR eggNOG; COG3028; LUCA. DR HOGENOM; HOG000013875; -. DR KO; K09889; -. DR OMA; HLIERWR; -. DR OrthoDB; EOG6RJV5H; -. DR BioCyc; NMEN122586:GHGG-871-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.60.30; -; 2. DR HAMAP; MF_00765; UPF0307; 1. DR InterPro; IPR023153; PSPTO4464-like_domain. DR InterPro; IPR006839; Ribosome-assoc_YjgA. DR Pfam; PF04751; DUF615; 1. DR PIRSF; PIRSF016183; UCP016183; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 168 UPF0307 protein NMB0840. FT /FTId=PRO_0000208219. SQ SEQUENCE 168 AA; 19101 MW; 8FEB9E0E1BF37D4B CRC64; MFEQEDEWIS KTQMKKQMND LQDLGMALTK LSNDTLKKIG LDADLYEAVT AYKKITSNGA LKRQAQFIGR LMRDTDPAPI EAFLAKLRGD DAAHNAFLQR VEQARVRLLA DDGALTQFMS DFPHADAGKL RTLIRNTKKE QEQNKPPKNF RALFQELKTV MENGDAEI // ID Y964_NEIMB Reviewed; 758 AA. AC Q9JZN9; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=Probable TonB-dependent receptor NMB0964; DE Flags: Precursor; GN OrderedLocusNames=NMB0964; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17038831; DOI=10.4161/hv.1.2.1651; RA Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.; RT "Characterization of the protein content of a meningococcal outer RT membrane vesicle vaccine by polyacrylamide gel electrophoresis and RT mass spectrometry."; RL Hum. Vaccin. 1:80-84(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=NZ98/254 / Serogroup B; RX PubMed=16645985; DOI=10.1002/pmic.200500821; RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.; RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine RT prepared from the group B strain NZ98/254."; RL Proteomics 6:3400-3413(2006). CC -!- FUNCTION: Probable receptor, TonB-dependent. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}. CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations CC which are used as vaccines in human. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62323.1; -; Genomic_DNA. DR RefSeq; NP_274002.1; NC_003112.2. DR RefSeq; WP_002244095.1; NC_003112.2. DR PDB; 4RDR; X-ray; 2.47 A; A=25-758. DR PDB; 4RDT; X-ray; 3.20 A; A/B=25-758. DR PDB; 4RVW; X-ray; 4.48 A; A=25-758. DR PDBsum; 4RDR; -. DR PDBsum; 4RDT; -. DR PDBsum; 4RVW; -. DR ProteinModelPortal; Q9JZN9; -. DR STRING; 122586.NMB0964; -. DR TCDB; 1.B.14.2.9; the outer membrane receptor (omr) family. DR PaxDb; Q9JZN9; -. DR EnsemblBacteria; AAF62323; AAF62323; NMB0964. DR GeneID; 903084; -. DR KEGG; nme:NMB0964; -. DR PATRIC; 20357415; VBINeiMen85645_1222. DR eggNOG; ENOG4105UGU; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000191365; -. DR KO; K02014; -. DR OMA; RYDKALI; -. DR OrthoDB; EOG64R616; -. DR BioCyc; NMEN122586:GHGG-1001-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 2. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Membrane; KW Receptor; Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 758 Probable TonB-dependent receptor NMB0964. FT /FTId=PRO_0000349888. FT MOTIF 741 758 TonB C-terminal box. FT STRAND 59 62 {ECO:0000244|PDB:4RDR}. FT HELIX 63 66 {ECO:0000244|PDB:4RDR}. FT HELIX 73 77 {ECO:0000244|PDB:4RDR}. FT STRAND 83 88 {ECO:0000244|PDB:4RDR}. FT TURN 89 91 {ECO:0000244|PDB:4RDR}. FT STRAND 92 97 {ECO:0000244|PDB:4RDR}. FT HELIX 102 104 {ECO:0000244|PDB:4RDR}. FT STRAND 105 109 {ECO:0000244|PDB:4RDR}. FT TURN 118 120 {ECO:0000244|PDB:4RDR}. FT HELIX 130 132 {ECO:0000244|PDB:4RDR}. FT STRAND 133 139 {ECO:0000244|PDB:4RDR}. FT HELIX 142 146 {ECO:0000244|PDB:4RDR}. FT STRAND 155 163 {ECO:0000244|PDB:4RDR}. FT HELIX 169 171 {ECO:0000244|PDB:4RDR}. FT STRAND 172 181 {ECO:0000244|PDB:4RDR}. FT TURN 182 184 {ECO:0000244|PDB:4RDR}. FT STRAND 187 196 {ECO:0000244|PDB:4RDR}. FT STRAND 198 212 {ECO:0000244|PDB:4RDR}. FT STRAND 214 216 {ECO:0000244|PDB:4RDT}. FT STRAND 218 220 {ECO:0000244|PDB:4RDT}. FT STRAND 224 226 {ECO:0000244|PDB:4RDT}. FT STRAND 231 242 {ECO:0000244|PDB:4RDR}. FT STRAND 245 261 {ECO:0000244|PDB:4RDR}. FT TURN 268 271 {ECO:0000244|PDB:4RDR}. FT STRAND 272 275 {ECO:0000244|PDB:4RDR}. FT HELIX 279 284 {ECO:0000244|PDB:4RDR}. FT HELIX 287 290 {ECO:0000244|PDB:4RDR}. FT HELIX 292 294 {ECO:0000244|PDB:4RDR}. FT HELIX 297 299 {ECO:0000244|PDB:4RDR}. FT TURN 300 302 {ECO:0000244|PDB:4RDT}. FT STRAND 306 309 {ECO:0000244|PDB:4RDR}. FT STRAND 326 342 {ECO:0000244|PDB:4RDR}. FT STRAND 348 366 {ECO:0000244|PDB:4RDR}. FT STRAND 369 387 {ECO:0000244|PDB:4RDR}. FT STRAND 390 410 {ECO:0000244|PDB:4RDR}. FT TURN 414 416 {ECO:0000244|PDB:4RDT}. FT STRAND 420 439 {ECO:0000244|PDB:4RDR}. FT STRAND 442 456 {ECO:0000244|PDB:4RDR}. FT HELIX 461 468 {ECO:0000244|PDB:4RDR}. FT STRAND 480 494 {ECO:0000244|PDB:4RDR}. FT STRAND 496 510 {ECO:0000244|PDB:4RDR}. FT HELIX 514 518 {ECO:0000244|PDB:4RDR}. FT STRAND 520 523 {ECO:0000244|PDB:4RDR}. FT HELIX 524 526 {ECO:0000244|PDB:4RDR}. FT STRAND 528 531 {ECO:0000244|PDB:4RDR}. FT STRAND 539 552 {ECO:0000244|PDB:4RDR}. FT STRAND 555 574 {ECO:0000244|PDB:4RDR}. FT STRAND 576 580 {ECO:0000244|PDB:4RDR}. FT STRAND 591 614 {ECO:0000244|PDB:4RDR}. FT STRAND 617 632 {ECO:0000244|PDB:4RDR}. FT STRAND 663 673 {ECO:0000244|PDB:4RDR}. FT STRAND 676 685 {ECO:0000244|PDB:4RDR}. FT STRAND 701 713 {ECO:0000244|PDB:4RDR}. FT STRAND 715 726 {ECO:0000244|PDB:4RDR}. FT TURN 739 742 {ECO:0000244|PDB:4RDR}. FT STRAND 749 758 {ECO:0000244|PDB:4RDR}. SQ SEQUENCE 758 AA; 85120 MW; 6BA342986968640B CRC64; MAQTTLKPIV LSILLINTPL LAQAHETEQS VDLETVSVVG KSRPRATSGL LHTSTASDKI ISGDTLRQKA VNLGDALDGV PGIHASQYGG GASAPVIRGQ TGRRIKVLNH HGETGDMADF SPDHAIMVDT ALSQQVEILR GPVTLLYSSG NVAGLVDVAD GKIPEKMPEN GVSGELGLRL SSGNLEKLTS GGINIGLGKN FVLHTEGLYR KSGDYAVPRY RNLKRLPDSH ADSQTGSIGL SWVGEKGFIG VAYSDRRDQY GLPAHSHEYD DCHADIIWQK SLINKRYLQL YPHLLTEEDI DYDNPGLSCG FHDDDNAHAH THSGRPWIDL RNKRYELRAE WKQPFPGFEA LRVHLNRNDY RHDEKAGDAV ENFFNNQTQN ARIELRHQPI GRLKGSWGVQ YLQQKSSALS AISEAVKQPM LLDNKVQHYS FFGVEQANWD NFTLEGGVRV EKQKASIQYD KALIDRENYY NHPLPDLGAH RQTARSFALS GNWYFTPQHK LSLTASHQER LPSTQELYAH GKHVATNTFE VGNKHLNKER SNNIELALGY EGDRWQYNLA LYRNRFGNYI YAQTLNDGRG PKSIEDDSEM KLVRYNQSGA DFYGAEGEIY FKPTPRYRIG VSGDYVRGRL KNLPSLPGRE DAYGNRPFIA QDDQNAPRVP AARLGFHLKA SLTDRIDANL DYYRVFAQNK LARYETRTPG HHMLNLGANY RRNTRYGEWN WYVKADNLLN QSVYAHSSFL SDTPQMGRSF TGGVNVKF // ID Y796_NEIMB Reviewed; 92 AA. AC P67259; Q9JRC2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 52. DE RecName: Full=UPF0125 protein NMB0796; GN OrderedLocusNames=NMB0796; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0125 (RnfH) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41209.1; -; Genomic_DNA. DR PIR; C81157; C81157. DR RefSeq; NP_273838.1; NC_003112.2. DR RefSeq; WP_002217575.1; NC_003112.2. DR ProteinModelPortal; P67259; -. DR STRING; 122586.NMB0796; -. DR PaxDb; P67259; -. DR EnsemblBacteria; AAF41209; AAF41209; NMB0796. DR GeneID; 902911; -. DR KEGG; nme:NMB0796; -. DR PATRIC; 20356979; VBINeiMen85645_1008. DR eggNOG; ENOG4105VDB; Bacteria. DR eggNOG; COG2914; LUCA. DR HOGENOM; HOG000261719; -. DR KO; K09801; -. DR OMA; GRINKIT; -. DR OrthoDB; EOG6Q8J4M; -. DR BioCyc; NMEN122586:GHGG-827-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.20.280; -; 1. DR HAMAP; MF_00460; UPF0125_RnfH; 1. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR005346; RnfH. DR Pfam; PF03658; Ub-RnfH; 1. DR SUPFAM; SSF54285; SSF54285; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 92 UPF0125 protein NMB0796. FT /FTId=PRO_0000192493. SQ SEQUENCE 92 AA; 10344 MW; 3A6EE518FFA6265F CRC64; MLEIEIVYGL PDRQVLKTMQ LAEGTTVRAA ALQSGLDGIF EDLNLHSAPL GIFGKAVKDD TPLRDGDRIE VYRPLLIDPK EARRKRVQNQ EE // ID YBEY_NEIMB Reviewed; 169 AA. AC Q9K0P7; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009}; GN Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; GN OrderedLocusNames=NMB0538; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved CC in late-stage 70S ribosome quality control and in maturation of CC the 3' terminus of the 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00009}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00009}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}. CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family. CC {ECO:0000255|HAMAP-Rule:MF_00009}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40967.1; -; Genomic_DNA. DR PIR; A81188; A81188. DR RefSeq; NP_273583.1; NC_003112.2. DR RefSeq; WP_002225585.1; NC_003112.2. DR ProteinModelPortal; Q9K0P7; -. DR STRING; 122586.NMB0538; -. DR PaxDb; Q9K0P7; -. DR EnsemblBacteria; AAF40967; AAF40967; NMB0538. DR GeneID; 902653; -. DR KEGG; nme:NMB0538; -. DR PATRIC; 20356333; VBINeiMen85645_0685. DR eggNOG; ENOG4105KGE; Bacteria. DR eggNOG; COG0319; LUCA. DR HOGENOM; HOG000132870; -. DR KO; K07042; -. DR OMA; NTKPATM; -. DR OrthoDB; EOG680X6D; -. DR BioCyc; NMEN122586:GHGG-564-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.390.30; -; 1. DR HAMAP; MF_00009; Endoribonucl_YbeY; 1. DR InterPro; IPR023091; MetalPrtase_cat_dom_prd. DR InterPro; IPR002036; YbeY. DR InterPro; IPR020549; YbeY_CS. DR Pfam; PF02130; UPF0054; 1. DR TIGRFAMs; TIGR00043; TIGR00043; 1. DR PROSITE; PS01306; UPF0054; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; KW Nuclease; Reference proteome; Ribosome biogenesis; rRNA processing; KW Zinc. FT CHAIN 1 169 Endoribonuclease YbeY. FT /FTId=PRO_0000102496. FT METAL 130 130 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 134 134 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 140 140 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. SQ SEQUENCE 169 AA; 19639 MW; BA21D528B7B86F6E CRC64; MKRTKKYPFL TLQRQRFHLN FENASSAAGI PAERDFYRWA WSALKNEYRR ADISLILLDE EEARAYNRDY RGKDYATNVL SFALNEGEIL PCQVSEKLYG DLIICPQVVL KEAAEQGKTP EQHFAHLTIH GTLHLMGYDH IEDDEAEIME AEEIRLMRAA GFPNPYQED // ID YCIB_NEIMB Reviewed; 176 AA. AC P65196; Q9JR24; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Probable intracellular septation protein A {ECO:0000255|HAMAP-Rule:MF_00189}; GN OrderedLocusNames=NMB0342; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in cell division; probably involved in CC intracellular septation. {ECO:0000255|HAMAP-Rule:MF_00189}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00189}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00189}. CC -!- SIMILARITY: Belongs to the YciB family. {ECO:0000255|HAMAP- CC Rule:MF_00189}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40785.1; -; Genomic_DNA. DR PIR; D81209; D81209. DR RefSeq; NP_273391.1; NC_003112.2. DR RefSeq; WP_002212347.1; NC_003112.2. DR STRING; 122586.NMB0342; -. DR PaxDb; P65196; -. DR EnsemblBacteria; AAF40785; AAF40785; NMB0342. DR GeneID; 902457; -. DR KEGG; nme:NMB0342; -. DR PATRIC; 20355831; VBINeiMen85645_0434. DR eggNOG; ENOG4107835; Bacteria. DR eggNOG; COG2917; LUCA. DR HOGENOM; HOG000062588; -. DR KO; K06190; -. DR OMA; FWVNFKV; -. DR OrthoDB; EOG6JHRJS; -. DR BioCyc; NMEN122586:GHGG-363-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00189; Intracell_septation_prot_A; 1. DR InterPro; IPR006008; Intracell_sepatation_prot_A. DR Pfam; PF04279; IspA; 1. DR TIGRFAMs; TIGR00997; ispZ; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Septation; KW Transmembrane; Transmembrane helix. FT CHAIN 1 176 Probable intracellular septation protein FT A. FT /FTId=PRO_0000206537. FT TRANSMEM 23 43 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 50 70 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 74 94 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 119 139 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 150 170 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. SQ SEQUENCE 176 AA; 19941 MW; 77D27F6AD8CD236A CRC64; MKFVSDLLSV ILFFATYTVT KNMIAATAVA LVAGVVQAAF LYWKYKKLDT MQWVGLVLIV VFGGATIVLG DSRFIMWKPS VLFWLGALFL WGSHLAGKNG LKASIGREIQ LPDAVWAKLT YMWVGFLIFM GIANWFVFTR FESQWVNYKM FGSTALMLVF FIIQGIYLST CLKKED // ID YACG_NEIMB Reviewed; 69 AA. AC Q9K155; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN OrderedLocusNames=NMB0330; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Inhibits all the catalytic activities of DNA gyrase by CC preventing its interaction with DNA. Acts by binding directly to CC the C-terminal domain of GyrB, which probably disrupts DNA binding CC by the gyrase. {ECO:0000255|HAMAP-Rule:MF_00649}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00649}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00649}; CC -!- SUBUNIT: Interacts with GyrB. {ECO:0000255|HAMAP-Rule:MF_00649}. CC -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family. CC {ECO:0000255|HAMAP-Rule:MF_00649}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40774.1; -; Genomic_DNA. DR PIR; F81210; F81210. DR RefSeq; NP_273379.1; NC_003112.2. DR RefSeq; WP_002224872.1; NC_003112.2. DR ProteinModelPortal; Q9K155; -. DR SMR; Q9K155; 9-45. DR STRING; 122586.NMB0330; -. DR PaxDb; Q9K155; -. DR EnsemblBacteria; AAF40774; AAF40774; NMB0330. DR GeneID; 902446; -. DR KEGG; nme:NMB0330; -. DR PATRIC; 20355799; VBINeiMen85645_0418. DR eggNOG; ENOG41067SF; Bacteria. DR eggNOG; COG3024; LUCA. DR HOGENOM; HOG000255917; -. DR KO; K09862; -. DR OMA; RIAGEPS; -. DR OrthoDB; EOG65F8ZX; -. DR BioCyc; NMEN122586:GHGG-351-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008657; F:DNA topoisomerase (ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.30.50.10; -; 1. DR HAMAP; MF_00649; DNA_gyrase_inhibitor_YacG; 1. DR InterPro; IPR005584; DNA_gyrase_inhibitor_YacG. DR InterPro; IPR013088; Znf_NHR/GATA. DR Pfam; PF03884; DUF329; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 69 DNA gyrase inhibitor YacG. FT /FTId=PRO_0000211711. FT METAL 13 13 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 16 16 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 32 32 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 36 36 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. SQ SEQUENCE 69 AA; 7841 MW; 2402316DAAA77096 CRC64; MTESRQTRLQ VKCPTCQTAV VWKPENAFRP FCSQRCKLID LGGWADGKYT VSGQTESLPE ISEPDMAYR // ID YIDC_NEIMB Reviewed; 545 AA. AC Q9JXS4; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Membrane protein insertase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Foldase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane integrase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane protein YidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN Name=yidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN OrderedLocusNames=NMB1907; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the insertion and/or proper folding and/or CC complex formation of integral membrane proteins into the membrane. CC Involved in integration of membrane proteins that insert both CC dependently and independently of the Sec translocase complex, as CC well as at least some lipoproteins. Aids folding of multispanning CC membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBUNIT: Interacts with the Sec translocase complex via SecD. CC Specifically interacts with transmembrane segments of nascent CC integral membrane proteins during membrane integration. CC {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01810}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01810}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01810}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42237.1; -; Genomic_DNA. DR PIR; B81028; B81028. DR RefSeq; NP_274901.1; NC_003112.2. DR RefSeq; WP_002221552.1; NC_003112.2. DR ProteinModelPortal; Q9JXS4; -. DR STRING; 122586.NMB1907; -. DR PaxDb; Q9JXS4; -. DR EnsemblBacteria; AAF42237; AAF42237; NMB1907. DR GeneID; 904258; -. DR KEGG; nme:NMB1907; -. DR PATRIC; 20359857; VBINeiMen85645_2433. DR eggNOG; ENOG4105DHW; Bacteria. DR eggNOG; COG0706; LUCA. DR HOGENOM; HOG000101822; -. DR KO; K03217; -. DR OMA; ELRHTPF; -. DR OrthoDB; EOG6X6RF2; -. DR BioCyc; NMEN122586:GHGG-1964-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051205; P:protein insertion into membrane; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR HAMAP; MF_01810; YidC_type1; 1. DR InterPro; IPR019998; Membr_insert_YidC. DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C. DR InterPro; IPR028053; Membr_insert_YidC_N. DR InterPro; IPR001708; Membrane_insert_OXA1/ALB3/YidC. DR PANTHER; PTHR12428; PTHR12428; 1. DR Pfam; PF02096; 60KD_IMP; 1. DR Pfam; PF14849; YidC_periplas; 1. DR PRINTS; PR00701; 60KDINNERMP. DR PRINTS; PR01900; YIDCPROTEIN. DR TIGRFAMs; TIGR03593; yidC_nterm; 1. DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Membrane; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 545 Membrane protein insertase YidC. FT /FTId=PRO_0000124733. FT TRANSMEM 350 370 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 424 444 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 461 481 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 498 518 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. SQ SEQUENCE 545 AA; 60723 MW; 166E85E56951ED0B CRC64; MDFKRLTAFF AIALVIMIGW EKMFPTPKPV PAPQQAAQQQ AVTASAEAAL APATPITVTT DTVQAVIDEK SGDLRRLTLL KYKATGDENK PFILFGDGKE YTYVAQSELL DAQGNNILKG IGFSAPKKQY SLEGDKVEVR LSAPETRGLK IDKVYTFTKG SYLVNVRFDI ANGSGQTANL SADYRIVRDH SEPEGQGYFT HSYVGPVVYT PEGNFQKVSF SDLDDDAKSG KSEAEYIRKT PTGWLGMIEH HFMSTWILQP KGRQSVCAAG ECNIDIKRRN DKLYSTSVSV PLAAIQNGAK AEASINLYAG PQTTSVIANI ADNLQLAKDY GKVHWFASPL FWLLNQLHNI IGNWGWAIIV LTIIVKAVLY PLTNASYRSM AKMRAAAPKL QAIKEKYGDD RMAQQQAMMQ LYTDEKINPL GGCLPMLLQI PVFIGLYWAL FASVELRQAP WLGWITDLSR ADPYYILPII MAATMFAQTY LNPPPTDPMQ AKMMKIMPLV FSVMFFFFPA GLVLYWVVNN LLTIAQQWHI NRSIEKQRAQ GEVVS // ID YHGF_NEIMB Reviewed; 757 AA. AC Q51152; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-MAY-2016, entry version 96. DE RecName: Full=Uncharacterized protein NMB0075; GN OrderedLocusNames=NMB0075; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=8655518; RA Petering H., Hammerschmidt S., Frosch M., van Putten J.P.M., RA Ison C.A., Robertson B.D.; RT "Genes associated with meningococcal capsule complex are also found in RT Neisseria gonorrhoeae."; RL J. Bacteriol. 178:3342-3345(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L09189; AAC37046.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40542.1; -; Genomic_DNA. DR PIR; A81242; A81242. DR RefSeq; NP_273139.1; NC_003112.2. DR RefSeq; WP_002224749.1; NC_003112.2. DR ProteinModelPortal; Q51152; -. DR SMR; Q51152; 2-715. DR STRING; 122586.NMB0075; -. DR PaxDb; Q51152; -. DR EnsemblBacteria; AAF40542; AAF40542; NMB0075. DR GeneID; 902181; -. DR KEGG; nme:NMB0075; -. DR PATRIC; 20355151; VBINeiMen85645_0109. DR eggNOG; ENOG4105BZM; Bacteria. DR eggNOG; COG2183; LUCA. DR HOGENOM; HOG000270497; -. DR KO; K06959; -. DR OMA; GFLRIRD; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NMEN122586:GHGG-81-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 1.10.10.650; -; 1. DR Gene3D; 1.10.150.310; -; 1. DR Gene3D; 1.10.3500.10; -; 2. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.420.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR023323; Tex-like_dom. DR InterPro; IPR023319; Tex-like_HTH_dom. DR InterPro; IPR018974; Tex-like_N. DR InterPro; IPR023097; Tex_RuvX-like_dom. DR InterPro; IPR032639; Tex_YqgF. DR InterPro; IPR006641; YqgF/RNaseH-like_dom. DR Pfam; PF00575; S1; 1. DR Pfam; PF09371; Tex_N; 1. DR Pfam; PF16921; Tex_YqgF; 1. DR SMART; SM00316; S1; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF47781; SSF47781; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 757 Uncharacterized protein NMB0075. FT /FTId=PRO_0000215108. FT DOMAIN 640 709 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT CONFLICT 265 266 WL -> CV (in Ref. 1; AAC37046). FT {ECO:0000305}. SQ SEQUENCE 757 AA; 83162 MW; 7B6851EEB5ED66AE CRC64; MNITQILSQE LSATAAQITA AVELLDDGAT VPFIARYRKE ATGGLDDTQL RRLAERLQYL RELEERKAVV LKSIEEQGKL SDDLRAQIEA ADNKTALEDL YLPYKPKRRT KAQIAREHGL QPLADVLLAE QSQDVEAAAQ GYLNENVPDA KAALDGARAI LMEQFAEDAE LIGTLRDKLW NEAEIHAQVV EGKETEGEKF SDYFDHREPV RTMPSHRALA VLRGRNEGVL NIALKYQPDD TPITRQSEYE QIIACRFKVS DGHKWLRDTV RLTWRAKIFL SLELEALGRL KEAADTDAIT VFARNLKDLL LVAPAGRLTT LGLDPGYRNG VKCAVVDDTG KLLDTVIVYL HQENNMLATL SRLIKQHGVK LIAIGNGTAS RETDKIAGEL VRGMPEMGLH KIVVSEAGAS IYSASELAAR EFPDLDVSLR GAVSIARRLQ DPLAELVKID PKSIGVGQYQ HDVNQNQLAK SLDAVVEDCV NAVGVDVNTA SAPLLARISG LNQTLAQNIV AYRDENGAFD SRKKLLKVPR LGEKTFEQAA GFLRINGGKE PLDASAVHPE AYPVVAKMLA QQGISAAELI GNRERVKQIK ASDFTDERFG LPTILDILSE LEKPGRDPRG EFQTASFAEG IHEISDLQVG MILEGVVSNV ANFGAFVDIG VHQDGLVHIS ALSNKFVQDP REVVKAGDVV KVKVLEVDAA RKRIALTMRL DDEPGGAKHK MPSENRSRER TAGRKPQRND RAPANSAMAD AFAKLKR // ID YIDD_NEIMB Reviewed; 73 AA. AC P67303; Q9JW47; Q9JXS5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 58. DE RecName: Full=Putative membrane protein insertion efficiency factor {ECO:0000255|HAMAP-Rule:MF_00386}; GN OrderedLocusNames=NMB1906; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Could be involved in insertion of integral membrane CC proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00386}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00386}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC -!- SIMILARITY: Belongs to the UPF0161 family. {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42236.1; -; Genomic_DNA. DR PIR; A81028; A81028. DR RefSeq; NP_274900.1; NC_003112.2. DR RefSeq; WP_002214730.1; NC_003112.2. DR STRING; 122586.NMB1906; -. DR PaxDb; P67303; -. DR EnsemblBacteria; AAF42236; AAF42236; NMB1906. DR GeneID; 904261; -. DR KEGG; nme:NMB1906; -. DR PATRIC; 20359855; VBINeiMen85645_2432. DR eggNOG; ENOG4105VAS; Bacteria. DR eggNOG; COG0759; LUCA. DR HOGENOM; HOG000231600; -. DR KO; K08998; -. DR OMA; PFSKGGV; -. DR OrthoDB; EOG61ZTN6; -. DR BioCyc; NMEN122586:GHGG-1963-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00386; UPF0161_YidD; 1. DR InterPro; IPR002696; Membr_insert_effic_factor. DR Pfam; PF01809; Haemolytic; 1. DR ProDom; PD004225; DUF37; 1. DR SMART; SM01234; Haemolytic; 1. DR TIGRFAMs; TIGR00278; TIGR00278; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome. FT CHAIN 1 73 Putative membrane protein insertion FT efficiency factor. FT /FTId=PRO_0000171844. SQ SEQUENCE 73 AA; 8237 MW; 237B1EEC45DBDA79 CRC64; MNFLLSKLLL GLIRFYQYCI SPLIPPRCRY TPTCSQYAVE AVKKYGAFKG GRLAIKRIAR CHPFGGHGHD PVP // ID ZUPT_NEIMB Reviewed; 269 AA. AC Q9K1H6; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Zinc transporter ZupT; GN Name=zupT; OrderedLocusNames=NMB0175; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Mediates zinc uptake. May also transport other divalent CC cations (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. ZupT CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40632.1; -; Genomic_DNA. DR PIR; G81230; G81230. DR RefSeq; NP_273233.1; NC_003112.2. DR RefSeq; WP_002224778.1; NC_003112.2. DR STRING; 122586.NMB0175; -. DR PaxDb; Q9K1H6; -. DR EnsemblBacteria; AAF40632; AAF40632; NMB0175. DR GeneID; 25048870; -. DR GeneID; 902282; -. DR KEGG; nme:NMB0175; -. DR PATRIC; 20355375; VBINeiMen85645_0217. DR eggNOG; ENOG4105DUN; Bacteria. DR eggNOG; COG0428; LUCA. DR HOGENOM; HOG000232704; -. DR KO; K07238; -. DR OMA; MIVASFT; -. DR OrthoDB; EOG6M3PH0; -. DR BioCyc; NMEN122586:GHGG-185-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006829; P:zinc II ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00548; ZupT; 1. DR InterPro; IPR003689; ZIP. DR InterPro; IPR023498; Zn_transptr_ZupT. DR Pfam; PF02535; Zip; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; KW Zinc; Zinc transport. FT CHAIN 1 269 Zinc transporter ZupT. FT /FTId=PRO_0000207275. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. SQ SEQUENCE 269 AA; 28425 MW; C301DBD7E1923FF9 CRC64; MPDFSMSNLA VAFSITLAAG LFTVLGSGLV MFSKTPNPRV LSFGLAFAGG AMVYVSLTEI FSKSSEAFAE IYDKDHAFAA ATMAFLAGMG GIALIDRLVP NPHETLDAQD PSFQESKRRH IARVGMMAAF AITAHNFPEG LATFFATLEN PAVGMPLALA IAIHNIPEGI SIAAPVYFAT RSRKKTVWAC LLSGLAEPLG AALGYLVLQP FLSPAVFGSV FGVIAGVMVF LALDELLPAA KRYSDGHETV YGLTTGMAVI AVSLVLFHF // ID YQGF_NEIMB Reviewed; 151 AA. AC Q9JZ16; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 86. DE RecName: Full=Putative pre-16S rRNA nuclease {ECO:0000255|HAMAP-Rule:MF_00651}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00651}; GN OrderedLocusNames=NMB1337; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Could be a nuclease involved in processing of the 5'-end CC of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}. CC -!- SIMILARITY: Belongs to the YqgF nuclease family. CC {ECO:0000255|HAMAP-Rule:MF_00651}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41712.1; -; Genomic_DNA. DR PIR; A81094; A81094. DR RefSeq; NP_274356.1; NC_003112.2. DR RefSeq; WP_002213272.1; NC_003112.2. DR ProteinModelPortal; Q9JZ16; -. DR STRING; 122586.NMB1337; -. DR PaxDb; Q9JZ16; -. DR EnsemblBacteria; AAF41712; AAF41712; NMB1337. DR GeneID; 903759; -. DR KEGG; nme:NMB1337; -. DR PATRIC; 20358329; VBINeiMen85645_1676. DR eggNOG; ENOG4107Y66; Bacteria. DR eggNOG; COG0816; LUCA. DR HOGENOM; HOG000016954; -. DR KO; K07447; -. DR OMA; LYEEWQP; -. DR OrthoDB; EOG6N94FV; -. DR BioCyc; NMEN122586:GHGG-1375-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000967; P:rRNA 5'-end processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.140; -; 1. DR HAMAP; MF_00651; Nuclease_YqgF; 1. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR005227; YqgF. DR InterPro; IPR006641; YqgF/RNaseH-like_dom. DR Pfam; PF03652; RuvX; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00250; RNAse_H_YqgF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Nuclease; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 151 Putative pre-16S rRNA nuclease. FT /FTId=PRO_0000172104. SQ SEQUENCE 151 AA; 16600 MW; 087E2DD332D6D472 CRC64; MHKIPKGTAL AFDFGEARIG VAQGDAELGL SHPLSTVTGG SNDEKFAAIA KLVQEWQPRY FVVGLPVHTD GTKHEMTHLS RKFGRRLNGR FNLPVYWVDE RLSSVYAESL LSEAQVFGKK RKSVLDQVAA QAILHGFFEG GPAECFNGRE G // ID Q9JRU7_NEIMB Unreviewed; 428 AA. AC Q9JRU7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|SAAS:SAAS00056000}; DE EC=2.7.7.4 {ECO:0000256|SAAS:SAAS00055979}; GN Name=cysN-2 {ECO:0000313|EMBL:AAF41574.1}; GN Synonyms=cysN-1 {ECO:0000313|EMBL:AAF41539.1}; GN OrderedLocusNames=NMB1153 {ECO:0000313|EMBL:AAF41539.1}, GN NMB1191 {ECO:0000313|EMBL:AAF41574.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41574.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41574.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41574.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41574.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41574.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity. CC {ECO:0000256|SAAS:SAAS00055961}. CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl CC sulfate. {ECO:0000256|SAAS:SAAS00056008}. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 1/3. {ECO:0000256|SAAS:SAAS00056006}. CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CC CysN. {ECO:0000256|SAAS:SAAS00055953}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. CysN/NodQ CC subfamily. {ECO:0000256|SAAS:SAAS00558207}. CC -!- SIMILARITY: Contains tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|SAAS:SAAS00055944}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41539.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41574.1; -; Genomic_DNA. DR PIR; A81111; A81111. DR RefSeq; NP_274181.1; NC_003112.2. DR RefSeq; NP_274217.1; NC_003112.2. DR RefSeq; WP_002225213.1; NC_003112.2. DR STRING; 122586.NMB1191; -. DR EnsemblBacteria; AAF41539; AAF41539; NMB1153. DR EnsemblBacteria; AAF41574; AAF41574; NMB1191. DR GeneID; 903574; -. DR GeneID; 903611; -. DR KEGG; nme:NMB1153; -. DR KEGG; nme:NMB1191; -. DR PATRIC; 20357885; VBINeiMen85645_1458. DR eggNOG; ENOG4105C3T; Bacteria. DR eggNOG; COG2895; LUCA. DR HOGENOM; HOG000229289; -. DR KO; K00956; -. DR OMA; GYMGRVE; -. DR OrthoDB; EOG6GR38Q; -. DR BioCyc; NMEN122586:GHGG-1189-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1226-MONOMER; -. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011779; SO4_adenylTrfase_lsu. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02034; CysN; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00444459}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW GTP-binding {ECO:0000256|RuleBase:RU000323, KW ECO:0000256|SAAS:SAAS00444415}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000323, KW ECO:0000256|SAAS:SAAS00444415, ECO:0000256|SAAS:SAAS00444459}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00444405, KW ECO:0000313|EMBL:AAF41574.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00444405, KW ECO:0000313|EMBL:AAF41574.1}. FT DOMAIN 6 226 Tr-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51722}. SQ SEQUENCE 428 AA; 46839 MW; DDD2431D9E7D2790 CRC64; MTAQHQTPLR FITAGSVDDG KSTLIGRLLY DSKALLSDQI KTLESGKSKG LKEAIDFSIL TDGLEAEREQ GITIDVAYRY FSTAKRKFII ADTPGHEQYT RNMVTGASTA SAAVVLVDAS QLDFGAQPLQ LLPQTKRHSA ILRQLNCPHI VVAVNKMDLL DYSEDKFNAI VEAYRRLAEQ LGLKDAHFVP MSALLGDNIV YPGGNMPWYK GEPLLSILET LPGADEVSRT ADDFYFPVQL VVRQDADKAD DFRGYQGRIE RGSVAVGQTV RIEPNGLTAE VSEIITPKGE VAQAFAGEAA TLRLDRDIDV SRGDLFVDKN SPLAPQKHLE ATLCWFDERP LNTARKYLLK HGTQTVPAKV GEIESVLDVR TLEQEAGAES LKMNDIAKVR INLQKPVTAT PYAENTAAGS FILIDEATYG TVAAGMIL // ID Q9JS34_NEIMB Unreviewed; 307 AA. AC Q9JS34; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|SAAS:SAAS00055732}; DE EC=2.7.7.4 {ECO:0000256|SAAS:SAAS00055732}; GN Name=cysD-2 {ECO:0000313|EMBL:AAF41575.1}; GN Synonyms=cysD-1 {ECO:0000313|EMBL:AAF41540.1}; GN OrderedLocusNames=NMB1154 {ECO:0000313|EMBL:AAF41540.1}, GN NMB1192 {ECO:0000313|EMBL:AAF41575.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41575.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41575.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41575.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41575.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41575.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl CC sulfate. {ECO:0000256|SAAS:SAAS00055726}. CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily. CC {ECO:0000256|SAAS:SAAS00558169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41540.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41575.1; -; Genomic_DNA. DR PIR; B81111; B81111. DR RefSeq; NP_274182.1; NC_003112.2. DR RefSeq; NP_274218.1; NC_003112.2. DR RefSeq; WP_002213549.1; NC_003112.2. DR STRING; 122586.NMB1192; -. DR EnsemblBacteria; AAF41540; AAF41540; NMB1154. DR EnsemblBacteria; AAF41575; AAF41575; NMB1192. DR GeneID; 903575; -. DR GeneID; 903612; -. DR KEGG; nme:NMB1154; -. DR KEGG; nme:NMB1192; -. DR PATRIC; 20357887; VBINeiMen85645_1459. DR eggNOG; ENOG4105C11; Bacteria. DR eggNOG; COG0175; LUCA. DR HOGENOM; HOG000263604; -. DR KO; K00957; -. DR OMA; LPSIYYT; -. DR OrthoDB; EOG6W45TZ; -. DR BioCyc; NMEN122586:GHGG-1190-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1227-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0019419; P:sulfate reduction; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 2. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011784; SO4_adenylTrfase_ssu. DR Pfam; PF01507; PAPS_reduct; 1. DR PIRSF; PIRSF002936; CysDAde_trans; 1. DR TIGRFAMs; TIGR02039; CysD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00444385}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00444385}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00444398, KW ECO:0000313|EMBL:AAF41575.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00444398, KW ECO:0000313|EMBL:AAF41575.1}. FT DOMAIN 31 260 PAPS_reduct. {ECO:0000259|Pfam:PF01507}. SQ SEQUENCE 307 AA; 34696 MW; 4BFF5DB3861D0FD3 CRC64; MTKTEPNNAQ LDWLESESIH IIREVAAECE NPALLFSGGK DSVVLLALAC KAFRLGSRPV KLPFPLVHID TGHNYPEVIA FRDAQAAKLN ARLIVGRVED SIAKGTVVLR KETDSRNAAQ AVTLLETIEA NGFDALMGGA RRDEEKARAK ERIFSFRDEF GQWDPKAQRP ELWSLYNTRL HKGENMRVFP ISNWTELDIW QYIARENLEL PPIYYSHRRE VVRRRGLLVP VTPLTPKMPS ETSEILDVRF RTVGDISCTC PVESTASTPT EIIRETAVAD ISERSATRLD DQASEAAMEK RKKEGYF // ID Q9JRY8_NEIMB Unreviewed; 218 AA. AC Q9JRY8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Nickel-dependent hydrogenase, b-type cytochrome subunit {ECO:0000313|EMBL:AAF41579.1}; GN OrderedLocusNames=NMB1158 {ECO:0000313|EMBL:AAF41544.1}, GN NMB1196 {ECO:0000313|EMBL:AAF41579.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41579.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41579.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41579.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41579.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41579.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41544.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41579.1; -; Genomic_DNA. DR PIR; F81111; F81111. DR RefSeq; NP_274186.1; NC_003112.2. DR RefSeq; NP_274222.1; NC_003112.2. DR RefSeq; WP_002225210.1; NC_003112.2. DR STRING; 122586.NMB1196; -. DR EnsemblBacteria; AAF41544; AAF41544; NMB1158. DR EnsemblBacteria; AAF41579; AAF41579; NMB1196. DR GeneID; 903579; -. DR GeneID; 903616; -. DR KEGG; nme:NMB1158; -. DR KEGG; nme:NMB1196; -. DR PATRIC; 20357895; VBINeiMen85645_1463. DR eggNOG; ENOG410909C; Bacteria. DR eggNOG; COG3658; LUCA. DR HOGENOM; HOG000271303; -. DR OMA; RWSRFAS; -. DR OrthoDB; EOG6WMHZQ; -. DR BioCyc; NMEN122586:GHGG-1194-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1231-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF01292; Ni_hydr_CYTB; 1. DR SUPFAM; SSF81342; SSF81342; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 217 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 218 AA; 24021 MW; A1CFCCB7494B1563 CRC64; MKNKTKVWDL PTRLFHWLLA ASLPFMWYSA KAGGDMLQWH TRVGLFVLFL LVFRLCWGIW GSDTARFSRF VQGWAGIRGY LKNGIPEHIQ PGHNPLGALM VVALLAAVSF QVGTGLFAAD ENTFSTNGYL NHLVSEHTGS LMRKIHLNFF KLLAVFSAIH IAAVAAYRVF KKKNLILPMI TGFKYIEGKT SIRFAGKAAL AAALSVASLA AAAILLLS // ID Q9JRV6_NEIMB Unreviewed; 124 AA. AC Q9JRV6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42113.1}; GN OrderedLocusNames=NMB0501 {ECO:0000313|EMBL:AAF40933.1}, GN NMB1773 {ECO:0000313|EMBL:AAF42113.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42113.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42113.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42113.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF42113.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42113.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40933.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42113.1; -; Genomic_DNA. DR PIR; D81190; D81190. DR RefSeq; NP_273547.1; NC_003112.2. DR RefSeq; NP_274773.1; NC_003112.2. DR RefSeq; WP_002224016.1; NC_003112.2. DR STRING; 122586.NMB1773; -. DR EnsemblBacteria; AAF40933; AAF40933; NMB0501. DR EnsemblBacteria; AAF42113; AAF42113; NMB1773. DR GeneID; 902617; -. DR GeneID; 903326; -. DR KEGG; nme:NMB0501; -. DR KEGG; nme:NMB1773; -. DR PATRIC; 20356252; VBINeiMen85645_0646. DR HOGENOM; HOG000027879; -. DR OMA; EMELFQK; -. DR OrthoDB; EOG6716WJ; -. DR BioCyc; NMEN122586:GHGG-1828-MONOMER; -. DR BioCyc; NMEN122586:GHGG-526-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 124 AA; 14756 MW; D0E83AA4E41F2F11 CRC64; MKNFNVVKES LRELGIKQGF DLYEKATTEK LNSEDPLDLQ WLSNYSSDWN DELEEDFDSF FQHMKEYQYA IDNEDIKSAC SSLCEAMLYV GNIKNFFEFL KSDMIRLLRG ESKTTDFQWP QFDE // ID Q7DDP6_NEIMB Unreviewed; 131 AA. AC Q7DDP6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=TspB-related protein {ECO:0000313|EMBL:AAF40917.1}; GN OrderedLocusNames=NMB0480 {ECO:0000313|EMBL:AAF40917.1}, GN NMB0976 {ECO:0000313|EMBL:AAF41380.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40917.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40917.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40917.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF40917.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40917.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40917.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41380.1; -; Genomic_DNA. DR PIR; A81137; A81137. DR RefSeq; NP_273527.1; NC_003112.2. DR RefSeq; NP_274013.1; NC_003112.2. DR RefSeq; WP_002225310.1; NC_003112.2. DR STRING; 122586.NMB0976; -. DR EnsemblBacteria; AAF40917; AAF40917; NMB0480. DR EnsemblBacteria; AAF41380; AAF41380; NMB0976. DR GeneID; 902597; -. DR GeneID; 903096; -. DR KEGG; nme:NMB0480; -. DR KEGG; nme:NMB0976; -. DR PATRIC; 20356216; VBINeiMen85645_0628. DR HOGENOM; HOG000218903; -. DR OMA; VIKYTNL; -. DR OrthoDB; EOG6RFZZX; -. DR BioCyc; NMEN122586:GHGG-1013-MONOMER; -. DR BioCyc; NMEN122586:GHGG-505-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008708; Neisseria_TspB. DR Pfam; PF05616; Neisseria_TspB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 131 AA; 14070 MW; 6191EC4F7E340D16 CRC64; MMYSFEANAN AVKISETVSV DTGQGAKIHK FVPKNSKTYS SDLIKTVDLT HIPTGAKARI NAKITASVSR AGVLAGVGKL ARLGAKFSTR AVPYVGTALL AHDVYETFKE DIQARGYQYD PETDKFAKVS G // ID Q9JRV5_NEIMB Unreviewed; 437 AA. AC Q9JRV5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41551.1}; GN OrderedLocusNames=NMB1128 {ECO:0000313|EMBL:AAF41516.1}, GN NMB1166 {ECO:0000313|EMBL:AAF41551.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41551.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41551.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41551.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41551.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41516.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41551.1; -; Genomic_DNA. DR PIR; G81117; G81117. DR RefSeq; NP_274157.1; NC_003112.2. DR RefSeq; NP_274193.1; NC_003112.2. DR RefSeq; WP_002225226.1; NC_003112.2. DR STRING; 122586.NMB1166; -. DR EnsemblBacteria; AAF41516; AAF41516; NMB1128. DR EnsemblBacteria; AAF41551; AAF41551; NMB1166. DR GeneID; 903549; -. DR GeneID; 903586; -. DR KEGG; nme:NMB1128; -. DR KEGG; nme:NMB1166; -. DR PATRIC; 20357831; VBINeiMen85645_1431. DR eggNOG; ENOG4107S11; Bacteria. DR eggNOG; COG2907; LUCA. DR HOGENOM; HOG000220835; -. DR KO; K06954; -. DR OMA; DNGNHLL; -. DR OrthoDB; EOG664CCP; -. DR BioCyc; NMEN122586:GHGG-1164-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1201-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR017830; Squal-assoc_FAD-dep_deSatase. DR Pfam; PF01593; Amino_oxidase; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR03467; HpnE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 429 Amino_oxidase. FT {ECO:0000259|Pfam:PF01593}. SQ SEQUENCE 437 AA; 47115 MW; D0F24E6941ED3BF4 CRC64; MMNTPHPRPK IAVIGAGWAG LSAAVTLARH ADVTLFEAGR QAGGRARTLA GNTDGFGFLD NGQHILLGAY RGVLRLMKTI GSDPRAAFLR VPLHWHMHGG LQFRALPLPA PLHILGGVLL ARRAPTAFKA KLLADMSDLQ KSARLGQPDT TVAQWLKQRN VPRAAVMQFW QPLVWGALNT PLETASLRVL CNVLSDGVLT KKSGSDYLLP KQDLGAIVAE PALADLQRLG ADIRLETRVC RLNTLPDGKV LVNGEAFDAA VPATAPYHAA ALLPEGTPEH VQTAYQNLRY HAITTVYLRY AEPVRLPAPL TGLADGTVQW LLCRGRLGLP ENEVSAVISV SDRVGAFANR AWADKAHADL KRILPHLGEP EAVRVITEKR ATTAADAPPP DLSWLHRHRI FPAGDYLHPD YPATLEAAVQ SGFASAEACL QSLSDAV // ID Q9JRT9_NEIMB Unreviewed; 318 AA. AC Q9JRT9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Pilin gene inverting protein PivNM-1A {ECO:0000313|EMBL:AAF41907.1}; DE SubName: Full=Pilin gene inverting protein PivNM-1B {ECO:0000313|EMBL:AAF41976.1}; GN Name=pivNM-1B {ECO:0000313|EMBL:AAF41976.1}; GN Synonyms=pivNM-1A {ECO:0000313|EMBL:AAF41907.1}; GN OrderedLocusNames=NMB1552 {ECO:0000313|EMBL:AAF41907.1}, GN NMB1625 {ECO:0000313|EMBL:AAF41976.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41976.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41976.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41976.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41976.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41907.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41976.1; -; Genomic_DNA. DR PIR; E81070; E81070. DR RefSeq; NP_274559.1; NC_003112.2. DR RefSeq; NP_274631.1; NC_003112.2. DR RefSeq; WP_002222496.1; NC_003112.2. DR STRING; 122586.NMB1625; -. DR EnsemblBacteria; AAF41907; AAF41907; NMB1552. DR EnsemblBacteria; AAF41976; AAF41976; NMB1625. DR GeneID; 904033; -. DR GeneID; 904103; -. DR KEGG; nme:NMB1552; -. DR KEGG; nme:NMB1625; -. DR PATRIC; 20358938; VBINeiMen85645_1983. DR eggNOG; ENOG4108QQA; Bacteria. DR eggNOG; COG3547; LUCA. DR HOGENOM; HOG000130878; -. DR KO; K07486; -. DR OMA; KERTAFK; -. DR OrthoDB; EOG62VNHT; -. DR BioCyc; NMEN122586:GHGG-1593-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1674-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR003346; Transposase_20. DR InterPro; IPR002525; Transposase_N. DR Pfam; PF01548; DEDD_Tnp_IS110; 1. DR Pfam; PF02371; Transposase_20; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 149 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. SQ SEQUENCE 318 AA; 36863 MW; EB1717E0B1E80B23 CRC64; MNIIGLDISK DTIDATLHKT NGSIHYIKFK NNDDGLKQFR LWIKGNRIRK VYIGMEATGI YYEKAADMLS SYYTVYVINP LKIKDYGKSR FNRTKTDKAD SNLIADYIKR HQDTLIPYQI PKNKALQKLI NLKNQLHQHQ KQIKNRLHST EEDFIRNIHQ DLIDTIQDKM EQVKIAISEQ IKKQTDNNHY RNLQTIPSIG KDTASVLYAQ LTEKHFKTAN QFVSYAGLNP AIIQSGTSVR GRGRLSRYGN RRLKSTLYMP ALCAYRFNAF PKLINNLKKA GKPKMVIIVA IMRKLAKLAY YIVKTGQPYD AERHRLNQ // ID Q9JRY6_NEIMB Unreviewed; 367 AA. AC Q9JRY6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41977.1}; GN OrderedLocusNames=NMB1551 {ECO:0000313|EMBL:AAF41906.1}, GN NMB1626 {ECO:0000313|EMBL:AAF41977.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41977.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41977.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41977.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41977.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000213|PDB:2R2A} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-196. RA Osipiuk J., Patterson S., Wu R., Clancy S., Joachimiak A.; RT "Crystal structure of N-terminal domain of zonular occludens toxin RT from Neisseria meningitidis."; RL Submitted (AUG-2007) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41906.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41977.1; -; Genomic_DNA. DR PIR; E81060; E81060. DR RefSeq; NP_274558.1; NC_003112.2. DR RefSeq; NP_274632.1; NC_003112.2. DR RefSeq; WP_002219059.1; NC_003112.2. DR PDB; 2R2A; X-ray; 1.82 A; A/B=1-196. DR PDBsum; 2R2A; -. DR STRING; 122586.NMB1626; -. DR EnsemblBacteria; AAF41906; AAF41906; NMB1551. DR EnsemblBacteria; AAF41977; AAF41977; NMB1626. DR GeneID; 904031; -. DR GeneID; 904101; -. DR KEGG; nme:NMB1551; -. DR KEGG; nme:NMB1626; -. DR PATRIC; 20358934; VBINeiMen85645_1981. DR eggNOG; ENOG4108UST; Bacteria. DR eggNOG; ENOG4111MTZ; LUCA. DR HOGENOM; HOG000218807; -. DR KO; K10954; -. DR OMA; KSAEVHT; -. DR OrthoDB; EOG6C8MWQ; -. DR BioCyc; NMEN122586:GHGG-1592-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1675-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008900; Zona_occludens_tox. DR Pfam; PF05707; Zot; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2R2A}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 224 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 12 16 Sulfate binding. {ECO:0000213|PDB:2R2A}. SQ SEQUENCE 367 AA; 41120 MW; A30432AA4A7C4807 CRC64; MAEICLITGT PGSGKTLKMV SMMANDEMFK PDENGIRRKV FTNIKGLKIP HTYIETDAKK LPKSTDEQLS AHDMYEWIKK PENIGSIVIV DEAQDVWPAR SAGSKIPENV QWLNTHRHQG IDIFVLTQGP KLLDQNLRTL VRKHYHIASN KMGMRTLLEW KICADDPVKM ASSAFSSIYT LDKKVYDLYE SAEVHTVNKV KRSKWFYTLP VIVLLIPVFV GLSYKMLSSY GKKQEEPAAQ ESAATEQQAV LPDKTEGEPV NNGNLTADMF VPTLSEKPES KPIYNGVRQV RTFEYIAGCI EGGRTGCACY SHQGTALKEV TELMCKDYVK NGLPFNPYKE ESQGQEVQQS AQQHSDRAQV ATLGGKP // ID Q9JRY5_NEIMB Unreviewed; 218 AA. AC Q9JRY5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41555.1}; GN OrderedLocusNames=NMB1132 {ECO:0000313|EMBL:AAF41520.1}, GN NMB1170 {ECO:0000313|EMBL:AAF41555.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41555.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41555.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41555.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41555.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41555.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41520.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41555.1; -; Genomic_DNA. DR PIR; C81118; C81118. DR RefSeq; NP_274161.1; NC_003112.2. DR RefSeq; NP_274197.1; NC_003112.2. DR RefSeq; WP_010980896.1; NC_003112.2. DR STRING; 122586.NMB1170; -. DR EnsemblBacteria; AAF41520; AAF41520; NMB1132. DR EnsemblBacteria; AAF41555; AAF41555; NMB1170. DR GeneID; 903553; -. DR GeneID; 903590; -. DR KEGG; nme:NMB1132; -. DR KEGG; nme:NMB1170; -. DR PATRIC; 20357839; VBINeiMen85645_1435. DR eggNOG; ENOG4108N02; Bacteria. DR eggNOG; ENOG4110WZH; LUCA. DR HOGENOM; HOG000218950; -. DR OMA; YLMKTVI; -. DR OrthoDB; EOG622PP9; -. DR BioCyc; NMEN122586:GHGG-1168-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1205-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018306; Phage_T5_Orf172_DNA-bd. DR Pfam; PF10544; T5orf172; 1. DR SMART; SM00974; T5orf172; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 12 93 T5orf172. {ECO:0000259|SMART:SM00974}. SQ SEQUENCE 218 AA; 24980 MW; A6C4683654A79381 CRC64; MEKSGIVYLM KTVIKGVYKI GISDVSNFEG RMRHLENNGY ANVAGLERIL AVKTDNYKEK ENLLHEIFSK SRIGDTELFA VDENLVKRLF LSLRGEIVFP KNETAESEFE KSVHERRQEG NAGSGRKQLL DLVRRGHREY PYALPRLLAG AAFYKPKKSK IRLFKEAYFG KSGTRLTDEI ADGIHIYTCF SRADLEKAYS EYLELFKSES DAEGRKPQ // ID Q9JRZ8_NEIMB Unreviewed; 203 AA. AC Q9JRZ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=RNA methyltransferase, TrmH family {ECO:0000313|EMBL:AAF41563.1}; GN OrderedLocusNames=NMB1141 {ECO:0000313|EMBL:AAF41528.1}, GN NMB1179 {ECO:0000313|EMBL:AAF41563.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41563.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41563.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41563.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41563.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41563.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41528.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41563.1; -; Genomic_DNA. DR PIR; D81116; D81116. DR RefSeq; NP_274169.2; NC_003112.2. DR RefSeq; NP_274205.2; NC_003112.2. DR STRING; 122586.NMB1179; -. DR EnsemblBacteria; AAF41528; AAF41528; NMB1141. DR EnsemblBacteria; AAF41563; AAF41563; NMB1179. DR GeneID; 903562; -. DR GeneID; 903599; -. DR KEGG; nme:NMB1141; -. DR KEGG; nme:NMB1179; -. DR PATRIC; 20357857; VBINeiMen85645_1444. DR eggNOG; ENOG4108RWN; Bacteria. DR eggNOG; COG0566; LUCA. DR HOGENOM; HOG000218799; -. DR KO; K03437; -. DR OMA; GCAHLWS; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; NMEN122586:GHGG-1177-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1214-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAF41563.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAF41563.1}. FT DOMAIN 56 194 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. SQ SEQUENCE 203 AA; 21482 MW; 913A10BE67455FE7 CRC64; MPSEEVRKLT AVLPEDGFFS VSDGILKKIS SLTCADDVLA LIDIPDAGAL PAGGDCVVLD GVQDPGNVGT VLRSAAAAGI GAVILGKGCA DAWSPKVLRA GMGAHFLSEI YPQADLEIWL VRYKGRVFAT ALREEKQAVL YGEDLCEPTA WVFGNEGAGV GKAVLDRADK CVRIPMHDAT ESLNVAMAAT ICLFEQMRQR AAY // ID Q9JRU2_NEIMB Unreviewed; 51 AA. AC Q9JRU2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41570.1}; GN OrderedLocusNames=NMB1148 {ECO:0000313|EMBL:AAF41535.1}, GN NMB1186 {ECO:0000313|EMBL:AAF41570.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41570.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41570.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41570.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41570.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41570.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41535.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41570.1; -; Genomic_DNA. DR PIR; C81117; C81117. DR STRING; 122586.NMB1186; -. DR EnsemblBacteria; AAF41535; AAF41535; NMB1148. DR EnsemblBacteria; AAF41570; AAF41570; NMB1186. DR PATRIC; 20357873; VBINeiMen85645_1452. DR OrthoDB; EOG6CZQWR; -. DR BioCyc; NMEN122586:GHGG-1184-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1221-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 51 AA; 5162 MW; E2441E272E45C620 CRC64; MSPTPIMETV SAVFSSGASC PSTSPVFETG AGFEPSIGST GIPFRQDAPR A // ID Q9JS19_NEIMB Unreviewed; 94 AA. AC Q9JS19; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62310.1}; GN OrderedLocusNames=NMB0483 {ECO:0000313|EMBL:AAF62310.1}, GN NMB0973 {ECO:0000313|EMBL:AAF41377.1}, GN NMB1744 {ECO:0000313|EMBL:AAF42087.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62310.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62310.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62310.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF62310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62310.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41377.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42087.1; -; Genomic_DNA. DR EMBL; AE002098; AAF62310.1; -; Genomic_DNA. DR PIR; G81047; G81047. DR RefSeq; NP_273530.1; NC_003112.2. DR RefSeq; NP_274010.1; NC_003112.2. DR RefSeq; NP_274745.1; NC_003112.2. DR RefSeq; WP_002222080.1; NC_003112.2. DR STRING; 122586.NMB1744; -. DR EnsemblBacteria; AAF41377; AAF41377; NMB0973. DR EnsemblBacteria; AAF42087; AAF42087; NMB1744. DR EnsemblBacteria; AAF62310; AAF62310; NMB0483. DR GeneID; 902600; -. DR GeneID; 903093; -. DR GeneID; 903353; -. DR KEGG; nme:NMB0483; -. DR KEGG; nme:NMB0973; -. DR KEGG; nme:NMB1744; -. DR HOGENOM; HOG000218812; -. DR OrthoDB; EOG6X112N; -. DR BioCyc; NMEN122586:GHGG-1010-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1799-MONOMER; -. DR BioCyc; NMEN122586:GHGG-508-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 89 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 94 AA; 10033 MW; 5F02CE31563903F3 CRC64; MFGGRLKNAP SITAKHFLKE NIMKFINTCR KYGAKLAVVT AAPLALAAHA NATLPDTAKN ALEAAKADGM EAGWIVVGIF AALFVFSIVK RVMK // ID Q9JRT4_NEIMB Unreviewed; 94 AA. AC Q9JRT4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41978.1}; GN OrderedLocusNames=NMB1550 {ECO:0000313|EMBL:AAF41905.1}, GN NMB1627 {ECO:0000313|EMBL:AAF41978.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41978.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41978.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41978.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41978.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41978.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41905.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41978.1; -; Genomic_DNA. DR PIR; F81060; F81060. DR RefSeq; NP_274557.1; NC_003112.2. DR RefSeq; NP_274633.1; NC_003112.2. DR RefSeq; WP_002222494.1; NC_003112.2. DR STRING; 122586.NMB1627; -. DR EnsemblBacteria; AAF41905; AAF41905; NMB1550. DR EnsemblBacteria; AAF41978; AAF41978; NMB1627. DR GeneID; 904011; -. DR GeneID; 904099; -. DR KEGG; nme:NMB1550; -. DR KEGG; nme:NMB1627; -. DR PATRIC; 20358932; VBINeiMen85645_1980. DR HOGENOM; HOG000219042; -. DR OrthoDB; EOG6J1DHC; -. DR BioCyc; NMEN122586:GHGG-1591-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1676-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019670; DUF2523. DR Pfam; PF10734; DUF2523; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 80 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 94 AA; 9941 MW; F5280D82E026EC5B CRC64; MKLLAALIPL LMSVAGRILT ALGLMAVTYS GVDRLVAHFQ QAITNSITGA PQAMLQLFYI SGGGTVLNIL FGAIAFILSF KQMTKLATSI GKKK // ID Q7DDG2_NEIMB Unreviewed; 78 AA. AC Q7DDG2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41529.1}; GN OrderedLocusNames=NMB1142 {ECO:0000313|EMBL:AAF41529.1}, GN NMB1180 {ECO:0000313|EMBL:AAF41564.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41529.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41529.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41529.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41529.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41529.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41529.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41564.1; -; Genomic_DNA. DR PIR; E81116; E81116. DR STRING; 122586.NMB1180; -. DR EnsemblBacteria; AAF41529; AAF41529; NMB1142. DR EnsemblBacteria; AAF41564; AAF41564; NMB1180. DR PATRIC; 20357861; VBINeiMen85645_1446. DR HOGENOM; HOG000218953; -. DR OrthoDB; EOG6ZH2NK; -. DR BioCyc; NMEN122586:GHGG-1178-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1215-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 78 AA; 8404 MW; 0405A8FDDE92D7CA CRC64; MYRFYAAVAV FLCGCFEAQE GGIAEGRAVE THLIVQCRGG GGFGLGVVEM VLTDIAQNRA NGIRTNKEFG KKFVKSTN // ID Q9JRX0_NEIMB Unreviewed; 52 AA. AC Q9JRX0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41578.1}; GN OrderedLocusNames=NMB1157 {ECO:0000313|EMBL:AAF41543.1}, GN NMB1195 {ECO:0000313|EMBL:AAF41578.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41578.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41578.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41578.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41578.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41578.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41543.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41578.1; -; Genomic_DNA. DR PIR; E81111; E81111. DR STRING; 122586.NMB1195; -. DR EnsemblBacteria; AAF41543; AAF41543; NMB1157. DR EnsemblBacteria; AAF41578; AAF41578; NMB1195. DR PATRIC; 20357893; VBINeiMen85645_1462. DR BioCyc; NMEN122586:GHGG-1193-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1230-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 52 AA; 6162 MW; BD5857FF839EDBD5 CRC64; MPSEALFALR TASPHHANGL NARNGFRPFF FRNRYKTENR RIRSRPHIAF SF // ID Q7DDP4_NEIMB Unreviewed; 92 AA. AC Q7DDP4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40919.1}; GN OrderedLocusNames=NMB0482 {ECO:0000313|EMBL:AAF40919.1}, GN NMB0974 {ECO:0000313|EMBL:AAF41378.1}, GN NMB1745 {ECO:0000313|EMBL:AAF42088.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40919.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40919.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40919.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF40919.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40919.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40919.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41378.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42088.1; -; Genomic_DNA. DR PIR; H81192; H81192. DR RefSeq; NP_273529.1; NC_003112.2. DR RefSeq; NP_274011.1; NC_003112.2. DR RefSeq; NP_274746.1; NC_003112.2. DR RefSeq; WP_002215768.1; NC_003112.2. DR STRING; 122586.NMB1745; -. DR EnsemblBacteria; AAF40919; AAF40919; NMB0482. DR EnsemblBacteria; AAF41378; AAF41378; NMB0974. DR EnsemblBacteria; AAF42088; AAF42088; NMB1745. DR GeneID; 902599; -. DR GeneID; 903094; -. DR GeneID; 903352; -. DR KEGG; nme:NMB0482; -. DR KEGG; nme:NMB0974; -. DR KEGG; nme:NMB1745; -. DR HOGENOM; HOG000218811; -. DR OMA; CWCRRIA; -. DR OrthoDB; EOG6Z3KNP; -. DR BioCyc; NMEN122586:GHGG-1011-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1800-MONOMER; -. DR BioCyc; NMEN122586:GHGG-507-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 87 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 92 AA; 10505 MW; 277AF2A40219AD31 CRC64; MYYQVGNKCL EKHQAENLYF SLVVPRIKEN GQIVRPEYNG SLWKMSDGQP LRLLLAECSP KDNLQSGLET GWIVFGILAS VYFVSLLKKV LK // ID Q9JS68_NEIMB Unreviewed; 65 AA. AC Q9JS68; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41546.1}; GN OrderedLocusNames=NMB1123 {ECO:0000313|EMBL:AAF41511.1}, GN NMB1161 {ECO:0000313|EMBL:AAF41546.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41546.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41546.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41546.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41546.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41546.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41511.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41546.1; -; Genomic_DNA. DR PIR; C81120; C81120. DR STRING; 122586.NMB1161; -. DR EnsemblBacteria; AAF41511; AAF41511; NMB1123. DR EnsemblBacteria; AAF41546; AAF41546; NMB1161. DR PATRIC; 20357819; VBINeiMen85645_1425. DR HOGENOM; HOG000071284; -. DR OrthoDB; EOG68SW4N; -. DR BioCyc; NMEN122586:GHGG-1159-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1196-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7704 MW; 03BB0E85B970F04E CRC64; MRILILASRT AQNRAAGFNI RTRFGFCILQ NPNLLFKFKL NSGVVVWYSG LTKIRTRRRS RRQYK // ID Q9JS30_NEIMB Unreviewed; 103 AA. AC Q9JS30; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41983.1}; GN OrderedLocusNames=NMB1544 {ECO:0000313|EMBL:AAF41899.1}, GN NMB1633 {ECO:0000313|EMBL:AAF41983.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41983.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41983.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41983.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41983.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41983.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41899.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41983.1; -; Genomic_DNA. DR PIR; C81061; C81061. DR RefSeq; NP_274551.1; NC_003112.2. DR RefSeq; NP_274639.1; NC_003112.2. DR RefSeq; WP_002212531.1; NC_003112.2. DR STRING; 122586.NMB1633; -. DR EnsemblBacteria; AAF41899; AAF41899; NMB1544. DR EnsemblBacteria; AAF41983; AAF41983; NMB1633. DR GeneID; 903971; -. DR GeneID; 904085; -. DR KEGG; nme:NMB1544; -. DR KEGG; nme:NMB1633; -. DR PATRIC; 20358922; VBINeiMen85645_1975. DR HOGENOM; HOG000218819; -. DR OrthoDB; EOG6JDWGV; -. DR BioCyc; NMEN122586:GHGG-1585-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1682-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 103 AA; 11032 MW; 4ED8E3B8BF45B164 CRC64; MFNQTQTVTY PATFLGAKKF KGEIDGSNID TCSVLVATPL PAQSGNAVGF TAAQMKFGDS KNFSKLENLK YPCEVMVTVE MTSTGKGMVP SLIDFQVAEK PKG // ID Q9JS69_NEIMB Unreviewed; 121 AA. AC Q9JS69; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41565.1}; GN OrderedLocusNames=NMB1143 {ECO:0000313|EMBL:AAF41530.1}, GN NMB1181 {ECO:0000313|EMBL:AAF41565.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41565.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41565.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41565.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41565.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41565.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41530.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41565.1; -; Genomic_DNA. DR PIR; F81116; F81116. DR RefSeq; NP_274171.1; NC_003112.2. DR RefSeq; NP_274207.1; NC_003112.2. DR RefSeq; WP_002222466.1; NC_003112.2. DR STRING; 122586.NMB1181; -. DR EnsemblBacteria; AAF41530; AAF41530; NMB1143. DR EnsemblBacteria; AAF41565; AAF41565; NMB1181. DR GeneID; 903564; -. DR GeneID; 903601; -. DR KEGG; nme:NMB1143; -. DR KEGG; nme:NMB1181; -. DR PATRIC; 20357863; VBINeiMen85645_1447. DR HOGENOM; HOG000218954; -. DR OMA; KNCKFFY; -. DR OrthoDB; EOG610446; -. DR BioCyc; NMEN122586:GHGG-1179-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1216-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 121 AA; 14532 MW; 0245A18BE67180A7 CRC64; MWGRYEKLRI FYDPTRAIYD SGADYLTREK HRLVVIANSA WGLLLNLSCY YDEVLEKRKI PFGKQEIDDD MDKVSALKRK FKDISEIKVG DGWEYPFNYE QGMKELDEVL LKYIPFFEEE R // ID Q9JRU5_NEIMB Unreviewed; 66 AA. AC Q9JRU5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41982.1}; GN OrderedLocusNames=NMB1545 {ECO:0000313|EMBL:AAF41900.1}, GN NMB1632 {ECO:0000313|EMBL:AAF41982.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41982.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41982.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41982.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41982.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41982.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41900.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41982.1; -; Genomic_DNA. DR PIR; B81061; B81061. DR RefSeq; NP_274552.1; NC_003112.2. DR RefSeq; NP_274638.1; NC_003112.2. DR RefSeq; WP_002212530.1; NC_003112.2. DR STRING; 122586.NMB1632; -. DR EnsemblBacteria; AAF41900; AAF41900; NMB1545. DR EnsemblBacteria; AAF41982; AAF41982; NMB1632. DR GeneID; 903972; -. DR GeneID; 904086; -. DR KEGG; nme:NMB1545; -. DR KEGG; nme:NMB1632; -. DR PATRIC; 20358924; VBINeiMen85645_1976. DR HOGENOM; HOG000218818; -. DR OrthoDB; EOG6K405M; -. DR BioCyc; NMEN122586:GHGG-1586-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1681-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 66 AA; 7576 MW; E1C199083EBF7F5B CRC64; MKFEERFIVQ DLETHDFIYP DPFGDVGFTQ NIKSAGQFES YEDALNSGIN EIGGGFQIFQ FFVKSE // ID Q7DDG9_NEIMB Unreviewed; 113 AA. AC Q7DDG9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 91. DE SubName: Full=Ferredoxin, 2Fe-2S type {ECO:0000313|EMBL:AAF41522.1}; GN Name=fdx-1 {ECO:0000313|EMBL:AAF41522.1}; GN Synonyms=fdx-2 {ECO:0000313|EMBL:AAF41557.1}; GN OrderedLocusNames=NMB1134 {ECO:0000313|EMBL:AAF41522.1}, GN NMB1172 {ECO:0000313|EMBL:AAF41557.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41522.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41522.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41522.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41522.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41522.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41522.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41557.1; -; Genomic_DNA. DR PIR; E81118; E81118. DR RefSeq; NP_274163.1; NC_003112.2. DR RefSeq; NP_274199.1; NC_003112.2. DR RefSeq; WP_002217209.1; NC_003112.2. DR SMR; Q7DDG9; 2-111. DR STRING; 122586.NMB1172; -. DR EnsemblBacteria; AAF41522; AAF41522; NMB1134. DR EnsemblBacteria; AAF41557; AAF41557; NMB1172. DR GeneID; 903555; -. DR GeneID; 903592; -. DR KEGG; nme:NMB1134; -. DR KEGG; nme:NMB1172; -. DR PATRIC; 20357843; VBINeiMen85645_1437. DR eggNOG; ENOG4108ZIT; Bacteria. DR eggNOG; COG0633; LUCA. DR HOGENOM; HOG000244519; -. DR KO; K04755; -. DR OMA; SACGGVC; -. DR OrthoDB; EOG6KMB9X; -. DR BioCyc; NMEN122586:GHGG-1170-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1207-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR001055; Adrenodoxin. DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR011536; Fdx_isc. DR Pfam; PF00111; Fer2; 1. DR PRINTS; PR00355; ADRENODOXIN. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR02007; fdx_isc; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00814; ADX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU000391}; KW Iron-sulfur {ECO:0000256|RuleBase:RU000391}; KW Metal-binding {ECO:0000256|RuleBase:RU000391}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 105 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. SQ SEQUENCE 113 AA; 12460 MW; C9383A1FDB2D0E77 CRC64; MPKITVLPHT TLCPEGAVID NAPEGKTVLD VLLDHDIEVD HACEKSCACT TCHVIIRKGF DSLEEPTELE EDLLDQAWGL EADSRLSCQA VVAGEDLIVE IPKYTINHAR EEH // ID Q7DDH5_NEIMB Unreviewed; 123 AA. AC Q7DDH5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41513.1}; GN OrderedLocusNames=NMB1125 {ECO:0000313|EMBL:AAF41513.1}, GN NMB1163 {ECO:0000313|EMBL:AAF41548.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41513.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41513.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41513.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41513.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41513.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41513.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41548.1; -; Genomic_DNA. DR PIR; E81120; E81120. DR RefSeq; NP_274154.1; NC_003112.2. DR RefSeq; NP_274190.1; NC_003112.2. DR RefSeq; WP_002213579.1; NC_003112.2. DR STRING; 122586.NMB1163; -. DR EnsemblBacteria; AAF41513; AAF41513; NMB1125. DR EnsemblBacteria; AAF41548; AAF41548; NMB1163. DR GeneID; 903546; -. DR GeneID; 903583; -. DR KEGG; nme:NMB1125; -. DR KEGG; nme:NMB1163; -. DR PATRIC; 20357823; VBINeiMen85645_1427. DR eggNOG; ENOG4105Y0J; Bacteria. DR eggNOG; COG4259; LUCA. DR HOGENOM; HOG000265554; -. DR OMA; YQYYQQD; -. DR OrthoDB; EOG6Q8J49; -. DR BioCyc; NMEN122586:GHGG-1161-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1198-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014508; UCP020555_TPR-like. DR Pfam; PF16068; DUF4810; 1. DR PIRSF; PIRSF020555; UCP020555; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 123 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006747853. SQ SEQUENCE 123 AA; 13496 MW; 9813BF15B8EDF40A CRC64; MMNPKTLSRL SLCAAVLALT ACGGNGQKSL YYYGGYPDTV YEGLKNDDTS LGKQTEKMEK YFVEAGNKKM NAAPGAHAHL GLLLSRSGDK EGAFRQFEEE KRLFPESGVF MDFLMKTGKG GKR // ID Q7DDG5_NEIMB Unreviewed; 133 AA. AC Q7DDG5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41526.1}; GN OrderedLocusNames=NMB1138 {ECO:0000313|EMBL:AAF41526.1}, GN NMB1176 {ECO:0000313|EMBL:AAF41561.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41526.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41526.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41526.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41526.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41526.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41526.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41561.1; -; Genomic_DNA. DR PIR; A81119; A81119. DR RefSeq; NP_274167.1; NC_003112.2. DR RefSeq; NP_274203.1; NC_003112.2. DR RefSeq; WP_002217207.1; NC_003112.2. DR STRING; 122586.NMB1176; -. DR EnsemblBacteria; AAF41526; AAF41526; NMB1138. DR EnsemblBacteria; AAF41561; AAF41561; NMB1176. DR GeneID; 903559; -. DR GeneID; 903596; -. DR KEGG; nme:NMB1138; -. DR KEGG; nme:NMB1176; -. DR PATRIC; 20357851; VBINeiMen85645_1441. DR eggNOG; ENOG4105VEJ; Bacteria. DR eggNOG; COG1188; LUCA. DR HOGENOM; HOG000216822; -. DR KO; K04762; -. DR OMA; RFYKTRT; -. DR OrthoDB; EOG64NB4B; -. DR BioCyc; NMEN122586:GHGG-1174-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1211-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:InterPro. DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro. DR GO; GO:0034605; P:cellular response to heat; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR025708; HSP15. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF01479; S4; 1. DR PIRSF; PIRSF016821; HSP15; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS50889; S4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 10 72 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 133 AA; 15591 MW; 7C4423C8166DE3FE CRC64; MKDKHDSSAM RLDKWLWAAR FFKTRSLAQK HIELGRVQVN GSKVKNSKTI DIGDIIDLTL NSLPYKIKVK GLNHQRRPAS EARLLYEEDA KTATLREERK QLDQFSRITS AYPDGRPTKR DRRQLDRLKK GDW // ID Q9JRW6_NEIMB Unreviewed; 321 AA. AC Q9JRW6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41637.1}; GN OrderedLocusNames=NMB1251 {ECO:0000313|EMBL:AAF41631.1}, GN NMB1259 {ECO:0000313|EMBL:AAF41637.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41637.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41637.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41637.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41637.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41637.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41631.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41637.1; -; Genomic_DNA. DR PIR; D81104; D81104. DR RefSeq; NP_274274.1; NC_003112.2. DR RefSeq; NP_274281.1; NC_003112.2. DR RefSeq; WP_002225187.1; NC_003112.2. DR EnsemblBacteria; AAF41631; AAF41631; NMB1251. DR EnsemblBacteria; AAF41637; AAF41637; NMB1259. DR GeneID; 903673; -. DR GeneID; 903681; -. DR KEGG; nme:NMB1251; -. DR KEGG; nme:NMB1259; -. DR PATRIC; 20358103; VBINeiMen85645_1564. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; EYLWNIE; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-1288-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1297-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38065 MW; C20FAF11747DE9E3 CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDPFIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JS37_NEIMB Unreviewed; 94 AA. AC Q9JS37; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41981.1}; GN OrderedLocusNames=NMB1546 {ECO:0000313|EMBL:AAF41901.1}, GN NMB1631 {ECO:0000313|EMBL:AAF41981.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41981.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41981.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41981.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41981.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41981.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41901.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41981.1; -; Genomic_DNA. DR PIR; E81071; E81071. DR RefSeq; NP_274553.1; NC_003112.2. DR RefSeq; NP_274637.1; NC_003112.2. DR RefSeq; WP_010980955.1; NC_003112.2. DR STRING; 122586.NMB1631; -. DR EnsemblBacteria; AAF41901; AAF41901; NMB1546. DR EnsemblBacteria; AAF41981; AAF41981; NMB1631. DR GeneID; 903994; -. DR GeneID; 904087; -. DR KEGG; nme:NMB1546; -. DR KEGG; nme:NMB1631; -. DR PATRIC; 20358926; VBINeiMen85645_1977. DR HOGENOM; HOG000219038; -. DR OMA; TMNIVKK; -. DR OrthoDB; EOG63NMPN; -. DR BioCyc; NMEN122586:GHGG-1587-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1680-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 43 {ECO:0000256|SAM:SignalP}. FT CHAIN 44 94 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006751898. FT TRANSMEM 59 80 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 94 AA; 10197 MW; 450AE86285BE4A19 CRC64; MKQVKKSSYF KYQKRKKTMN IVKKYAVKAA LAAGIFTPAI VMADTFDPSA IGTQVANVIM GFVSMVSAVG MAAITVILAI QGFKMAWSMI KSVK // ID Q9JRU9_NEIMB Unreviewed; 290 AA. AC Q9JRU9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Putative phytoene synthase {ECO:0000313|EMBL:AAF41553.1}; GN OrderedLocusNames=NMB1130 {ECO:0000313|EMBL:AAF41518.1}, GN NMB1168 {ECO:0000313|EMBL:AAF41553.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41553.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41553.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41553.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41553.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41553.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41518.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41553.1; -; Genomic_DNA. DR PIR; A81118; A81118. DR RefSeq; NP_274159.1; NC_003112.2. DR RefSeq; NP_274195.1; NC_003112.2. DR RefSeq; WP_002225224.1; NC_003112.2. DR STRING; 122586.NMB1168; -. DR EnsemblBacteria; AAF41518; AAF41518; NMB1130. DR EnsemblBacteria; AAF41553; AAF41553; NMB1168. DR GeneID; 903551; -. DR GeneID; 903588; -. DR KEGG; nme:NMB1130; -. DR KEGG; nme:NMB1168; -. DR PATRIC; 20357835; VBINeiMen85645_1433. DR eggNOG; ENOG4105FE1; Bacteria. DR eggNOG; COG1562; LUCA. DR HOGENOM; HOG000220849; -. DR KO; K02291; -. DR OMA; RKFWLAW; -. DR OrthoDB; EOG63FW00; -. DR BioCyc; NMEN122586:GHGG-1166-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1203-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:InterPro. DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR002060; Squ/phyt_synthse. DR InterPro; IPR017828; Squalene/phytoene_synth. DR InterPro; IPR019845; Squalene/phytoene_synthase_CS. DR Pfam; PF00494; SQS_PSY; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR TIGRFAMs; TIGR03465; HpnD; 1. DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 290 AA; 33046 MW; DC867E8D1DBDA2A9 CRC64; MKGLDYCRQK AEESRSSFLS GFRFLTQEKR DAVTVLYAFC RELDDVVDEC SNPDVAQATL NWWRGDLDKV FGGAMPEHPV NQALRQVKET FKLPKYELEA LIDGMQMDLV QARYGSFEEL KLYCHRVAGV VGCLIARILG FSDDQTLEYA DKMGLALQLT NIIRDVGEDA RRGRIYLPME EMRRFDVPAS VILQCSPTGN FAELMAFQIK RARETYREAV SLLPDADKKA QKVGLVMAAV YYELLNEIDR DGAQNVLKYK IALPSPRKKR IALKTWLFGF KPRPGTPERA // ID Q9JS54_NEIMB Unreviewed; 101 AA. AC Q9JS54; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41566.1}; GN OrderedLocusNames=NMB1144 {ECO:0000313|EMBL:AAF41531.1}, GN NMB1182 {ECO:0000313|EMBL:AAF41566.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41566.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41566.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41566.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41566.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41566.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41531.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41566.1; -; Genomic_DNA. DR PIR; G81116; G81116. DR RefSeq; NP_274172.1; NC_003112.2. DR RefSeq; NP_274208.1; NC_003112.2. DR RefSeq; WP_002222465.1; NC_003112.2. DR STRING; 122586.NMB1182; -. DR EnsemblBacteria; AAF41531; AAF41531; NMB1144. DR EnsemblBacteria; AAF41566; AAF41566; NMB1182. DR GeneID; 903565; -. DR GeneID; 903602; -. DR KEGG; nme:NMB1144; -. DR KEGG; nme:NMB1182; -. DR PATRIC; 20357865; VBINeiMen85645_1448. DR HOGENOM; HOG000218955; -. DR OMA; FSANVYE; -. DR OrthoDB; EOG64FKHK; -. DR BioCyc; NMEN122586:GHGG-1180-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1217-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 101 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006751893. SQ SEQUENCE 101 AA; 10802 MW; 283D3858BE9559E4 CRC64; MRVSKIIGSM LLVTAVQTVF SANVYACRHN GKTSYSQTPG KHCTNAGLGR DRVYSSVRPA VKDRAEDAGV GDYSDTVRDE HVQNPKGNAQ KDGSAAGIKP H // ID Q9JS28_NEIMB Unreviewed; 321 AA. AC Q9JS28; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF42456.1}; GN OrderedLocusNames=NMB0225 {ECO:0000313|EMBL:AAF40681.1}, GN NMB1050 {ECO:0000313|EMBL:AAF41448.1}, GN NMB2148 {ECO:0000313|EMBL:AAF42456.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42456.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42456.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42456.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF42456.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42456.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40681.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41448.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42456.1; -; Genomic_DNA. DR PIR; B81000; B81000. DR RefSeq; NP_273282.1; NC_003112.2. DR RefSeq; NP_274084.1; NC_003112.2. DR RefSeq; NP_275133.1; NC_003112.2. DR RefSeq; WP_002217985.1; NC_003112.2. DR STRING; 122586.NMB2148; -. DR EnsemblBacteria; AAF40681; AAF40681; NMB0225. DR EnsemblBacteria; AAF41448; AAF41448; NMB1050. DR EnsemblBacteria; AAF42456; AAF42456; NMB2148. DR GeneID; 902337; -. DR GeneID; 903187; -. DR GeneID; 903224; -. DR KEGG; nme:NMB0225; -. DR KEGG; nme:NMB1050; -. DR KEGG; nme:NMB2148; -. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; TEMAGHK; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-1087-MONOMER; -. DR BioCyc; NMEN122586:GHGG-2213-MONOMER; -. DR BioCyc; NMEN122586:GHGG-240-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38006 MW; 4FDB4DCA1974834C CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS QTIKQRKRQP YKLDSQLIQH IDTLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JS22_NEIMB Unreviewed; 47 AA. AC Q9JS22; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41571.1}; GN OrderedLocusNames=NMB1149 {ECO:0000313|EMBL:AAF41536.1}, GN NMB1187 {ECO:0000313|EMBL:AAF41571.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41571.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41571.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41571.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41571.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41571.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41536.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41571.1; -; Genomic_DNA. DR PIR; D81117; D81117. DR RefSeq; NP_274177.1; NC_003112.2. DR RefSeq; NP_274213.1; NC_003112.2. DR RefSeq; WP_010980902.1; NC_003112.2. DR STRING; 122586.NMB1187; -. DR EnsemblBacteria; AAF41536; AAF41536; NMB1149. DR EnsemblBacteria; AAF41571; AAF41571; NMB1187. DR GeneID; 903570; -. DR GeneID; 903607; -. DR KEGG; nme:NMB1149; -. DR KEGG; nme:NMB1187; -. DR BioCyc; NMEN122586:GHGG-1185-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1222-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5161 MW; 58A3CEA914A7A997 CRC64; MHSIFWGFAH FFGVPPSSNS VPSRLPTVMS ASCKADSTFF RILVSGR // ID Q9JRX5_NEIMB Unreviewed; 96 AA. AC Q9JRX5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42085.1}; GN OrderedLocusNames=NMB0485 {ECO:0000313|EMBL:AAF40921.1}, GN NMB0971 {ECO:0000313|EMBL:AAF41375.1}, GN NMB1742 {ECO:0000313|EMBL:AAF42085.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42085.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42085.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42085.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF42085.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42085.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40921.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41375.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42085.1; -; Genomic_DNA. DR PIR; E81047; E81047. DR RefSeq; NP_273532.1; NC_003112.2. DR RefSeq; NP_274008.1; NC_003112.2. DR RefSeq; NP_274743.1; NC_003112.2. DR RefSeq; WP_002222082.1; NC_003112.2. DR STRING; 122586.NMB1742; -. DR EnsemblBacteria; AAF40921; AAF40921; NMB0485. DR EnsemblBacteria; AAF41375; AAF41375; NMB0971. DR EnsemblBacteria; AAF42085; AAF42085; NMB1742. DR GeneID; 902602; -. DR GeneID; 903091; -. DR GeneID; 903356; -. DR KEGG; nme:NMB0485; -. DR KEGG; nme:NMB0971; -. DR KEGG; nme:NMB1742; -. DR eggNOG; ENOG41076QY; Bacteria. DR eggNOG; ENOG410ZDM4; LUCA. DR HOGENOM; HOG000218819; -. DR OMA; YKHLPFP; -. DR OrthoDB; EOG6JDWGV; -. DR BioCyc; NMEN122586:GHGG-1008-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1797-MONOMER; -. DR BioCyc; NMEN122586:GHGG-510-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 96 AA; 10396 MW; B4F98B8F38D18195 CRC64; MNIQLQGHIV GVKKINGQIE GKSFDYCCLI VATPLDSSQG NALGSSTTEY DFGGSANFEQ FRNAQFPIEA NLNVEIVTTG KTQKLKVIGF QLVKKG // ID Q7DD91_NEIMB Unreviewed; 321 AA. AC Q7DD91; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF42060.1}; GN OrderedLocusNames=NMB1713 {ECO:0000313|EMBL:AAF42060.1}, GN NMB1770 {ECO:0000313|EMBL:AAF42110.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42060.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42060.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42060.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF42060.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42060.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42060.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42110.1; -; Genomic_DNA. DR RefSeq; NP_274716.1; NC_003112.2. DR RefSeq; NP_274770.1; NC_003112.2. DR RefSeq; WP_002221064.1; NC_003112.2. DR EnsemblBacteria; AAF42060; AAF42060; NMB1713. DR EnsemblBacteria; AAF42110; AAF42110; NMB1770. DR GeneID; 903329; -. DR GeneID; 903389; -. DR KEGG; nme:NMB1713; -. DR KEGG; nme:NMB1770; -. DR PATRIC; 20359387; VBINeiMen85645_2199. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; LINIRTH; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-1768-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1825-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38063 MW; DCBBF12BE4E5F37D CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDTLIRRKLS PEQVCAYLCK HHRITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JS13_NEIMB Unreviewed; 211 AA. AC Q9JS13; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41569.1}; GN OrderedLocusNames=NMB1147 {ECO:0000313|EMBL:AAF41534.1}, GN NMB1185 {ECO:0000313|EMBL:AAF41569.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41569.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41569.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41569.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41569.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41569.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41534.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41569.1; -; Genomic_DNA. DR PIR; B81117; B81117. DR RefSeq; NP_274175.1; NC_003112.2. DR RefSeq; NP_274211.1; NC_003112.2. DR RefSeq; WP_002225216.1; NC_003112.2. DR STRING; 122586.NMB1185; -. DR EnsemblBacteria; AAF41534; AAF41534; NMB1147. DR EnsemblBacteria; AAF41569; AAF41569; NMB1185. DR GeneID; 903568; -. DR GeneID; 903605; -. DR KEGG; nme:NMB1147; -. DR KEGG; nme:NMB1185; -. DR PATRIC; 20357871; VBINeiMen85645_1451. DR eggNOG; ENOG4105PNM; Bacteria. DR eggNOG; COG2843; LUCA. DR HOGENOM; HOG000022575; -. DR OMA; VRYGFVS; -. DR OrthoDB; EOG64FKBH; -. DR BioCyc; NMEN122586:GHGG-1183-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1220-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019079; Capsule_synth_CapA. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF09587; PGA_cap; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 18 131 PGA_cap. {ECO:0000259|Pfam:PF09587}. SQ SEQUENCE 211 AA; 23140 MW; 673CA4533728F571 CRC64; MNIKYSGIEN RFETAILKKN GVRSGFVSFA PNLAAVKLND YAKVRKRITK TKQKADIVIV MFHGGAEGKQ AEHLPFDTEI FYGENRGNVV EFARLAVDSG ADVVFGQGPH VTRAVELYRD RFISYSGGNF ATYGAINTSG ISGIAPIFKI ITDKQGRFVS GNIIPITQVG DKIPKIDPEK TVIGRIIYLN RSDFPKGNGL DVSPDGSITR R // ID Q9JRY9_NEIMB Unreviewed; 458 AA. AC Q9JRY9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 113. DE RecName: Full=UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase {ECO:0000256|HAMAP-Rule:MF_02020}; DE EC=6.3.2.45 {ECO:0000256|HAMAP-Rule:MF_02020}; DE AltName: Full=Murein peptide ligase {ECO:0000256|HAMAP-Rule:MF_02020}; DE AltName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_02020}; GN Name=mpl-2 {ECO:0000313|EMBL:AAF41567.1}; GN Synonyms=mpl {ECO:0000256|HAMAP-Rule:MF_02020}, GN mpl-1 {ECO:0000313|EMBL:AAF41532.1}; GN OrderedLocusNames=NMB1145 {ECO:0000313|EMBL:AAF41532.1}, GN NMB1183 {ECO:0000313|EMBL:AAF41567.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41567.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41567.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41567.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41567.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41567.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000213|PDB:3EAG} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-323. RA Chang C., Hendricks R., Clancy S., Joachimiak A.; RT "The crystal structure of UDP-N-acetylmuramate:L-alanyl-gamma-D- RT glutamyl-meso-diaminopimelateligase (MPL) from Neisseria RT meningitides."; RL Submitted (AUG-2008) to the PDB data bank. CC -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D- CC glutamyl-meso-diaminopimelate by linking it to UDP-N- CC acetylmuramate. {ECO:0000256|HAMAP-Rule:MF_02020}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + CC phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso- CC 2,6-diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_02020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02020}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000256|HAMAP-Rule:MF_02020}. CC -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41532.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41567.1; -; Genomic_DNA. DR PIR; E81112; E81112. DR RefSeq; NP_274173.1; NC_003112.2. DR RefSeq; NP_274209.1; NC_003112.2. DR RefSeq; WP_002225218.1; NC_003112.2. DR PDB; 3EAG; X-ray; 2.55 A; A/B=1-323. DR PDBsum; 3EAG; -. DR STRING; 122586.NMB1183; -. DR EnsemblBacteria; AAF41532; AAF41532; NMB1145. DR EnsemblBacteria; AAF41567; AAF41567; NMB1183. DR GeneID; 903566; -. DR GeneID; 903603; -. DR KEGG; nme:NMB1145; -. DR KEGG; nme:NMB1183; -. DR PATRIC; 20357867; VBINeiMen85645_1449. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR HOGENOM; HOG000256032; -. DR KO; K02558; -. DR OMA; CDANVYP; -. DR OrthoDB; EOG64BQ73; -. DR BioCyc; NMEN122586:GHGG-1181-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1218-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02020; Mpl; 1. DR InterPro; IPR005757; Mpl. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01081; mpl; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3EAG}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02020, KW ECO:0000256|RuleBase:RU003630}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02020}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02020}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02020}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02020}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02020, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AAF41567.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02020}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02020, KW ECO:0000256|RuleBase:RU003630}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02020}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 104 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 110 301 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 321 369 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 112 118 ATP. {ECO:0000256|HAMAP-Rule:MF_02020}. SQ SEQUENCE 458 AA; 49574 MW; A0888952F2973C86 CRC64; MKHIHIIGIG GTFMGGLAAI AKEAGFEVSG CDAKMYPPMS TQLEALGIDV YEGFDAAQLD EFKADVYVIG NVAKRGMDVV EAILNLGLPY ISGPQWLSEN VLHHHWVLGV AGTHGKTTTA SMLAWVLEYA GLAPGFLIGG VPENFGVSAR LPQTPRQDPN SQSPFFVIEA DEYDTAFFDK RSKFVHYRPR TAVLNNLEFD HADIFADLGA IQTQFHYLVR TVPSEGLIVC NGRQQSLQDT LDKGCWTPVE KFGTEHGWQA GEANADGSFD VLLDGKTAGR VKWDLMGRHN RMNALAVIAA ARHVGVDIQT ACEALGAFKN VKRRMEIKGT ANGITVYDDF AHHPTAIETT IQGLRQRVGG ARILAVLEPR SNTMKLGTMK SALPVSLKEA DQVFCYAGGV DWDVAEALAP LGGRLNVGKD FDAFVAEIVK NAEVGDHILV MSNGGFGGIH GKLLEALR // ID Q9JS17_NEIMB Unreviewed; 125 AA. AC Q9JS17; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42114.1}; GN OrderedLocusNames=NMB0500 {ECO:0000313|EMBL:AAF40932.1}, GN NMB1774 {ECO:0000313|EMBL:AAF42114.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42114.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42114.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42114.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF42114.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42114.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000213|PDB:3NYM} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS). RA Zhang R., Tan K., Volkart L., Bargassa M., Joachimiak A.; RT "The crystal structure of functionally unknown protein from Neisseria RT meningitidis MC58."; RL Submitted (JUL-2010) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40932.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42114.1; -; Genomic_DNA. DR PIR; E81192; E81192. DR RefSeq; NP_273546.1; NC_003112.2. DR RefSeq; NP_274774.1; NC_003112.2. DR RefSeq; WP_002217880.1; NC_003112.2. DR PDB; 3NYM; X-ray; 1.90 A; A/B=1-125. DR PDBsum; 3NYM; -. DR STRING; 122586.NMB1774; -. DR EnsemblBacteria; AAF40932; AAF40932; NMB0500. DR EnsemblBacteria; AAF42114; AAF42114; NMB1774. DR GeneID; 902616; -. DR GeneID; 903325; -. DR KEGG; nme:NMB0500; -. DR KEGG; nme:NMB1774; -. DR PATRIC; 20356250; VBINeiMen85645_0645. DR HOGENOM; HOG000027879; -. DR OrthoDB; EOG6TFCZH; -. DR BioCyc; NMEN122586:GHGG-1829-MONOMER; -. DR BioCyc; NMEN122586:GHGG-525-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3NYM}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT REGION 76 78 Sulfate binding. {ECO:0000213|PDB:3NYM}. FT BINDING 51 51 Acetate. {ECO:0000213|PDB:3NYM}. SQ SEQUENCE 125 AA; 14438 MW; 61BD5011A3EE6B04 CRC64; METLNDIKKI LINVGLYQGF DLTDPKVSEE VNHETANMKW IKDYTSDGNW DNEFKEDLKN FLDYMEVCQL ALNDKNFKIA SNSLFMAMIY AGNLSLIFDS IKTDISTLLS AEYKKNSFSW PSLDE // ID Q9JS32_NEIMB Unreviewed; 47 AA. AC Q9JS32; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41558.1}; GN OrderedLocusNames=NMB1135 {ECO:0000313|EMBL:AAF41523.1}, GN NMB1173 {ECO:0000313|EMBL:AAF41558.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41558.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41558.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41558.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41558.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41558.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41523.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41558.1; -; Genomic_DNA. DR PIR; F81118; F81118. DR RefSeq; NP_274164.1; NC_003112.2. DR RefSeq; NP_274200.1; NC_003112.2. DR RefSeq; WP_009346130.1; NC_003112.2. DR STRING; 122586.NMB1173; -. DR EnsemblBacteria; AAF41523; AAF41523; NMB1135. DR EnsemblBacteria; AAF41558; AAF41558; NMB1173. DR GeneID; 903556; -. DR GeneID; 903593; -. DR KEGG; nme:NMB1135; -. DR KEGG; nme:NMB1173; -. DR PATRIC; 20357845; VBINeiMen85645_1438. DR BioCyc; NMEN122586:GHGG-1171-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1208-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5102 MW; 4DDDFFEC6BEE3E40 CRC64; MHRYLSVLQP EKPPAGYSGL NLNQYSVASP CRTICTVCGS PPCPDFC // ID Q7DDP3_NEIMB Unreviewed; 65 AA. AC Q7DDP3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40920.1}; GN OrderedLocusNames=NMB0484 {ECO:0000313|EMBL:AAF40920.1}, GN NMB0972 {ECO:0000313|EMBL:AAF41376.1}, GN NMB1743 {ECO:0000313|EMBL:AAF42086.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40920.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40920.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40920.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF40920.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40920.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40920.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41376.1; -; Genomic_DNA. DR EMBL; AE002098; AAF42086.1; -; Genomic_DNA. DR PIR; E81136; E81136. DR RefSeq; NP_273531.1; NC_003112.2. DR RefSeq; NP_274009.1; NC_003112.2. DR RefSeq; NP_274744.1; NC_003112.2. DR RefSeq; WP_002215770.1; NC_003112.2. DR STRING; 122586.NMB1743; -. DR EnsemblBacteria; AAF40920; AAF40920; NMB0484. DR EnsemblBacteria; AAF41376; AAF41376; NMB0972. DR EnsemblBacteria; AAF42086; AAF42086; NMB1743. DR GeneID; 902601; -. DR GeneID; 903092; -. DR GeneID; 903355; -. DR KEGG; nme:NMB0484; -. DR KEGG; nme:NMB0972; -. DR KEGG; nme:NMB1743; -. DR HOGENOM; HOG000218902; -. DR OrthoDB; EOG6K405M; -. DR BioCyc; NMEN122586:GHGG-1009-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1798-MONOMER; -. DR BioCyc; NMEN122586:GHGG-509-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7378 MW; E9B45489DB12F2E5 CRC64; MQKVYVVQSV STGDFLYLSP ETGDIGHTKL ITNADYFYDF EEAINAGLEE IGNQYEFVVF GFLKD // ID Q7DDG6_NEIMB Unreviewed; 65 AA. AC Q7DDG6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41525.1}; GN OrderedLocusNames=NMB1137 {ECO:0000313|EMBL:AAF41525.1}, GN NMB1175 {ECO:0000313|EMBL:AAF41560.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41525.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41525.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41525.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41525.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41525.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41525.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41560.1; -; Genomic_DNA. DR PIR; E81114; E81114. DR RefSeq; NP_274166.1; NC_003112.2. DR RefSeq; NP_274202.1; NC_003112.2. DR RefSeq; WP_002222472.1; NC_003112.2. DR STRING; 122586.NMB1175; -. DR EnsemblBacteria; AAF41525; AAF41525; NMB1137. DR EnsemblBacteria; AAF41560; AAF41560; NMB1175. DR GeneID; 903558; -. DR GeneID; 903595; -. DR KEGG; nme:NMB1137; -. DR KEGG; nme:NMB1175; -. DR PATRIC; 20357849; VBINeiMen85645_1440. DR eggNOG; ENOG4105WVQ; Bacteria. DR eggNOG; COG2975; LUCA. DR HOGENOM; HOG000262066; -. DR OMA; AIQQAWI; -. DR OrthoDB; EOG6ZD6DN; -. DR BioCyc; NMEN122586:GHGG-1173-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1210-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR Gene3D; 1.10.10.600; -; 1. DR InterPro; IPR007479; ISC_FeS_clus_asmbl_IscsX. DR Pfam; PF04384; Fe-S_assembly; 1. DR PIRSF; PIRSF039003; IscX; 1. DR SUPFAM; SSF140319; SSF140319; 1. DR TIGRFAMs; TIGR03412; iscX_yfhJ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7663 MW; 8B07D69268378281 CRC64; MKWTDTQRIA EELYDLHGET IDPRTVRFTQ LRDLIMALPE FDDDPARCGE RILEAVQQAW IDEAE // ID Q9JRT0_NEIMB Unreviewed; 239 AA. AC Q9JRT0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 92. DE SubName: Full=Oxidoreductase, short chain dehydrogenase/reductase family {ECO:0000313|EMBL:AAF41550.1}; GN OrderedLocusNames=NMB1127 {ECO:0000313|EMBL:AAF41515.1}, GN NMB1165 {ECO:0000313|EMBL:AAF41550.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41550.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41550.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41550.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41550.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41550.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41515.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41550.1; -; Genomic_DNA. DR PIR; F81117; F81117. DR RefSeq; NP_274156.1; NC_003112.2. DR RefSeq; NP_274192.1; NC_003112.2. DR RefSeq; WP_002225227.1; NC_003112.2. DR STRING; 122586.NMB1165; -. DR EnsemblBacteria; AAF41515; AAF41515; NMB1127. DR EnsemblBacteria; AAF41550; AAF41550; NMB1165. DR GeneID; 903548; -. DR GeneID; 903585; -. DR KEGG; nme:NMB1127; -. DR KEGG; nme:NMB1165; -. DR PATRIC; 20357829; VBINeiMen85645_1430. DR eggNOG; ENOG4105UBK; Bacteria. DR eggNOG; COG1028; LUCA. DR OMA; QAGRIIF; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NMEN122586:GHGG-1163-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1200-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 239 AA; 25917 MW; FCA8D6FE098848A0 CRC64; MATLSDKTIL VTGASQGLGE QVAKAYAAAG ATVILVARHQ KKLEKVYDAI VEAGYPEPFA ICFDLISAEE KEFEHFAATI AEATQGKLDG IVHCAGYFYA LSPLDFQTVA EWVNQYRINT VAPMGLTRAL FPLLKQSPDA SVIFVGESHG ETPKAYWGGF GASKAALNYL CKVAADEWER FGNLRANVLV PGPINSPQRI KSHPGEAKSE RKSYGDVLPA FVWWASAESK GRSGEIVYL // ID Q9JS43_NEIMB Unreviewed; 227 AA. AC Q9JS43; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41559.1}; GN OrderedLocusNames=NMB1136 {ECO:0000313|EMBL:AAF41524.1}, GN NMB1174 {ECO:0000313|EMBL:AAF41559.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41559.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41559.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41559.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000313|EMBL:AAF41559.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41559.1}; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Ciecko A., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T.M., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., DeBoy R.T., Pizza M., Grandi G., RA Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41524.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41559.1; -; Genomic_DNA. DR PIR; G81118; G81118. DR RefSeq; NP_274201.1; NC_003112.2. DR RefSeq; WP_010980897.1; NC_003112.2. DR STRING; 122586.NMB1174; -. DR EnsemblBacteria; AAF41524; AAF41524; NMB1136. DR EnsemblBacteria; AAF41559; AAF41559; NMB1174. DR GeneID; 903594; -. DR KEGG; nme:NMB1174; -. DR HOGENOM; HOG000027810; -. DR OMA; FLPACRI; -. DR OrthoDB; EOG6038W3; -. DR BioCyc; NMEN122586:GHGG-1172-MONOMER; -. DR BioCyc; NMEN122586:GHGG-1209-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 227 AA; 25432 MW; 36154D01049BA2DE CRC64; MTRCGIRDGL CFFLPACRIF PSLRETERDG GAADKLEIAS FKLRTGGGHA FYRNRETAAR PGKAFRNLRV DEPTLGAQHC RIATGSRFIQ GNQVAPVLVV KANRYSGEDM LPVQYLIQFA YQQNQAVKLL HLRQGIRMVG SGINQFGQFC GKHIVHQSSL SVETPLFGAV ESDLFGRDNS SQIRTTHRLV LDVLSGELKH SAILKGRQFC RNIFYTASMP DDKRKFI // ID Q9K0X2_NEIMB Unreviewed; 389 AA. AC Q9K0X2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 71. DE SubName: Full=Putative AcnD-accessory protein PrpF {ECO:0000313|EMBL:AAF40872.1}; GN OrderedLocusNames=NMB0434 {ECO:0000313|EMBL:AAF40872.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40872.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40872.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40872.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40872.1; -; Genomic_DNA. DR PIR; D81200; D81200. DR RefSeq; NP_273482.1; NC_003112.2. DR RefSeq; WP_002224932.1; NC_003112.2. DR ProteinModelPortal; Q9K0X2; -. DR SMR; Q9K0X2; 2-386. DR PaxDb; Q9K0X2; -. DR EnsemblBacteria; AAF40872; AAF40872; NMB0434. DR GeneID; 902550; -. DR KEGG; nme:NMB0434; -. DR PATRIC; 20356070; VBINeiMen85645_0550. DR eggNOG; ENOG4105C7F; Bacteria. DR eggNOG; COG2828; LUCA. DR HOGENOM; HOG000220029; -. DR KO; K09788; -. DR OMA; AASRQHT; -. DR OrthoDB; EOG6DC6FS; -. DR BioCyc; NMEN122586:GHGG-458-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:InterPro. DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro. DR InterPro; IPR012709; PrpF. DR InterPro; IPR007400; PrpF_protein. DR Pfam; PF04303; PrpF; 1. DR TIGRFAMs; TIGR02334; prpF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 389 AA; 40968 MW; E9631A56E029D246 CRC64; MPQIKIPAVY YRGGTSKGVF FKRSDLPEAA REAGSARDKI LLRVLGSPDP YGKQIDGLGN ASSSTSKAVI LDKSERADHD VDYLFGQVSI DKPFVDWSGN CGNLTAAVGA FSIEQGLVDK GKIPSDGICT VKIWQKNIGK TIIAHVPMQN GAVLETGDFE LDGVTFPAAE VQIEFLDPAD GEGSMFPTGN LVDEIDVPNI GRLKATLINA GIPTVFLNAA DLGYTGKELQ DDINNDAAAL EKFEKIRAYG ALKMGLISDV SEAAARAHTP KVAFVAPAAD YTASSGKTVN AADIDLLVRA LSMGKLHHAM MGTASVAIAT AAAVPGTLVN LAAGGGTRKE VRFGHPSGTL RVGAAAECQD GQWTATKAVM SRSARVMMEG WVRVPEDCF // ID Q9JY67_NEIMB Unreviewed; 1067 AA. AC Q9JY67; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Multiple transferable resistance system protein MtrD {ECO:0000313|EMBL:AAF42062.1}; GN Name=mtrD {ECO:0000313|EMBL:AAF42062.1}; GN OrderedLocusNames=NMB1715 {ECO:0000313|EMBL:AAF42062.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42062.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42062.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42062.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division CC (RND) (TC 2.A.6) family. {ECO:0000256|SAAS:SAAS00536972}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42062.1; -; Genomic_DNA. DR PIR; E81051; E81051. DR RefSeq; NP_274718.1; NC_003112.2. DR RefSeq; WP_002224969.1; NC_003112.2. DR ProteinModelPortal; Q9JY67; -. DR STRING; 122586.NMB1715; -. DR PaxDb; Q9JY67; -. DR EnsemblBacteria; AAF42062; AAF42062; NMB1715. DR GeneID; 903387; -. DR KEGG; nme:NMB1715; -. DR PATRIC; 20359391; VBINeiMen85645_2201. DR eggNOG; ENOG4105BZS; Bacteria. DR eggNOG; COG0841; LUCA. DR HOGENOM; HOG000158129; -. DR KO; K18138; -. DR OMA; FFGWFNA; -. DR OrthoDB; EOG683S5M; -. DR BioCyc; NMEN122586:GHGG-1770-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 3.30.2090.10; -; 2. DR InterPro; IPR027463; AcrB_DN_DC_subdom. DR InterPro; IPR001036; Acrflvin-R. DR InterPro; IPR004764; HAE1. DR InterPro; IPR000731; SSD. DR Pfam; PF00873; ACR_tran; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR SUPFAM; SSF82714; SSF82714; 2. DR TIGRFAMs; TIGR00915; 2A0602; 1. DR PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 10 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 384 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 390 411 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 432 456 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 468 491 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 536 554 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 871 889 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 896 913 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 933 957 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 982 1002 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 1014 1036 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 368 493 SSD (sterol-sensing). FT {ECO:0000259|PROSITE:PS50156}. SQ SEQUENCE 1067 AA; 113974 MW; A85545371B7943C2 CRC64; MAKFFIDRPI FAWVISIFII AAGIFGIKSL PVSQYPSVAA PTITLRATYP GASAQVMEDS VLSVIERNMN GVEGLDYMST SADSSGSGSV SLTFTPDTDE NLAQVEVQNK LSEVLSTLPA TVQQYGVTVS KARSNFLMIV MLSSDVQSTE EMNDYAQRNI VPELQRIEGV GQVRLFGAQR AMRIWVDPKK LQNYNLSFAD VGSALSAQNV QISAGSIGSL PAVRGQTVTA TVTAQGQLGT AEEFGNVILR ANTDGSNVYL KDVARVGLGM EDYSSSTRLN GVNTTGMAVM LSNSGNAMAT AKAVKERMAT LEKYFPQGMS WKTPYDTSKF VEISIEKVIH TLIEAMVLVF VVMYLFLQNI RYTLIPTIVV PISLLGGFAF ISYMGMSINV LTMFAMVLVI GIVVDDAIVV VENVERIMAG EGLPPKEATK KAMGQISGAV IGITAVLISV FVPLAMFSGA TGNIYKQFAL TMASSIAFSA FLALTLTPAL CATMLKTIPK GHHEEKKGFF GWFNKKFNSW THGYEGRVAK VLRKTFRMMV VYIGLAVVGV FLFMRLPTSF LPTEDQGFVM VSVQLPAGAT QERTNATLAQ VTQLAKSIPE IENIITVSGF SFSGSGQNMA MGFAILKDWN ERTAPGSDAV AIAGKLTGMM MGTLKDGFGI AVVPPPILEL GNGSGLSINL QDRNNTGHTA LLAKRNELIQ KMRASGLFDP STVRAGGLED SPQLKIDINR AAAAAQGISF ADIRTALASA LSSSYVSDFP NQGRLQRVMV QADEDARMQP ADILNLTVPN KSGVAVPLST IATVSWENGT EQSVRFNGYP SMKLSASPAT GVSTGQAMAA VQKMVDELGG GYSLEWGGQS REEAKGGSQT LILYGLAVAA VFLVLAALYE SWSIPLAVIL VIPLGLIGAA AGVTGRNLFE GLLGSVPSFA NDIYFQVGFV TVMGLSAKNA ILIIEFAKDL QAQGKSAVEA ALEAARLRFR PIIMTSFAFI LGVVPLYIAG GASSASQRAI GTTVFWGMLI GTLLSVFLVP LFYVVVRKFF KETAHEHEMA VKHAAEAGIT GSDDSQH // ID Q9JYN0_NEIMB Unreviewed; 284 AA. AC Q9JYN0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Segregation and condensation protein A {ECO:0000256|SAAS:SAAS00093938}; GN Name=scpA {ECO:0000313|EMBL:AAF41860.1}; GN OrderedLocusNames=NMB1504 {ECO:0000313|EMBL:AAF41860.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41860.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41860.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41860.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates in chromosomal partition during cell CC division. May act via the formation of a condensin-like complex CC containing Smc and ScpB that pull DNA away from mid-cell into both CC cell halves. {ECO:0000256|SAAS:SAAS00093941}. CC -!- SUBUNIT: Component of a cohesin-like complex composed of ScpA, CC ScpB and the Smc homodimer, in which ScpA and ScpB bind to the CC head domain of Smc. The presence of the three proteins is required CC for the association of the complex with DNA. CC {ECO:0000256|SAAS:SAAS00093944}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00093943}. CC -!- SIMILARITY: Belongs to the ScpA family. CC {ECO:0000256|SAAS:SAAS00573610}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41860.1; -; Genomic_DNA. DR PIR; D81075; D81075. DR RefSeq; NP_274512.1; NC_003112.2. DR RefSeq; WP_002225073.1; NC_003112.2. DR STRING; 122586.NMB1504; -. DR PaxDb; Q9JYN0; -. DR EnsemblBacteria; AAF41860; AAF41860; NMB1504. DR GeneID; 903945; -. DR KEGG; nme:NMB1504; -. DR PATRIC; 20358790; VBINeiMen85645_1905. DR eggNOG; ENOG4108KVX; Bacteria. DR eggNOG; COG1354; LUCA. DR HOGENOM; HOG000242825; -. DR KO; K05896; -. DR OMA; RKQNFNI; -. DR OrthoDB; EOG6CZQPX; -. DR BioCyc; NMEN122586:GHGG-1544-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR HAMAP; MF_01805; ScpA; 1. DR InterPro; IPR003768; ScpA. DR Pfam; PF02616; SMC_ScpA; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|SAAS:SAAS00464525}; KW Cell division {ECO:0000256|SAAS:SAAS00464525}; KW Chromosome partition {ECO:0000256|SAAS:SAAS00464515}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00464526}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 284 AA; 31826 MW; CFEF8BCC1A722D16 CRC64; MPPIPAPSAP SEHTVAWVFG QPVTDLPQDL FIPPDALKVV LGSFQGPLDL LLYLIRKQNI DVLDIPMVKI TEQYLHYIAQ IETYQFDLAA EYLLMAAMLI EIKSRLLLPR TETVEDEEAD PRAELVRRLL AYEQMKLAAQ GLDALPRAGR DFAWAYLPLE IAVEAKLPEV YITDLTQAWL GILSRAKHTR SHEVIKETIS VRAQMTAILR RLNGHGICRF HDLFNPKQGA AYVVVNFIAL LELAKEGLVR IVQEDGFGEI RISLNHEGAH SDGISGTRGG RDVF // ID Q9K0P8_NEIMB Unreviewed; 274 AA. AC Q9K0P8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40966.1}; GN OrderedLocusNames=NMB0537 {ECO:0000313|EMBL:AAF40966.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40966.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40966.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40966.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2PLI} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 187-274 IN COMPLEX WITH RP ZINC. RA Nocek B., Duggan E., Gu M., Joachimiak A.; RT "Structure of putative Mg2+ and Co2+ transporter(CorC)associated RT region from Neisseria meningitidis MC58."; RL Submitted (APR-2007) to the PDB data bank. RN [3] {ECO:0000213|PDB:3OI8} RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 24-176. RA Zhang R., Tan K., Li H., Cobb G., Joachimiak A.; RT "The crystal structure of functionally unknown conserved protein RT domain from Neisseria meningitidis MC58."; RL Submitted (AUG-2010) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40966.1; -; Genomic_DNA. DR PIR; H81187; H81187. DR RefSeq; NP_273582.1; NC_003112.2. DR RefSeq; WP_002222904.1; NC_003112.2. DR PDB; 2PLI; X-ray; 1.70 A; A/B/C/D=187-274. DR PDB; 3OI8; X-ray; 1.99 A; A/B=24-176. DR PDBsum; 2PLI; -. DR PDBsum; 3OI8; -. DR ProteinModelPortal; Q9K0P8; -. DR SMR; Q9K0P8; 191-274. DR STRING; 122586.NMB0537; -. DR PaxDb; Q9K0P8; -. DR EnsemblBacteria; AAF40966; AAF40966; NMB0537. DR GeneID; 902652; -. DR KEGG; nme:NMB0537; -. DR PATRIC; 20356331; VBINeiMen85645_0684. DR eggNOG; ENOG4108JU5; Bacteria. DR eggNOG; COG4535; LUCA. DR HOGENOM; HOG000062294; -. DR KO; K06189; -. DR OMA; QMISIKA; -. DR OrthoDB; EOG60W7V4; -. DR BioCyc; NMEN122586:GHGG-563-MONOMER; -. DR EvolutionaryTrace; Q9K0P8; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 2. DR Pfam; PF03471; CorC_HlyC; 1. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2PLI, ECO:0000213|PDB:3OI8}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000213|PDB:2PLI}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000213|PDB:2PLI}. FT DOMAIN 64 123 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 128 185 CBS. {ECO:0000259|PROSITE:PS51371}. FT METAL 193 193 Zinc 1. {ECO:0000213|PDB:2PLI}. FT METAL 196 196 Zinc 1; via pros nitrogen. FT {ECO:0000213|PDB:2PLI}. FT METAL 212 212 Zinc 2. {ECO:0000213|PDB:2PLI}. FT METAL 228 228 Zinc 2. {ECO:0000213|PDB:2PLI}. FT METAL 240 240 Zinc 3; via tele nitrogen. FT {ECO:0000213|PDB:2PLI}. FT METAL 246 246 Zinc 3. {ECO:0000213|PDB:2PLI}. SQ SEQUENCE 274 AA; 31150 MW; BF842B9BDAD957D4 CRC64; MDGAQPKTNF FERLIARLAR EPDSAEDVLN LLRQAHEQEV FDADTLLRLE KVLDFSDLEV RDAMITRSRM NVLKENDSIE RITAYVIDTA HSRFPVIGED KDEVLGILHA KDLLKYMFNP EQFHLKSILR PAVFVPEGKS LTALLKEFRE QRNHMAIVID EYGGTSGLVT FEDIIEQIVG EIEDEFDEDD SADNIHAVSS ERWRIHAATE IEDINTFFGT EYSSEEADTI GGLVIQELGH LPVRGEKVLI GGLQFTVARA DNRRLHTLMA TRVK // ID Q9JYJ2_NEIMB Unreviewed; 257 AA. AC Q9JYJ2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Transcriptional regulator, DeoR family {ECO:0000313|EMBL:AAF41915.1}; GN OrderedLocusNames=NMB1561 {ECO:0000313|EMBL:AAF41915.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41915.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41915.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41915.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH deoR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000712}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41915.1; -; Genomic_DNA. DR PIR; F81069; F81069. DR RefSeq; NP_274568.1; NC_003112.2. DR RefSeq; WP_002225036.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ2; -. DR STRING; 122586.NMB1561; -. DR PaxDb; Q9JYJ2; -. DR EnsemblBacteria; AAF41915; AAF41915; NMB1561. DR GeneID; 904128; -. DR KEGG; nme:NMB1561; -. DR PATRIC; 20358978; VBINeiMen85645_2008. DR eggNOG; ENOG4105E98; Bacteria. DR eggNOG; COG1349; LUCA. DR HOGENOM; HOG000224685; -. DR KO; K02444; -. DR OMA; ADRQTRC; -. DR OrthoDB; EOG6XSZXW; -. DR BioCyc; NMEN122586:GHGG-1602-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014036; DeoR_C. DR InterPro; IPR001034; DeoR_HTH. DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00455; DeoRC; 1. DR Pfam; PF08220; HTH_DeoR; 1. DR PRINTS; PR00037; HTHLACR. DR SMART; SM00420; HTH_DEOR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00894; HTH_DEOR_1; 1. DR PROSITE; PS51000; HTH_DEOR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00589027}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00132188}; KW Transcription regulation {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00132188}. FT DOMAIN 4 59 HTH deoR-type DNA-binding. FT {ECO:0000259|PROSITE:PS51000}. SQ SEQUENCE 257 AA; 28064 MW; 143F22FBE6AE9528 CRC64; MKPKIQRHGE ILSLVRRHQF MSVDELAAAL DVTPQTIRRD IRELEEVGSL KRHHGGASSG GNLPEGLPAD RQTRCQNEKN AIARLIAEHI PDGSSLFVSI GTTMEAVVSE LVRRRGSLRV ITNNIHAASI ASARTDYTVI ITSGVVRPLD GGITGVATVD FINQFKVDYA VMSTHGVESD GSLLDDDYKE VSVMQAMIAN ARVRFLGVDH SKFRSNALVR LGDITAFDKV FTDRLPDTAM QKMLKEAGVE CLIADAV // ID Q9JYF0_NEIMB Unreviewed; 268 AA. AC Q9JYF0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Amino acid ABC transporter, periplasmic amino acid-binding protein {ECO:0000313|EMBL:AAF41964.1}; GN OrderedLocusNames=NMB1612 {ECO:0000313|EMBL:AAF41964.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41964.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41964.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41964.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 CC family. {ECO:0000256|RuleBase:RU003744}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41964.1; -; Genomic_DNA. DR PIR; B81063; B81063. DR RefSeq; NP_274618.1; NC_003112.2. DR RefSeq; WP_002222181.1; NC_003112.2. DR ProteinModelPortal; Q9JYF0; -. DR STRING; 122586.NMB1612; -. DR PaxDb; Q9JYF0; -. DR EnsemblBacteria; AAF41964; AAF41964; NMB1612. DR GeneID; 902102; -. DR KEGG; nme:NMB1612; -. DR PATRIC; 20359112; VBINeiMen85645_2068. DR eggNOG; ENOG4106PMH; Bacteria. DR eggNOG; COG0834; LUCA. DR HOGENOM; HOG000031895; -. DR KO; K02030; -. DR OMA; GYVAKND; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; NMEN122586:GHGG-1660-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001320; Iontro_rcpt. DR InterPro; IPR018313; SBP_3_CS. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00062; PBPb; 1. DR SMART; SM00079; PBPe; 1. DR PROSITE; PS01039; SBP_BACTERIAL_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328318. FT DOMAIN 38 262 PBPb. {ECO:0000259|SMART:SM00062}. SQ SEQUENCE 268 AA; 29017 MW; 171784ECD6DCC47F CRC64; MNMKKWIAAA LACSALALSA CGGQGKDTAA PAANPDKVYR VASNAEFAPF ESLDSKGNVE GFDVDLMNAM AKAGNFKIEF KHQPWDSLFP ALNNGDADVV MSGVTITDDR KQSMDFSDPY FEITQVVLVP KGKKVSSSED LKNMNKVGVV TGYTGDFSVS KLLGNDNPKI ARFENVPLII KELENGGLDS VVSDSAVIAN YVKNNPAKGM DFVTLPDFTT EHYGIAVRKG DEATVKMLND ALEKVRESGE YDKIYAKYFA KEDGQAAK // ID Q9K186_NEIMB Unreviewed; 348 AA. AC Q9K186; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Peptidylprolyl isomerase {ECO:0000256|RuleBase:RU363014}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014}; GN OrderedLocusNames=NMB0281 {ECO:0000313|EMBL:AAF40735.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40735.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40735.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40735.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363014, CC ECO:0000256|SAAS:SAAS00523013}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|SAAS:SAAS00551936}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40735.1; -; Genomic_DNA. DR PIR; B81216; B81216. DR RefSeq; NP_273337.1; NC_003112.2. DR RefSeq; WP_010980770.1; NC_003112.2. DR ProteinModelPortal; Q9K186; -. DR STRING; 122586.NMB0281; -. DR PaxDb; Q9K186; -. DR DNASU; 902392; -. DR EnsemblBacteria; AAF40735; AAF40735; NMB0281. DR GeneID; 902392; -. DR KEGG; nme:NMB0281; -. DR PATRIC; 20355652; VBINeiMen85645_0350. DR eggNOG; ENOG4105DBD; Bacteria. DR eggNOG; COG0760; LUCA. DR HOGENOM; HOG000219125; -. DR KO; K03771; -. DR OMA; APNATHE; -. DR OrthoDB; EOG6M9DS4; -. DR BioCyc; NMEN122586:GHGG-296-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR023058; PPIase_PpiC_CS. DR InterPro; IPR015391; SurA_N. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF09312; SurA_N; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS01096; PPIC_PPIASE_1; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 4: Predicted; KW Chaperone {ECO:0000256|SAAS:SAAS00502901}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Rotamase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Signal {ECO:0000256|RuleBase:RU363014}. FT SIGNAL 1 21 {ECO:0000256|RuleBase:RU363014}. FT CHAIN 22 348 Peptidylprolyl isomerase. FT {ECO:0000256|RuleBase:RU363014}. FT /FTId=PRO_5006529489. FT DOMAIN 206 304 PpiC. {ECO:0000259|PROSITE:PS50198}. SQ SEQUENCE 348 AA; 37384 MW; F21C9885FF40AC25 CRC64; MMKIKALMIA AALLAAADVH AAPQKAKTAS AKAAKAAKAA KVAKVAKVAK VAATAQKEAA PAQQQGGIRF SDGIAAVADN EVITRRRLAE AVAEAKANLP KDAQISESEL SRQVLMQLVN QSLIVQAGKR RNIQASEAEI DAVVAKNPAL KNLSPAQRRD FADNIIAEKV RQQAVMQNSR VSEAEIDAFL EQAQKQGITL PEGAPLRQYR AQHILIKADS ENAAVGAEST IRKIYGEARS GTDFSSLARQ YSQDASAGNG GDLGWFADGV MVPAFEEAVH ALKPGQVGAP VRTQFGWHII KLNEVRDAGT PQERIRNSVR QYIFQQKAEQ ATVNLLRDLH SGAYVDIR // ID Q9K1E6_NEIMB Unreviewed; 658 AA. AC Q9K1E6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 103. DE SubName: Full=Glutathione-regulated potassium-efflux system protein {ECO:0000313|EMBL:AAF40666.1}; GN Name=kefB {ECO:0000313|EMBL:AAF40666.1}; GN OrderedLocusNames=NMB0209 {ECO:0000313|EMBL:AAF40666.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40666.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40666.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40666.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 CC (CPA2) transporter (TC 2.A.37) family. CC {ECO:0000256|SAAS:SAAS00575609}. CC -!- SIMILARITY: Contains RCK C-terminal domain. CC {ECO:0000256|SAAS:SAAS00510227}. CC -!- SIMILARITY: Contains RCK N-terminal domain. CC {ECO:0000256|SAAS:SAAS00510231}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40666.1; -; Genomic_DNA. DR PIR; B81225; B81225. DR RefSeq; NP_273267.1; NC_003112.2. DR RefSeq; WP_002243958.1; NC_003112.2. DR ProteinModelPortal; Q9K1E6; -. DR STRING; 122586.NMB0209; -. DR PaxDb; Q9K1E6; -. DR DNASU; 902317; -. DR EnsemblBacteria; AAF40666; AAF40666; NMB0209. DR GeneID; 902317; -. DR KEGG; nme:NMB0209; -. DR PATRIC; 20355459; VBINeiMen85645_0258. DR eggNOG; ENOG4105CKD; Bacteria. DR eggNOG; COG0475; LUCA. DR eggNOG; COG1226; LUCA. DR HOGENOM; HOG000179077; -. DR KO; K03455; -. DR OMA; RELMPVH; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; NMEN122586:GHGG-220-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006153; Cation/H_exchanger. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF00999; Na_H_Exchanger; 1. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Antiport {ECO:0000256|SAAS:SAAS00513511}; KW Cell membrane {ECO:0000256|SAAS:SAAS00510238}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ion transport {ECO:0000256|SAAS:SAAS00513546}; KW Membrane {ECO:0000256|SAAS:SAAS00510238, KW ECO:0000256|SAAS:SAAS00513498, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00513498, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00513498, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|SAAS:SAAS00513511, KW ECO:0000256|SAAS:SAAS00513546}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 234 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 316 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 328 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 359 382 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 410 532 RCK N-terminal. FT {ECO:0000259|PROSITE:PS51201}. FT DOMAIN 572 656 RCK C-terminal. FT {ECO:0000259|PROSITE:PS51202}. SQ SEQUENCE 658 AA; 71197 MW; B216DBD029219BCB CRC64; MNEFSLAPIV IVLLVSVITV ILCRKFNIPS MLGYLLVGFL AGPGMLSLIP KSHATDYLGE IGIVFLMFSI GLEFSLPKLR AMRRLVFGLG GLQVGITMLS VMGILMLTGV PFNWAFAVSG ALAMSSTAIV SRILSEKTEL GQPHGQMAMG VLLMQDIAVV PLMILIPALA GGGDGNIWAA LGLAFAKMLL TLGLLFFVGS KIMSRWFRMV AKRKSSELFM INVLLVTLGV AYLTELEGLS MALGAFVAGM LLSETEYRFQ VEDDIRPFRD ILLGFFFITV GMKLDIQALI GGWRQVLMLL AMLLVLKALV VFAIAFKMKH SVGDSLKTAL YLAQGGEFGF VMLAIAGQLD MVSPEWEQAA TAAVLLSMII APFLLGGSDA LVGRLVKSSW DMKSLDLHSM LVETMSKSDH VLIVGFGRGG QTVGRVLAQE DIPYFALDLD IARVQVARSA GEPVSFGDAK RREVLEAAGL GRAKMVVVTL NNMHETQHVL DNVLSMYPNM PVYVRATNDD YVKTFTDIGA EEAVSDTKET GLVLAGYAML GNGASYRHVY QTMANIRHSR YAALEGLFVG SDDEAGFGEN GETVRHAFPL AAEAYAVGKT VGTLPMAAYG IKLLFVRRRT GRIENPDASF TLEGGDVLVV AGKKEEIISF ENWSLQGI // ID Q9JZ81_NEIMB Unreviewed; 590 AA. AC Q9JZ81; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00577562}; DE EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00577562}; GN OrderedLocusNames=NMB1249 {ECO:0000313|EMBL:AAF41629.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41629.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41629.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41629.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00577673}. CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00577406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41629.1; -; Genomic_DNA. DR PIR; B81104; B81104. DR RefSeq; NP_274272.1; NC_003112.2. DR RefSeq; WP_002225189.1; NC_003112.2. DR ProteinModelPortal; Q9JZ81; -. DR STRING; 122586.NMB1249; -. DR PaxDb; Q9JZ81; -. DR EnsemblBacteria; AAF41629; AAF41629; NMB1249. DR GeneID; 903671; -. DR KEGG; nme:NMB1249; -. DR PATRIC; 20358095; VBINeiMen85645_1560. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR HOGENOM; HOG000218968; -. DR KO; K07673; -. DR OMA; FLQIQLT; -. DR OrthoDB; EOG6JX7HQ; -. DR BioCyc; NMEN122586:GHGG-1286-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR029095; NarX-like_N. DR InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ. DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF07730; HisKA_3; 1. DR Pfam; PF13675; PilJ; 1. DR PIRSF; PIRSF003167; STHK_NarX/NarQ; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00577298}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|SAAS:SAAS00577625}; KW Membrane {ECO:0000256|SAAS:SAAS00577774, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00577298}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00577625}; KW Transmembrane {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00577723}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 187 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 186 238 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 393 587 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 590 AA; 66469 MW; A4AE3589B67B30AE CRC64; MILPARFSDG ISLSLRLKLL TGLWVGLAAL SVVLTLLLSL RLENAASVIE EAGNLRMQAY RLAYMAGEGS PRAQIDNQVA EFEKSLKRIA QSDAIHPLIP SDTPLAYDLI QSMLIIDWQA HILPPLQSYR RPTQVDLYRF AGNIELFLQA LENANEKNTW WLRRFQWAIM LMTLVSSVLM LFWHQIWVIR PLQALREGAE RIGRRCFDIP VPEGGTPEFK QVGRCFNQMG GRLKILYDDL EGQVAEQTRS LEKQNQNLTL LYQTTRDLHQ SYIPQQAAEH FLNRILPAVG ADSGRVCLDG GSDVYVSIHH ADCGTAASDL GKYHEEIFPI EYQNETLGRL LLSFPNGISL DEDDRILLQT LGRQLGVSLA GAKQEEEKRL LAVLQERNLI AQGLHDSIAQ ALTFLNLQVQ MLETAFAENK REEAAENISF IKTGVQECYE DVRELLLNFR TKISNKEFPE AVADLFARFT QQTGITVETA WENGSFLPPQ EAQLQMIFIL QESLSNIRKH ARATHVKFTL SEHGGRFTMT IQDNGQGFDT EKIGEPTGSH VGLHIMQERA KRIHAVLEIR SQAQQGTTVS LTVASEESLK // ID Q9JZ61_NEIMB Unreviewed; 675 AA. AC Q9JZ61; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Transporter, BCCT family {ECO:0000313|EMBL:AAF41653.1}; GN OrderedLocusNames=NMB1277 {ECO:0000313|EMBL:AAF41653.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41653.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41653.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41653.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family. CC {ECO:0000256|SAAS:SAAS00598409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41653.1; -; Genomic_DNA. DR PIR; E81101; E81101. DR RefSeq; NP_274297.1; NC_003112.2. DR RefSeq; WP_002225178.1; NC_003112.2. DR ProteinModelPortal; Q9JZ61; -. DR STRING; 122586.NMB1277; -. DR PaxDb; Q9JZ61; -. DR EnsemblBacteria; AAF41653; AAF41653; NMB1277. DR GeneID; 903699; -. DR KEGG; nme:NMB1277; -. DR PATRIC; 20358177; VBINeiMen85645_1600. DR eggNOG; ENOG4105C94; Bacteria. DR eggNOG; COG1292; LUCA. DR HOGENOM; HOG000053241; -. DR KO; K02168; -. DR OMA; DDWLKIN; -. DR OrthoDB; EOG6D8B89; -. DR BioCyc; NMEN122586:GHGG-1315-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR018093; BCCT_CS. DR InterPro; IPR000060; BCCT_transptr. DR Pfam; PF02028; BCCT; 1. DR TIGRFAMs; TIGR00842; bcct; 1. DR PROSITE; PS01303; BCCT; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00492880}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00492880, KW ECO:0000256|SAAS:SAAS00492882, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00492882, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00492882, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00492893}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 286 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 340 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 352 377 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 433 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 445 464 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 476 496 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 675 AA; 76283 MW; 4EEC798C51D40196 CRC64; MSLSEFIERR TSFNPMVILT TLFFVCVLVV LVLTVPDQVQ MWLDRAKEVI FTEFSWFYVL TFSIFLGFLL ILSVSSLGNI RLGRDEDVPE FGFLSWLAML FAAGMGVGLM FFGVAEPLMH YFSDITAGTP EHRQQQALLH TVFHWGVHAW SVYGTIALAL AYFGFRYKLP LALRSCFYPL LKEKISGRFG DAIDIMALLA TFFGIITTLG FGASQLGAGL QEMGWIAENS FSVQVLIIAA VMSLAVVSAI SGVGKGVKVL SELNLGLAFL LLFFVLAAGP TVYLLSAFGD NIGNYLGNLV RLSFKTYAYE REHKPWFESW TVLYWAWWCS WAPFVGLFIA RISKGRTIRE FVFGVLLIPG LFGVLWFTVF GNTAIWLNDG VAGGMLEKMT SSPETLLFKF FNYLPLPELT SIVSLLVISL FFVTSADSGI YVLNNITSRD KGLSAPRWQA VMWGVLMSAV AVLLMRSGGL GNLQSMTLIV SLPFALLMLI MCFSLWKGLS ADKKYFETRV NPTSVFWTGG KWKERLVQIM SQTQEQDILK FLKQTASPAM HELQRELSEE YGLSVRVDKM FHRDEPAIEF VIRKETMRDF MYGIKSVGQD VSDQLINDGK LPHIRHQTTY KPYAYFFDGR VGYDVQYMNK DELIADILKN YERYLMLLDD VGQELMAHEQ VELAE // ID Q9JZV4_NEIMB Unreviewed; 222 AA. AC Q9JZV4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=Fimbrial protein FimT {ECO:0000313|EMBL:AAF62321.1}; GN Name=fimT {ECO:0000313|EMBL:AAF62321.1}; GN OrderedLocusNames=NMB0886 {ECO:0000313|EMBL:AAF62321.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62321.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62321.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62321.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62321.1; -; Genomic_DNA. DR RefSeq; NP_273927.1; NC_003112.2. DR RefSeq; WP_002230433.1; NC_003112.2. DR ProteinModelPortal; Q9JZV4; -. DR STRING; 122586.NMB0886; -. DR PaxDb; Q9JZV4; -. DR EnsemblBacteria; AAF62321; AAF62321; NMB0886. DR GeneID; 903005; -. DR KEGG; nme:NMB0886; -. DR PATRIC; 20357179; VBINeiMen85645_1103. DR eggNOG; ENOG4107NRK; Bacteria. DR eggNOG; COG4970; LUCA. DR HOGENOM; HOG000218893; -. DR KO; K08084; -. DR OMA; AFNHIAF; -. DR OrthoDB; EOG6Z3KHV; -. DR BioCyc; NMEN122586:GHGG-922-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro. DR InterPro; IPR012902; N_methyl_site. DR InterPro; IPR022346; T2SS_GspH. DR Pfam; PF12019; GspH; 1. DR Pfam; PF13544; N_methyl_2; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 14 32 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 44 205 GspH. {ECO:0000259|Pfam:PF12019}. SQ SEQUENCE 222 AA; 24956 MW; D63E9F04714FC4C8 CRC64; MCTRKQQGFT LTELLIVMVI AAIMAMIALP NMSQWIASRR IASHAERIAN LLRFSRGEAV RLNLPVYICP VQVKKDGTPN NKCDSGKKGQ GMLAFGDKNG NKGYDNDTED VLLRSVVLND DINDKRINYA FNHIAFGQTQ PTTDRVVWTF NQNGTFGYTK DQHLTKQSSF FYSDGYIQIV LTDAKAVSAD EKKFRSAVVL INSSGRVEVC PRGDRRTMCQ YK // ID Q9JYX0_NEIMB Unreviewed; 346 AA. AC Q9JYX0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 105. DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:AAF41759.1}; GN OrderedLocusNames=NMB1395 {ECO:0000313|EMBL:AAF41759.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41759.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41759.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41759.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361277}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|RuleBase:RU361277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41759.1; -; Genomic_DNA. DR PIR; C81088; C81088. DR RefSeq; NP_274409.1; NC_003112.2. DR RefSeq; WP_002225132.1; NC_003112.2. DR ProteinModelPortal; Q9JYX0; -. DR STRING; 122586.NMB1395; -. DR PaxDb; Q9JYX0; -. DR EnsemblBacteria; AAF41759; AAF41759; NMB1395. DR GeneID; 903817; -. DR KEGG; nme:NMB1395; -. DR PATRIC; 20358477; VBINeiMen85645_1750. DR eggNOG; ENOG4105E2A; Bacteria. DR eggNOG; COG1063; LUCA. DR HOGENOM; HOG000294694; -. DR KO; K18369; -. DR OMA; AWECARP; -. DR OrthoDB; EOG6BGP28; -. DR BioCyc; NMEN122586:GHGG-1433-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR027399; ADH_N_assoc. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF13823; ADH_N_assoc; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU361277}. SQ SEQUENCE 346 AA; 37326 MW; 32361F5E47242496 CRC64; MKAMVYHGAN DIRFEEKPRP QIIDPTDAVV KIVKTTICGT DLGIWKGKNP EVADGRILGH EGIGIVEEVG EAVKNIKVGD KVIISCVSKC CTCDNCKTQL YSHCRNGGWI LGYMIDGTQA EYVRTPYADN SLVPLPDNVN EEIALLLSDA LPTAHEIGVQ YGDVKPGDTV FIAGAGPVGM SALLTAQLYS PAAIIVCDMD ENRLKLAKEL GATHTINPAS GEVSKQVFAI VGEDGVDCAI EAVGIPATWN MCQDIVKPGG HIAVVGVHGQ SVDFKLEKLW IKKLAITTGL VNANTTEMLM KAISSSSVDY TKMLTHHFKF SELEKAYDVF KHAAENQVMK VVLEAD // ID Q9JZH2_NEIMB Unreviewed; 606 AA. AC Q9JZH2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Gamma-glutamyltranspeptidase {ECO:0000313|EMBL:AAF41454.1}; DE EC=2.3.2.2 {ECO:0000313|EMBL:AAF41454.1}; GN Name=ggt {ECO:0000313|EMBL:AAF41454.1}; GN OrderedLocusNames=NMB1057 {ECO:0000313|EMBL:AAF41454.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41454.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41454.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41454.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41454.1; -; Genomic_DNA. DR PIR; D81126; D81126. DR RefSeq; NP_274091.1; NC_003112.2. DR RefSeq; WP_002225268.1; NC_003112.2. DR ProteinModelPortal; Q9JZH2; -. DR STRING; 122586.NMB1057; -. DR PaxDb; Q9JZH2; -. DR EnsemblBacteria; AAF41454; AAF41454; NMB1057. DR GeneID; 903474; -. DR KEGG; nme:NMB1057; -. DR PATRIC; 20357655; VBINeiMen85645_1344. DR eggNOG; ENOG4105CFB; Bacteria. DR eggNOG; COG0405; LUCA. DR HOGENOM; HOG000175619; -. DR KO; K00681; -. DR OMA; STSHFVI; -. DR OrthoDB; EOG62K1RV; -. DR BioCyc; NMEN122586:GHGG-1094-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003840; F:gamma-glutamyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PANTHER; PTHR11686; PTHR11686; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR00066; g_glut_trans; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAF41454.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41454.1}. SQ SEQUENCE 606 AA; 65071 MW; 9EA5D7FCC50352C4 CRC64; MPCMNHQSNS GEGVLVAKTY LLTALIMSMT ISGCQVIHAN QGKVNTHSAV ITGADAHTPE HATGLTEQKQ VIASDFMVAS ANPLATQAGY DILKQGGSAA DAMVAVQTTL SLVEPQSSGL GGGAFVLYWD NTAKTLTTFD GRETAPMRAT PELFLDKDGQ PLKFMEAVVG GRSVGTPAIP KLMETIHQRY GVLPWGKLFD TPIRLAKQGF EVSPRLAISV EQNQQHLARY PKTAAYFLPN GVPLQAGSLL KNLEFADSVQ ALAAQGAKAL HTGKYAQNIV SVVQNAKDNP GQLSLQDLSD YQVVERPPVC VTYRIYEVCG MGAPSSGGIA VGQILGILNE FSPNQVGYDA EGLRLLGDAS RLAFADRDVY LGDPDFVPVP IRQLISKDYL KHRSQLLEQS DKALPSVSAG DFIHEWVSSQ AIELPSTSHI SIVDKAGNVL SMTTSIENAF GSTLMANGYL LNNELTDFSF EPIKQGKQVA NRVEPGKRPR SSMAPTIVFK AGKPYMAIGS PGGSRIIGYV AKTIVAHSDW NMDIQNAISA PNLLNRFGSY ELETGTTAVQ WQQALNDLGY KTDVRELNSG VQAIIIEPSR LVGGADPRRE GRVMGD // ID Q9K020_NEIMB Unreviewed; 252 AA. AC Q9K020; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41219.1}; GN OrderedLocusNames=NMB0806 {ECO:0000313|EMBL:AAF41219.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41219.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41219.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41219.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family. CC {ECO:0000256|SAAS:SAAS00568434}. CC -!- SIMILARITY: Contains S4 RNA-binding domain. CC {ECO:0000256|SAAS:SAAS00568442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41219.1; -; Genomic_DNA. DR PIR; E81155; E81155. DR RefSeq; NP_273848.1; NC_003112.2. DR RefSeq; WP_002225415.1; NC_003112.2. DR ProteinModelPortal; Q9K020; -. DR STRING; 122586.NMB0806; -. DR PaxDb; Q9K020; -. DR EnsemblBacteria; AAF41219; AAF41219; NMB0806. DR GeneID; 902921; -. DR KEGG; nme:NMB0806; -. DR PATRIC; 20356999; VBINeiMen85645_1018. DR eggNOG; ENOG4105FE9; Bacteria. DR eggNOG; COG1187; LUCA. DR HOGENOM; HOG000044956; -. DR KO; K06182; -. DR OMA; HKERIFP; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; NMEN122586:GHGG-837-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|SAAS:SAAS00485707}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 14 80 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 252 AA; 28143 MW; DBF6B8115EEBA54B CRC64; MNPKISSDHT EDAVRLSKRM AQLGLCSRRE ADGYIEQGWV TVNGKTAVLG QKVSPADRIE LNKKAHEQQA ARITILLNKP VGYVSAQAEK GYKSAAELIT PENHWEGDTG RIRFDPKHKI GLAPAGRLDI DSVGLLVLTQ DGRIAKQLIG ENSGSEKEYL VRVRGKLDEK GLALLNHGLS LDGEKLRPAQ VEWQNEDQLR FVLKQGKKRQ IRRMCELVGL RVVGLKRIRM GKVKLGRLPP GKWRYLAPGE SF // ID Q9JY54_NEIMB Unreviewed; 737 AA. AC Q9JY54; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AAF42080.1}; DE EC=2.7.6.5 {ECO:0000313|EMBL:AAF42080.1}; GN Name=relA {ECO:0000313|EMBL:AAF42080.1}; GN OrderedLocusNames=NMB1735 {ECO:0000313|EMBL:AAF42080.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42080.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42080.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42080.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5-' CC diphosphate) is a mediator of the stringent response that CC coordinates a variety of cellular activities in response to CC changes in nutritional abundance. {ECO:0000256|RuleBase:RU003847}. CC -!- SIMILARITY: Belongs to the relA/spoT family. CC {ECO:0000256|RuleBase:RU003847}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42080.1; -; Genomic_DNA. DR PIR; F81049; F81049. DR RefSeq; NP_274738.1; NC_003112.2. DR RefSeq; WP_002224958.1; NC_003112.2. DR ProteinModelPortal; Q9JY54; -. DR STRING; 122586.NMB1735; -. DR PaxDb; Q9JY54; -. DR DNASU; 903364; -. DR EnsemblBacteria; AAF42080; AAF42080; NMB1735. DR GeneID; 903364; -. DR KEGG; nme:NMB1735; -. DR PATRIC; 20359433; VBINeiMen85645_2222. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR HOGENOM; HOG000018300; -. DR KO; K00951; -. DR OMA; TEIGHNC; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; NMEN122586:GHGG-1790-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000313|EMBL:AAF42080.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42080.1}. FT DOMAIN 666 737 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 737 AA; 82558 MW; 08F373F070FC2481 CRC64; MTAISPIQDT QSATLQELRE WFDSYCAALP DNDKNLIGTA WLLAQEHYPA DAATPYGEPL PDHFLGAAQM VHELDLLPDA VAATLLADIG RYVPDWNLLV SERCNSTVAE LVKGVDEVQK LTHFARVDSL ATPEERAQQA ETMRKMLLAM VTDIRVVLIK LAMRTRTLQF LSNAPDSPEK RAVAKETLDI FAPLANRLGV WQLKWQLEDL GFRHQKPEKY REIALLLDEK RTERLEYIEN FLNILRGELK KYNVHFEVAG RPKHIYSIYK KMVKKKLSFD GLFDIRAVRI LVDTVPECYT TLGIVHSLWQ PIPGEFDDYI ANPKGNGYKS LHTVIVGPED KGVEVQIRTF DMHQFNEFGV AAHWRYKEGG KGDSAYEQKI AWLRQLLDWR ENMAESGKED LAAAFKTELF NDTIYVLTPH GKVLSLPTGA TPIDFAYALH SSIGDRCRGA KVEGQIVPLS TPLENGQRVE IITAKEGHPS VNWLYEGWVK SNKAIGKIRA YIRQQNADTV REEGRVQLDK QLAKLTPKPN LQELAENLGY KKPEDLYTAV GQGEISNRAI QKACGTLNEP PPVPVSETTI VKQSKIKKGG KNGVLIDGED GLMTTLAKCC KPAPPDDIIG FVTRERGISV HRKTCPSFQH LAEHAPEKVL DASWAALQEG QVFAVDIEIR AQDRSGLLRD VSDALARHKL NVTAVQTQSR DLEASMRFTL EVKQVNDLPR VLASLGDVKG VLSVTRL // ID Q9JYC5_NEIMB Unreviewed; 154 AA. AC Q9JYC5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Leucine-responsive regulatory protein {ECO:0000313|EMBL:AAF41999.1}; GN Name=lrp {ECO:0000313|EMBL:AAF41999.1}; GN OrderedLocusNames=NMB1650 {ECO:0000313|EMBL:AAF41999.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41999.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41999.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41999.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 3 HTH asnC-type DNA-binding domains. CC {ECO:0000256|RuleBase:RU000704}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41999.1; -; Genomic_DNA. DR PIR; A81059; A81059. DR RefSeq; NP_274655.1; NC_003112.2. DR RefSeq; WP_002216720.1; NC_003112.2. DR ProteinModelPortal; Q9JYC5; -. DR SMR; Q9JYC5; 4-153. DR STRING; 122586.NMB1650; -. DR PaxDb; Q9JYC5; -. DR EnsemblBacteria; AAF41999; AAF41999; NMB1650. DR GeneID; 903466; -. DR KEGG; nme:NMB1650; -. DR PATRIC; 20359222; VBINeiMen85645_2123. DR eggNOG; ENOG4105EW9; Bacteria. DR eggNOG; COG1522; LUCA. DR HOGENOM; HOG000115327; -. DR KO; K03719; -. DR OMA; LVFVEIK; -. DR OrthoDB; EOG6F29D2; -. DR BioCyc; NMEN122586:GHGG-1699-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000704}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000704}; KW Transcription regulation {ECO:0000256|RuleBase:RU000704}. FT DOMAIN 4 65 HTH asnC-type DNA-binding. FT {ECO:0000259|PROSITE:PS50956}. SQ SEQUENCE 154 AA; 17832 MW; FAFD9726E2B1943B CRC64; MKELDKIDFR ILKILQQNAR IPMTELAEKV GLSTTPVTER VRRLEREHYI SGYHAHLNPH LLGKPLLVFV ELKLQSKSGN IFEDFKKEVL KIPQIMECHL VSGEYDYLIK VRLPDMSAYR DMLGNILLQL PAASESRSYV VMEEVKENPV LDLD // ID Q9JYC8_NEIMB Unreviewed; 472 AA. AC Q9JYC8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Putative amino acid symporter {ECO:0000313|EMBL:AAF41996.1}; GN OrderedLocusNames=NMB1647 {ECO:0000313|EMBL:AAF41996.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41996.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41996.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41996.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU363064}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363064}. CC -!- SIMILARITY: Belongs to the sodium:alanine (SAF) symporter family. CC {ECO:0000256|RuleBase:RU363064}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41996.1; -; Genomic_DNA. DR PIR; F81058; F81058. DR RefSeq; NP_274652.1; NC_003112.2. DR RefSeq; WP_002237261.1; NC_003112.2. DR STRING; 122586.NMB1647; -. DR PaxDb; Q9JYC8; -. DR EnsemblBacteria; AAF41996; AAF41996; NMB1647. DR GeneID; 903469; -. DR KEGG; nme:NMB1647; -. DR PATRIC; 20359214; VBINeiMen85645_2119. DR eggNOG; ENOG4105BZG; Bacteria. DR eggNOG; COG1115; LUCA. DR HOGENOM; HOG000255107; -. DR KO; K03310; -. DR OMA; WMWLSAV; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NMEN122586:GHGG-1696-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR30330; PTHR30330; 1. DR Pfam; PF01235; Na_Ala_symp; 1. DR PRINTS; PR00175; NAALASMPORT. DR TIGRFAMs; TIGR00835; agcS; 1. DR PROSITE; PS00873; NA_ALANINE_SYMP; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU363064}; KW Cell membrane {ECO:0000256|RuleBase:RU363064}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Symport {ECO:0000256|RuleBase:RU363064}; KW Transmembrane {ECO:0000256|RuleBase:RU363064}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363064}; KW Transport {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 20 38 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 71 94 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 100 121 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 155 174 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 180 208 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 220 238 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 250 270 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 310 332 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 361 380 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 392 410 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 422 438 Helical. {ECO:0000256|RuleBase:RU363064}. SQ SEQUENCE 472 AA; 50465 MW; 6EAD257B41C7D68F CRC64; MENILSVLVG TVNRFLWDYL LIYALLGIGL FFTLYLGAPQ ITKLGAGFKS VFGGLFAKGD KDDKSLSQFQ ALAVAISAQI GTGNVAGVAT AITAGGPGAI FWMWVSAVLG MSTIFAEALL AQKYRVVSHG KYIGGPAFYI THGLTPKIGR GAARFLSGFF SIALIIALGF IGNATQANSI ASAVTIAFDV PSLAVGIVLA VLAGMVVIGG VNRIANIAQF VVPFMAVVYI LCAVVILFEF SDHIVPMFNH IFTAAFNPEA VLGGAAGIGM REAIRFGVAR GLFSNEAGMG STPHAHATAD VKHPVQQGMA AFVGVFIDTI LVCTATALII LLTDANLSGE QGAAVTQFAF NKAFPGFGSQ LLAVCLTFFA FTTIIGWYYF GESNIRFLFR GRHLGIYRAL VLLAIVLGTL GKVDLVWSLS DMFNGFMVIP NLIALFLLRK EIRAIYDDYL AQKKAGRDLS YQYEFHEFHD KG // ID Q9K1D9_NEIMB Unreviewed; 376 AA. AC Q9K1D9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:AAF40674.1}; GN Name=pglA {ECO:0000313|EMBL:AAF40674.1}; GN OrderedLocusNames=NMB0218 {ECO:0000313|EMBL:AAF40674.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40674.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40674.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40674.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40674.1; -; Genomic_DNA. DR PIR; F81224; F81224. DR RefSeq; NP_273275.1; NC_003112.2. DR RefSeq; WP_002221887.1; NC_003112.2. DR ProteinModelPortal; Q9K1D9; -. DR STRING; 122586.NMB0218; -. DR PaxDb; Q9K1D9; -. DR EnsemblBacteria; AAF40674; AAF40674; NMB0218. DR GeneID; 902330; -. DR KEGG; nme:NMB0218; -. DR PATRIC; 20355508; VBINeiMen85645_0278. DR eggNOG; ENOG4105CGN; Bacteria. DR eggNOG; ENOG410XNZB; LUCA. DR HOGENOM; HOG000257101; -. DR OMA; SYYREGI; -. DR OrthoDB; EOG6091DG; -. DR BioCyc; NMEN122586:GHGG-233-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13477; Glyco_trans_4_2; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40674.1}. FT DOMAIN 2 137 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13477}. FT DOMAIN 198 352 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 376 AA; 42095 MW; 02655C843D8488E7 CRC64; MKIVFITTVA SSIYGFRAPV IKKLIGKNHQ VYAFVSEFSD NELDIIREMG VTPVTYRSNR SGLNPFSDIK STFLIFKELK KISPDLVFPY FAKPVIFGTF AAKLAGVPRI VGMLEGLGFA FTPQPEGIPL KTKIIKGILI ALYRIALPML ESLIVLNPDD KDELTDKYGI KIKNIHILGG IGLDLRQYPY SEADIPDEKE PVKFLFIGRF LKEKGIDDFI RAAEQVKDKY PDTVFTALGA IDKSRGGGGD LERLAARDII RFPGFVNNVS EVIKEHHIFV LPSYYREGVP RSTQEAMAVG RAVITTDVPG CRETVADKVN GFLIEPWNPR ILAEKMIYFI ENREAVRLMG NASYAIAKDK FDAEKVDLKL LDILKA // ID Q9K051_NEIMB Unreviewed; 116 AA. AC Q9K051; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Putative type IV pilus assembly protein PilZ {ECO:0000313|EMBL:AAF41183.1}; GN OrderedLocusNames=NMB0770 {ECO:0000313|EMBL:AAF41183.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41183.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41183.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41183.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41183.1; -; Genomic_DNA. DR PIR; G81159; G81159. DR RefSeq; NP_273812.1; NC_003112.2. DR RefSeq; WP_002214009.1; NC_003112.2. DR STRING; 122586.NMB0770; -. DR PaxDb; Q9K051; -. DR EnsemblBacteria; AAF41183; AAF41183; NMB0770. DR GeneID; 902885; -. DR KEGG; nme:NMB0770; -. DR PATRIC; 20356913; VBINeiMen85645_0975. DR eggNOG; COG3215; LUCA. DR HOGENOM; HOG000290810; -. DR KO; K02676; -. DR OMA; GIFVPTQ; -. DR OrthoDB; EOG69SKDG; -. DR BioCyc; NMEN122586:GHGG-801-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro. DR InterPro; IPR009875; PilZ_domain. DR Pfam; PF07238; PilZ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 88 PilZ. {ECO:0000259|Pfam:PF07238}. SQ SEQUENCE 116 AA; 12862 MW; E9FE4F8DCAD3C9A3 CRC64; MSDGQNIPAK MMSLQLKDMN LLYSSYMPFL EHGGLFVQTN DVFSIGDDIL LAVEILNFPK LFLPTKVAWI NPARTSSKPK GVGLAFTKHE NCLKVKDQIE VELGNTIGGS RPTFTM // ID Q9JY17_NEIMB Unreviewed; 680 AA. AC Q9JY17; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|RuleBase:RU363016}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363016}; GN Name=recG {ECO:0000256|RuleBase:RU363016, GN ECO:0000313|EMBL:AAF42127.1}; GN OrderedLocusNames=NMB1788 {ECO:0000313|EMBL:AAF42127.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42127.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42127.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42127.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Critical role in recombination and DNA repair. Helps CC process Holliday junction intermediates to mature products by CC catalyzing branch migration. Has a DNA unwinding activity CC characteristic of a DNA helicase with a 3'- to 5'- polarity. CC Unwinds branched duplex DNA (Y-DNA). CC {ECO:0000256|RuleBase:RU363016}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|RuleBase:RU363016}. CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily. CC {ECO:0000256|RuleBase:RU363016}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|RuleBase:RU363016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42127.1; -; Genomic_DNA. DR PIR; E81043; E81043. DR RefSeq; NP_274787.1; NC_003112.2. DR RefSeq; WP_002225638.1; NC_003112.2. DR ProteinModelPortal; Q9JY17; -. DR STRING; 122586.NMB1788; -. DR PaxDb; Q9JY17; -. DR EnsemblBacteria; AAF42127; AAF42127; NMB1788. DR GeneID; 903311; -. DR KEGG; nme:NMB1788; -. DR PATRIC; 20359541; VBINeiMen85645_2276. DR eggNOG; ENOG4105CB5; Bacteria. DR eggNOG; COG1200; LUCA. DR HOGENOM; HOG000036617; -. DR KO; K03655; -. DR OMA; YEDETRI; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; NMEN122586:GHGG-1843-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033454; RecG_wedge. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF17191; RecG_wedge; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00643; recG; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAF42127.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|RuleBase:RU363016}; KW DNA recombination {ECO:0000256|RuleBase:RU363016}; KW DNA repair {ECO:0000256|RuleBase:RU363016}; KW Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:AAF42127.1}; KW Hydrolase {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAF42127.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAF42127.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 275 436 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 469 615 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 680 AA; 74860 MW; EEAF31D21CF80AE1 CRC64; MMSPETRKQL KITDVSAKKL DKLNLHTAWD LVLHLPLRYE DETHIMPIKD APIGVPCQVE GEVIHQEVTF KPRKQLIVQI ADGSGSVLFL RFIHFYASHQ KQTAVGKRIR AVGEIKHGFY GDEMIHPKIR DAEGGGLAES LTPVYPTVNG LNQPTLRRII QTALDVTPLH DTLPDALLCR LKLPHLAESL RLLHSPPPSF TIHQLSDGTL PAWQRLKFDE LLAQQLSMRL ARQKRIGGTA AALGGDGTLT QALRQALPFA LTDAQEKVVS EICRDMAQTY PMHRLLQGDV GSGKTIVAAL SALTAIESGA QVAVMAPTEI LAEQHFIKFK QWLEPLGIEV VRLFGSLRKK AKDEAKAKLA DGSVKIAVGT HALFSDGVAF HNLGLTIVDE QHRFGVAQRL ALKNKGREVH QLMMSATPIP RTLAMSFFAD LDVSVIDELP PGRTPIKTRL VNNVRRAEVE GFVLGTCRKG RQAYWVCPLI EESETLQLQT AAETLARLQT ALPELNIGLV HGRMKAAEKA EVMARFSSGG LNVLVATTVI EVGVDVPNAA LMVIEHAERM GLAQLHQLRG RVGRGAAESV CVLLFAEPLG ELAKARLKVI YEHTDGFEIA RQDLNIRGPG EFLGARQSGV PMLRFAKLEE DLHLLEQARE TAPMLIEQNP EIVEAHLARW LSGREGYLGV // ID Q9K1K5_NEIMB Unreviewed; 419 AA. AC Q9K1K5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|SAAS:SAAS00013752}; DE EC=2.1.1.- {ECO:0000256|SAAS:SAAS00500186}; GN Name=rsmB {ECO:0000313|EMBL:AAF40571.1}; GN OrderedLocusNames=NMB0112 {ECO:0000313|EMBL:AAF40571.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40571.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40571.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40571.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00013721}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RsmB/NOP family. CC {ECO:0000256|SAAS:SAAS00546407}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40571.1; -; Genomic_DNA. DR PIR; B81236; B81236. DR RefSeq; NP_273170.1; NC_003112.2. DR RefSeq; WP_002224763.1; NC_003112.2. DR ProteinModelPortal; Q9K1K5; -. DR STRING; 122586.NMB0112; -. DR PaxDb; Q9K1K5; -. DR EnsemblBacteria; AAF40571; AAF40571; NMB0112. DR GeneID; 902216; -. DR KEGG; nme:NMB0112; -. DR PATRIC; 20355237; VBINeiMen85645_0152. DR eggNOG; ENOG4105CYJ; Bacteria. DR eggNOG; COG0144; LUCA. DR HOGENOM; HOG000037300; -. DR KO; K03500; -. DR OMA; LRVNRQH; -. DR OrthoDB; EOG6091D0; -. DR BioCyc; NMEN122586:GHGG-118-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.940.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR InterPro; IPR023267; RCMT. DR InterPro; IPR004573; rRNA_ssu_MeTfrase_B. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR Pfam; PF01029; NusB; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF48013; SSF48013; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00563; rsmB; 1. DR PROSITE; PS01153; NOL1_NOP2_SUN; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00423093}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00500183, KW ECO:0000313|EMBL:AAF40571.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|SAAS:SAAS00500180}; KW rRNA processing {ECO:0000256|SAAS:SAAS00423078}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00500162}; KW Transferase {ECO:0000256|SAAS:SAAS00500183, KW ECO:0000313|EMBL:AAF40571.1}. FT DOMAIN 164 419 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. SQ SEQUENCE 419 AA; 46310 MW; 61CC2E7C72BEF450 CRC64; MSMALAQKLA ADSIAAVAEG RNLQDVLAQI RTAHPDLMAQ ENGALQDIAY GCQRYLGSLK HMLAQMLKKP IGNPQLESLL LAALYQLHYT RNAPHAVVNE AVESIAKIGR GQYRSFANAV LRRFLRERDK LVASCKKDDV AKHNLPLWWV AYLKNHYPKH WHNIAAALQS HPPMTLRVNR RHGNAESYLE KLVAEGIAAK ALDEYAVTLE EAVPVNRLPG FSDGIVSVQD FGAQQAAYLL NPKDGERILD ACAAPGGKTG HILELADCRV TALDIDAGRL KRVEDNIARL GFQTASTACA DAQDLSAWYD GKPFDAVLAD VPCTASGVAR RNPDVKWLRR PTDALKTARQ QEALLDALWQ VLKSGGRMLI ATCSVFVEEN DGQLQKFLNR HADAELIESR VLLPNKHQDG FYYALIQKQ // ID Q9JY84_NEIMB Unreviewed; 81 AA. AC Q9JY84; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Acyl carrier protein {ECO:0000313|EMBL:AAF42044.1}; GN Name=acp-2 {ECO:0000313|EMBL:AAF42044.1}; GN OrderedLocusNames=NMB1696 {ECO:0000313|EMBL:AAF42044.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42044.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42044.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42044.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42044.1; -; Genomic_DNA. DR PIR; B81052; B81052. DR RefSeq; NP_274700.1; NC_003112.2. DR RefSeq; WP_002222119.1; NC_003112.2. DR ProteinModelPortal; Q9JY84; -. DR STRING; 122586.NMB1696; -. DR PaxDb; Q9JY84; -. DR EnsemblBacteria; AAF42044; AAF42044; NMB1696. DR GeneID; 903408; -. DR KEGG; nme:NMB1696; -. DR PATRIC; 20359349; VBINeiMen85645_2181. DR eggNOG; ENOG4105WBY; Bacteria. DR eggNOG; COG0236; LUCA. DR HOGENOM; HOG000178184; -. DR KO; K02078; -. DR OMA; DHIKRQT; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; NMEN122586:GHGG-1751-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.1200.10; -; 1. DR InterPro; IPR009081; PP-bd_ACP. DR Pfam; PF00550; PP-binding; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 76 Acyl carrier. FT {ECO:0000259|PROSITE:PS50075}. SQ SEQUENCE 81 AA; 9506 MW; AB40942AFB729A22 CRC64; MTEQEIYRLL RDTLTELFEI EPERITPDTN LYEDLEIDSI DAIDLIDRIK RETGRKLQAE DFRNVRTVND VVQAVLKIQA G // ID Q9JYN6_NEIMB Unreviewed; 405 AA. AC Q9JYN6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448}; GN Name=lysC {ECO:0000313|EMBL:AAF41854.1}; GN OrderedLocusNames=NMB1498 {ECO:0000313|EMBL:AAF41854.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41854.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41854.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41854.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2RE1} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 242-405. RA Chang C., Li H., Gu M., Joachimiak A.; RT "Crystal structure of aspartokinase alpha and beta subunits."; RL Submitted (SEP-2007) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. {ECO:0000256|RuleBase:RU003448}. CC -!- SIMILARITY: Belongs to the aspartokinase family. CC {ECO:0000256|RuleBase:RU003448}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41854.1; -; Genomic_DNA. DR PIR; F81076; F81076. DR RefSeq; NP_274506.1; NC_003112.2. DR RefSeq; WP_002225078.1; NC_003112.2. DR PDB; 2RE1; X-ray; 2.75 A; A/B=242-405. DR PDBsum; 2RE1; -. DR ProteinModelPortal; Q9JYN6; -. DR SMR; Q9JYN6; 246-404. DR STRING; 122586.NMB1498; -. DR PaxDb; Q9JYN6; -. DR EnsemblBacteria; AAF41854; AAF41854; NMB1498. DR GeneID; 903923; -. DR KEGG; nme:NMB1498; -. DR PATRIC; 20358776; VBINeiMen85645_1898. DR eggNOG; ENOG4105CFH; Bacteria. DR eggNOG; COG0527; LUCA. DR HOGENOM; HOG000293093; -. DR KO; K00928; -. DR OMA; INIMMIS; -. DR OrthoDB; EOG6NSGHC; -. DR BioCyc; NMEN122586:GHGG-1538-MONOMER; -. DR EvolutionaryTrace; Q9JYN6; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase_dom. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR027795; GATS-like_ACT_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR PIRSF; PIRSF000726; Asp_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 2. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2RE1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AAF41854.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003448, KW ECO:0000313|EMBL:AAF41854.1}. FT DOMAIN 266 340 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 346 405 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 405 AA; 43412 MW; FADF39E71DF3C9F7 CRC64; MALIVHKYGG TSVGSPERIK NVAKRVAKAR AEGHDIVVVV SAMSGETNRL VALAHEMQEH PDPRELDVVL ATGEQVTIGL LAMALKDIGV DAKSYTGWQV ALKTDTAHTK ARIESIDDEK MRADLTAGKV VIVAGFQGIS SEGDISTLGR GGSDTSAVAL AAALKADECQ IYTDVDGVYT TDPRVVPEAR RMDTVTFEEM IELASLGSKV LQIRSVEFAG KYKVRLRVLS SLQDGGNGTL ITFEEDDNME RAAVTGIAFD KNQARINVRG VPDKPGVAYQ ILGAVADANI EVDMIIQNVG SEGTTDFSFT VPRGDYKQTL EILSERQDSI GAASIDGDDT VCKVSAVGLG MRSHVGVAAK IFRTLAEEGI NIQMISTSEI KVSVLIDEKY MELATRVLHK AFNLG // ID Q9JZF5_NEIMB Unreviewed; 222 AA. AC Q9JZF5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=DnaA-related protein {ECO:0000313|EMBL:AAF41471.1}; GN OrderedLocusNames=NMB1076 {ECO:0000313|EMBL:AAF41471.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41471.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41471.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41471.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2KJQ} RP STRUCTURE BY NMR OF 12-149. RA Wu Y., Maglaqui M., Eletsky A., Ciccosanti C., Sathyamoorthy B., RA Jiang M., Garcia E., Nair R., Rost B., Swapna G., Acton T., Xiao R., RA Everett J., Montelione G.T., Szyperski T.; RT "Solution Structure Of Protein NMB1076 From Neisseria meningitidis. RT Northeast Structural Genomics Consortium Target MR101B."; RL Submitted (JUN-2009) to the PDB data bank. CC -!- SIMILARITY: Belongs to the DnaA family. CC {ECO:0000256|SAAS:SAAS00555179}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41471.1; -; Genomic_DNA. DR PIR; G81124; G81124. DR RefSeq; NP_274109.1; NC_003112.2. DR RefSeq; WP_002213636.1; NC_003112.2. DR PDB; 2KJQ; NMR; -; A=12-149. DR PDBsum; 2KJQ; -. DR ProteinModelPortal; Q9JZF5; -. DR STRING; 122586.NMB1076; -. DR PaxDb; Q9JZF5; -. DR EnsemblBacteria; AAF41471; AAF41471; NMB1076. DR GeneID; 903495; -. DR KEGG; nme:NMB1076; -. DR PATRIC; 20357709; VBINeiMen85645_1371. DR eggNOG; ENOG4108KZ1; Bacteria. DR eggNOG; COG0593; LUCA. DR HOGENOM; HOG000256538; -. DR KO; K10763; -. DR OMA; GWGLVYQ; -. DR OrthoDB; EOG6038W4; -. DR BioCyc; NMEN122586:GHGG-1113-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013317; DnaA. DR InterPro; IPR017788; Hda. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00308; Bac_DnaA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03420; DnaA_homol_Hda; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2KJQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 83 198 Bac_DnaA. {ECO:0000259|Pfam:PF00308}. SQ SEQUENCE 222 AA; 25427 MW; ECB0D2AA88FC9086 CRC64; MNQLIFDFAA HDYPSFDKFL GTENAELVYV LRHKHGQFIY VWGEEGAGKS HLLQAWVAQA LEAGKNAAYI DAASMPLTDA AFEAEYLAVD QVEKLGNEEQ ALLFSIFNRF RNSGKGFLLL GSEYTPQQLV IREDLRTRMA YCLVYEVKPL TDQEKIDALA SMAAARQVTV DSEIFEYLLK HWRRDMDSLM MMLDTLDNYA VTMGKRITLP LLRQLLKQQE TQ // ID Q9K056_NEIMB Unreviewed; 339 AA. AC Q9K056; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042}; DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042}; GN Name=lepB {ECO:0000313|EMBL:AAF41178.1}; GN OrderedLocusNames=NMB0765 {ECO:0000313|EMBL:AAF41178.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41178.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41178.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41178.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or CC leader sequences from secreted and periplasmic proteins. CC {ECO:0000256|RuleBase:RU362042}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; CC Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU362042}. CC -!- SIMILARITY: Belongs to the peptidase S26 family. CC {ECO:0000256|RuleBase:RU362042}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU362042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41178.1; -; Genomic_DNA. DR PIR; B81162; B81162. DR RefSeq; NP_273807.1; NC_003112.2. DR RefSeq; WP_002244066.1; NC_003112.2. DR ProteinModelPortal; Q9K056; -. DR STRING; 122586.NMB0765; -. DR MEROPS; S26.001; -. DR PaxDb; Q9K056; -. DR EnsemblBacteria; AAF41178; AAF41178; NMB0765. DR GeneID; 902880; -. DR KEGG; nme:NMB0765; -. DR PATRIC; 20356903; VBINeiMen85645_0970. DR eggNOG; ENOG4105C3F; Bacteria. DR eggNOG; COG0681; LUCA. DR HOGENOM; HOG000003674; -. DR KO; K03100; -. DR OMA; NTDMFRS; -. DR OrthoDB; EOG6KDKTM; -. DR BioCyc; NMEN122586:GHGG-796-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro. DR Gene3D; 2.10.109.10; -; 2. DR InterPro; IPR000223; Pept_S26A_signal_pept_1. DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR019533; Peptidase_S26. DR PANTHER; PTHR12383; PTHR12383; 2. DR Pfam; PF00717; Peptidase_S24; 1. DR Pfam; PF10502; Peptidase_S26; 1. DR PRINTS; PR00727; LEADERPTASE. DR SUPFAM; SSF51306; SSF51306; 1. DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1. DR PROSITE; PS00760; SPASE_I_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU362042}; KW Membrane {ECO:0000256|RuleBase:RU362042}; KW Protease {ECO:0000256|RuleBase:RU362042}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362042}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}. FT TRANSMEM 39 71 Helical. {ECO:0000256|RuleBase:RU362042}. FT TRANSMEM 92 113 Helical. {ECO:0000256|RuleBase:RU362042}. FT DOMAIN 118 200 Peptidase_S24. FT {ECO:0000259|Pfam:PF00717}. FT DOMAIN 287 323 Peptidase_S26. FT {ECO:0000259|Pfam:PF10502}. SQ SEQUENCE 339 AA; 37662 MW; 676D03135F93E56D CRC64; MNTMLMSGAA AALLAGIILY FKSDKKRQEN GEWSSGLEYA YILTAVGVFA ALSLFMSFTA VFLIFVVLCG TAWGVYKYRL KTHPEISESS HFGDYFGSFF PTVLVLFLIR SFIAEPFQIP SSSMRPGLIK GDFILVGKFS YGLRVPVLNN IFIPTGKIER GDVVVFNYPL QPEMTYIKRI VGIPGDVVEY RDKILTVNGK PTSDIPDGTY RYPDDTDPSE IHNTDMFRSG LDGKSFNILK KEGQPAVSLP VLGKYTSDIM SENGYSIEQS GLEHCQYADD GSGFVCKVPE GRYFAMGDNR DNSADSRYWG FVDDKLVVGK AMFILMNFGD FGRSGTAIR // ID Q9K0X3_NEIMB Unreviewed; 868 AA. AC Q9K0X3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Aconitate hydratase 1 {ECO:0000313|EMBL:AAF40871.1}; DE EC=4.2.1.3 {ECO:0000313|EMBL:AAF40871.1}; GN Name=acnA {ECO:0000313|EMBL:AAF40871.1}; GN OrderedLocusNames=NMB0433 {ECO:0000313|EMBL:AAF40871.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40871.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40871.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40871.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40871.1; -; Genomic_DNA. DR PIR; C81200; C81200. DR RefSeq; NP_273481.1; NC_003112.2. DR RefSeq; WP_002224931.1; NC_003112.2. DR ProteinModelPortal; Q9K0X3; -. DR STRING; 122586.NMB0433; -. DR PaxDb; Q9K0X3; -. DR PRIDE; Q9K0X3; -. DR EnsemblBacteria; AAF40871; AAF40871; NMB0433. DR GeneID; 902549; -. DR KEGG; nme:NMB0433; -. DR PATRIC; 20356066; VBINeiMen85645_0548. DR eggNOG; ENOG4108I0Z; Bacteria. DR eggNOG; COG1048; LUCA. DR HOGENOM; HOG000025703; -. DR KO; K01681; -. DR OMA; CSASTRW; -. DR OrthoDB; EOG67DPHM; -. DR BioCyc; NMEN122586:GHGG-457-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR PANTHER; PTHR11670; PTHR11670; 2. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF52016; SSF52016; 1. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR02333; 2met_isocit_dHY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF40871.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 73 539 Aconitase. {ECO:0000259|Pfam:PF00330}. FT DOMAIN 661 792 Aconitase_C. {ECO:0000259|Pfam:PF00694}. SQ SEQUENCE 868 AA; 95097 MW; 1179C795F538B037 CRC64; MAANQRYRKP LPGTDLEYYD ARAACEDIKP GSYDKLPYTS RILAENLVNR ADKVDLPTLQ SWLGQLIEGK QEIDFPWYPA RVVCHDILGQ TALVDLAGLR DAIAEKGGDP AKVNPVVQTQ LIVDHSLAVE CGGYDPDAFR KNREIEDRRN EDRFHFINWT KTAFENVDVI PAGNGIMHQI NLEKMSPVVQ VKNGVAFPDT CVGTDSHTPH VDSLGVISVG VGGLEAETVM LGRASMMRLP DIVGVELNGK RQAGITATDI VLALTEFLRK ERVVGAFVEF FGEGARSLSI GDRATISNMT PEFGATAAMF AIDEQTIDYL KLTGRDDAQV KLVETYAKTA GLWADALKTA VYPRVLKFDL SSVTRNMAGP SNPHARFATA DLAAKGLAKP YEEPSDGQMP DGSVIIAAIT SCTNTSNPRN VVAAALLARN ANRLGLKRKP WVKSSFAPGS KVAEIYLKEA GLLPEMEKLG FGIVAFACTT CNGMSGALDP KIQKEIIDRD LYATAVLSGN RNFDGRIHPY AKQAFLASPP LVVAYALAGS IRFDIENDVL GVADGKEIRL KDIWPADEEI DAVVAEYVKP QQFRDVYVPM FDTGTAQKAP SPLYDWRPMS TYIRRPPYWE GALAGERTLR GMRPLAILPD NITTDHLSPS NAILAVSAAG EYLAKMGLPE EDFNSYATHR GDHLTAQRAT FANPKLFNEM VKNEDGSVRQ GSFARVEPEG ETMRMWEAIE TYMNRKQPLI IIAGADYGQG SSRDWAAKGV RLAGVEAIVA EGFERIHRTN LIGMGVLPLQ FKPDTNRHTL QLDGTETYDV VGERTPRCDL TLVIHRKNGE TVEVPVTCCL DTAEEVLVYE AGGVLQRFAQ DFLEGNAA // ID Q7DD92_NEIMB Unreviewed; 213 AA. AC Q7DD92; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=GDSL lipase family protein {ECO:0000313|EMBL:AAF42023.1}; GN OrderedLocusNames=NMB1674 {ECO:0000313|EMBL:AAF42023.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42023.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42023.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42023.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42023.1; -; Genomic_DNA. DR PIR; D81057; D81057. DR RefSeq; NP_274679.1; NC_003112.2. DR RefSeq; WP_002220465.1; NC_003112.2. DR ProteinModelPortal; Q7DD92; -. DR STRING; 122586.NMB1674; -. DR PaxDb; Q7DD92; -. DR EnsemblBacteria; AAF42023; AAF42023; NMB1674. DR GeneID; 903436; -. DR KEGG; nme:NMB1674; -. DR PATRIC; 20359290; VBINeiMen85645_2153. DR eggNOG; ENOG4108UJV; Bacteria. DR eggNOG; COG2755; LUCA. DR HOGENOM; HOG000261382; -. DR OMA; KPMNRRI; -. DR OrthoDB; EOG6PGK4B; -. DR BioCyc; NMEN122586:GHGG-1728-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.1110; -; 1. DR InterPro; IPR013830; SGNH_hydro. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF13472; Lipase_GDSL_2; 1. DR SUPFAM; SSF52266; SSF52266; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 43 198 SGNH_hydro. {ECO:0000259|Pfam:PF13472}. SQ SEQUENCE 213 AA; 22955 MW; 9AABEB3BB02FA8FD CRC64; MPSEKPMNRR TFLLGAGALL LTACGRKSAR THAKIPEGST VLALGDSLTF GYGANPGESY PAQLQKLTGW NIVNGGVSGD TSAQALSRLP ALLARKPKLV IVGIGGNDFL RKVPKEQTRA NIAKIIETVQ KENIPAVLVG VPHITLGALF GHLSDHPLYE DLSEEYGIPL FGGAWAEILG DNNLKSDQIH ANGKGYRKFA EDLNQFLRKQ GFR // ID Q9K099_NEIMB Unreviewed; 96 AA. AC Q9K099; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62320.1}; GN OrderedLocusNames=NMB0716 {ECO:0000313|EMBL:AAF62320.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62320.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62320.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62320.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62320.1; -; Genomic_DNA. DR RefSeq; NP_273758.1; NC_003112.2. DR RefSeq; WP_002222762.1; NC_003112.2. DR PaxDb; Q9K099; -. DR EnsemblBacteria; AAF62320; AAF62320; NMB0716. DR GeneID; 902828; -. DR KEGG; nme:NMB0716; -. DR PATRIC; 20356783; VBINeiMen85645_0913. DR HOGENOM; HOG000218850; -. DR OMA; QESVECG; -. DR OrthoDB; EOG6RZB2N; -. DR BioCyc; NMEN122586:GHGG-744-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 96 AA; 10320 MW; 94D5054722C0FBC9 CRC64; MAKYFTETGI SVREHFDFFG EFVVSPAARS GDLALTYGLR LEAGEEGLSL AELFDKRSDS QEPVEGGRID IGGFMLTAKE VDGGGNIGSM GLKVLR // ID Q9K1P1_NEIMB Unreviewed; 237 AA. AC Q9K1P1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Putative hydrolase {ECO:0000313|EMBL:AAF40511.1}; GN OrderedLocusNames=NMB0040 {ECO:0000313|EMBL:AAF40511.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40511.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40511.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40511.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40511.1; -; Genomic_DNA. DR PIR; B81245; B81245. DR ProteinModelPortal; Q9K1P1; -. DR STRING; 122586.NMB0040; -. DR PaxDb; Q9K1P1; -. DR EnsemblBacteria; AAF40511; AAF40511; NMB0040. DR PATRIC; 20355037; VBINeiMen85645_0055. DR eggNOG; ENOG4107I2D; Bacteria. DR eggNOG; COG1011; LUCA. DR HOGENOM; HOG000266042; -. DR OMA; KSHALPF; -. DR OrthoDB; EOG6Z0Q8F; -. DR BioCyc; NMEN122586:GHGG-41-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR010237; Pyr-5-nucltdase. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR01993; Pyr-5-nucltdase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF40511.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 187 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 237 AA; 26837 MW; E9059942D1D907D5 CRC64; MQENPTVWLF DLDNTLHDAD AGIFTLINRA MTRYMARRLK LSESAASDLR QDYWHRYGAT LAGLQIHHPE IDIAEFLRES HPIDAILTRL HGMPETQNTL SRLKGRKAVF SNGPSFYVRA VVNALGLENR FDALFGTDDF GLLYKPNPQA YLNVCRLLDV PPECCIMVDD SADNLHQAKA LGMKTVRFGA KSHALPFIDA SVSDMAQLAR YAETLSEHRQ NHYNTPYPPK IRKKSHA // ID Q9K077_NEIMB Unreviewed; 479 AA. AC Q9K077; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|SAAS:SAAS00035571}; GN OrderedLocusNames=NMB0741 {ECO:0000313|EMBL:AAF41154.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41154.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41154.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41154.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5- CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble CC position (U34) in tRNA. Catalyzes the FAD-dependent demodification CC of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a CC methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form CC mnm(5)s(2)U34. {ECO:0000256|SAAS:SAAS00035574}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA containing 5- CC aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA CC containing 5-methylaminomethyl-2-thiouridylate. CC {ECO:0000256|SAAS:SAAS00035555}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00035593}. CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family. CC {ECO:0000256|SAAS:SAAS00548796}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC methyltransferase superfamily. tRNA (mnm(5)s(2)U34)- CC methyltransferase family. {ECO:0000256|SAAS:SAAS00548795}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41154.1; -; Genomic_DNA. DR PIR; D81162; D81162. DR RefSeq; NP_273783.1; NC_003112.2. DR RefSeq; WP_010980833.1; NC_003112.2. DR ProteinModelPortal; Q9K077; -. DR STRING; 122586.NMB0741; -. DR PaxDb; Q9K077; -. DR EnsemblBacteria; AAF41154; AAF41154; NMB0741. DR GeneID; 902856; -. DR KEGG; nme:NMB0741; -. DR PATRIC; 20356853; VBINeiMen85645_0945. DR eggNOG; ENOG4108BYJ; Bacteria. DR eggNOG; COG0665; LUCA. DR HOGENOM; HOG000218856; -. DR OMA; HPSCGLY; -. DR OrthoDB; EOG61P6QH; -. DR BioCyc; NMEN122586:GHGG-772-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR03197; MnmC_Cterm; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00433914}; KW FAD {ECO:0000256|SAAS:SAAS00433920}; KW Flavoprotein {ECO:0000256|SAAS:SAAS00433920}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00433928}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00433927}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00433923}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00433924}; KW Transferase {ECO:0000256|SAAS:SAAS00433928}; KW tRNA processing {ECO:0000256|SAAS:SAAS00433926}. FT DOMAIN 71 444 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 479 AA; 52792 MW; 5CB4D7D11A5BE367 CRC64; MQCLQFDSIN LIEHILPDVR FWLVPPSRTH HLHEHFHHIS WQTEAIPQTE SKPDKPWFAL PQTSERQKPE HILVIGAGIS GAATAHALAS HGISVTVLEA RKAAQAASGN RQGLLYAKIS PHDTEQTELL LAGYGYTKRL LGHILPESET WGGNGIIHLN YSRTEQQRNH ELGLQKHHNH LYRSITSAEA EKIAGIPLSV PYDHPSCGLY WQHGVWLNPP AFVRTLLNHP LIGLHEDTPL TDISHDGEKW IASTPNGTFT ATHIIYCTGA NSPYLPETNL AALPLRQIRG QTGLTPSTPF SEQLRCAVSG ESYISPSWHG LHCYGASFIP NSSHTGWNEA EEASNRQALA HLNPALSESL FAANPNPQKH QGHAAIRCDS PDHLPLVGAL GDIAAMRQTY TKLALDKNYR IDTPCPYLPN AYVNTAHGTR GLATAPICAA AIAAQILGLP HPFSQRLRHA LHPNRTIIRA IVRRKDLTP // ID Q9K034_NEIMB Unreviewed; 220 AA. AC Q9K034; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Amino acid ABC transporter, permease protein {ECO:0000313|EMBL:AAF41201.1}; GN OrderedLocusNames=NMB0788 {ECO:0000313|EMBL:AAF41201.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41201.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41201.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41201.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00561696}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41201.1; -; Genomic_DNA. DR PIR; A81159; A81159. DR RefSeq; NP_273830.1; NC_003112.2. DR RefSeq; WP_010980845.1; NC_003112.2. DR STRING; 122586.NMB0788; -. DR PaxDb; Q9K034; -. DR EnsemblBacteria; AAF41201; AAF41201; NMB0788. DR GeneID; 902903; -. DR KEGG; nme:NMB0788; -. DR PATRIC; 20356963; VBINeiMen85645_1000. DR eggNOG; ENOG4105E5Q; Bacteria. DR eggNOG; COG0765; LUCA. DR HOGENOM; HOG000267552; -. DR KO; K10009; -. DR OMA; IYWCFCW; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NMEN122586:GHGG-819-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00450258}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450258, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450217}. FT TRANSMEM 12 38 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 50 78 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 186 206 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 14 207 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 220 AA; 24149 MW; 9765D1D9703F015A CRC64; MIVSAFLPMV KAGFAVSLPL AAASFVIGMM IAVAVALVRI MPAGGIVRKI LLKLVEFYIS VIRGTPLLVQ LVIVFYGLPS VGIYIDPIPA AIIGFSLNVG AYASETIRAA ILSVPKGQWE AGFSIGMTYM QTFRRIVAPQ AFRVAVPPLS NEFIGLFKNT SLAAVVTVTE LFRVAQETAN RTYDFLPVYI EAALVYWCFC KVLFLIQARL EKRFDRYVAK // ID Q9K1D3_NEIMB Unreviewed; 397 AA. AC Q9K1D3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40683.1}; GN OrderedLocusNames=NMB0227 {ECO:0000313|EMBL:AAF40683.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40683.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40683.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40683.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the NRAMP family. CC {ECO:0000256|SAAS:SAAS00588612}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40683.1; -; Genomic_DNA. DR PIR; E81223; E81223. DR RefSeq; NP_273284.1; NC_003112.2. DR RefSeq; WP_002215592.1; NC_003112.2. DR STRING; 122586.NMB0227; -. DR PaxDb; Q9K1D3; -. DR EnsemblBacteria; AAF40683; AAF40683; NMB0227. DR GeneID; 902339; -. DR KEGG; nme:NMB0227; -. DR PATRIC; 20355530; VBINeiMen85645_0289. DR eggNOG; ENOG4105C5A; Bacteria. DR eggNOG; COG1914; LUCA. DR HOGENOM; HOG000138596; -. DR OMA; GFITQTA; -. DR OrthoDB; EOG6V1M34; -. DR BioCyc; NMEN122586:GHGG-242-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001046; NRAMP_fam. DR InterPro; IPR006311; TAT_signal. DR PANTHER; PTHR11706; PTHR11706; 1. DR Pfam; PF01566; Nramp; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00482029}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00482029, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 100 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 206 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310 326 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 332 355 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 367 392 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 397 AA; 41219 MW; 380E7EAE1FACC208 CRC64; MSDQKNRRNA LIGAAFLMAT SAIGPGFLTQ TATFTQALAA SFGFVILLSI LLDIGAQLNI WRIVAVSEKQ AQDIANQVLP GAGYFLAVLI VMGGLAFNIG NVGGAGLGLN LLTGLSPETG AVISGVIAIG VFLFKEAGKV MDKFAQVMGF VMIALTVYVA WQANPPLADA AVHTFMPEKL DAMAIVTLVG GTVGGYITFA GAHRLLDAGI KGKSALPEVS QSSVRAILIA SIMRIVLFLA VLGVVSQGVQ LNPDNPASTP FEYAAGYIGL LIFGVVIWAA SITSVIGAAY TSVSFFSGLS PSIERNKNKW IIAFIAVSTA VFSTIGKPAQ VLVFVGALNG LILPISLGLI LIAAYKTKIV GDYKHPLWLT VSGVIVVGLM AVLSAITISK YIGGLFG // ID Q9JXF0_NEIMB Unreviewed; 168 AA. AC Q9JXF0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Aut protein {ECO:0000313|EMBL:AAF42395.1}; GN Name=aut {ECO:0000313|EMBL:AAF42395.1}; GN OrderedLocusNames=NMB2076 {ECO:0000313|EMBL:AAF42395.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42395.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42395.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42395.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D- CC manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno- CC heptose. {ECO:0000256|SAAS:SAAS00558028}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate + CC ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate. CC {ECO:0000256|SAAS:SAAS00054936}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4. CC {ECO:0000256|SAAS:SAAS00054951}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42395.1; -; Genomic_DNA. DR PIR; C81009; C81009. DR RefSeq; NP_275066.1; NC_003112.2. DR RefSeq; WP_002223191.1; NC_003112.2. DR ProteinModelPortal; Q9JXF0; -. DR STRING; 122586.NMB2076; -. DR PaxDb; Q9JXF0; -. DR EnsemblBacteria; AAF42395; AAF42395; NMB2076. DR GeneID; 903988; -. DR KEGG; nme:NMB2076; -. DR PATRIC; 20360312; VBINeiMen85645_2656. DR eggNOG; ENOG4107Z67; Bacteria. DR eggNOG; COG2870; LUCA. DR HOGENOM; HOG000284154; -. DR OMA; RGHATYL; -. DR OrthoDB; EOG68Q0W4; -. DR BioCyc; NMEN122586:GHGG-2139-MONOMER; -. DR UniPathway; UPA00356; UER00439. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR011914; RfaE_dom_II. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR02199; rfaE_dom_II; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00444127}; KW Carbohydrate metabolism {ECO:0000256|SAAS:SAAS00444124}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00444127}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00444162}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00444162}. FT DOMAIN 34 128 CTP_transf_like. FT {ECO:0000259|Pfam:PF01467}. SQ SEQUENCE 168 AA; 17798 MW; C99B06029661D652 CRC64; MVDAWSVPDF ESKICPPEAL AARLALLPRP LVFTNGCFDI LHRGHVTYLA QARSMGDALV LALNTDASVR RLGKGGDRPV NPLENRAAVA AALESVDLVT WFDGDTPAAL IEAVKPEILV KGGDWAADKI VGAAETLARG GQVFSIPFLH QTSTTKTLAK IRAAEGGK // ID Q9JXS8_NEIMB Unreviewed; 367 AA. AC Q9JXS8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=DNA polymerase III subunit beta {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00018186}; DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00018259}; GN Name=dnaN {ECO:0000313|EMBL:AAF42232.1}; GN OrderedLocusNames=NMB1902 {ECO:0000313|EMBL:AAF42232.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42232.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42232.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42232.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. CC This DNA polymerase also exhibits 3' to 5' exonuclease activity. CC The beta chain is required for initiation of replication once it CC is clamped onto DNA, it slides freely (bidirectional and ATP- CC independent) along duplex DNA. {ECO:0000256|PIRNR:PIRNR000804}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|PIRNR:PIRNR000804, CC ECO:0000256|SAAS:SAAS00018252}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000804, CC ECO:0000256|SAAS:SAAS00346815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42232.1; -; Genomic_DNA. DR PIR; C81030; C81030. DR RefSeq; NP_274896.1; NC_003112.2. DR RefSeq; WP_002223059.1; NC_003112.2. DR ProteinModelPortal; Q9JXS8; -. DR STRING; 122586.NMB1902; -. DR PaxDb; Q9JXS8; -. DR EnsemblBacteria; AAF42232; AAF42232; NMB1902. DR GeneID; 904268; -. DR KEGG; nme:NMB1902; -. DR PATRIC; 20359845; VBINeiMen85645_2427. DR eggNOG; ENOG4105CZ8; Bacteria. DR eggNOG; COG0592; LUCA. DR HOGENOM; HOG000071791; -. DR KO; K02338; -. DR OMA; THQIRLK; -. DR OrthoDB; EOG65J53F; -. DR BioCyc; NMEN122586:GHGG-1959-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR001001; DNA_polIII_beta. DR InterPro; IPR022635; DNA_polIII_beta_C. DR InterPro; IPR022637; DNA_polIII_beta_cen. DR InterPro; IPR022634; DNA_polIII_beta_N. DR Pfam; PF00712; DNA_pol3_beta; 1. DR Pfam; PF02767; DNA_pol3_beta_2; 1. DR Pfam; PF02768; DNA_pol3_beta_3; 1. DR PIRSF; PIRSF000804; DNA_pol_III_b; 1. DR SMART; SM00480; POL3Bc; 1. DR TIGRFAMs; TIGR00663; dnan; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425025}; KW DNA replication {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425008}; KW DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}. FT DOMAIN 5 119 DNA_pol3_beta. FT {ECO:0000259|Pfam:PF00712}. FT DOMAIN 131 244 DNA_pol3_beta_2. FT {ECO:0000259|Pfam:PF02767}. FT DOMAIN 247 366 DNA_pol3_beta_3. FT {ECO:0000259|Pfam:PF02768}. SQ SEQUENCE 367 AA; 40853 MW; B4E984D19132A490 CRC64; MLILQAERDS LLKPLQAVTG IVERRHTLPI LSNVLIEGKG GQTKLLATDL EIQIDTAGPE GGAGDFRITT NAKKFQDILR ALPAGALVSL DWDDSRLTLK AGKSRFALQT LPAADFPMMN VGEDISATFS LEQERFKTML SQVQYSMAVQ DIRYYLNGLL MQVEGSQLRL VATDGHRLAY AACAIDADLP RAEVILPRKT VLELFKLLNN PDDPIQIELL DKQVRFQCNG TTIVSKVIDG KFPDFNRVIP LDNDKIFVLS RAELLGALER ASILANEKFR GARLFLQPGL LSVVCSNNEQ EEAREEIEIA YQGGELEVGF NIGYLMDVLR NIHSDDMQLA FGDANRSTLF TVPNNPNFKY IVMPMRI // ID Q9K0Q2_NEIMB Unreviewed; 209 AA. AC Q9K0Q2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000256|PIRNR:PIRNR001435}; DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000256|PIRNR:PIRNR001435}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942}; GN Name=nth {ECO:0000256|HAMAP-Rule:MF_00942, GN ECO:0000313|EMBL:AAF40962.1}; GN OrderedLocusNames=NMB0533 {ECO:0000313|EMBL:AAF40962.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40962.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40962.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40962.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. The DNA N-glycosylase activity CC releases various damaged pyrimidines from DNA by cleaving the N- CC glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The CC AP-lyase activity cleaves the phosphodiester bond 3' to the AP CC site by a beta-elimination, leaving a 3'-terminal unsaturated CC sugar and a product with a terminal 5'-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00942}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00942, CC ECO:0000256|PIRNR:PIRNR001435}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00942, CC ECO:0000256|PIRNR:PIRNR001435}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942, CC ECO:0000256|PIRNR:PIRNR001435}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP- CC Rule:MF_00942, ECO:0000256|PIRNR:PIRNR001435}. CC -!- SIMILARITY: Contains 1 HhH domain. {ECO:0000256|HAMAP- CC Rule:MF_00942}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40962.1; -; Genomic_DNA. DR PIR; D81187; D81187. DR RefSeq; NP_273578.1; NC_003112.2. DR RefSeq; WP_002217860.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q2; -. DR SMR; Q9K0Q2; 1-208. DR STRING; 122586.NMB0533; -. DR PaxDb; Q9K0Q2; -. DR EnsemblBacteria; AAF40962; AAF40962; NMB0533. DR GeneID; 902648; -. DR KEGG; nme:NMB0533; -. DR PATRIC; 20356319; VBINeiMen85645_0678. DR eggNOG; ENOG4105CSM; Bacteria. DR eggNOG; COG0177; LUCA. DR HOGENOM; HOG000252206; -. DR KO; K10773; -. DR OMA; HHALILF; -. DR OrthoDB; EOG6H4KC5; -. DR BioCyc; NMEN122586:GHGG-559-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF10576; EndIII_4Fe-2S; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR TIGRFAMs; TIGR01083; nth; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942}; KW Endonuclease {ECO:0000313|EMBL:AAF40962.1}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435, ECO:0000313|EMBL:AAF40962.1}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000256|PIRNR:PIRNR001435}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:AAF40962.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW Nuclease {ECO:0000313|EMBL:AAF40962.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 38 185 ENDO3c. {ECO:0000259|SMART:SM00478}. FT METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 197 197 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 203 203 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. SQ SEQUENCE 209 AA; 23630 MW; B034374F4A3AF708 CRC64; MNRHIRQEIF ERFRAANPHP TTELNFNSPF ELLIAVLLSA QATDVGVNKA TAKLFPVADT PQAMLDLGLD GVMEYTKTIG LYKTKSKHIM QTCRILLEKY NGEVPEDREA LESLPGVGRK TANVVLNTAF GHPVMAVDTH IFRVSNRTKI APGKDVREVE DKLMRFIPKE FLMDAHHWLI LHGRYTCKAL KPQCQTCIIN DLCEYPAKA // ID Q9JYX1_NEIMB Unreviewed; 611 AA. AC Q9JYX1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Phosphogluconate dehydratase {ECO:0000313|EMBL:AAF41757.1}; DE EC=4.2.1.12 {ECO:0000313|EMBL:AAF41757.1}; GN Name=edd {ECO:0000313|EMBL:AAF41757.1}; GN OrderedLocusNames=NMB1393 {ECO:0000313|EMBL:AAF41757.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41757.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41757.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41757.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the IlvD/Edd family. CC {ECO:0000256|SAAS:SAAS00543775}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41757.1; -; Genomic_DNA. DR PIR; A81088; A81088. DR RefSeq; NP_274407.1; NC_003112.2. DR RefSeq; WP_002222315.1; NC_003112.2. DR ProteinModelPortal; Q9JYX1; -. DR SMR; Q9JYX1; 6-607. DR STRING; 122586.NMB1393; -. DR PaxDb; Q9JYX1; -. DR EnsemblBacteria; AAF41757; AAF41757; NMB1393. DR GeneID; 903815; -. DR KEGG; nme:NMB1393; -. DR PATRIC; 20358473; VBINeiMen85645_1748. DR eggNOG; ENOG4105C01; Bacteria. DR eggNOG; COG0129; LUCA. DR HOGENOM; HOG000173157; -. DR KO; K01690; -. DR OMA; KVDVRQK; -. DR OrthoDB; EOG61ZTBF; -. DR BioCyc; NMEN122586:GHGG-1431-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004456; F:phosphogluconate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IEA:InterPro. DR InterPro; IPR004786; 6-phosphgluc_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR PANTHER; PTHR21000; PTHR21000; 1. DR Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR01196; edd; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|SAAS:SAAS00427188, ECO:0000313|EMBL:AAF41757.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 611 AA; 66181 MW; BA4A965CA2427823 CRC64; MNTTPIHSKL AEITGRIIER SRPTREKYLA KIRSAKQMGR LERNQLGCSN LAHGYAAMPK SIKIEMLQET VPNLGIITAY NDMVSAHQPF KDFPDQIKDE AQKNGATAQV AGGTPAMCDG ITQGYAGMEL SLFSRDVIAM STAIGLSHQM FDGSLFMGVC DKIVPGLMIG ALSFGHIPGI FVPAGPMSSG IGNKEKARTR QLFAEGKVGR NELLKSEMGS YHSPGTCTFY GTANSNQMMM EMMGVHLPAA AFVHPYTDLR EALTRYAAGH LARGIKNGTI KPLGEMLTEK SFINALIGLM ATGGSTNHTM HLVAMARAAG VILNWDDFDE ISSIIPLLIR VYPNGKADVN HFTAAGGLPF VIRELLNAGL LHDDVDTVVG HGMRHYTKEP FLIDGKLEWR EAPETSGNDD ILRKADNPFS PDGGLRLMKG NIGRGVIKVS AVREGCRIIE APAIVFNDQR EVLAAFERGE LERDFVCVVR YQGPRANGMP ELHKLTPPLG ILQDRGFKVA LLTDGRMSGA SGKVPASIHM TPEALMGGNI AKIRTGDLIR FDSVSGELNV LINETEWNAR EVESIDLGAN QQGCGRELFA NFRSMTSSAE TGAMSFGGEF A // ID Q4W577_NEIMB Unreviewed; 499 AA. AC Q4W577; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Protease DO {ECO:0000313|EMBL:AAY52159.1}; DE EC=3.4.21.- {ECO:0000313|EMBL:AAY52159.1}; GN Name=htrA {ECO:0000313|EMBL:AAY52159.1}; GN OrderedLocusNames=NMB0532 {ECO:0000313|EMBL:AAY52159.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52159.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52159.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52159.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52159.1; -; Genomic_DNA. DR RefSeq; NP_273577.1; NC_003112.2. DR RefSeq; WP_002225590.1; NC_003112.2. DR ProteinModelPortal; Q4W577; -. DR STRING; 122586.NMB0532; -. DR PaxDb; Q4W577; -. DR EnsemblBacteria; AAY52159; AAY52159; NMB0532. DR GeneID; 903199; -. DR KEGG; nme:NMB0532; -. DR PATRIC; 20356317; VBINeiMen85645_0677. DR eggNOG; ENOG4105C0H; Bacteria. DR eggNOG; COG0265; LUCA. DR HOGENOM; HOG000223640; -. DR KO; K04771; -. DR OMA; IDQKDAS; -. DR OrthoDB; EOG61ZTDN; -. DR BioCyc; NMEN122586:GHGG-558-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011782; Pept_S1C_Do. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001940; Peptidase_S1C. DR Pfam; PF13180; PDZ_2; 2. DR PRINTS; PR00834; PROTEASES2C. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 2. DR SUPFAM; SSF50494; SSF50494; 1. DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1. DR PROSITE; PS50106; PDZ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAY52159.1}; KW Protease {ECO:0000313|EMBL:AAY52159.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 499 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004246137. FT DOMAIN 302 381 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 499 AA; 52519 MW; 43923F6705C02DA4 CRC64; MFKKYQYLAL AALCAASLAG CDKAGSFFGA DKKEASFVER IEHTKDDGSV SMLLPDFAQL VQSEGPAVVN IQAAPAPRTQ NGSGNAENDS DPIADNDPFY EFFKRLVPNM PEIPQEEADD GGLNFGSGFI ISKDGYILTN THVVTGMGSI KVLLNDKREY TAKLIGSDVQ SDVALLKIDA TEELPVVKIG NPKDLKPGEW VAAIGAPFGF DNSVTAGIVS AKGRSLPNES YTPFIQTDVA INPGNSGGPL FNLKGQVVGI NSQIYSRSGG FMGISFAIPI DVAMNVAEQL KNTGKVQRGQ LGVIIQEVSY GLAQSFGLDK AGGALIAKIL PGSPAERAGL QAGDIVLSLD GGEIRSSGDL PVMVGAITPG KEVSLGVWRK GEEITIKVKL GNAAEHIGAS SKTDEAPYTE QQSGTFSVES AGITLQTHTD SSGGHLVVVR VSDAAERAGL RRGDEILAVG QVPVNDEAGF RKAMDKAGKN VPLLIMRRGN TLFIALNLQ // ID Q9JZ67_NEIMB Unreviewed; 543 AA. AC Q9JZ67; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41647.1}; GN OrderedLocusNames=NMB1270 {ECO:0000313|EMBL:AAF41647.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41647.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41647.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41647.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41647.1; -; Genomic_DNA. DR PIR; H81102; H81102. DR RefSeq; NP_274291.1; NC_003112.2. DR RefSeq; WP_010980913.1; NC_003112.2. DR ProteinModelPortal; Q9JZ67; -. DR STRING; 122586.NMB1270; -. DR PaxDb; Q9JZ67; -. DR EnsemblBacteria; AAF41647; AAF41647; NMB1270. DR GeneID; 903692; -. DR KEGG; nme:NMB1270; -. DR PATRIC; 20358155; VBINeiMen85645_1589. DR eggNOG; ENOG4106R49; Bacteria. DR eggNOG; COG0500; LUCA. DR eggNOG; COG4797; LUCA. DR HOGENOM; HOG000218982; -. DR OMA; REIMYFA; -. DR OrthoDB; EOG6SV55B; -. DR BioCyc; NMEN122586:GHGG-1308-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR025714; Methyltranfer_dom. DR InterPro; IPR018773; MeTrfase_reg_dom_prd. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF13847; Methyltransf_31; 1. DR Pfam; PF10119; MethyTransf_Reg; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 79 190 Methyltranfer_dom. FT {ECO:0000259|Pfam:PF13847}. FT DOMAIN 255 337 MethyTransf_Reg. FT {ECO:0000259|Pfam:PF10119}. SQ SEQUENCE 543 AA; 61395 MW; 8D6C671EC0BB3A7E CRC64; MNWLNLRAIV PSDKQNMPNK KKKAAFARAA TENGVPDVSN IKNSYDDLMY ESGAFSQTAI NNLEARARLM GLQPAPAANA KVLELGCSMG GNIITQALYY PDAEFVGIDL SGRQVAQGNA IIEKMGLKNV RLEEKDILTI DESFGKFDYI IVHGIWSWVP DAVKDKIFSI CWNNLTKHGI AYISYNVYPG WKRQEQLREI MYFAGRDVLE EPLEARTRKG LDALKALAEI LENDKGLDGG GKLPAIQKIL NHNFYYIAHE YMEAFNDPIY VNGFIEWANR HRLAYIGDTN LHVSFVSWMA EHTRERILAL AGDDYIAKEF YSDILSDRQF RRSLLCREEV GDTVRRDESV AVEVIESLNF RPARGETINF DENDILLSGI RDVMKTGEAF KTEDVAENLA RRFPGLEFDR MKINSQLLLQ TILGRFSVSS DNAGKPFFED HKTYVPARFT NYAAAFVEHG AEAFVRPANR YNESTPSFGY GHLYIMRQLS RPTSKQALIE TVAENLNIVS TTPDGLTFHP PAEVYVEEIL ADLADRHFLV SAD // ID Q9K1D0_NEIMB Unreviewed; 735 AA. AC Q9K1D0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=DNA helicase {ECO:0000256|SAAS:SAAS00553569}; DE EC=3.6.4.12 {ECO:0000256|SAAS:SAAS00553569}; GN Name=uvrD {ECO:0000313|EMBL:AAF40687.1}; GN OrderedLocusNames=NMB0232 {ECO:0000313|EMBL:AAF40687.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40687.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40687.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40687.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|SAAS:SAAS00553768}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|SAAS:SAAS00597767}. CC -!- SIMILARITY: Contains uvrD-like helicase ATP-binding domain. CC {ECO:0000256|SAAS:SAAS00553567}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40687.1; -; Genomic_DNA. DR PIR; A81224; A81224. DR RefSeq; NP_273289.1; NC_003112.2. DR RefSeq; WP_010980762.1; NC_003112.2. DR ProteinModelPortal; Q9K1D0; -. DR SMR; Q9K1D0; 8-645. DR STRING; 122586.NMB0232; -. DR PaxDb; Q9K1D0; -. DR EnsemblBacteria; AAF40687; AAF40687; NMB0232. DR GeneID; 902343; -. DR KEGG; nme:NMB0232; -. DR PATRIC; 20355540; VBINeiMen85645_0294. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR HOGENOM; HOG000033016; -. DR KO; K03657; -. DR OMA; HYRTQKG; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; NMEN122586:GHGG-247-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 2. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01075; uvrD; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAF40687.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAF40687.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAF40687.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAF40687.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 12 289 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 290 569 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. SQ SEQUENCE 735 AA; 82241 MW; 38F18212DEAAC318 CRC64; MFPDQSAPNL LQGLNPEQLS AVTWPPQSAL VLAGAGSGKT RVLTTRIAWL LQSGQASVHS IMAVTFTNKA AKEMQTRLGA MIPINVRAMW LGTFHGLCHR FLRLHHRDAG LPSSFQILDG GDQLSLIKRL LKSLNIAEEI IAPRSLQGFI NAQKESGLRA SVLSAPDPHT RRMIECYAEY DKICQREGVV DFAELMLRSY EMLQNNEILR QHYQNRFNHI LVDEFQDTNK LQYAWLKLIA GNHAAVFAVG DDDQSIYRFR GASVGNMTAL MEEFHIDAPV KLEQNYRSVG NILAAANAVI ENNDERLGKN LRTDAEAGDK IRYYSAFTDL EEARFILDET KALEREGWDL DEIAVLYRSN AQSRVIEQSL FRSGIPYKIY GGLRFYERQE IKHALAYLRL AVNPDDDNAL LRVINFPPRG IGARTVENLQ TASNEQGITL WQAACNAGAK AAKVVAFVRL IEALRNQVGQ LSLSEIIVGI LKDSGLTEHY RTQKGDNQDR LDNLDELVNA AIEFKPEDSN FEILPENISD DPAFPILAFL SNAALESGEN QAGAGEKAVQ LMTVHAAKGL EFNAVFLTGM EEGRFPSEMS LAERGGLEEE RRLMYVAITR ARKRLYITMA QQRMLHGQTQ FGIVSRFVEE IPPEVLHYLS VKKPAYDSYG NTRQTAASKD KIIDDYKQPQ TYAGFRIGQN VRHAKFGTGV IIDAADKGES ARLTINFGKQ GVKELDTKFA KLEEM // ID Q9JZ03_NEIMB Unreviewed; 418 AA. AC Q9JZ03; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Putative fmu and fmv protein {ECO:0000313|EMBL:AAF41725.1}; GN OrderedLocusNames=NMB1351 {ECO:0000313|EMBL:AAF41725.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41725.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41725.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41725.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00494853}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RsmB/NOP family. CC {ECO:0000256|SAAS:SAAS00534162}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41725.1; -; Genomic_DNA. DR PIR; B81093; B81093. DR RefSeq; NP_274369.1; NC_003112.2. DR RefSeq; WP_002222346.1; NC_003112.2. DR ProteinModelPortal; Q9JZ03; -. DR STRING; 122586.NMB1351; -. DR PaxDb; Q9JZ03; -. DR EnsemblBacteria; AAF41725; AAF41725; NMB1351. DR GeneID; 903773; -. DR KEGG; nme:NMB1351; -. DR PATRIC; 20358359; VBINeiMen85645_1691. DR eggNOG; ENOG4105CYJ; Bacteria. DR eggNOG; COG0144; LUCA. DR HOGENOM; HOG000037301; -. DR KO; K03500; -. DR OMA; RRMEFAH; -. DR OrthoDB; EOG6091D0; -. DR BioCyc; NMEN122586:GHGG-1389-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR031341; Methyltr_RsmF_N. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR023267; RCMT. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR Pfam; PF17125; Methyltr_RsmF_N; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00494850}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00494849}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|SAAS:SAAS00494848}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00494847}; KW Transferase {ECO:0000256|SAAS:SAAS00494849}. FT DOMAIN 141 418 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. SQ SEQUENCE 418 AA; 46373 MW; 164C777241D070A1 CRC64; MNAAQLDHTA KVLAEMLTFK QPADAVLSAY FREHKKLGSQ DRHEIAETAF AALRHYQKIS TALRRPHAQP RKAALAALVL GRSTNISQIK DLLDEEETAF LGNLKARKTE FSDSLNTAAE LPQWLVEQLK QHWREEEILA FGRSINQPAP LDIRVNTLKG KRDKVLPLLQ AESADAEATP YSPWGIRLKN KIALNKHELF LDGTLEVQDE GSQLLALLVG AKRGEIIVDF CAGAGGKTLA VGAQMANKGR IYAFDIAEKR LANLKPRMTR AGLTNIHPER IGSEHDARIA RLAGKADRVL VDAPCSGLGT LRRNPDLKYR QSAETVANLL EQQHSILDAA SKLVKPQGRL VYATCSILPE ENELQVERFL SEHPEFEPVN CAELLAGLKI DLDTGKYLRL NSARHQTDGF FAAVLQRK // ID Q9K0Y3_NEIMB Unreviewed; 423 AA. AC Q9K0Y3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Putative lipid II flippase FtsW {ECO:0000256|HAMAP-Rule:MF_00913}; DE AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913}; GN Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913, GN ECO:0000313|EMBL:AAF40859.1}; GN OrderedLocusNames=NMB0421 {ECO:0000313|EMBL:AAF40859.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40859.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40859.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40859.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein. Transports lipid-linked CC peptidoglycan precursors from the inner to the outer leaflet of CC the cytoplasmic membrane. {ECO:0000256|HAMAP-Rule:MF_00913}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00913}. Note=Localizes to the division septum. CC {ECO:0000256|HAMAP-Rule:MF_00913}. CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40859.1; -; Genomic_DNA. DR PIR; H81200; H81200. DR RefSeq; NP_273469.1; NC_003112.2. DR RefSeq; WP_002218795.1; NC_003112.2. DR STRING; 122586.NMB0421; -. DR PaxDb; Q9K0Y3; -. DR EnsemblBacteria; AAF40859; AAF40859; NMB0421. DR GeneID; 902537; -. DR KEGG; nme:NMB0421; -. DR PATRIC; 20356038; VBINeiMen85645_0534. DR eggNOG; ENOG4105CNI; Bacteria. DR eggNOG; COG0772; LUCA. DR HOGENOM; HOG000282689; -. DR KO; K03588; -. DR OMA; NIGWIRI; -. DR OrthoDB; EOG68M4JQ; -. DR BioCyc; NMEN122586:GHGG-445-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00913; FtsW_proteobact; 1. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; Cell_cycle_FtsW/RodA. DR InterPro; IPR013437; FtsW. DR PANTHER; PTHR30474; PTHR30474; 2. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000313|EMBL:AAF40859.1}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000313|EMBL:AAF40859.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00913}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00913}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00913}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000256|SAAS:SAAS00481328}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00913}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000256|SAAS:SAAS00481328}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000256|SAAS:SAAS00481328}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00913}. FT TRANSMEM 25 45 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 59 79 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 87 107 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 122 142 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 189 209 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 210 230 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 233 253 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 310 330 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 359 379 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 386 406 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00913}. SQ SEQUENCE 423 AA; 47354 MW; CB9FB1AFE4E026AA CRC64; MGDGVHTLLL DRPIVRDGRK FDAPLLWMVV LMTAFSLLMI YSASVYLASK EGGDQFFYLT RQAGFVVAGL IASGLLWFLC RMRTWRRLVP WIFALSGLLL VVVLIAGREI NGATRWIPLG PLNFQPTELF KLAVILYLAS LFTRREEVLR SMESLGWQSI WRGTANLIMS ATNPQARRET LEMYGRFRAI ILPIMLVAFG LVLIMVQPDF GSFVVITVIA VGMLFLAGLP WKYFFVLVGS VLGGMVLMIT AAPYRVQRVV AFLDPWKDPQ GAGYQLTHSL MAIGRGEWFG MGLGASLSKR GFLPEAHTDF IFAIIAEEFG FFGMCVLIFC YGWLVVRAFS IGKQSRDLGL TFNAYIASGI GIWIGIQSFF NIGVNIGALP TKGLTLPLMS YGGSSVFFML ISMMLLLRID YENRRKMRGY RVE // ID Q9K108_NEIMB Unreviewed; 221 AA. AC Q9K108; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:AAF40831.1}; DE EC=5.4.2.6 {ECO:0000313|EMBL:AAF40831.1}; GN Name=pgmB {ECO:0000313|EMBL:AAF40831.1}; GN OrderedLocusNames=NMB0391 {ECO:0000313|EMBL:AAF40831.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40831.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40831.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40831.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40831.1; -; Genomic_DNA. DR PIR; G81203; G81203. DR RefSeq; NP_273440.1; NC_003112.2. DR RefSeq; WP_002224909.1; NC_003112.2. DR ProteinModelPortal; Q9K108; -. DR SMR; Q9K108; 3-221. DR STRING; 122586.NMB0391; -. DR PaxDb; Q9K108; -. DR EnsemblBacteria; AAF40831; AAF40831; NMB0391. DR GeneID; 902506; -. DR KEGG; nme:NMB0391; -. DR PATRIC; 20355945; VBINeiMen85645_0490. DR eggNOG; ENOG4107URF; Bacteria. DR eggNOG; COG0637; LUCA. DR HOGENOM; HOG000248341; -. DR KO; K01838; -. DR OMA; EMIKRIT; -. DR OrthoDB; EOG6KMBB8; -. DR BioCyc; NMEN122586:GHGG-413-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:UniProtKB-EC. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase. DR InterPro; IPR010972; Beta-phosphoglucomutase. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01990; bPGM; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF40831.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 184 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 221 AA; 23702 MW; 875FE3F86A61D57E CRC64; MTFTAVLFDL DGVITDTAEY HYRAWKKLAE ELGISIDRKF NEQLKGVSRD DSLKRILAHG GKTVSEAEFA ELTRRKNDNY VEMIQAVKPE DVYPGILPLL EALRANGKKI ALASASKNGP FLLERMGLTH FFDAIADPAA VAHSKPAPDI FLAAAEGVDA DIRQCIGIED AAAGVAAIKA AGALPIGVGK AEDLGSDIAL VSGTAELTYA YLQSVWEQSG R // ID Q9JXB7_NEIMB Unreviewed; 635 AA. AC Q9JXB7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42442.1}; GN OrderedLocusNames=NMB2134 {ECO:0000313|EMBL:AAF42442.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42442.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42442.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42442.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|SAAS:SAAS00560981}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42442.1; -; Genomic_DNA. DR PIR; G81003; G81003. DR RefSeq; NP_275119.1; NC_003112.2. DR RefSeq; WP_010981030.1; NC_003112.2. DR ProteinModelPortal; Q9JXB7; -. DR STRING; 122586.NMB2134; -. DR PaxDb; Q9JXB7; -. DR EnsemblBacteria; AAF42442; AAF42442; NMB2134. DR GeneID; 903298; -. DR KEGG; nme:NMB2134; -. DR PATRIC; 20360448; VBINeiMen85645_2720. DR eggNOG; ENOG4105CFU; Bacteria. DR eggNOG; COG0729; LUCA. DR HOGENOM; HOG000263477; -. DR KO; K07278; -. DR OMA; VDPGPQT; -. DR OrthoDB; EOG6F81K6; -. DR BioCyc; NMEN122586:GHGG-2199-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR InterPro; IPR000184; Bac_surfAg_D15. DR InterPro; IPR010827; Surface_Ag_variable_number. DR Pfam; PF01103; Bac_surface_Ag; 1. DR Pfam; PF07244; POTRA; 1. PE 4: Predicted; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00560982}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00560982, KW ECO:0000256|SAAS:SAAS00560990}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00560990}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00560990}. FT DOMAIN 363 635 Bac_surface_Ag. FT {ECO:0000259|Pfam:PF01103}. SQ SEQUENCE 635 AA; 69802 MW; 2B371F4A7A9DDA98 CRC64; MPSEASRPVR TVLKSKAATP MHDTRTMMIK PTALLLPALF FFPHAYAPAA DLSENKAAGF ALFKNKSPDT ESVKLKPKFP VLIDTQDSEI KDMVEEHLPL ITQQQEEVLD KEQTGFLAEE APDNVKTMLR SKGYFSSKVS LTEKDGAYTV HITPGPRTKI ANVGVAILGD ILSDGNLAEY YRNALENWQQ PVGSDFDQDS WENSKTSVLG AVTRKAYPLA KLGNTQAAVN PDTATADLNV VVDSGRPIAF GDFEITGTQR YPEQIVSGLA RFQPGMPYDL DLLLDFQQAL EQNGHYSGAS VQADFDRLQG DRVPVKVSVT EVKRHKLETG IRLDSEYGLG GKIAYDYYNL FNKGYIGSVV WDMDKYETTL AAGISQPRNY RGNYWTSNVS YNRSTTQNLE KRAFSGGVWY VRDRAGIDAR LGAEFLAEGR KIPGSAVDLG NSHATMLTAS WKRQLLNNVL HPENGHYLDG KIGTTLGTFL SSTALIRTSA RAGYFFTPEN KKLGTFIIRG QAGYTVARDN ADVPSGLMFR SGGASSVRGY ELDSIGLAGP NGSVLPERAL LVGSLEYQLP FTRTLSGAVF HDMGDAAANF KRMKLKHGSG LGVRWFSPLA PFSFDIAYGH SDKKIRWHIS LGTRF // ID Q9K0M9_NEIMB Unreviewed; 351 AA. AC Q9K0M9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|RuleBase:RU363002}; DE EC=2.7.1.180 {ECO:0000256|RuleBase:RU363002}; GN Name=apbE {ECO:0000313|EMBL:AAF40991.1}; GN OrderedLocusNames=NMB0563 {ECO:0000313|EMBL:AAF40991.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40991.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40991.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40991.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the CC FMN moiety of FAD and its covalent binding to the hydroxyl group CC of a threonine residue in a target flavoprotein. CC {ECO:0000256|RuleBase:RU363002}. CC -!- CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L- CC threonine + AMP. {ECO:0000256|RuleBase:RU363002}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Note=Magnesium. Can also use manganese. CC {ECO:0000256|PIRSR:PIRSR006268-2}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU363002}. CC -!- SIMILARITY: Belongs to the ApbE family. CC {ECO:0000256|RuleBase:RU363002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40991.1; -; Genomic_DNA. DR PIR; F81184; F81184. DR RefSeq; NP_273607.1; NC_003112.2. DR RefSeq; WP_002242382.1; NC_003112.2. DR ProteinModelPortal; Q9K0M9; -. DR STRING; 122586.NMB0563; -. DR PaxDb; Q9K0M9; -. DR EnsemblBacteria; AAF40991; AAF40991; NMB0563. DR GeneID; 902678; -. DR KEGG; nme:NMB0563; -. DR PATRIC; 20356403; VBINeiMen85645_0721. DR eggNOG; ENOG4105CJ2; Bacteria. DR eggNOG; COG1477; LUCA. DR HOGENOM; HOG000080808; -. DR KO; K03734; -. DR OMA; MGTFWRV; -. DR OrthoDB; EOG6CGCF7; -. DR BioCyc; NMEN122586:GHGG-589-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0017013; P:protein flavinylation; IEA:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like. DR Pfam; PF02424; ApbE; 1. DR PIRSF; PIRSF006268; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU363002}; KW Cell membrane {ECO:0000256|RuleBase:RU363002}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|RuleBase:RU363002}; KW Lipoprotein {ECO:0000256|RuleBase:RU363002, KW ECO:0000313|EMBL:AAF40991.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR006268-2, KW ECO:0000256|RuleBase:RU363002}; KW Membrane {ECO:0000256|RuleBase:RU363002}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR006268-2, KW ECO:0000256|RuleBase:RU363002}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU363002}. FT METAL 187 187 Magnesium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR006268-2}. FT METAL 303 303 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006268-2}. FT METAL 307 307 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006268-2}. SQ SEQUENCE 351 AA; 38662 MW; C96EAC2098726E2B CRC64; MPSETRLPNF IRVLIFALGF IFLNACSEQT AQTVTLQGET MGTTYTVKYL SNNRDKLPSP AEIQKRIDDA LKEVNRQMST YQPDSEISRF NQHTAGKPLR ISSDFAHVTA EAVRLNRLTH GALDVTVGPL VNLWGFGPDK SVTREPSPEQ IKQAASYTGI DKIILKQGKD YASLSKTHPK AYLDLSSIAK GFGVDKVAGE LEKYGIQNYL VEIGGELHGK GKNARGEPWR IGIEQPNIVQ GGNTQIIVPL NNRSLATSGD YRIFHVDKNG KRLSHIINPN NKRPISHNLA SISVVADSAM TADGLSTGLF VLGETEALKL AEREKLAVFL IVRDKGGYRT AMSSEFEKLL R // ID Q9K044_NEIMB Unreviewed; 424 AA. AC Q9K044; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=Putative uroporphyrin-III C-methyltransferase HemX {ECO:0000313|EMBL:AAF41191.1}; GN OrderedLocusNames=NMB0778 {ECO:0000313|EMBL:AAF41191.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41191.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41191.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41191.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41191.1; -; Genomic_DNA. DR PIR; G81160; G81160. DR RefSeq; NP_273820.1; NC_003112.2. DR RefSeq; WP_010980843.1; NC_003112.2. DR STRING; 122586.NMB0778; -. DR PaxDb; Q9K044; -. DR EnsemblBacteria; AAF41191; AAF41191; NMB0778. DR GeneID; 902893; -. DR KEGG; nme:NMB0778; -. DR PATRIC; 20356933; VBINeiMen85645_0985. DR eggNOG; ENOG4105ECF; Bacteria. DR eggNOG; COG2959; LUCA. DR HOGENOM; HOG000218864; -. DR KO; K02496; -. DR OMA; VSASWWQ; -. DR OrthoDB; EOG6X10V3; -. DR BioCyc; NMEN122586:GHGG-809-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR007470; HemX. DR Pfam; PF04375; HemX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000313|EMBL:AAF41191.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41191.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 53 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 424 AA; 46319 MW; 728266A5CC1D730A CRC64; MPSETSSPRK ENETEVHIPA APFIVKQSGS NALAVCALVL AALGLGTSGF LFVQGQNVLK NQELAFNQKI DKAALGESEN AALLKDNLNR QAAIQSELDR LDGNVKANGE QILEMQKSYR ELTKGRADWL VDETETILNL AAQQLVLTGN IQTAVGVLEH IDSRLSRFNQ AELLPIKQAV SSDLAELKNR PYVDISGTAL RLDRLETAVS GLPLMLDGVL KPGVQVKNEA ASASWWQNVW EKSLGTLKGL VEIRRLENND AMLISPEQAY FVRENLRLRL LDARTALMQR NSEVYQGDLN NAEAAVRQYF DAKSPATQSW LKELAELKAL DVRMTADDGL KNSLNAVRAY RDGTRMTAAE NQEAEQAASE PANEKTASEP AAASDVKTIE APSLPSERKP EQPAKKQTVP EKAGRSPSAK GERA // ID Q9JXP2_NEIMB Unreviewed; 245 AA. AC Q9JXP2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 109. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF42277.1}; GN OrderedLocusNames=NMB1948 {ECO:0000313|EMBL:AAF42277.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42277.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42277.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42277.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in CC methionine import. Responsible for energy coupling to the CC transport system. {ECO:0000256|SAAS:SAAS00340993}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MetN), two transmembrane proteins (MetI) and a solute-binding CC protein (MetQ). {ECO:0000256|SAAS:SAAS00340960}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine CC importer (TC 3.A.1.24) family. {ECO:0000256|SAAS:SAAS00537373}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42277.1; -; Genomic_DNA. DR PIR; E81023; E81023. DR RefSeq; NP_274942.1; NC_003112.2. DR RefSeq; WP_002225835.1; NC_003112.2. DR ProteinModelPortal; Q9JXP2; -. DR STRING; 122586.NMB1948; -. DR PaxDb; Q9JXP2; -. DR EnsemblBacteria; AAF42277; AAF42277; NMB1948. DR GeneID; 904202; -. DR KEGG; nme:NMB1948; -. DR PATRIC; 20359949; VBINeiMen85645_2479. DR eggNOG; ENOG4108EHQ; Bacteria. DR eggNOG; COG1135; LUCA. DR KO; K02071; -. DR OMA; THGLEVI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-2005-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0015821; P:methionine transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR026253; ABC_MetN. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24220:SF186; PTHR24220:SF186; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW Amino-acid transport {ECO:0000256|SAAS:SAAS00419735}; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00419679, ECO:0000313|EMBL:AAF42277.1}; KW Cell membrane {ECO:0000256|SAAS:SAAS00419761}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|SAAS:SAAS00419641}; KW Membrane {ECO:0000256|SAAS:SAAS00419761}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00419679, ECO:0000313|EMBL:AAF42277.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|SAAS:SAAS00419735}. FT DOMAIN 2 242 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 245 AA; 27049 MW; 2DC395FB0C3D0A44 CRC64; MIILDKVSKH YQTRDKTRFA AVEPTSLEIR DGEIFGLMGY SGAGKSTLLR LINLLERPDS GKVNVCGQEL TALDAAALRQ ARQNIGMVFQ QFNLLSNRTV ADNVAFPLEI AGWPSEKIKA RVKECLEIVG LTERAGHYPA QLSGGQKQRV GIARALAPKP QVILADEPTS ALDPATTRSV LECLEDINKR FNVTIVIVTH EMSVIRRLCD RAALLDKGKV VEIVEVRGNQ IHAQSDIGRE LIRED // ID Q9JYZ1_NEIMB Unreviewed; 273 AA. AC Q9JYZ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00094448}; DE EC=6.3.1.5 {ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00094492}; GN OrderedLocusNames=NMB1364 {ECO:0000313|EMBL:AAF41738.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41738.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41738.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41738.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). {ECO:0000256|RuleBase:RU003812, CC ECO:0000256|SAAS:SAAS00094467}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC {ECO:0000256|RuleBase:RU004252, ECO:0000256|SAAS:SAAS00094445}. CC -!- SIMILARITY: Belongs to the NAD synthetase family. CC {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00573607}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41738.1; -; Genomic_DNA. DR PIR; A81090; A81090. DR RefSeq; NP_274382.1; NC_003112.2. DR RefSeq; WP_009348575.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ1; -. DR STRING; 122586.NMB1364; -. DR PaxDb; Q9JYZ1; -. DR EnsemblBacteria; AAF41738; AAF41738; NMB1364. DR GeneID; 903786; -. DR KEGG; nme:NMB1364; -. DR PATRIC; 20358391; VBINeiMen85645_1707. DR eggNOG; ENOG4107RW9; Bacteria. DR eggNOG; COG0171; LUCA. DR HOGENOM; HOG000238069; -. DR KO; K01916; -. DR OMA; CARLRMA; -. DR OrthoDB; EOG64JFM7; -. DR BioCyc; NMEN122586:GHGG-1402-MONOMER; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 1. DR TIGRFAMs; TIGR00552; nadE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00464970}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00464931}; KW NAD {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00464912}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00464970}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 258 NAD_synthase. {ECO:0000259|Pfam:PF02540}. SQ SEQUENCE 273 AA; 30365 MW; EDAED1C1044CAA4B CRC64; MMRIFSTGGK MDTQAVITHI ARWLDEYAAR ANAKGFVVGV SGGIDSAVVS ALAARTGRPT LLLDMPIRQH PGQLERARLH IRNLQRQYAN VSAQTVDLTD TFQTFEQTVG AHQTAFDSQP LSLANARSRL RMLTLYYYGQ IHGLLVTGTG NKIEDFGVGF FTKYGDGGVD ISPIADLTKT QVYRLAEALG VDEAIQKAPP TDGLWDTERT DEEQMGASYP ELEWAMGVYG TRKPEDFEGR QREVLEIYTR LHRAMQHKIN PIPVCRIPPE LLG // ID Q9K1E7_NEIMB Unreviewed; 279 AA. AC Q9K1E7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 105. DE SubName: Full=Ferredoxin, 4Fe-4S bacterial type {ECO:0000313|EMBL:AAF40665.1}; GN OrderedLocusNames=NMB0208 {ECO:0000313|EMBL:AAF40665.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40665.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40665.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40665.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|SAAS:SAAS00561197}. CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. CC RnfB subfamily. {ECO:0000256|SAAS:SAAS00561201}. CC -!- SIMILARITY: Contains 4Fe-4S domain. CC {ECO:0000256|SAAS:SAAS00508687}. CC -!- SIMILARITY: Contains 4Fe-4S ferredoxin-type domains. CC {ECO:0000256|SAAS:SAAS00506731}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40665.1; -; Genomic_DNA. DR PIR; A81225; A81225. DR RefSeq; NP_273266.1; NC_003112.2. DR RefSeq; WP_002243957.1; NC_003112.2. DR ProteinModelPortal; Q9K1E7; -. DR STRING; 122586.NMB0208; -. DR PaxDb; Q9K1E7; -. DR EnsemblBacteria; AAF40665; AAF40665; NMB0208. DR GeneID; 902316; -. DR KEGG; nme:NMB0208; -. DR PATRIC; 20355457; VBINeiMen85645_0257. DR eggNOG; ENOG4107RIG; Bacteria. DR eggNOG; COG2878; LUCA. DR HOGENOM; HOG000262939; -. DR OMA; LPNRCPP; -. DR OrthoDB; EOG60SCM3; -. DR BioCyc; NMEN122586:GHGG-219-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR007202; 4Fe-4S_dom. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB. DR Pfam; PF04060; FeS; 1. DR TIGRFAMs; TIGR01944; rnfB; 1. DR PROSITE; PS51656; 4FE4S; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|SAAS:SAAS00506732}; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00506743}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|SAAS:SAAS00506721}; KW Iron {ECO:0000256|SAAS:SAAS00506732, ECO:0000256|SAAS:SAAS00506743}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00506732, KW ECO:0000256|SAAS:SAAS00506743}; KW Membrane {ECO:0000256|SAAS:SAAS00506718}; KW Metal-binding {ECO:0000256|SAAS:SAAS00506732, KW ECO:0000256|SAAS:SAAS00506743}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Repeat {ECO:0000256|SAAS:SAAS00506735}; KW Transport {ECO:0000256|SAAS:SAAS00506721}. FT DOMAIN 1 58 4Fe-4S. {ECO:0000259|PROSITE:PS51656}. FT DOMAIN 70 99 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 100 129 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT COILED 159 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 279 AA; 30305 MW; 42C17E4D12A22426 CRC64; MTATAAAIDR LLPQTQCREC GYDGCLPYAQ AVATGEAYNL CAPGGETVIR DISALLGKPF VAPAKTQAKA LARIDETACI GCTACIRACP ADAIMGAGKL MHTVIADECT GCGLCVAPCP VDCIHMQPVA DTVLPRARRF SLSADSRFAA AEHARTRYLK RNERKQREAD ERKAMLAERE AAVRNARPQT PDTPKKPTFN PADLIAKAMA KAQTQQDRLA AADNRKDYQA KQIAEARERA ELRRAQRDMK YGSDSEKAAA LEYLKQYKAK QEAAQNTAS // ID Q9JXB6_NEIMB Unreviewed; 1405 AA. AC Q9JXB6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42443.1}; GN OrderedLocusNames=NMB2135 {ECO:0000313|EMBL:AAF42443.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42443.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42443.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42443.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42443.1; -; Genomic_DNA. DR PIR; H81003; H81003. DR RefSeq; NP_275120.1; NC_003112.2. DR RefSeq; WP_009348724.1; NC_003112.2. DR STRING; 122586.NMB2135; -. DR PaxDb; Q9JXB6; -. DR EnsemblBacteria; AAF42443; AAF42443; NMB2135. DR GeneID; 903264; -. DR KEGG; nme:NMB2135; -. DR PATRIC; 20360450; VBINeiMen85645_2721. DR eggNOG; ENOG4105MA0; Bacteria. DR eggNOG; COG2911; LUCA. DR HOGENOM; HOG000218696; -. DR KO; K09800; -. DR OMA; DTPWSSS; -. DR OrthoDB; EOG6Z3KF9; -. DR BioCyc; NMEN122586:GHGG-2200-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007452; TamB. DR Pfam; PF04357; TamB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 73 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 1405 AA; 148732 MW; F627DB86E053B5DC CRC64; MATSDGIAAN HFETDIMTDT APTDTDPTEN GTRKMPSEHR PTPPAKKRRP LLKLSAALLS VLILAVCFLG WLAGTEAGLR FGLYQIPSWF GVNISSQNLK GTLLDGFDGD NWSIETEGAD LKISRFRFAW KPSELMRRSL HITEISAGDI AIVTKPTPPK EERPPLSLPD SIDLPAAVYL DRFETGKISM GKAFDKQTVY LERLDASYRY DRKGHRLDLK AADTPWSSSS GAASVGLKKP FALDTAIYTK GGLEGKTIHS TARLSGSLKD VRAELAIDGG NIRLSGKSVI HPFAESLDKT LEEVLVKGFN INPAAFVPSL PDAGLNFDLT AIPSFSDGIA LEGSLDLENT KAGFADRNGI PVRQVLGGFV IRQDGTVHIG NTSAALLGRG GIRLSGKIDT EKDILDLNIG INSVGAEDVL QTAFKGRLDG SIGIGGTTAS PKISWQLGIG TARTDGSLAI ASDPANGQRK LVLDTVNIAA GQGSLTAQGY LELFKDRLLK LDIRSRAFDP SRIDPQLPAG NINGSINLAG ELAKEKFTGK MRFLPGTFNG VPIAGSADIV YESRHLPRAA VDLRLGRNII KTDGGFGKKG DRLNLNITAP DLSRFGFGLA GSLNVRGHLS GDLDGGIRTF ETDLSGAARN LHIGKAADIR SLDFTLKGSP DTSRPIRADI KGSRLSLSGG AAVVDTADLM LDGTGVQHRI RTHAAMTLDG KPFKFDLDAS GGINRELTRW KGSIGILDIG GAFNLKLQNR MTLEAGAERV AASAANWQAM GGSLNLQHFS WDKKTGISAK GGAHGLHIAE LHNFFKPPFE HNLVLNGDWD VAYGRNARGY LNISRQSGDA VLPGGQALGL NAFSLKTRFQ NDRIGILLDG GARFGRINAD LGIANAFGGN MANAPLGGRI TASLPDLGAL KPFLPAAAQN ITGSLNAAAQ IGGRVGSPSV NAAVNGSSNY GKINGNITVG QSRSFDTAPL GGRLNLTVAD AEVFRNFLPV GQTVKGSLNA AVTLGGSIAD PHLGGSINGD KLYYRNQTQG IILDNGSLRS HIAGRKWVID SLKFRHEGTA ELSGTVGMEN SGPDVDIGAV FDKYRILSRP NRRLTVSGNT RLRYSPQKGI SVTGMIKTDQ GLFGSQKSSM PSVGDDVVVL GEVKKEAAAP LPVNMNLTLD LNDGIRFAGY GADVTIGGKL TLTAQSGGSV RGVGTVRVIK GRYKAYGQDL DITKGTVSFV GPLNDPNLNI RAERRLSPVG AGVEILGSLN SPRITLTANE PMSEKDKLSW LILNRAGSGS SGDNAALSAA AGALLAGQIN DRIGLVDDLG FTSKRSRNAQ TGELNPAEQV LTVGKQLTGK LYIGYEYSIS SAEQSVKLIY RLTRAIQAVA RIGSRSSGGE LTYTIRFDRF SGSDKKDSAG NGKGK // ID Q9K1N1_NEIMB Unreviewed; 263 AA. AC Q9K1N1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925}; DE Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925}; DE Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925}; DE EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925}; DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925}; GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925, GN ECO:0000313|EMBL:AAF40524.1}; GN OrderedLocusNames=NMB0055 {ECO:0000313|EMBL:AAF40524.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40524.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40524.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40524.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:1YQG, ECO:0000213|PDB:2AG8} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP. RX PubMed=16233902; DOI=10.1016/j.jmb.2005.08.036; RA Nocek B., Chang C., Li H., Lezondra L., Holzle D., Collart F., RA Joachimiak A.; RT "Crystal structures of delta1-pyrroline-5-carboxylate reductase from RT human pathogens Neisseria meningitides and Streptococcus pyogenes."; RL J. Mol. Biol. 354:91-106(2005). CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate CC (PCA) to L-proline. {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. {ECO:0000256|HAMAP-Rule:MF_01925}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40524.1; -; Genomic_DNA. DR PIR; E81243; E81243. DR RefSeq; NP_273120.1; NC_003112.2. DR RefSeq; WP_002243933.1; NC_003112.2. DR PDB; 1YQG; X-ray; 1.90 A; A=1-263. DR PDB; 2AG8; X-ray; 2.10 A; A=1-263. DR PDBsum; 1YQG; -. DR PDBsum; 2AG8; -. DR ProteinModelPortal; Q9K1N1; -. DR SMR; Q9K1N1; 1-263. DR STRING; 122586.NMB0055; -. DR PaxDb; Q9K1N1; -. DR EnsemblBacteria; AAF40524; AAF40524; NMB0055. DR GeneID; 902157; -. DR KEGG; nme:NMB0055; -. DR PATRIC; 20355103; VBINeiMen85645_0089. DR eggNOG; ENOG4105II7; Bacteria. DR eggNOG; COG0345; LUCA. DR HOGENOM; HOG000230246; -. DR KO; K00286; -. DR OMA; RTFNEHQ; -. DR OrthoDB; EOG6JB16S; -. DR BioCyc; NMEN122586:GHGG-56-MONOMER; -. DR UniPathway; UPA00098; UER00361. DR EvolutionaryTrace; Q9K1N1; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.3730.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01925; P5C_reductase; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029036; P5CR_dimer. DR InterPro; IPR028939; ProC_N. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR Pfam; PF03807; F420_oxidored; 1. DR Pfam; PF14748; P5CR_dimer; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00112; proC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1YQG, ECO:0000213|PDB:2AG8}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}; KW NADP {ECO:0000213|PDB:2AG8, ECO:0000256|HAMAP-Rule:MF_01925}; KW Nucleotide-binding {ECO:0000213|PDB:2AG8}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925, KW ECO:0000313|EMBL:AAF40524.1}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 90 F420_oxidored. FT {ECO:0000259|Pfam:PF03807}. FT DOMAIN 154 258 P5CR_dimer. {ECO:0000259|Pfam:PF14748}. FT NP_BIND 10 11 NADP. {ECO:0000213|PDB:2AG8}. FT NP_BIND 31 36 NADP. {ECO:0000213|PDB:2AG8}. FT NP_BIND 87 89 NADP. {ECO:0000213|PDB:2AG8}. FT BINDING 65 65 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:2AG8}. FT BINDING 111 111 NADP. {ECO:0000213|PDB:2AG8}. SQ SEQUENCE 263 AA; 28341 MW; A8DE0DD667167A1C CRC64; MNVYFLGGGN MAAAVAGGLV KQGGYRIYIA NRGAEKRERL EKELGVETSA TLPELHSDDV LILAVKPQDM EAACKNIRTN GALVLSVAAG LSVGTLSRYL GGTRRIVRVM PNTPGKIGLG VSGMYAEAEV SETDRRIADR IMKSVGLTVW LDDEEKMHGI TGISGSGPAY VFYLLDALQN AAIRQGFDMA EARALSLATF KGAVALAEQT GEDFEKLQKN VTSKGGTTHE AVEAFRRHRV AEAISEGVCA CVRRSQEMER QYQ // ID Q9K0F4_NEIMB Unreviewed; 422 AA. AC Q9K0F4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=MafB-related protein {ECO:0000313|EMBL:AAF62314.1}; GN OrderedLocusNames=NMB0653 {ECO:0000313|EMBL:AAF62314.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62314.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62314.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62314.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62314.1; -; Genomic_DNA. DR RefSeq; NP_273695.1; NC_003112.2. DR RefSeq; WP_002248696.1; NC_003112.2. DR STRING; 122586.NMB0653; -. DR PaxDb; Q9K0F4; -. DR EnsemblBacteria; AAF62314; AAF62314; NMB0653. DR GeneID; 902765; -. DR KEGG; nme:NMB0653; -. DR PATRIC; 20356607; VBINeiMen85645_0822. DR eggNOG; ENOG41068QY; Bacteria. DR eggNOG; ENOG410XWQY; LUCA. DR HOGENOM; HOG000219102; -. DR OMA; DQWMQEN; -. DR OrthoDB; EOG67HJSG; -. DR BioCyc; NMEN122586:GHGG-680-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR029100; Ntox50. DR Pfam; PF06255; DUF1020; 2. DR Pfam; PF15542; Ntox50; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 422 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327763. FT DOMAIN 327 412 Ntox50. {ECO:0000259|Pfam:PF15542}. SQ SEQUENCE 422 AA; 45845 MW; B5428F16A296585F CRC64; MKPLRRLTNL LAACAVAAAA LIQPALAADL AQDPFITDNA QRQHYEPGGK YHLFGDPRGS VSDRTGKINV IQDYTHQMGN LLIQQANING TIGYHTRFSG HGHEEHAPFD NHAADSASEE KGNVDEGFTV YRLNWEGHEH HPADAYDGPK GGNYPKPTGA RDEYTYHVNG TARSIKLNPT DTRSIRQRIS DNYSNLGSNF SDRADEANRK MFEHNAKLDR WGNSMEFING VAAGALNPFI SAGEAVDQWM QENPNAAETV EALVNVLPFA KVKNLTKAAK PGKAAVSGDF SDSYKHNTAS RLSQSVDGEM FQTRNVDFKA KSIGTKIHDG AQGKHISGHR NYIEGKSTLN QNINPQELLN GIHSGAYPVI SKGARGNPVV DFGYPIGSDG KSGLSTNFGT IHSGKNGVHI VPANPKTIKK VQ // ID Q7DD48_NEIMB Unreviewed; 101 AA. AC Q7DD48; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Cell division protein ZapA {ECO:0000256|SAAS:SAAS00072473}; GN OrderedLocusNames=NMB2058 {ECO:0000313|EMBL:AAF42378.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42378.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42378.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42378.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Activator of cell division through the inhibition of CC FtsZ GTPase activity, therefore promoting FtsZ assembly into CC bundles of protofilaments necessary for the formation of the CC division Z ring. It is recruited early at mid-cell but it is not CC essential for cell division. {ECO:0000256|SAAS:SAAS00375380}. CC -!- SUBUNIT: Homodimer. Interacts with FtsZ. CC {ECO:0000256|SAAS:SAAS00375387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00072470}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42378.1; -; Genomic_DNA. DR PIR; C81012; C81012. DR RefSeq; NP_275048.1; NC_003112.2. DR RefSeq; WP_002215011.1; NC_003112.2. DR ProteinModelPortal; Q7DD48; -. DR STRING; 122586.NMB2058; -. DR PaxDb; Q7DD48; -. DR EnsemblBacteria; AAF42378; AAF42378; NMB2058. DR GeneID; 904022; -. DR KEGG; nme:NMB2058; -. DR PATRIC; 20360272; VBINeiMen85645_2636. DR eggNOG; ENOG4105W8B; Bacteria. DR eggNOG; COG3027; LUCA. DR HOGENOM; HOG000263522; -. DR KO; K09888; -. DR OMA; GFDMNEF; -. DR OrthoDB; EOG69SKDP; -. DR BioCyc; NMEN122586:GHGG-2121-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR InterPro; IPR007838; Cell_div_ZapA-like. DR Pfam; PF05164; ZapA; 1. DR SUPFAM; SSF102829; SSF102829; 1. PE 4: Predicted; KW Cell cycle {ECO:0000256|SAAS:SAAS00452627}; KW Cell division {ECO:0000256|SAAS:SAAS00452627}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00452647}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Septation {ECO:0000256|SAAS:SAAS00452627}. FT DOMAIN 6 72 ZapA. {ECO:0000259|Pfam:PF05164}. SQ SEQUENCE 101 AA; 10909 MW; 18938C359C04FCB6 CRC64; MNIEQVHIEV MHARLTVNTP AEEKDTLLQA VGMLNGKAEA IREGGRVADS EKIVIMAALN VVHDLLKTSL NGGDLAIGDF ARKIADMDNA CQKALSRLAQ E // ID Q7DDM5_NEIMB Unreviewed; 311 AA. AC Q7DDM5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464}; GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464, GN ECO:0000313|EMBL:AAF41035.1}; GN OrderedLocusNames=NMB0608 {ECO:0000313|EMBL:AAF41035.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41035.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41035.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41035.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000256|HAMAP- CC Rule:MF_01464, ECO:0000256|SAAS:SAAS00541769}. CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF-YajC and YidC. {ECO:0000256|HAMAP- CC Rule:MF_01464}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01464}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41035.1; -; Genomic_DNA. DR PIR; A81179; A81179. DR RefSeq; NP_273652.1; NC_003112.2. DR RefSeq; WP_002219655.1; NC_003112.2. DR ProteinModelPortal; Q7DDM5; -. DR STRING; 122586.NMB0608; -. DR PaxDb; Q7DDM5; -. DR EnsemblBacteria; AAF41035; AAF41035; NMB0608. DR GeneID; 902722; -. DR KEGG; nme:NMB0608; -. DR PATRIC; 20356501; VBINeiMen85645_0770. DR eggNOG; ENOG4108JIS; Bacteria. DR eggNOG; COG0341; LUCA. DR HOGENOM; HOG000245914; -. DR KO; K03074; -. DR OMA; IDMNLEV; -. DR OrthoDB; EOG676Z5R; -. DR BioCyc; NMEN122586:GHGG-634-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01464_B; SecF_B; 1. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR InterPro; IPR005665; SecF_bac. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF02355; SecD_SecF; 1. DR PRINTS; PR01755; SECFTRNLCASE. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR00966; 3a0501s07; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01464}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}. FT TRANSMEM 15 35 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 133 153 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 172 192 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 250 270 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 272 292 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. SQ SEQUENCE 311 AA; 34369 MW; 13EC50706778F129 CRC64; MELFKIKRDI PFMSYGKLTT FISLVTFIAA VFFLVTRGLN FSVEFTGGTV MEVQYQQGAD VNKMRERLDT LKIGDVQVQA LGTNKHIMIR LPNKEGVTSA QLSNQVMDLL KKDSPDVTLR QVEFIGPQVG EELVSNGLMA LGFVVIGIII YLSMRFEWRF AVSAIIANMH DIVIILGCFA FFQWEFSLTV LAGILAVLGY SVNESVVVFD RIRENFRKPA MRGHAVPEVI DNAITATMSR TIITHGSTEA MVVSMLVFGG AALHGFSMAL TIGIVFGIYS SVLVASPLLL MFGLSRDNIG KEPKKKEEIV V // ID Q9K1P4_NEIMB Unreviewed; 109 AA. AC Q9K1P4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=PhnA protein {ECO:0000313|EMBL:AAF40508.1}; GN Name=phnA {ECO:0000313|EMBL:AAF40508.1}; GN OrderedLocusNames=NMB0037 {ECO:0000313|EMBL:AAF40508.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40508.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40508.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40508.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40508.1; -; Genomic_DNA. DR PIR; G81244; G81244. DR RefSeq; NP_273103.1; NC_003112.2. DR RefSeq; WP_002225768.1; NC_003112.2. DR ProteinModelPortal; Q9K1P4; -. DR SMR; Q9K1P4; 2-108. DR STRING; 122586.NMB0037; -. DR PaxDb; Q9K1P4; -. DR EnsemblBacteria; AAF40508; AAF40508; NMB0037. DR GeneID; 902140; -. DR KEGG; nme:NMB0037; -. DR PATRIC; 20355029; VBINeiMen85645_0051. DR eggNOG; ENOG4108Z8G; Bacteria. DR eggNOG; COG2824; LUCA. DR HOGENOM; HOG000228486; -. DR KO; K06193; -. DR OMA; SCLYEWN; -. DR OrthoDB; EOG6J752H; -. DR BioCyc; NMEN122586:GHGG-38-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR004624; PhnA. DR InterPro; IPR013988; PhnA_C. DR InterPro; IPR013987; PhnA_N. DR Pfam; PF03831; PhnA; 1. DR Pfam; PF08274; PhnA_Zn_Ribbon; 1. DR TIGRFAMs; TIGR00686; phnA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 30 PhnA_Zn_Ribbon. FT {ECO:0000259|Pfam:PF08274}. FT DOMAIN 43 109 PhnA. {ECO:0000259|Pfam:PF03831}. SQ SEQUENCE 109 AA; 11758 MW; 249E5C7EE009E4D3 CRC64; MSLPPCPQCA SEYTYEDGGQ YICPECAHEW NETESAADLA AQVRDANGAV LQNGDTVILI KDLKVKGSSM VIKQGTKVKG IRLQEGDHNI GCKIDGSAMN LKSEFVKKA // ID Q9K0S5_NEIMB Unreviewed; 650 AA. AC Q9K0S5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40934.1}; GN OrderedLocusNames=NMB0502 {ECO:0000313|EMBL:AAF40934.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40934.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40934.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40934.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40934.1; -; Genomic_DNA. DR PIR; E81190; E81190. DR RefSeq; NP_273548.1; NC_003112.2. DR RefSeq; WP_002225606.1; NC_003112.2. DR STRING; 122586.NMB0502; -. DR PaxDb; Q9K0S5; -. DR EnsemblBacteria; AAF40934; AAF40934; NMB0502. DR GeneID; 902618; -. DR KEGG; nme:NMB0502; -. DR PATRIC; 20356254; VBINeiMen85645_0647. DR eggNOG; ENOG4107EI8; Bacteria. DR eggNOG; COG3210; LUCA. DR OrthoDB; EOG6FFS4T; -. DR BioCyc; NMEN122586:GHGG-527-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR029501; EndoU_bac. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF14436; EndoU_bacteria; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 119 270 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 286 334 PT-VENN. {ECO:0000259|Pfam:PF04829}. FT DOMAIN 504 649 EndoU_bacteria. FT {ECO:0000259|Pfam:PF14436}. SQ SEQUENCE 650 AA; 69949 MW; 4B7C182DE67B532B CRC64; MRKVCASART RSMIYGSMPS EKLTIFQTAF VMQVNIQIPY ILPRCVRAED TPYACYLKQL QVTKDVNWNQ VQLAYDKWDY KQEGLTGAGA AIIALAVTVV TAGAGAGAAL GLNGAAAAAT DAAFASLASQ ASVSLINNKG NIGNTLKELG RSSTVKNLMV AVATAGVADK IGASALNNVS DKQWINNLTV NLANAGSAAL INTAVNGGSL KDNLEANILA ALVNTAHGEA ASKIKQLDQH YITHKIAHAI AGCAAAAANK GKCQDGAIGA AVGEIVGEAL TNGKNPDTLT AKEREQILAY SKLVAGTVSG VVGGDVNAAA NAAEVAVKNN QLSDKEGREF DNEMTACAKQ NNPQLCRKNT VKKYQNVADK RLAASIAICT DISRSTECRT IRKQHLIDSR SLHSSWEAGL IGKDDEWYKL FSKSYTQADL ALQSYHLNTA AKSWLQSGNT KPLSEWMSDQ GYTLISGVNP RFIPIPRGFV KQNTPITNVK YPEGISFDTN LKRHLANADG FSQKQGIKGA HNRTNFMAEL NSRGGRVKSE TQTDIEGITR IKYEIPTLDR TGKPDGGFKE ISSIKTVYNP KKFSDDKILQ MAQNAASQGY SKASKIAQNE RTKSISERKN VIQFSETFDG IKFRSYFDVN TGRITNIHPE // ID Q9K0L1_NEIMB Unreviewed; 222 AA. AC Q9K0L1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=IS1016C2 transposase {ECO:0000313|EMBL:AAF41011.1}; GN OrderedLocusNames=NMB0583 {ECO:0000313|EMBL:AAF41011.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41011.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41011.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41011.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41011.1; -; Genomic_DNA. DR PIR; A81182; A81182. DR RefSeq; NP_273627.1; NC_003112.2. DR RefSeq; WP_002225556.1; NC_003112.2. DR PaxDb; Q9K0L1; -. DR EnsemblBacteria; AAF41011; AAF41011; NMB0583. DR GeneID; 902698; -. DR KEGG; nme:NMB0583; -. DR PATRIC; 20356451; VBINeiMen85645_0745. DR eggNOG; ENOG4105S1F; Bacteria. DR eggNOG; ENOG4111JFI; LUCA. DR HOGENOM; HOG000218644; -. DR KO; K07488; -. DR OMA; IREVICY; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NMEN122586:GHGG-609-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. DR SMART; SM01126; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 222 AA; 25288 MW; 005FBD7C71B36223 CRC64; MLPSKYEDNA LQIKEKSTER TAPFFVLEVT ARSAADILGI HPNSAALFYR KIRTVINHHL ALAADEVFEG PVEPDESDFG GRRKGRRGRG AAGKVVVFGI LKRNGRVYTV VVDNAKSETL LPVIKKKIMP DSIVYTDSLS SYDKLDVSGF IHYRINHSKE CADRQNHING IENFWNQAKR VLRKYNGIDR KSFPLFLKEC EFRFNFGTPS QQLKILRDWC GI // ID Q9JYQ0_NEIMB Unreviewed; 160 AA. AC Q9JYQ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Acyl CoA thioester hydrolase family protein {ECO:0000313|EMBL:AAF41838.1}; GN OrderedLocusNames=NMB1482 {ECO:0000313|EMBL:AAF41838.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41838.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41838.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41838.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41838.1; -; Genomic_DNA. DR PIR; G81079; G81079. DR RefSeq; NP_274490.1; NC_003112.2. DR RefSeq; WP_002225088.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ0; -. DR STRING; 122586.NMB1482; -. DR PaxDb; Q9JYQ0; -. DR EnsemblBacteria; AAF41838; AAF41838; NMB1482. DR GeneID; 903904; -. DR KEGG; nme:NMB1482; -. DR PATRIC; 20358730; VBINeiMen85645_1874. DR eggNOG; ENOG4108S4H; Bacteria. DR eggNOG; COG1607; LUCA. DR HOGENOM; HOG000044842; -. DR OMA; SMDEMVF; -. DR OrthoDB; EOG65XN1H; -. DR BioCyc; NMEN122586:GHGG-1522-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR033120; HOTDOG_ACOT. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR006683; Thioestr_dom. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR PROSITE; PS51770; HOTDOG_ACOT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41838.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 120 HotDog ACOT-type. FT {ECO:0000259|PROSITE:PS51770}. SQ SEQUENCE 160 AA; 17880 MW; 152768F1BDBDCFE0 CRC64; MTQQRQLPSH ELIMSELMMP DTANFSGNVH GGELLLLLDQ VAYSCASRYS GNYCVTLSVD KVLFKEPIHV GDLVTFYASV NYTGRTSMEI GIRVEAQNIR TGEIRHTNSC YFTMVAVKDG KPVPVPPLEI LTDRQRCRYE KAKKRRDISL QASGDVSCGC // ID Q9K184_NEIMB Unreviewed; 210 AA. AC Q9K184; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015}; DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015}; GN OrderedLocusNames=NMB0283 {ECO:0000313|EMBL:AAF40736.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40736.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40736.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40736.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: A cytokinin riboside 5'-phosphate + H(2)O = a CC cytokinin + D-ribose 5'-phosphate. CC {ECO:0000256|RuleBase:RU363015}. CC -!- SIMILARITY: Belongs to the LOG family. CC {ECO:0000256|RuleBase:RU363015}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40736.1; -; Genomic_DNA. DR PIR; C81216; C81216. DR RefSeq; NP_273339.1; NC_003112.2. DR RefSeq; WP_002215682.1; NC_003112.2. DR ProteinModelPortal; Q9K184; -. DR STRING; 122586.NMB0283; -. DR PaxDb; Q9K184; -. DR EnsemblBacteria; AAF40736; AAF40736; NMB0283. DR GeneID; 902394; -. DR KEGG; nme:NMB0283; -. DR PATRIC; 20355662; VBINeiMen85645_0355. DR eggNOG; ENOG4105CNZ; Bacteria. DR eggNOG; COG1611; LUCA. DR HOGENOM; HOG000156897; -. DR KO; K06966; -. DR OMA; DHADYAF; -. DR OrthoDB; EOG6DRPKX; -. DR BioCyc; NMEN122586:GHGG-298-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-EC. DR GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR005269; LOG. DR InterPro; IPR031100; LOG_fam. DR Pfam; PF03641; Lysine_decarbox; 1. DR TIGRFAMs; TIGR00730; TIGR00730; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytokinin biosynthesis {ECO:0000256|RuleBase:RU363015}; KW Hydrolase {ECO:0000256|RuleBase:RU363015}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 210 AA; 22744 MW; 6AF4C849715EA793 CRC64; MENTNRVPEQ ARYDAERRQA DEALAGVFPA VSIFGSARTP QNHADYAFAC RLARRLSDSG IAVISGGGPG IMEAANKGAF AGKSVSVGLN IVLPHEQKPN PYQDIALRFS RFAERKAVFF RYSQAYVVMP GGFGTLDELF EILTLVQTGK VPPRPIVLVG KAFWSGLAEW INAQLLARGL ISEGAVSLFA ISDDEDEIVA YLSEHGLQTA // ID Q9K0J1_NEIMB Unreviewed; 88 AA. AC Q9K0J1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41033.1}; GN OrderedLocusNames=NMB0606 {ECO:0000313|EMBL:AAF41033.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41033.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41033.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41033.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41033.1; -; Genomic_DNA. DR PIR; G81178; G81178. DR RefSeq; NP_273650.1; NC_003112.2. DR RefSeq; WP_002214291.1; NC_003112.2. DR ProteinModelPortal; Q9K0J1; -. DR STRING; 122586.NMB0606; -. DR PaxDb; Q9K0J1; -. DR EnsemblBacteria; AAF41033; AAF41033; NMB0606. DR GeneID; 902720; -. DR KEGG; nme:NMB0606; -. DR PATRIC; 20356497; VBINeiMen85645_0768. DR eggNOG; ENOG4105VIE; Bacteria. DR eggNOG; COG1862; LUCA. DR HOGENOM; HOG000018859; -. DR KO; K03210; -. DR OMA; ADGQAQN; -. DR OrthoDB; EOG6WQDDS; -. DR BioCyc; NMEN122586:GHGG-632-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003849; Preprotein_translocase_YajC. DR Pfam; PF02699; YajC; 1. DR PRINTS; PR01853; YAJCTRNLCASE. DR SMART; SM01323; YajC; 1. DR TIGRFAMs; TIGR00739; yajC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 88 AA; 9709 MW; C751556C81A8EE44 CRC64; MNQAVAQFAP LVLIMVVFYF LIMRPQQKKF KAHQAMLAAL KVGDKVVLAA GFKGKVTRVG EQFFTVDIGQ GTKIEVEVER NAIAAKVD // ID Q9K1R2_NEIMB Unreviewed; 305 AA. AC Q9K1R2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Cell division protein FtsX {ECO:0000256|PIRNR:PIRNR003097}; GN OrderedLocusNames=NMB0008 {ECO:0000313|EMBL:AAF40487.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40487.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40487.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40487.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular CC division. {ECO:0000256|PIRNR:PIRNR003097}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|PIRNR:PIRNR003097}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC FtsX subfamily. {ECO:0000256|PIRNR:PIRNR003097}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40487.1; -; Genomic_DNA. DR PIR; F81247; F81247. DR RefSeq; NP_273074.1; NC_003112.2. DR RefSeq; WP_002225753.1; NC_003112.2. DR STRING; 122586.NMB0008; -. DR PaxDb; Q9K1R2; -. DR EnsemblBacteria; AAF40487; AAF40487; NMB0008. DR GeneID; 902110; -. DR KEGG; nme:NMB0008; -. DR PATRIC; 20354945; VBINeiMen85645_0009. DR eggNOG; ENOG4105CRP; Bacteria. DR eggNOG; COG2177; LUCA. DR HOGENOM; HOG000270397; -. DR KO; K09811; -. DR OMA; ITIFARR; -. DR OrthoDB; EOG60W7WW; -. DR BioCyc; NMEN122586:GHGG-8-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR004513; ABC_transpt_FtsX. DR Pfam; PF02687; FtsX; 1. DR PIRSF; PIRSF003097; FtsX; 1. DR TIGRFAMs; TIGR00439; ftsX; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|PIRNR:PIRNR003097, KW ECO:0000313|EMBL:AAF40487.1}; KW Cell division {ECO:0000256|PIRNR:PIRNR003097, KW ECO:0000313|EMBL:AAF40487.1}; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR003097}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR003097}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|PIRNR:PIRNR003097, KW ECO:0000256|SAAS:SAAS00573714, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 293 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 180 294 FtsX. {ECO:0000259|Pfam:PF02687}. SQ SEQUENCE 305 AA; 34135 MW; 7144881CA7AB9A03 CRC64; MSIIHYLSLH VESARTALKQ LLRQPFGTLL TLMMLAVAMT LPLFMHLGIQ SGQSVLGKLN ESPQITIYME TSAAQSDSDT VRSLLARDKR LDNIRFIGKE DGLEELQSNL DQNLISMLDG NPLPDVFIVT PDPATTPAQM QAIYRDITKL PMVESASMDT EWVQTLYQIN EFIRKILWFL SLTLGMAFVL VAHNTIRLQI LSRKEEIEIT KLLGAPASFI RRPFLYQAMW QSILSAAVSL GLCGWLLSAV RPLVDAIFKP YGLNIGWRFF YAGELGLVFG FVIALGVFGA WLATTQHLLG FKAKK // ID Q9JXL1_NEIMB Unreviewed; 322 AA. AC Q9JXL1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Iron(III) ABC transporter, permease protein {ECO:0000313|EMBL:AAF42317.1}; GN OrderedLocusNames=NMB1990 {ECO:0000313|EMBL:AAF42317.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42317.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42317.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42317.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. CC {ECO:0000256|SAAS:SAAS00535775}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42317.1; -; Genomic_DNA. DR PIR; E81018; E81018. DR RefSeq; NP_274982.1; NC_003112.2. DR RefSeq; WP_010981018.1; NC_003112.2. DR ProteinModelPortal; Q9JXL1; -. DR STRING; 122586.NMB1990; -. DR PaxDb; Q9JXL1; -. DR EnsemblBacteria; AAF42317; AAF42317; NMB1990. DR GeneID; 904141; -. DR KEGG; nme:NMB1990; -. DR PATRIC; 20360077; VBINeiMen85645_2543. DR eggNOG; ENOG4105DHS; Bacteria. DR eggNOG; COG4606; LUCA. DR HOGENOM; HOG000045408; -. DR KO; K02015; -. DR OMA; VFMLLIR; -. DR OrthoDB; EOG61ZTDC; -. DR BioCyc; NMEN122586:GHGG-2047-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00417415}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00417415, KW ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417373}. FT TRANSMEM 53 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 222 240 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 315 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 322 AA; 34512 MW; B4607F6B3DAC9109 CRC64; MTAKPFSLNL TNLLLLAVLF AVSLSVGVAD FRWSDVFSLS DSQQVMFISR LPRTFAIVLT GASMAVAGMI MQILMRNRFV EPSMVGASQS AALGLLLMTL LLPAAPLPAK MSVAAVAALI GMLVFMLLIR RLPPTAQLMV PLVGIIFGGV IEAVATFIAY ENEMLQMLGV WQQGDFSSVL LGRYELLWIT GGLAVFAYLI ADRLTILGLG ETVSVNLGLN RTAVLWSGLI IVALITSLVI VTVGNIPFIG LVVPNIISRL MGDRLRQSLP AVALLGASLV LLCDIIGRVI VFPFEIPVST VFGVLGTALF LWLLLRKPAY AV // ID Q9K191_NEIMB Unreviewed; 318 AA. AC Q9K191; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40730.1}; GN OrderedLocusNames=NMB0276 {ECO:0000313|EMBL:AAF40730.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40730.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40730.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40730.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40730.1; -; Genomic_DNA. DR PIR; A81217; A81217. DR RefSeq; NP_273332.1; NC_003112.2. DR RefSeq; WP_002224842.1; NC_003112.2. DR ProteinModelPortal; Q9K191; -. DR STRING; 122586.NMB0276; -. DR ESTHER; neime-NMB0276; abh_upf0017. DR PaxDb; Q9K191; -. DR EnsemblBacteria; AAF40730; AAF40730; NMB0276. DR GeneID; 902387; -. DR KEGG; nme:NMB0276; -. DR PATRIC; 20355638; VBINeiMen85645_0343. DR eggNOG; ENOG4105DNZ; Bacteria. DR eggNOG; COG0429; LUCA. DR HOGENOM; HOG000264007; -. DR KO; K07019; -. DR OMA; HLQTLWG; -. DR OrthoDB; EOG6C5RKG; -. DR BioCyc; NMEN122586:GHGG-291-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000952; AB_hydrolase_4_CS. DR InterPro; IPR012020; ABHD4. DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS01133; UPF0017; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 318 AA; 34921 MW; 9D906608777BDA36 CRC64; MILTPPDTPF FLRNGNADTI AAKFLQRPAP AYRRELLPDS TGKTKVAYDF SDGISPDAPL VVLFHGLEGS SRSHYAVELM LAVRDRGWHG VVVHFRSCGG IANTAPVFYH LGDTAEIAFT LDTFAARYRE IYAVGVSLGG NALAKYLGEQ GKKALPQAAA VISAPVDAEA AGRRFDSGIT RLLYTRYFLR TLIPKAKSLQ GFQTAFAAGC KTLGEFDDRF TAPLHGFADR HDYYRQTSCK PLLKHVAKPL LLLNAVNDPF LPPEALPRAD EVSEAVTLFQ PAYGGHVGFV SSTGGRLHLQ WLPQTVLSYF DSFRTNRR // ID Q9K0C4_NEIMB Unreviewed; 514 AA. AC Q9K0C4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931, GN ECO:0000313|EMBL:AAF41108.1}; GN OrderedLocusNames=NMB0690 {ECO:0000313|EMBL:AAF41108.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41108.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41108.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41108.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. CC {ECO:0000256|HAMAP-Rule:MF_01931}. CC -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate + CC L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate CC + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRNR:PIRNR000485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01931}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRNR:PIRNR000485}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000256|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC purine/pyrimidine phosphoribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41108.1; -; Genomic_DNA. DR PIR; A81170; A81170. DR RefSeq; NP_273732.1; NC_003112.2. DR RefSeq; WP_002225492.1; NC_003112.2. DR ProteinModelPortal; Q9K0C4; -. DR SMR; Q9K0C4; 2-485. DR STRING; 122586.NMB0690; -. DR PaxDb; Q9K0C4; -. DR EnsemblBacteria; AAF41108; AAF41108; NMB0690. DR GeneID; 902802; -. DR KEGG; nme:NMB0690; -. DR PATRIC; 20356707; VBINeiMen85645_0875. DR eggNOG; ENOG4105CBA; Bacteria. DR eggNOG; COG0034; LUCA. DR HOGENOM; HOG000033687; -. DR KO; K00764; -. DR OMA; AARVHMG; -. DR OrthoDB; EOG6KT2Q1; -. DR BioCyc; NMEN122586:GHGG-718-MONOMER; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_01931; PurF; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005854; PurF. DR Pfam; PF00156; Pribosyltran; 1. DR PIRSF; PIRSF000485; Amd_phspho_trans; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01134; purF; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AAF41108.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AAF41108.1}. FT DOMAIN 2 241 Glutamine amidotransferase type-2. FT {ECO:0000256|HAMAP-Rule:MF_01931, FT ECO:0000259|PROSITE:PS51278}. FT ACT_SITE 2 2 For GATase activity. FT {ECO:0000256|PIRSR:PIRSR000485-1}. FT ACT_SITE 2 2 Nucleophile. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 310 310 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 372 372 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 373 373 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. SQ SEQUENCE 514 AA; 56108 MW; DD27A33BD581A6CF CRC64; MCGVLGLVSH EPVNQLLYDG LQMLQHRGQD AAGIATAEGG TFHMHKGKGM VREVFRTRNM RDLTGNAGIA HVRYPTAGNA GSSAEAQPFY VSSPFGIVLA HNGNLTNTAE LYENVCNKHL RHVNTSSDSE VLLNVFAHEL RREVSKNADP HRLNADNIFN AVAQVHRLVR GAYGVIAMIA GYGMLAFRDP YGIRPLVLGS QTDSEGRKSY AVASESVAFN ALTYDLERDI RPGEAVFVGF DGTMIARQCS DRAKLSPCLF EYVYFARPDS VIDGVSVYQS RLDMGVSLAE KIKRELPVDG IDVVMPIPDT SRPSAMELAV HLDKPYREGL IKNRYIGRTF IMPGQATRKK SVRQKLSPME TEFAGKSVLL VDDSIVRGTT SREIVEMVRA AGARKVYIAS AAPEVRYPNV YGIDMPTREE LIANGRSAAE IAAEIGADGI VFQDLGDLEA VVKALNPKIE SFDSSCFNGI YQTGDIDDAY LDRLSAEKSG CGGLKIHPSR MEHSISISDA GDEE // ID Q9JY46_NEIMB Unreviewed; 316 AA. AC Q9JY46; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Pilin gene inverting protein PivNM-2 {ECO:0000313|EMBL:AAF42093.1}; GN Name=pivNM-2 {ECO:0000313|EMBL:AAF42093.1}; GN OrderedLocusNames=NMB1750 {ECO:0000313|EMBL:AAF42093.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42093.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42093.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42093.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42093.1; -; Genomic_DNA. DR PIR; G81045; G81045. DR RefSeq; NP_274751.1; NC_003112.2. DR RefSeq; WP_002219741.1; NC_003112.2. DR STRING; 122586.NMB1750; -. DR PaxDb; Q9JY46; -. DR EnsemblBacteria; AAF42093; AAF42093; NMB1750. DR GeneID; 903347; -. DR KEGG; nme:NMB1750; -. DR PATRIC; 20359469; VBINeiMen85645_2240. DR eggNOG; ENOG4105T1S; Bacteria. DR eggNOG; COG3547; LUCA. DR HOGENOM; HOG000130878; -. DR KO; K07486; -. DR OMA; CFGVLKT; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NMEN122586:GHGG-1805-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR003346; Transposase_20. DR InterPro; IPR002525; Transposase_N. DR Pfam; PF01548; DEDD_Tnp_IS110; 1. DR Pfam; PF02371; Transposase_20; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 148 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. SQ SEQUENCE 316 AA; 36601 MW; 9231E5F4EC07327D CRC64; MYLGIDVSKL TIDCCLIVDG QNYQKKFQNN KGGFEQLINW LQSHKVNDKL HCVCEATGTY YEALAEYLYS RYTITVENPR KIKGYAIAEL QRSKTDTQDA KLIAQYCQDR KHKLKAWKPP TKEQKQLQEI ARYLDYLKQQ RATEKAKQHE APDYIKSHIQ TTISNLTAQI QIVKKQLLQF YKDNPSYNNL RKRLKTITGI GEQATAVLLS TYKRHEFKNA RQFTAYLGLD PRKFQSGTSV NGKSRISKIG SSEIRKSLYM PALVAYRCNA FPEFVGRLKN KGKHIKLILI AIMRKLAVIA FTILQNGQDF QVERYK // ID Q9JY91_NEIMB Unreviewed; 333 AA. AC Q9JY91; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=L-asparaginase I {ECO:0000313|EMBL:AAF42036.1}; DE EC=3.5.1.1 {ECO:0000313|EMBL:AAF42036.1}; GN Name=ansA {ECO:0000313|EMBL:AAF42036.1}; GN OrderedLocusNames=NMB1688 {ECO:0000313|EMBL:AAF42036.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42036.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42036.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42036.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42036.1; -; Genomic_DNA. DR PIR; A81054; A81054. DR RefSeq; NP_274692.1; NC_003112.2. DR RefSeq; WP_010980972.1; NC_003112.2. DR ProteinModelPortal; Q9JY91; -. DR STRING; 122586.NMB1688; -. DR PaxDb; Q9JY91; -. DR EnsemblBacteria; AAF42036; AAF42036; NMB1688. DR GeneID; 903419; -. DR KEGG; nme:NMB1688; -. DR PATRIC; 20359327; VBINeiMen85645_2170. DR eggNOG; COG0252; LUCA. DR HOGENOM; HOG000227974; -. DR KO; K01424; -. DR OMA; LECYGSG; -. DR OrthoDB; EOG683S61; -. DR BioCyc; NMEN122586:GHGG-1743-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1170; -; 1. DR Gene3D; 3.40.50.40; -; 1. DR InterPro; IPR006034; Asparaginase/glutaminase. DR InterPro; IPR020827; Asparaginase/glutaminase_AS1. DR InterPro; IPR027473; L-asparaginase_C. DR InterPro; IPR027474; L-asparaginase_N. DR Pfam; PF00710; Asparaginase; 1. DR PIRSF; PIRSF001220; L-ASNase_gatD; 1. DR PRINTS; PR00139; ASNGLNASE. DR SMART; SM00870; Asparaginase; 1. DR SUPFAM; SSF53774; SSF53774; 1. DR PROSITE; PS00144; ASN_GLN_ASE_1; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42036.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 181 Asparaginase. {ECO:0000259|Pfam:PF00710}. FT REGION 88 89 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR001220-2}. FT ACT_SITE 16 16 O-isoaspartyl threonine intermediate. FT {ECO:0000256|PIRSR:PIRSR001220-1}. FT BINDING 57 57 Substrate. FT {ECO:0000256|PIRSR:PIRSR001220-2}. SQ SEQUENCE 333 AA; 35888 MW; 206189A6C86B211F CRC64; MMSMKQKIFV LYTGGTIGMT QSSEGLRPDT ALVSQALSPF SDGLDFEWHV CNPLIDSSSV TLQHWRDWLD IIADKLPSCD GILILHGTDS MAYTANLLAL ALQGLGKPIV LTGSQWPYAA ENSDAPRNLS TAVAAFSLKL KQTVIAFDGK LYPAVGSSKV STETAAGFDN PHFGTLAEWD ETRGWHNLRL PSQDAAAVSD GLKIRYPDPQ AKIAVRTLIP GFAVQELADG LGQLPAQALI LQSYGHGNTP ADEGFIRAVR DFARQGKLLL NISQVRQGKT AAVYAQGNAF RNSGIINGGK CNLETATALM TLAVSQGWGK EDVYKELVRL KLV // ID Q9JYR5_NEIMB Unreviewed; 163 AA. AC Q9JYR5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41822.1}; GN OrderedLocusNames=NMB1464 {ECO:0000313|EMBL:AAF41822.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41822.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41822.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41822.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41822.1; -; Genomic_DNA. DR PIR; D81080; D81080. DR RefSeq; NP_274474.1; NC_003112.2. DR RefSeq; WP_002219860.1; NC_003112.2. DR ProteinModelPortal; Q9JYR5; -. DR STRING; 122586.NMB1464; -. DR PaxDb; Q9JYR5; -. DR EnsemblBacteria; AAF41822; AAF41822; NMB1464. DR GeneID; 903886; -. DR KEGG; nme:NMB1464; -. DR PATRIC; 20358681; VBINeiMen85645_1850. DR eggNOG; ENOG4108UK5; Bacteria. DR eggNOG; COG1943; LUCA. DR HOGENOM; HOG000117045; -. DR KO; K07491; -. DR OMA; YRRHVDY; -. DR OrthoDB; EOG65XN2G; -. DR BioCyc; NMEN122586:GHGG-1504-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR Pfam; PF01797; Y1_Tnp; 1. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 163 AA; 19774 MW; C14DDB79D47D722C CRC64; MKYRRFYRNG GTYFFTVVTN KRQKILTDDA VRLALRQAVM AVRERYPFEI LAWVLMPDHL HTIWRLPDND SAYSERWRQI KRHSQYLIGG NLRLWQKRFW EYTIRDEADF AWHFDYLHFN PVKHGYVGQI SDWGFSTFHR YVKQGIYPHN WGGGNADFSI GYD // ID Q7DD65_NEIMB Unreviewed; 78 AA. AC Q7DD65; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=ATP synthase subunit c {ECO:0000256|SAAS:SAAS00242779}; GN Name=atpE {ECO:0000313|EMBL:AAF42268.1}; GN OrderedLocusNames=NMB1939 {ECO:0000313|EMBL:AAF42268.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42268.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42268.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42268.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000256|SAAS:SAAS00499073}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000256|RuleBase:RU004221}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42268.1; -; Genomic_DNA. DR PIR; D81025; D81025. DR RefSeq; NP_274933.1; NC_003112.2. DR RefSeq; WP_002214801.1; NC_003112.2. DR ProteinModelPortal; Q7DD65; -. DR STRING; 122586.NMB1939; -. DR PaxDb; Q7DD65; -. DR EnsemblBacteria; AAF42268; AAF42268; NMB1939. DR GeneID; 904213; -. DR KEGG; nme:NMB1939; -. DR PATRIC; 20359925; VBINeiMen85645_2467. DR eggNOG; ENOG4105KY6; Bacteria. DR eggNOG; COG0636; LUCA. DR HOGENOM; HOG000235244; -. DR KO; K02110; -. DR OMA; WGLICSK; -. DR OrthoDB; EOG68H8G3; -. DR BioCyc; NMEN122586:GHGG-1996-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro. DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR Gene3D; 1.20.20.10; -; 1. DR InterPro; IPR000454; ATPase_F0-cplx_csu. DR InterPro; IPR005953; ATPase_F0-cplx_csu_bac/chlpt. DR InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS. DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR SUPFAM; SSF81333; SSF81333; 1. DR TIGRFAMs; TIGR01260; ATP_synt_c; 1. DR PROSITE; PS00605; ATPASE_C; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00499070}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU003372}; KW Hydrolase {ECO:0000313|EMBL:AAF42268.1}; KW Ion transport {ECO:0000256|RuleBase:RU003372}; KW Membrane {ECO:0000256|SAAS:SAAS00499070, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003372}. FT TRANSMEM 48 72 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 68 ATP-synt_C. {ECO:0000259|Pfam:PF00137}. SQ SEQUENCE 78 AA; 7815 MW; 53EA2B212E90D432 CRC64; MGLIAIACGL IVALGALGAS IGIAMVGSKY LESSARQPEL IGPLQTKLFL IAGLIDAAFL IGVAIALLFA FVNPFAGA // ID Q9JXR4_NEIMB Unreviewed; 308 AA. AC Q9JXR4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446}; DE EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446}; GN Name=fabD {ECO:0000313|EMBL:AAF42248.1}; GN OrderedLocusNames=NMB1918 {ECO:0000313|EMBL:AAF42248.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42248.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42248.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42248.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA CC + a malonyl-[acyl-carrier-protein]. CC {ECO:0000256|PIRNR:PIRNR000446}. CC -!- SIMILARITY: Belongs to the fabD family. CC {ECO:0000256|PIRNR:PIRNR000446}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42248.1; -; Genomic_DNA. DR PIR; B81026; B81026. DR RefSeq; NP_274912.1; NC_003112.2. DR RefSeq; WP_002225819.1; NC_003112.2. DR ProteinModelPortal; Q9JXR4; -. DR SMR; Q9JXR4; 3-300. DR STRING; 122586.NMB1918; -. DR PaxDb; Q9JXR4; -. DR EnsemblBacteria; AAF42248; AAF42248; NMB1918. DR GeneID; 904244; -. DR KEGG; nme:NMB1918; -. DR PATRIC; 20359883; VBINeiMen85645_2446. DR eggNOG; ENOG4105CJF; Bacteria. DR eggNOG; COG0331; LUCA. DR HOGENOM; HOG000036503; -. DR KO; K00645; -. DR OMA; FHCALMQ; -. DR OrthoDB; EOG6W19KW; -. DR BioCyc; NMEN122586:GHGG-1975-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.366.10; -; 2. DR InterPro; IPR001227; Ac_transferase_dom. DR InterPro; IPR014043; Acyl_transferase. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc. DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. DR InterPro; IPR020801; PKS_acyl_transferase. DR Pfam; PF00698; Acyl_transf_1; 1. DR PIRSF; PIRSF000446; Mct; 1. DR SMART; SM00827; PKS_AT; 1. DR SUPFAM; SSF52151; SSF52151; 2. DR SUPFAM; SSF55048; SSF55048; 1. DR TIGRFAMs; TIGR00128; fabD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000446, KW ECO:0000313|EMBL:AAF42248.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR000446, KW ECO:0000313|EMBL:AAF42248.1}. FT ACT_SITE 90 90 {ECO:0000256|PIRSR:PIRSR000446-1}. FT ACT_SITE 199 199 {ECO:0000256|PIRSR:PIRSR000446-1}. SQ SEQUENCE 308 AA; 31723 MW; A18026509A1FD4CC CRC64; MSFAFFFPGQ GSQSLGMMNG FAEHAIVKNT FAEASAILGQ DLWAMINGSD AEIIGQTVNT QPIMLAAGVA VYRAYLEAGG KTPAAVAGHS LGEYTALVAA GALNFADAVK LVRLRAELMQ SAVPQGVGAM AAILGLEDEQ VKAICAEAAQ SEVVEAVNFN SPGQIVIAGN AAAVGRAMAA AKEAGAKRAL PLPVSVPSHC SLMKPAADKL AEALKTVEIK QPQIRVIHNA DVAAYDDADK IKDALVRQLY SPVRWTETVN ALVSDGIAES AECGPGKVLA GLAKRINKAA ACSALTDAGQ VAAFIEAH // ID Q9K1E4_NEIMB Unreviewed; 796 AA. AC Q9K1E4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 118. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00555050}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646}; GN Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898, GN ECO:0000313|EMBL:AAF40668.1}; GN OrderedLocusNames=NMB0212 {ECO:0000313|EMBL:AAF40668.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40668.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40668.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40668.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898, CC ECO:0000256|SAAS:SAAS00470725}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt CC bridges with both the protein and the DNA. Can also accept other CC divalent metal cations, such as Mn(2+) or Ca(2+). CC {ECO:0000256|HAMAP-Rule:MF_01898}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming CC negative supercoils. Not all organisms have 2 type II CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40668.1; -; Genomic_DNA. DR PIR; D81225; D81225. DR RefSeq; NP_273269.1; NC_003112.2. DR RefSeq; WP_002243960.1; NC_003112.2. DR ProteinModelPortal; Q9K1E4; -. DR SMR; Q9K1E4; 14-380. DR STRING; 122586.NMB0212; -. DR PaxDb; Q9K1E4; -. DR EnsemblBacteria; AAF40668; AAF40668; NMB0212. DR GeneID; 902324; -. DR KEGG; nme:NMB0212; -. DR PATRIC; 20355478; VBINeiMen85645_0263. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR HOGENOM; HOG000075155; -. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; NMEN122586:GHGG-227-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 2. DR HAMAP; MF_01898; GyrB; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR011557; GyrB. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR013759; Topo_IIA_cen_dom. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 2. DR TIGRFAMs; TIGR01059; gyrB; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528655}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01898}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528650}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00445358}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00445373}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528655}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528650}. FT DOMAIN 421 536 Toprim. {ECO:0000259|PROSITE:PS50880}. FT METAL 427 427 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01898}. FT METAL 501 501 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01898}. FT METAL 501 501 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_01898}. FT METAL 503 503 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_01898}. FT SITE 452 452 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_01898}. FT SITE 455 455 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_01898}. SQ SEQUENCE 796 AA; 88187 MW; 0D2D6E6C8807A6FD CRC64; MTEQKHEEYG ADSIQVLEGL EAVRKRPGMY IGDTQDGSGL HHMVFEVLDN AIDEALAGHC DKITVTIHAD HSVSVADNGR GMPTGIHPKE GRSAAEVIMT VLHAGGKFDN NSYKISGGLH GVGVSVVNAL SDWVTLTIYR DGKEHFVRFV RGETEEPLKI VGDSDKKGTT VRFLASTETF GNVEYSFDIL AKRIRELSFL NNGVDIELTD ERDGKHESFA LSGGVAGFVQ YMNRKKTPLH EKIFYAFGEK DGMSVECAMQ WNDSYQESVQ CFTNNIPQRD GGTHLTALRQ VMTRTINNYI EANEVAKKAK VETAGDDMRE GLTCVLSVKL PDPKFSSQTK DKLVSGEIGP VVNEVISQAL TDFLEENPNE AKIITGKIVD AARAREAARK AREITRRKGV MDGLGLPGKL ADCQEKDPAL SELYLVEGDS AGGSAMQGRD RKFQAILPLK GKILNVEKAR FEKMLASQEV ATLITALGAG IGKEEFNAEK LRYHRIIIMT DADVDGAHIR TLLLTFFYRQ MPELVERGYI YIAQPPLYKA KYGKQERYLK DELEKDQWLL GLALEKAKII SDGRTIEGAE LADTAKQFLL AKTVIEQESR FVDELVLRAM LHASPIDLTS SENADKAVAE LSGLLDEKEV ALERIEGHEG HRFIKITRKL HGNVMVSYIE PKFLNSKAYQ TLTQTAAALK GMVGEGAKLY KGENGYDADS FETALDILMS VAQKGMSIQR YKGLGEMNPE QLWETTMDPA VRRLLKVRIE DAIAADEVFV TLMGDEVEPR RAFIENNALI AQNIDA // ID Q9K1C8_NEIMB Unreviewed; 179 AA. AC Q9K1C8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40689.1}; GN OrderedLocusNames=NMB0234 {ECO:0000313|EMBL:AAF40689.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40689.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40689.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40689.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40689.1; -; Genomic_DNA. DR PIR; A81221; A81221. DR RefSeq; NP_273291.1; NC_003112.2. DR RefSeq; WP_002224822.1; NC_003112.2. DR ProteinModelPortal; Q9K1C8; -. DR STRING; 122586.NMB0234; -. DR PaxDb; Q9K1C8; -. DR EnsemblBacteria; AAF40689; AAF40689; NMB0234. DR GeneID; 902345; -. DR KEGG; nme:NMB0234; -. DR PATRIC; 20355544; VBINeiMen85645_0296. DR eggNOG; ENOG4105GQ3; Bacteria. DR eggNOG; ENOG410YR80; LUCA. DR HOGENOM; HOG000218647; -. DR OMA; IDNEFEE; -. DR OrthoDB; EOG6V1M5K; -. DR BioCyc; NMEN122586:GHGG-249-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1580.10; -; 1. DR InterPro; IPR018958; SMI1/KNR4-like_dom. DR SMART; SM00860; SMI1_KNR4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 28 167 SMI1_KNR4. {ECO:0000259|SMART:SM00860}. SQ SEQUENCE 179 AA; 20354 MW; 365257A129F78B3B CRC64; MSQVFKDFDL SSVWKTNSWA DENYKEAPFT PEILAAVESE LGYKLPQSFI ELMAVQNGGI FVKNCFPTTQ RNSWAENHVQ ICEVSGIGFE KEGSLCGAMG QKLWLEEWEY PPIGVYFAND PSGGHAMFAL DYRACGKDGE PKVVFVEQES DFEIVELAPD FETFIRSLRH EDEFIDEEI // ID Q9K1E2_NEIMB Unreviewed; 678 AA. AC Q9K1E2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:AAF40670.1}; DE EC=3.4.24.70 {ECO:0000313|EMBL:AAF40670.1}; GN Name=prlC {ECO:0000313|EMBL:AAF40670.1}; GN OrderedLocusNames=NMB0214 {ECO:0000313|EMBL:AAF40670.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40670.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40670.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40670.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU003435}; CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435}; CC -!- SIMILARITY: Belongs to the peptidase M3 family. CC {ECO:0000256|RuleBase:RU003435}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40670.1; -; Genomic_DNA. DR PIR; B81224; B81224. DR RefSeq; NP_273271.1; NC_003112.2. DR RefSeq; WP_002243961.1; NC_003112.2. DR ProteinModelPortal; Q9K1E2; -. DR STRING; 122586.NMB0214; -. DR PaxDb; Q9K1E2; -. DR EnsemblBacteria; AAF40670; AAF40670; NMB0214. DR GeneID; 902326; -. DR KEGG; nme:NMB0214; -. DR PATRIC; 20355486; VBINeiMen85645_0267. DR eggNOG; ENOG4105DGW; Bacteria. DR eggNOG; COG0339; LUCA. DR HOGENOM; HOG000245986; -. DR KO; K01414; -. DR OMA; VMRPPAY; -. DR OrthoDB; EOG6WHNPN; -. DR BioCyc; NMEN122586:GHGG-229-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 1.10.1370.10; -; 2. DR Gene3D; 1.20.1050.40; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR024077; Neurolysin/TOP_dom2. DR InterPro; IPR024080; Neurolysin/TOP_N. DR InterPro; IPR001567; Pept_M3A_M3B. DR Pfam; PF01432; Peptidase_M3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU003435}; KW Metal-binding {ECO:0000256|RuleBase:RU003435}; KW Metalloprotease {ECO:0000256|RuleBase:RU003435}; KW Protease {ECO:0000256|RuleBase:RU003435}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU003435}. SQ SEQUENCE 678 AA; 76054 MW; B1C4405EB878B6C2 CRC64; MTDNALLHLG EEPRFDQIKT EDIKPALQTA IAEAREQIAA IKAQTHTGWA NTVEPLTGIT ERVGRIWGVV SHLNSVADTP ELRAVYNELM PEITVFFTEI GQDIELYNRF KTIKNSPEFD TLSPAQKTKL NHDLRDFVLS GAELPPEQQA ELAKLQTEGA QLSAKFSQNV LDATDAFGIY FDDAAPLAGI PEDALAMFAA AAQSESKTGY KIGLQIPHYL AVIQYADNRE LREQIYRAYV TRASELSDDG KFDNTANIDR TLANALQTAK LLGFKNYAEL SLATKMADTP EQVLNFLHDL ARRAKPYAEK DLAEVKAFAR ESLNLADLQP WDLGYASEKL REAKYAFSET EVKKYFPVGK VLNGLFAQIK KLYGIGFTEK TVPVWHKDVR YFELQQNGET IGGVYMDLYA REGKRGGAWM NDYKGRRRFS DGTLQLPTAY LVCNFAPPVG GREARLSHDE ILILFHETGH GLHHLLTQVD ELGVSGINGV EWDAVELPSQ FMENFVWEYN VLAQMSAHEE TGVPLPKELF DKMLAAKNFQ RGMFLVRQME FALFDMMIYS EDDEGRLKNW QQVLDSVRKK VAVIQPPEYN RFALSFGHIF AGGYSAGYYS YAWAEVLSAD AYAAFEESDD VAATGKRFWQ EILAVGGSRS AAESFKAFRG REPSIDALLR HSGFDNAV // ID Q9JZV0_NEIMB Unreviewed; 162 AA. AC Q9JZV0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Type IV pilin-related protein {ECO:0000313|EMBL:AAF62322.1}; GN OrderedLocusNames=NMB0890 {ECO:0000313|EMBL:AAF62322.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62322.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62322.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62322.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62322.1; -; Genomic_DNA. DR RefSeq; NP_273931.1; NC_003112.2. DR RefSeq; WP_010980866.1; NC_003112.2. DR ProteinModelPortal; Q9JZV0; -. DR SMR; Q9JZV0; 39-157. DR STRING; 122586.NMB0890; -. DR PaxDb; Q9JZV0; -. DR EnsemblBacteria; AAF62322; AAF62322; NMB0890. DR GeneID; 903009; -. DR KEGG; nme:NMB0890; -. DR PATRIC; 20357187; VBINeiMen85645_1107. DR HOGENOM; HOG000218897; -. DR KO; K02655; -. DR OMA; YIEKGYQ; -. DR OrthoDB; EOG6FZ4D4; -. DR BioCyc; NMEN122586:GHGG-926-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro. DR InterPro; IPR000983; Bac_GSPG_pilin. DR InterPro; IPR012902; N_methyl_site. DR InterPro; IPR025922; Pilin_PilX-like. DR Pfam; PF13633; N_methyl_3; 1. DR Pfam; PF11530; Pilin_PilX; 1. DR PRINTS; PR00813; BCTERIALGSPG. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 162 AA; 18113 MW; 305F66FE28E973F8 CRC64; MMSNKMEQKG FTLIEMMIVV AILGIISVIA IPSYQSYIEK GYQSQLYTEM VGINNISKQF ILKNPLDDNQ TIENKLEIFV SGYKMNPKIA KKYSVSVKFV DKEKSRAYRL VGVPKAGTGY TLSVWMNSVG DGYKCRDAAS AQAHLETLSS DVGCEAFSNR KK // ID Q7DDC8_NEIMB Unreviewed; 378 AA. AC Q7DDC8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|RuleBase:RU362016}; DE EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016}; GN OrderedLocusNames=NMB1304 {ECO:0000313|EMBL:AAF41679.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41679.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41679.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41679.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S- CC formylglutathione + NAD(P)H. {ECO:0000256|RuleBase:RU362016}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU362016}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III subfamily. {ECO:0000256|RuleBase:RU362016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41679.1; -; Genomic_DNA. DR PIR; F81097; F81097. DR RefSeq; NP_274323.1; NC_003112.2. DR RefSeq; WP_002220876.1; NC_003112.2. DR ProteinModelPortal; Q7DDC8; -. DR SMR; Q7DDC8; 6-377. DR STRING; 122586.NMB1304; -. DR PaxDb; Q7DDC8; -. DR EnsemblBacteria; AAF41679; AAF41679; NMB1304. DR GeneID; 903726; -. DR KEGG; nme:NMB1304; -. DR PATRIC; 20358249; VBINeiMen85645_1636. DR eggNOG; ENOG4107QPD; Bacteria. DR eggNOG; COG1062; LUCA. DR HOGENOM; HOG000294674; -. DR KO; K00121; -. DR OMA; DCINPKE; -. DR OrthoDB; EOG6K9QDH; -. DR BioCyc; NMEN122586:GHGG-1342-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 2. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|RuleBase:RU362016}; KW NAD {ECO:0000256|RuleBase:RU362016}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362016}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU362016}. SQ SEQUENCE 378 AA; 40479 MW; 439EE1606780D9A4 CRC64; MEMKQADSTI KSRAAVAFAP NQPLQIVEID VEMPRKGEVL IRNTHTGVCH TDAFTLSGSD PEGVFPVVLG HEGAGVVVAV GEGVSSVKPG DHVIPLYTAE CGECEFCCSG KTNLCVSVRD TQGKGLMPDG TTRFSYQGQP IYHYMGCSTF SEYSVVAEVS LAKINPEANH EQVCLLGCGV TTGIGAVHNT AKVQEGDSVA VFGLGAIGLA VVQGARQAKA GRIIAIDTNP SKFELAKQFG ATDCLNPNDY DKPIKDVLLD INKWGIDHTF ECIGNVNVMR QALESAHRGW GQSIIIGVAG AGQEISTRPF QLVTGRVWKG SAFGGVKGRS ELPKMVEDSM KGDIELEPFV THTMTLDQIN KAFDLMHEGK SIRAVIHY // ID Q9K1K1_NEIMB Unreviewed; 397 AA. AC Q9K1K1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=DNA processing chain A {ECO:0000313|EMBL:AAF40575.1}; GN Name=dprA {ECO:0000313|EMBL:AAF40575.1}; GN OrderedLocusNames=NMB0116 {ECO:0000313|EMBL:AAF40575.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40575.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40575.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40575.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40575.1; -; Genomic_DNA. DR PIR; F81236; F81236. DR RefSeq; NP_273174.1; NC_003112.2. DR RefSeq; WP_002224767.1; NC_003112.2. DR ProteinModelPortal; Q9K1K1; -. DR STRING; 122586.NMB0116; -. DR PaxDb; Q9K1K1; -. DR DNASU; 902220; -. DR EnsemblBacteria; AAF40575; AAF40575; NMB0116. DR GeneID; 902220; -. DR KEGG; nme:NMB0116; -. DR PATRIC; 20355245; VBINeiMen85645_0156. DR eggNOG; ENOG4105C79; Bacteria. DR eggNOG; COG0758; LUCA. DR HOGENOM; HOG000003904; -. DR KO; K04096; -. DR OMA; GWEPRAR; -. DR OrthoDB; EOG6DG2TK; -. DR BioCyc; NMEN122586:GHGG-122-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009294; P:DNA mediated transformation; IEA:InterPro. DR InterPro; IPR003488; DprA. DR Pfam; PF02481; DNA_processg_A; 1. DR TIGRFAMs; TIGR00732; dprA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 397 AA; 42650 MW; 60ABC0D0C9E6C77E CRC64; MTEDERFAWL QLAFTPYIGA ESFLLLMRRF GSAQNALSAP AEQVAALIRH KQALEAWRNA EKRALARQAA EAALEWEMRD GCRLMLLQDE DFPEMLTQGL TAPPVLFLRG NVQLLHKPSA AIVGSRHATP QAMRIAKDFG KSLGGKGIPV VSGMASGIDT AAHQGALQAE GGTIAVWGTG IDRIYPPVNK NLAYEIAEKG LIVSEFPIGT RPYAGNFPRR NRLIAALSQV TLVVEAALES GSLITARLAA EMGREVMAVP GSIDNPHSKG CHKLIKDGAK LVECLDDILN ECPGLLQNTG ASSYSINKGI PEKRITAVQT ASDQLSLPEG KMPSEKTENR PVGGSILDRM GFDPVHPDVL AGQLAMPAAD LYAALLELEL DGSVAAMPGG RYQRIRT // ID Q7DDD0_NEIMB Unreviewed; 230 AA. AC Q7DDD0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887}; GN Name=rsuA {ECO:0000313|EMBL:AAF41674.1}; GN OrderedLocusNames=NMB1298 {ECO:0000313|EMBL:AAF41674.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41674.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41674.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41674.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family. CC {ECO:0000256|RuleBase:RU003887, ECO:0000256|SAAS:SAAS00545889}. CC -!- SIMILARITY: Contains S4 RNA-binding domain. CC {ECO:0000256|SAAS:SAAS00568442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41674.1; -; Genomic_DNA. DR PIR; E81099; E81099. DR RefSeq; NP_274318.1; NC_003112.2. DR RefSeq; WP_002225170.1; NC_003112.2. DR ProteinModelPortal; Q7DDD0; -. DR STRING; 122586.NMB1298; -. DR PaxDb; Q7DDD0; -. DR EnsemblBacteria; AAF41674; AAF41674; NMB1298. DR GeneID; 903720; -. DR KEGG; nme:NMB1298; -. DR PATRIC; 20358225; VBINeiMen85645_1624. DR eggNOG; ENOG4105I08; Bacteria. DR eggNOG; COG1187; LUCA. DR HOGENOM; HOG000044954; -. DR KO; K06183; -. DR OMA; LQAGDWR; -. DR OrthoDB; EOG6TFCPK; -. DR BioCyc; NMEN122586:GHGG-1336-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 1 70 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 230 AA; 26069 MW; FFC784CE962D7983 CRC64; MKLIKYLQYQ GIGSRKQCQW LIAGGYVFIN GTCMDDTDAD IDSSSVETLD IDGEAVTVVP EPYFYIMLNK PEDYETSHKP KHYRSVFSLF PDNMRNIDMQ AVGRLDADTT GVLLITNDGK LNHSLTSPSR KIPKLYEVTL KHPTGETLCE TLKNGVLLHD ENETVCAADA VLKNPTTLLL TITEGKYHQV KRMIAAAGNR VQHLHRRRFA HLETENLKPG EWKFIECPKF // ID Q9K054_NEIMB Unreviewed; 233 AA. AC Q9K054; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684, ECO:0000256|SAAS:SAAS00035261}; DE Short=MTA/SAH nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=MTAN {ECO:0000256|HAMAP-Rule:MF_01684}; DE EC=3.2.2.9 {ECO:0000256|HAMAP-Rule:MF_01684, ECO:0000256|SAAS:SAAS00035196}; DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; GN Name=pfs {ECO:0000313|EMBL:AAF41180.1}; GN Synonyms=mtnN {ECO:0000256|HAMAP-Rule:MF_01684}; GN OrderedLocusNames=NMB0767 {ECO:0000313|EMBL:AAF41180.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41180.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41180.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41180.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3EEI} RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS). RA Ho M., Rinaldo-matthis A., Brown R.L., Norris G.E., Tyler P.C., RA Furneaux R.H., Almo S.C., Schramm V.L.; RT "Crystal structure of 5'-methylthioadenosine/S-adenosylhomocysteine RT nucleosidase from neisseria meningitidis in complex with methylthio- RT immucillin-A."; RL Submitted (SEP-2008) to the PDB data bank. CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic CC bond in both 5'-methylthioadenosine (MTA) and S- CC adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding CC thioribose, 5'-methylthioribose and S-ribosylhomocysteine, CC respectively. {ECO:0000256|HAMAP-Rule:MF_01684, CC ECO:0000256|SAAS:SAAS00035153}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-(5- CC deoxy-D-ribos-5-yl)-L-homocysteine + adenine. {ECO:0000256|HAMAP- CC Rule:MF_01684, ECO:0000256|SAAS:SAAS00035191}. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl- CC 5-thio-D-ribose + adenine. {ECO:0000256|HAMAP-Rule:MF_01684, CC ECO:0000256|SAAS:SAAS00035176}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from CC S-methyl-5'-thioadenosine (hydrolase route): step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_01684, ECO:0000256|SAAS:SAAS00035194}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01684, CC ECO:0000256|SAAS:SAAS00548801}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41180.1; -; Genomic_DNA. DR PIR; D81159; D81159. DR RefSeq; NP_273809.1; NC_003112.2. DR RefSeq; WP_002244067.1; NC_003112.2. DR PDB; 3EEI; X-ray; 1.78 A; A/B=1-233. DR PDBsum; 3EEI; -. DR ProteinModelPortal; Q9K054; -. DR STRING; 122586.NMB0767; -. DR PaxDb; Q9K054; -. DR EnsemblBacteria; AAF41180; AAF41180; NMB0767. DR GeneID; 902882; -. DR KEGG; nme:NMB0767; -. DR PATRIC; 20356907; VBINeiMen85645_0972. DR eggNOG; ENOG4105DUF; Bacteria. DR eggNOG; COG0775; LUCA. DR HOGENOM; HOG000259346; -. DR KO; K01243; -. DR OMA; LLERCKP; -. DR OrthoDB; EOG64JFVR; -. DR BioCyc; NMEN122586:GHGG-798-MONOMER; -. DR UniPathway; UPA00904; UER00871. DR EvolutionaryTrace; Q9K054; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1580; -; 1. DR HAMAP; MF_01684; Salvage_MtnN; 1. DR InterPro; IPR010049; MTA_SAH_Nsdase. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR PANTHER; PTHR21234; PTHR21234; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3EEI}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01684, KW ECO:0000256|SAAS:SAAS00432671}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosidase {ECO:0000313|EMBL:AAF41180.1}; KW Hydrolase {ECO:0000313|EMBL:AAF41180.1}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01684, KW ECO:0000256|SAAS:SAAS00432671}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 230 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}. FT REGION 177 178 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01684}. FT ACT_SITE 15 15 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_01684}. FT ACT_SITE 201 201 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_01684}. FT BINDING 81 81 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01684}. FT BINDING 156 156 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_01684}. SQ SEQUENCE 233 AA; 24696 MW; E179E7C9F6FD0A5F CRC64; MSLKTVAVIG AMEQEIELLR EMMENVKAVS FGRFSAYEGE LAGKRMVLAL SGIGKVNAAV ATAWIIREFA ADCVINTGSA GGLGKGLKVG DVVIGTETAH HDVDVTAFGY AWGQVPQLPA RFASDGILIE AAKRAARTFE GAAVEQGLIV SGDRFVHSSE GVAEIRKHFP EVKAVEMEAA AIAQTCHQLE TPFVIIRAVS DSADEKADIS FDEFLKTAAA NSAKMVAEIV KSL // ID Q9K027_NEIMB Unreviewed; 655 AA. AC Q9K027; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458, GN ECO:0000313|EMBL:AAF41211.1}; GN OrderedLocusNames=NMB0798 {ECO:0000313|EMBL:AAF41211.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41211.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41211.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41211.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc CC metallopeptidase for both cytoplasmic and membrane proteins. Plays CC a role in the quality control of integral membrane proteins. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {ECO:0000256|RuleBase:RU003651}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41211.1; -; Genomic_DNA. DR PIR; E81157; E81157. DR RefSeq; NP_273840.1; NC_003112.2. DR RefSeq; WP_002219513.1; NC_003112.2. DR ProteinModelPortal; Q9K027; -. DR SMR; Q9K027; 149-403. DR STRING; 122586.NMB0798; -. DR MEROPS; M41.001; -. DR PaxDb; Q9K027; -. DR EnsemblBacteria; AAF41211; AAF41211; NMB0798. DR GeneID; 902913; -. DR KEGG; nme:NMB0798; -. DR PATRIC; 20356983; VBINeiMen85645_1010. DR eggNOG; ENOG4105C3H; Bacteria. DR eggNOG; COG0465; LUCA. DR HOGENOM; HOG000217276; -. DR KO; K03798; -. DR OMA; NMDILHS; -. DR OrthoDB; EOG6PKFBJ; -. DR BioCyc; NMEN122586:GHGG-829-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Cell cycle {ECO:0000313|EMBL:AAF41211.1}; KW Cell division {ECO:0000313|EMBL:AAF41211.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01458}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 5 25 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 26 105 Periplasmic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 106 126 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 127 655 Cytoplasmic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT DOMAIN 192 331 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 200 207 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 423 423 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 422 422 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT METAL 426 426 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. FT METAL 498 498 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01458}. SQ SEQUENCE 655 AA; 72162 MW; D6618DEB4B890539 CRC64; MGNTFKSILV WVALGIGLMA AFNALDGKKE DNGQIEYSQF IQQVNNGEVS GVNIEGSVVS GYLIKGERTD KSTFFTNAPL DDNLIKTLLD KNVRVKVTPE EKPSALAALF YSLLPVLLLI GAWFYFMRMQ TGGGGKGGAF SFGKSRARLL DKDANKVTFA DVAGCDEAKE EVQEIVDYLK APNRYQSLGG RVPRGILLAG SPGTGKTLLA KAIAGEAGVP FFSISGSDFV EMFVGVGASR VRDMFEQAKK NAPCIIFIDE IDAVGRQRGA GLGGGNDERE QTLNQLLVEM DGFESNQTVI VIAATNRPDV LDPALQRPGR FDRQVVVPLP DIRGREQILN VHSKKVPLDE SVDLLSLARG TPGFSGADLA NLVNEAALFA GRRNKVKVDQ SDFEDAKDKI YMGPERRSMV MHEDEKRATA YHESGHAIVA ESLPFTDPVH KVTIMPRGRA LGLTWQLPER DRISMYKDQM LSQLSILFGG RIAEDIFVGR ISTGASNDFE RATQMAREMV TRYGMSDKMG VMVYAENEGE VFLGRSVTRS QNISEKTQQD IDAEIRRILD EQYQVAYKIL DENRDKMETM CKALMEWETI DRDQVLEIMA GKQPSPPKDY SHNLRENADA AEDNAPHAPT REETEAPAPA DTASTESEQQ PENKA // ID Q9JZY9_NEIMB Unreviewed; 453 AA. AC Q9JZY9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Poly(A) polymerase I {ECO:0000256|HAMAP-Rule:MF_00957}; DE Short=PAP I {ECO:0000256|HAMAP-Rule:MF_00957}; DE EC=2.7.7.19 {ECO:0000256|HAMAP-Rule:MF_00957}; GN Name=pcnB {ECO:0000256|HAMAP-Rule:MF_00957, GN ECO:0000313|EMBL:AAF41254.1}; GN OrderedLocusNames=NMB0843 {ECO:0000313|EMBL:AAF41254.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41254.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41254.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41254.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which CC usually targets these RNAs for decay. Plays a significant role in CC the global control of gene expression, through influencing the CC rate of transcript degradation, and in the general RNA quality CC control. {ECO:0000256|HAMAP-Rule:MF_00957}. CC -!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1). CC {ECO:0000256|HAMAP-Rule:MF_00957}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. {ECO:0000256|HAMAP-Rule:MF_00957, CC ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00534214}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41254.1; -; Genomic_DNA. DR PIR; H81151; H81151. DR RefSeq; NP_273884.1; NC_003112.2. DR RefSeq; WP_002244079.1; NC_003112.2. DR ProteinModelPortal; Q9JZY9; -. DR STRING; 122586.NMB0843; -. DR PaxDb; Q9JZY9; -. DR EnsemblBacteria; AAF41254; AAF41254; NMB0843. DR GeneID; 902957; -. DR KEGG; nme:NMB0843; -. DR PATRIC; 20357075; VBINeiMen85645_1056. DR eggNOG; ENOG4105DJ0; Bacteria. DR eggNOG; COG0617; LUCA. DR HOGENOM; HOG000256526; -. DR KO; K00970; -. DR OMA; RFMAKLD; -. DR OrthoDB; EOG6PZX7Q; -. DR BioCyc; NMEN122586:GHGG-874-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00957; PolyA_pol; 1. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR010206; PolA_pol_I. DR InterPro; IPR025866; PolyA_pol_arg_C_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12626; PolyA_pol_arg_C; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR TIGRFAMs; TIGR01942; pcnB; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|SAAS:SAAS00415369}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_00957}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|SAAS:SAAS00415369}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAF41254.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00415356}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00957}; KW Transferase {ECO:0000313|EMBL:AAF41254.1}. FT DOMAIN 55 176 PolyA_pol. {ECO:0000259|Pfam:PF01743}. FT DOMAIN 205 252 PolyA_pol_RNAbd. FT {ECO:0000259|Pfam:PF12627}. FT DOMAIN 319 441 PolyA_pol_arg_C. FT {ECO:0000259|Pfam:PF12626}. FT ACT_SITE 73 73 {ECO:0000256|HAMAP-Rule:MF_00957}. FT ACT_SITE 75 75 {ECO:0000256|HAMAP-Rule:MF_00957}. FT ACT_SITE 147 147 {ECO:0000256|HAMAP-Rule:MF_00957}. SQ SEQUENCE 453 AA; 51654 MW; 0BE14F3EB63F7212 CRC64; MLKKWLNKML PSGRSSKKAE SKTVIPAERH NIRAEMLSFA AENVIRRLKG TGFQAYVVGG AVRDLLLGIE PKDFDVATDA TPEQVHKLFR RSRIIGRRFQ IVHVMNGAET IEVTTFRGGA KVHQNARGRI MKDNTYGSIE EDAMRRDFTC NALYYDPEKE EILDFHNGIA DVAAHRLVMI GDAAERYQED PVRILRAIRL SGKLGFELSE ETAAPIAESI CRLKHEPVAR LFDEIMKLLF SGHARECLKR LNGFDIPDDI HLLLNALRVS DGIAGKMTVL ALKNTDERLR ADKSVSVGFV LAALMWPELE RHWKSNLQQG LKPAPALSDA INTMRETVER GWGVPQRFSA TMREIWMFQP QFENRKGARP HKLFAQARFR AAYDFLLLRA ETGNADRALA EWWTAFQTAS TEQRSEMTKN EAAARHEKNE GQAKKRRRRR RKPKPKVVGT DWE // ID Q9JZK2_NEIMB Unreviewed; 201 AA. AC Q9JZK2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41416.1}; GN OrderedLocusNames=NMB1016 {ECO:0000313|EMBL:AAF41416.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41416.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41416.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41416.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains Smr domain. {ECO:0000256|SAAS:SAAS00577534}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41416.1; -; Genomic_DNA. DR PIR; H81131; H81131. DR RefSeq; NP_274050.1; NC_003112.2. DR RefSeq; WP_002221065.1; NC_003112.2. DR ProteinModelPortal; Q9JZK2; -. DR STRING; 122586.NMB1016; -. DR PaxDb; Q9JZK2; -. DR EnsemblBacteria; AAF41416; AAF41416; NMB1016. DR GeneID; 903154; -. DR KEGG; nme:NMB1016; -. DR PATRIC; 20357563; VBINeiMen85645_1298. DR eggNOG; ENOG4108DG9; Bacteria. DR eggNOG; COG2840; LUCA. DR HOGENOM; HOG000257488; -. DR OMA; RCILIIH; -. DR OrthoDB; EOG6XDGX6; -. DR BioCyc; NMEN122586:GHGG-1053-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002625; Smr_dom. DR Pfam; PF01713; Smr; 1. DR SMART; SM00463; SMR; 1. DR SUPFAM; SSF160443; SSF160443; 1. DR PROSITE; PS50828; SMR; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 116 194 Smr. {ECO:0000259|PROSITE:PS50828}. FT COILED 9 36 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 201 AA; 22983 MW; 4F54C45CE05EF195 CRC64; MNTDFQNILK QLGKQAQKEA AEKQAAEKNK QKQEQDFDFS QAVGQLSPLK NRQQYYAPPD KTPIKVRPKD NRADEENYFY IGSTYNDPPA SFSKNGQGKN DIQRLKNGYY PVVTDVDLHG YTQEEAQKVL NEFIAFTQKR GVCGEIIHGS GLGSKGYKPV LKNMTRNWLM QHPDVLAYAE PREGNDGCVR ILLKRKLRQQ D // ID Q9K091_NEIMB Unreviewed; 489 AA. AC Q9K091; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Type II restriction enzyme HgaI {ECO:0000313|EMBL:AAF41139.1}; DE EC=3.1.21.4 {ECO:0000313|EMBL:AAF41139.1}; GN OrderedLocusNames=NMB0726 {ECO:0000313|EMBL:AAF41139.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41139.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41139.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41139.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41139.1; -; Genomic_DNA. DR PIR; A81166; A81166. DR RefSeq; NP_273768.1; NC_003112.2. DR RefSeq; WP_002222756.1; NC_003112.2. DR STRING; 122586.NMB0726; -. DR PaxDb; Q9K091; -. DR EnsemblBacteria; AAF41139; AAF41139; NMB0726. DR GeneID; 902839; -. DR KEGG; nme:NMB0726; -. DR PATRIC; 20356809; VBINeiMen85645_0925. DR eggNOG; ENOG4108PQT; Bacteria. DR eggNOG; ENOG41109QK; LUCA. DR HOGENOM; HOG000086390; -. DR KO; K01155; -. DR OMA; ESHILNI; -. DR OrthoDB; EOG66QKXG; -. DR BioCyc; NMEN122586:GHGG-755-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41139.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 489 AA; 56756 MW; 3DD90B942BCEF106 CRC64; MTTARWVIDK HLQNFHILCK FAGILKTNSF ISVEDKAKLS EKLEKLDLYH RRNTGKSLDA TTHKIKELSF YMFGYRDVCG QVTQKFLFSP LGNLFLKHLD NNEYIQKIFL TMLWAIPFPH PYIKTDESIQ LYPMRLIFKL LSDERLDCKL FSYEYIYLIS FVKSADQNSY EKLVQDILVL RTCAEVKIKH QLTAENSRSH AYVNAAHEWE SYFSKTLTDA GVLQKTDGKI ICRLKHGKTE TYRKVTSSEF SIPKQLQEFV KKLQSAYSFS EMPLNLNDSD RLKIDVIKEI YSFYPKELLE EIGELKDEAA YELLHLPRLI EQYADNNNGT EAYLFEDVLE MGFNMFYNVE AKKIGGPGNT DLECLYITQK RKFAVEAKST KNKLSGINSG RLEDHKNKIK AIYTIVVTPR YVPAVLSDIR NCPIVIIRAN TFAEFLYNCL INRSSIPEID YRYFDEIIIK NLGKDISSEI SNLTMQQFAS NTTMEAYST // ID Q7DDL6_NEIMB Unreviewed; 66 AA. AC Q7DDL6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 54. DE SubName: Full=Putative bacterioferritin-associated ferredoxin {ECO:0000313|EMBL:AAF41165.1}; GN OrderedLocusNames=NMB0752 {ECO:0000313|EMBL:AAF41165.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41165.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41165.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41165.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41165.1; -; Genomic_DNA. DR PIR; G81163; G81163. DR RefSeq; NP_273794.1; NC_003112.2. DR RefSeq; WP_002214037.1; NC_003112.2. DR STRING; 122586.NMB0752; -. DR PaxDb; Q7DDL6; -. DR EnsemblBacteria; AAF41165; AAF41165; NMB0752. DR GeneID; 902867; -. DR KEGG; nme:NMB0752; -. DR PATRIC; 20356875; VBINeiMen85645_0956. DR eggNOG; ENOG41067SS; Bacteria. DR eggNOG; COG2906; LUCA. DR HOGENOM; HOG000262408; -. DR KO; K02192; -. DR OMA; FVCLCHA; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; NMEN122586:GHGG-783-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom. DR Pfam; PF04324; Fer2_BFD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 49 Fer2_BFD. {ECO:0000259|Pfam:PF04324}. SQ SEQUENCE 66 AA; 6659 MW; DB04BD1247782DC6 CRC64; MFVCICNAVT DHQIKETIAA GATTMGDLQS QLGVASCCGC CGELAASFLT AHNAQPTVTA GINVQA // ID Q9K1D8_NEIMB Unreviewed; 415 AA. AC Q9K1D8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|PIRNR:PIRNR000447}; DE EC=2.3.1.179 {ECO:0000256|PIRNR:PIRNR000447}; GN Name=fabF-1 {ECO:0000313|EMBL:AAF40675.1}; GN OrderedLocusNames=NMB0219 {ECO:0000313|EMBL:AAF40675.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40675.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40675.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40675.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}. CC -!- CATALYTIC ACTIVITY: (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + CC malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl- CC carrier-protein] + CO(2) + [acyl-carrier-protein]. CC {ECO:0000256|PIRNR:PIRNR000447}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|PIRNR:PIRNR000447}. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. CC {ECO:0000256|RuleBase:RU003694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40675.1; -; Genomic_DNA. DR PIR; G81224; G81224. DR RefSeq; NP_273276.1; NC_003112.2. DR RefSeq; WP_002224813.1; NC_003112.2. DR ProteinModelPortal; Q9K1D8; -. DR SMR; Q9K1D8; 3-412. DR STRING; 122586.NMB0219; -. DR PaxDb; Q9K1D8; -. DR EnsemblBacteria; AAF40675; AAF40675; NMB0219. DR GeneID; 902331; -. DR KEGG; nme:NMB0219; -. DR PATRIC; 20355510; VBINeiMen85645_0279. DR eggNOG; ENOG4105C0Q; Bacteria. DR eggNOG; COG0304; LUCA. DR HOGENOM; HOG000060165; -. DR KO; K09458; -. DR OMA; LNLDNPM; -. DR OrthoDB; EOG6DG2SR; -. DR BioCyc; NMEN122586:GHGG-234-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0033817; F:beta-ketoacyl-acyl-carrier-protein synthase II activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR PIRSF; PIRSF000447; KAS_II; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR03150; fabF; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000447, KW ECO:0000313|EMBL:AAF40675.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000447}; KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000447}; KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000447}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000447}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR000447, KW ECO:0000313|EMBL:AAF40675.1}. FT ACT_SITE 165 165 {ECO:0000256|PIRSR:PIRSR000447-1}. SQ SEQUENCE 415 AA; 43221 MW; 5C34542E6A51D36A CRC64; MSQRRVVITG LGQVSPVGNT VAEAWDTLLT GKSGIGAITR FDTSDINSRV AGEVRGFDIG QYISAKEARR MDVFIHYGIA AALQAIADSG LDDVENLDKD RIGVNIGSGI GGLPGIEVTG KAVIEGGARK INPFFIPGSL INLISGHVTI LKGYRGPSYG MVSACTTGAH AIGDSLRMIK YGDADIMVAG GAEGAISTLG VGGFAAMKAL STRNDDPATA SRPWDKGRDG FVIGEGAGIL VLEELEHAKK RGAKIYAEIV GFGMSSDAYH ITAPNEEGPA LAVTRALKDA GINPEDVDYV NAHGTSTPLG DANETKALKR AFGEHAYKTV VSSTKSMTGH LLGAAGGVEA VYSILAIHDG KIPPTINIFE QDVEAGCDLD YCANEARDAE IDVAISNSFG FGGTNGTLVF KRFKG // ID Q9K167_NEIMB Unreviewed; 158 AA. AC Q9K167; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40755.1}; GN OrderedLocusNames=NMB0309 {ECO:0000313|EMBL:AAF40755.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40755.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40755.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40755.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40755.1; -; Genomic_DNA. DR PIR; D81213; D81213. DR RefSeq; NP_273359.1; NC_003112.2. DR RefSeq; WP_002218702.1; NC_003112.2. DR ProteinModelPortal; Q9K167; -. DR STRING; 122586.NMB0309; -. DR PaxDb; Q9K167; -. DR EnsemblBacteria; AAF40755; AAF40755; NMB0309. DR GeneID; 902425; -. DR KEGG; nme:NMB0309; -. DR PATRIC; 20355731; VBINeiMen85645_0385. DR eggNOG; ENOG4105P0I; Bacteria. DR eggNOG; COG2954; LUCA. DR HOGENOM; HOG000004483; -. DR OMA; VWEVDVF; -. DR OrthoDB; EOG6DC6QR; -. DR BioCyc; NMEN122586:GHGG-329-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.40.320.10; -; 1. DR InterPro; IPR033469; CYTH-like_dom. DR InterPro; IPR023577; CYTH_domain. DR InterPro; IPR012042; NeuTTM/CthTTM-like. DR Pfam; PF01928; CYTH; 1. DR PIRSF; PIRSF016487; CYTH_UCP016487; 1. DR SMART; SM01118; CYTH; 1. DR SUPFAM; SSF55154; SSF55154; 1. DR PROSITE; PS51707; CYTH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 151 CYTH. {ECO:0000259|PROSITE:PS51707}. FT ACT_SITE 30 30 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR016487-1}. SQ SEQUENCE 158 AA; 18542 MW; 52D7DB6C143A9DF5 CRC64; MPIEIERRFL IGNDNWRQYA DEPLLLRQGY LSVEKERTVR VRIAGKQAWL TLKGYISEIS RSEFEYEIPL ADAEKMMETM CPFKMEKWRY PVRWGGSLFE IDVFLGDNAP LVVAEIELPD ENADFDRPDW LGREITADGM FTNAYLSRHP FSSWKNAV // ID Q9K0P0_NEIMB Unreviewed; 348 AA. AC Q9K0P0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 105. DE SubName: Full=Alcohol dehydrogenase, propanol-preferring {ECO:0000313|EMBL:AAF40975.1}; DE EC=1.1.1.1 {ECO:0000313|EMBL:AAF40975.1}; GN Name=adhP {ECO:0000313|EMBL:AAF40975.1}; GN OrderedLocusNames=NMB0546 {ECO:0000313|EMBL:AAF40975.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40975.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40975.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40975.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361277}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|RuleBase:RU361277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40975.1; -; Genomic_DNA. DR PIR; H81186; H81186. DR RefSeq; NP_273591.2; NC_003112.2. DR ProteinModelPortal; Q9K0P0; -. DR SMR; Q9K0P0; 3-341. DR STRING; 122586.NMB0546; -. DR PaxDb; Q9K0P0; -. DR PRIDE; Q9K0P0; -. DR EnsemblBacteria; AAF40975; AAF40975; NMB0546. DR GeneID; 902661; -. DR KEGG; nme:NMB0546; -. DR PATRIC; 20356353; VBINeiMen85645_0695. DR eggNOG; ENOG4105DQ4; Bacteria. DR eggNOG; COG1064; LUCA. DR HOGENOM; HOG000294685; -. DR KO; K13953; -. DR OMA; ATHCIVS; -. DR OrthoDB; EOG6BPDJN; -. DR BioCyc; NMEN122586:GHGG-572-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Oxidoreductase {ECO:0000313|EMBL:AAF40975.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU361277}. SQ SEQUENCE 348 AA; 36548 MW; 5412F925315D92EF CRC64; MKMQAVVVNK NVAGDVEVIE REVRPLEYGE ALVEVEYCGV CHTDLHVAAG DYGEKPGRVL GHEGIGLVKE VADGVKNLKV GDRVSIAWLF QSCGSCEYCN TGRETLCRSV LNAGYTADGG MATHCIVSAD YAVKVPEGLD PAQASSITCA GVTTYKAIKV SGVRPGQWIA IYGAGGLGNL GVQYAKKVFG AHVVAIDIND DKLAFAKETG ADLVVNAAKE DAAKVIQEKT GGAHAAVVTA VSAAAFNSAV NCVRAGGRVV AIGLPPESMD LSIPRLVLDG IEVVGSLVGT RKDLEEAFQF GAEGLVVPKV QLRALDEAPA IFQEMREGKI TGRMVIDMKK ECGCGHHH // ID Q9JXU0_NEIMB Unreviewed; 218 AA. AC Q9JXU0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000313|EMBL:AAF42219.1}; DE EC=2.1.1.77 {ECO:0000313|EMBL:AAF42219.1}; GN Name=pcm {ECO:0000313|EMBL:AAF42219.1}; GN OrderedLocusNames=NMB1885 {ECO:0000313|EMBL:AAF42219.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42219.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42219.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42219.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42219.1; -; Genomic_DNA. DR PIR; C81031; C81031. DR RefSeq; NP_274881.1; NC_003112.2. DR RefSeq; WP_002225794.1; NC_003112.2. DR ProteinModelPortal; Q9JXU0; -. DR STRING; 122586.NMB1885; -. DR PaxDb; Q9JXU0; -. DR EnsemblBacteria; AAF42219; AAF42219; NMB1885. DR GeneID; 904295; -. DR KEGG; nme:NMB1885; -. DR PATRIC; 20359805; VBINeiMen85645_2408. DR eggNOG; ENOG4108KE4; Bacteria. DR eggNOG; COG2518; LUCA. DR HOGENOM; HOG000257190; -. DR KO; K00573; -. DR OMA; ILRHEFV; -. DR OrthoDB; EOG644ZP2; -. DR BioCyc; NMEN122586:GHGG-1941-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR000682; PCMT. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11579; PTHR11579; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF42219.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42219.1}. SQ SEQUENCE 218 AA; 23868 MW; 58687AD7D508CEFF CRC64; MDFEKARFNM VEQQIRPWDV LDFDVLDALA EIPRELFVDE DLQGLAYADM ALPLANGHKM LEPKVVARLA QGLKLTKNDT VLEIGTGSGY ATALLAKLAG RVVSDDIDVE QQNRAKAVLD GLGLDNIDYV QNNGLTELSA GAPFDAVYVG GAVNLVPEVL KEQLKDGGRM VVIVGRKPVQ RALLITRRGD VFEEKVLFDT LVAHLDDKDA DPFGGFDF // ID Q9K037_NEIMB Unreviewed; 1204 AA. AC Q9K037; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; GN Name=recB {ECO:0000256|HAMAP-Rule:MF_01485, GN ECO:0000313|EMBL:AAF41198.1}; GN OrderedLocusNames=NMB0785 {ECO:0000313|EMBL:AAF41198.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41198.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41198.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41198.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit contributes ATPase, CC 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. Interacts with RecA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts CC with RecD. It interacts with RecA, facilitating its loading onto CC ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent CC ATPase and has ATP-dependent 3'-5' helicase function. This domain CC interacts with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00597767}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41198.1; -; Genomic_DNA. DR PIR; F81158; F81158. DR RefSeq; NP_273827.1; NC_003112.2. DR RefSeq; WP_002225423.1; NC_003112.2. DR ProteinModelPortal; Q9K037; -. DR STRING; 122586.NMB0785; -. DR PaxDb; Q9K037; -. DR EnsemblBacteria; AAF41198; AAF41198; NMB0785. DR GeneID; 902900; -. DR KEGG; nme:NMB0785; -. DR PATRIC; 20356955; VBINeiMen85645_0996. DR eggNOG; ENOG4107QKA; Bacteria. DR eggNOG; COG1074; LUCA. DR HOGENOM; HOG000258330; -. DR KO; K03582; -. DR OMA; IMIGDPK; -. DR OrthoDB; EOG6677M1; -. DR BioCyc; NMEN122586:GHGG-816-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 5. DR Gene3D; 3.90.320.10; -; 1. DR HAMAP; MF_01485; RecB; 1. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 4. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00609; recB; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00493105}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440586}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440586}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440068}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440824}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00493105}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440824, ECO:0000256|SAAS:SAAS00493105}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440824}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00493105}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 472 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 497 761 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. FT NP_BIND 23 30 ATP. {ECO:0000256|HAMAP-Rule:MF_01485}. FT REGION 1 873 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT REGION 927 1204 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT ACT_SITE 1121 1121 For nuclease activity. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 991 991 Magnesium; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 1107 1107 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT METAL 1121 1121 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01485}. SQ SEQUENCE 1204 AA; 134598 MW; 48D4BCCC56F1CFD4 CRC64; MSASIQAFDP LTVPISGTNL IEASAGTGKT YGIAALFTRL IVLEQKNVER VLVVTFTKAA TAELKTRLRG RLDDVLQVLE SKGIAKLGDD TLSDGIAAYC AEHHEGDTFL PELLKQALQK EGRTRLIVRL KAAIGQFDNA AIYTIHGFCQ RILRDYAFLC QAPFDVEMTE EDGDRLLIPA QDFWRERVSN DPVLAALALK RKAVPQTVLA QISRYLSRPY LNFRRPQADL KQAQRNAETS WQTICRLLPE LEAGFWRIHP DLNGNSYRKN SFGNLFKELA QKSAAGQLPF LDKDTHDRLL KLASDKLEAG LKKGKTPDAA VFAELQKLAD FGRDLNALEE AEEATMIRLQ LDLIEYLNRS LAEMKKSRRE RGFDDLLLDV HTALTDNPHA DTLARAVAEN WETALIDEFQ DTDPLQYEIF QKIFIAQNRP LFLVGDPKQA IYSFRGADIY AYLQAAEDAR HRYTLATNYR SHAALIGSIG ALFRLKERPF VLENIGYSEV GAARAESRLS PERPAVQVRW LHENDNEKAN KDVLRRRAAD YCADEIAHAL NEAARGRLNF KGCPLQSGDI AVLVRTHNEA VMVSAALKKR QVQSVLLSRE SVFASPEAAA LSALIGFWLE PRRAGTLRFV LTSSIFGYDA QQLHDFNQNE SEILHWAESA RTALDNWNKY GIFAAMQQFS QTHGIETRLL SRNNGRSLTN YFQLLELLAA EDAQNRNPAA LHKWLGDQIS LAENNSGDNR AIRLESDEDL VKIVTMHASK GLQYPLVYCP FAWDAQDTGP SDWQILHQGA NRTELLAKAQ LSEDEQKQYA DEEMAERLRL LYVALTRAEE QLNIYAAYST NTADNPLAYL IEGSPQDSRE TVRRAYACEK DGIAMLKRNW RRVADNAPSG TNFAFTENAP PPAAYRSNAG QTAEFAANSI PERGFRFVRH TSFTALSRHT QTPDGGEEDA CPSLDAAETS VPAMPSETPT ASDGISIHDF PKGTQAGLCL HEILEDFKFG QAAAGQETLI ADKLKKYGFE EIWLPAVAEM AEACRKTPLT GAYDLSDISP ECRCPEMGFT LHTEDFSLKR LRDWFARDDI RLPEVCRAAA ETLDFHTVNG FLNGFVDMVC QDPDGNICVI DYKSNHLGTD ASAYTQQAMD EAVAHHHYYL QALIYAVAAA RYFKLRGQPP AAVSVRYLFL RGLDGKGGGV WRWDIDAAAL EQIK // ID Q9K070_NEIMB Unreviewed; 312 AA. AC Q9K070; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Penicillin-binding protein 4 {ECO:0000313|EMBL:AAF41162.1}; GN OrderedLocusNames=NMB0749 {ECO:0000313|EMBL:AAF41162.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41162.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41162.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41162.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the peptidase S11 family. CC {ECO:0000256|RuleBase:RU004016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41162.1; -; Genomic_DNA. DR PIR; D81163; D81163. DR RefSeq; NP_273791.1; NC_003112.2. DR RefSeq; WP_002225443.1; NC_003112.2. DR ProteinModelPortal; Q9K070; -. DR STRING; 122586.NMB0749; -. DR PaxDb; Q9K070; -. DR EnsemblBacteria; AAF41162; AAF41162; NMB0749. DR GeneID; 902864; -. DR KEGG; nme:NMB0749; -. DR PATRIC; 20356869; VBINeiMen85645_0953. DR eggNOG; ENOG41061WM; Bacteria. DR eggNOG; COG1686; LUCA. DR HOGENOM; HOG000199620; -. DR KO; K07262; -. DR OMA; ESKMSIH; -. DR OrthoDB; EOG6RJV2H; -. DR BioCyc; NMEN122586:GHGG-780-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR018044; Peptidase_S11. DR InterPro; IPR001967; Peptidase_S11_N. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SUPFAM; SSF56601; SSF56601; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 312 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329366. FT DOMAIN 70 291 Peptidase_S11. FT {ECO:0000259|Pfam:PF00768}. SQ SEQUENCE 312 AA; 34135 MW; DC2AAD04415F37B6 CRC64; MSIHTLKRLP SSLLLGLCLS LPSAHLFADN DILGQFLEQN MLTSSDPIEI FAESTIHPTN TQAITGGLIL SSQSALVVNN KTGQILYQKN ADRIMPIASI SKLMSAMVVL DANLDMNETV TITPDEIDRI KGTGSRLAIG TALTRKKLLH LSLMSSENRA THALGRTYPG GMGAFVAAMN RKAQSLGMYG SRFYEPTGLN FQNVSTAKDL SLMVNAAAQY PQIRTNSTSN YASVQTKNGQ QNYKNSNALV REGMWNIELQ KTGYIREAGR SMVVKANIQN QPVTIVLLNS PTSATRVNDA RKIESWMLQQ RS // ID Q9JXL3_NEIMB Unreviewed; 714 AA. AC Q9JXL3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 97. DE SubName: Full=Iron-regulated outer membrane protein FrpB {ECO:0000313|EMBL:AAF42315.1}; GN Name=frpB {ECO:0000313|EMBL:AAF42315.1}; GN OrderedLocusNames=NMB1988 {ECO:0000313|EMBL:AAF42315.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42315.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42315.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42315.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU003357, ECO:0000256|SAAS:SAAS00558041}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000256|RuleBase:RU003357, ECO:0000256|SAAS:SAAS00558036}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42315.1; -; Genomic_DNA. DR PIR; C81018; C81018. DR RefSeq; NP_274980.1; NC_003112.2. DR RefSeq; WP_010981016.1; NC_003112.2. DR ProteinModelPortal; Q9JXL3; -. DR STRING; 122586.NMB1988; -. DR PaxDb; Q9JXL3; -. DR EnsemblBacteria; AAF42315; AAF42315; NMB1988. DR GeneID; 904143; -. DR KEGG; nme:NMB1988; -. DR PATRIC; 20360071; VBINeiMen85645_2540. DR eggNOG; ENOG41088IC; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000218731; -. DR KO; K16087; -. DR OMA; FRPNDIA; -. DR OrthoDB; EOG6JQGXW; -. DR BioCyc; NMEN122586:GHGG-2045-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015891; P:siderophore transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010917; TonB_rcpt_CS. DR InterPro; IPR010105; TonB_sidphr_rcpt. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01783; TonB-siderophor; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00444644}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00444644}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357, KW ECO:0000256|SAAS:SAAS00444615}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 714 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327676. FT DOMAIN 46 144 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 454 713 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 714 AA; 79150 MW; F8BABF5BDB14CDFE CRC64; MNTPLFRLSL LSLTLAAGFA HAAENNAKVV LDTVTVKGDR QGSKIRTNIV TLQQKDESTA TDMRELLKEE PSIDFGGGNG TSQFLTLRGM GQNSVDIKVD NAYSDSQILY HQGRFIVDPA LVKVVSVQKG AGSASAGIGA TNGAIITKTV DAQDLLKGLD KNWGVRLNSG FASNEGVSYG ASVFGKEGNF DGLFSYNRNN EKDYEAGKGF RNNFNGGKTV PYSALDKRSY LAKIGTSFGD GDHRIVLSHM KDQHRGIRTV REEFTVGGDK ERISMERQAP AYRETTQSNT NLAYTGKNLG FVEKLDANAY VLEKERYSAD DSGTGYAGNV KGPNHTQITT RGMNFNFDSR LAEQTLLKYG INYRHQEIKP QAFLNSQFKI EDKEKATDEE KNKNRENEKI AKAYRLTNPT KTDTGAYIEA IHEIDGFTLT GGLRYDRFKV KTHDGKTVSS NNLNPSFGVI WQPHEHWSFS ASHNYASRSP RLYDALQTHG KRGIISIADG TKAERARNTE IGFNYNDGTF AANGSYFWQT IKDALANPQN RHDSVAVREA VNAGYIKNHG YELGASYRTG GLTAKVGVSH SKPRFYDTHK DKLLSANPEF GAQVGRTWTA SLAYRFQNPN LEIGWRGRYV QKAVGSILVA GQKDRNGKLE NVVRKGFGVN DVFANWKPLG KDTLNVNLSV NNVFNTFYYP HSQRWTNTLP GVGRDVRLGV NYKF // ID Q9JYF6_NEIMB Unreviewed; 767 AA. AC Q9JYF6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_00936}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936}; GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00936, GN ECO:0000313|EMBL:AAF41957.1}; GN OrderedLocusNames=NMB1605 {ECO:0000313|EMBL:AAF41957.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41957.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41957.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41957.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Topoisomerase IV is essential for chromosome CC segregation. It relaxes supercoiled DNA. Performs the decatenation CC events required during the replication of a circular DNA molecule. CC {ECO:0000256|HAMAP-Rule:MF_00936}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_00936}. CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000256|HAMAP-Rule:MF_00936}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00936}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00936}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41957.1; -; Genomic_DNA. DR PIR; G81064; G81064. DR RefSeq; NP_274611.1; NC_003112.2. DR RefSeq; WP_002225016.1; NC_003112.2. DR ProteinModelPortal; Q9JYF6; -. DR STRING; 122586.NMB1605; -. DR PaxDb; Q9JYF6; -. DR EnsemblBacteria; AAF41957; AAF41957; NMB1605. DR GeneID; 904301; -. DR KEGG; nme:NMB1605; -. DR PATRIC; 20359090; VBINeiMen85645_2057. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR HOGENOM; HOG000076277; -. DR KO; K02621; -. DR OMA; RFTEDAY; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; NMEN122586:GHGG-1653-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_00936; ParC_type1; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR005742; TopoIV_A_Gneg. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00936}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00936}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00936}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00936}. FT DOMAIN 15 487 TOP4c. {ECO:0000259|SMART:SM00434}. FT COILED 452 486 {ECO:0000256|SAM:Coils}. FT ACT_SITE 126 126 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00936}. FT SITE 46 46 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00936}. FT SITE 82 82 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00936}. FT SITE 84 84 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00936}. FT SITE 125 125 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00936}. SQ SEQUENCE 767 AA; 84460 MW; 2DCE4A8F583613E6 CRC64; MNTQAHAPHT DSNTLMLGRY AERAYLEYAM SVVKGRALPE VSDGQKPVQR RILFAMRDMG LTAGAKPVKS ARVVGEILGK YHPHGDSSAY EAMVRMAQDF TLRYPLIDGI GNFGSRDGDG AAAMRYTEAR LTPIAELLLS EINQGTVDFV PNYDGAFDEP LHLPARLPMV LLNGASGIAV GMATEIPPHN LNEVTQAAIA LLKKPTLETA DLMQYIPAPD FAGGGQIITP ADELRRIYET GKGSVRVRAR YEIEKLARGQ WRVIVTELPP NANSAKILAE IEEQTNPKPK AGKKQLNQDQ LNTKKLMLDL IDRVRDESDG EHPVRLVFEP KSSRIDTDTF INTLMAQTSL EGNVSMNLVM MGLDNRPAQK NLKTILQEWL DFRTVTVTRR LKFRLNQVEK RLHILEGRLK VFLHIDEVIK VIRESDDPKA DLMAAFGLTE IQAEDILEIR LRQLARLEGF KLEKELNELR EEQGRLNILL SDENEKRKLI VKEMQADMKQ YGDARRTLVE EAGRAVLTQT TADEPITLIL SEKGWIRSRA GHNLDLSQTA FKEGDCLKQT LEGRTVLPVV ILDSSGRTYT LDAAEIPGGR GDGVPVSSLI ELQNGAKPVA MLTGLPEQHY LLSSSSGYGF ITKLGDMVGR VKAGKVVMTA DSGETVLPPV AVYASSFINP DCKIIAATSQ NRALAFPIGE LKIMAKGKGL QIIGLNAGES MTHTAVSSEL EILIESEGRR GAAHKDRIPI SLLEAKRGKK GRLLPISGSL KQLSSPK // ID Q9JZZ3_NEIMB Unreviewed; 443 AA. AC Q9JZZ3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=PmbA protein {ECO:0000313|EMBL:AAF41250.1}; GN Name=pmbA {ECO:0000313|EMBL:AAF41250.1}; GN OrderedLocusNames=NMB0839 {ECO:0000313|EMBL:AAF41250.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41250.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41250.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41250.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41250.1; -; Genomic_DNA. DR PIR; D81151; D81151. DR RefSeq; NP_273880.1; NC_003112.2. DR RefSeq; WP_002217529.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ3; -. DR STRING; 122586.NMB0839; -. DR PaxDb; Q9JZZ3; -. DR EnsemblBacteria; AAF41250; AAF41250; NMB0839. DR GeneID; 902953; -. DR KEGG; nme:NMB0839; -. DR PATRIC; 20357065; VBINeiMen85645_1051. DR eggNOG; ENOG4105CMS; Bacteria. DR eggNOG; COG0312; LUCA. DR HOGENOM; HOG000224928; -. DR KO; K03592; -. DR OMA; TCEVPVL; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; NMEN122586:GHGG-870-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 443 AA; 47829 MW; 728BD43D5EEE28A3 CRC64; MLFNHTASEL LDLCRRTLDL AKATGATAAE ADFSESLGQS VSVRLGEIEQ IEFQQDKSLD ITVYVGKRKG RASTADFSEK ALQDTVKAAI DIARHTAEDG CAGLADACLM AKHIGDPDLY HEWDLDTEAA VGLAKQCEQA ALNEDERIEN SEGAAVQTGH YQYVYGNTHG FAAHRQGTHH SISCSVVAAD ENGMQRDYWY DSACRHPDMD SPETIGQTAA RRTLRRLGSR SIPTGSYPVL FDTTVSGGLI GHLVGALSGG ALYRQSSFLI DSIGKKVLPD FLNLREEPHI PRSFRSSYFD AEGVATAPRF VIQNGIVEGY FLSSYSARKL GMQTTGNAGG AHNLYLNHTH ETQSDLLKEM GTGLLVTELM GQGANTITGD YSRGAAGFWV ENGVIAYPVH EITVAGRLQD MYRDIVGVAD DALRRSSNKI GSILIAGMTV AGS // ID Q9JZW5_NEIMB Unreviewed; 614 AA. AC Q9JZW5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41283.1}; GN OrderedLocusNames=NMB0872 {ECO:0000313|EMBL:AAF41283.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41283.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41283.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41283.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41283.1; -; Genomic_DNA. DR PIR; H81148; H81148. DR RefSeq; NP_273913.1; NC_003112.2. DR RefSeq; WP_002222668.1; NC_003112.2. DR ProteinModelPortal; Q9JZW5; -. DR STRING; 122586.NMB0872; -. DR PaxDb; Q9JZW5; -. DR EnsemblBacteria; AAF41283; AAF41283; NMB0872. DR GeneID; 902988; -. DR KEGG; nme:NMB0872; -. DR PATRIC; 20357141; VBINeiMen85645_1087. DR eggNOG; ENOG4105DJQ; Bacteria. DR eggNOG; COG0457; LUCA. DR HOGENOM; HOG000218891; -. DR OMA; NGGREPE; -. DR OrthoDB; EOG6J48V5; -. DR BioCyc; NMEN122586:GHGG-905-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 614 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327866. FT DOMAIN 456 558 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. FT DOMAIN 558 591 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 614 AA; 68662 MW; 91BA94B3BC77C12D CRC64; MLPNRFKMLT VLTATLIAGQ VSAAGGGAGD MKQPKEVGKV FRKQQRYSEE EIKNERARLA AVGERVNQIF TLLGGETALQ KGQAGTALAT YMLMLERTKS PEVAERALEM AVSLNAFEQA EMIYQKWRQI EPIPGKAQKR AGWLRNVLRE RGNQHLDGLE EVLAQADEGQ NRRVFLLLAQ AAVQQDGLAQ KASKAVRRAA LKYEHLPEAA VADVVFSVQG REKEKAIGAL QRLAKLDTEI LPPTLMTLRL TARKYPEILD GFFEQTDTQN LSAVWQEMEI MNLVSLHRLD DAYARLNVLL ERNPNADLYI QAAILAANRK EGASVIDGYA EKAYGRGTEE QRSRAALTAA MMYADRRDYA KVRQWLKKVS APEYLFDKGV LAAAAAVELD GGRAALRQIG RVRKLPEQQG RYFTADNLSK IQMLALSKLP DKREALRGLD KIIEKPPAGS NTELQAEALV QRSVVYDRLG KRKKMISDLE RAFRLAPDNA QIMNNLGYSL LTDSKRLDEG FALLQTAYQI NPDDTAVNDS IGWAYYLKGD AESALPYLRY SFENDPEPEV AAHLGEVLWA LGERDQAVDV WTQAAHLTGD KKIWRETLKR HGIALPQPSR KPRK // ID Q9JYK7_NEIMB Unreviewed; 642 AA. AC Q9JYK7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000256|HAMAP-Rule:MF_00963}; DE AltName: Full=Sigma-70 {ECO:0000256|HAMAP-Rule:MF_00963}; GN Name=rpoD {ECO:0000256|HAMAP-Rule:MF_00963, GN ECO:0000313|EMBL:AAF41893.1}; GN OrderedLocusNames=NMB1538 {ECO:0000313|EMBL:AAF41893.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41893.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41893.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41893.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Sigma factors are initiation factors that promote the CC attachment of RNA polymerase to specific initiation sites and are CC then released. This sigma factor is the primary sigma factor CC during exponential growth. {ECO:0000256|SAAS:SAAS00535554}. CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic CC core. {ECO:0000256|HAMAP-Rule:MF_00963, CC ECO:0000256|SAAS:SAAS00003340}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963, CC ECO:0000256|SAAS:SAAS00051670}. CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA CC subfamily. {ECO:0000256|SAAS:SAAS00535555}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41893.1; -; Genomic_DNA. DR PIR; F81072; F81072. DR RefSeq; NP_274545.1; NC_003112.2. DR RefSeq; WP_002225051.1; NC_003112.2. DR ProteinModelPortal; Q9JYK7; -. DR SMR; Q9JYK7; 394-531, 570-636. DR STRING; 122586.NMB1538; -. DR PaxDb; Q9JYK7; -. DR EnsemblBacteria; AAF41893; AAF41893; NMB1538. DR GeneID; 904073; -. DR KEGG; nme:NMB1538; -. DR PATRIC; 20358880; VBINeiMen85645_1949. DR eggNOG; ENOG4105DG1; Bacteria. DR eggNOG; COG0568; LUCA. DR HOGENOM; HOG000270272; -. DR KO; K03086; -. DR OMA; RDAKKEM; -. DR OrthoDB; EOG6XHC70; -. DR BioCyc; NMEN122586:GHGG-1579-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0001123; P:transcription initiation from bacterial-type RNA polymerase promoter; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 2. DR HAMAP; MF_00963; Sigma70_RpoD_SigA; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR009042; RNA_pol_sigma70_r1_2. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007624; RNA_pol_sigma70_r3. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR007631; RNA_pol_sigma_70_non-ess. DR InterPro; IPR007127; RNA_pol_sigma_70_r1_1. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR012760; RNA_pol_sigma_RpoD_C. DR InterPro; IPR028630; Sigma70_RpoD. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04546; Sigma70_ner; 1. DR Pfam; PF03979; Sigma70_r1_1; 1. DR Pfam; PF00140; Sigma70_r1_2; 1. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04539; Sigma70_r3; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 2. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02393; RpoD_Cterm; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS00715; SIGMA70_1; 1. DR PROSITE; PS00716; SIGMA70_2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963, KW ECO:0000256|SAAS:SAAS00416731}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00963, KW ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Sigma factor {ECO:0000256|HAMAP-Rule:MF_00963, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00963, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00963, KW ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 427 440 RNA_pol_sigma70. FT {ECO:0000259|PROSITE:PS00715}. FT DOMAIN 596 622 RNA_pol_sigma70. FT {ECO:0000259|PROSITE:PS00716}. FT DNA_BIND 597 616 H-T-H motif. {ECO:0000256|HAMAP- FT Rule:MF_00963}. FT REGION 403 473 Sigma-70 factor domain-2. FT {ECO:0000256|HAMAP-Rule:MF_00963}. FT REGION 482 558 Sigma-70 factor domain-3. FT {ECO:0000256|HAMAP-Rule:MF_00963}. FT REGION 571 624 Sigma-70 factor domain-4. FT {ECO:0000256|HAMAP-Rule:MF_00963}. FT COILED 290 324 {ECO:0000256|SAM:Coils}. FT COILED 354 402 {ECO:0000256|SAM:Coils}. FT MOTIF 427 430 Interaction with polymerase core subunit FT RpoC. {ECO:0000256|HAMAP-Rule:MF_00963}. SQ SEQUENCE 642 AA; 73832 MW; 113BFF516B894039 CRC64; MSRNQNHEEY QDDTRPLSIE EQRARLRQLI IMGKERGYIT YSEINDALPD DMSDADQIDN IVSMISGLGI QVTEHAPDAE DILLSDNAAV TDDDAVEEAE AALSSADSEF GRTTDPVRMY MREMGQVDLL TREDEIIIAK KIENALKNMV QAISACPGSI AEILELIEKI RKDEIRVDEV VEAIIDPNEV LLNELGLGHL ETTAPEKPSN DNSDENEDDE ESEEDADEIS AANLAELKQK VIGHFAQIEK DYKKMIGRLE KHHSRHKDYL AYRDAIANKL LEVRFATRQI DSLSSSLRGK VENIRKLERE IRDICLDRVH MERDYFIQNF LPEITNLEWI EEEIAKGRVW SDALDRFRHA ILEKQTELAD MEKETRISIE ELKEINKNMV SSEKETAAAK QEMIQANLRL VISIAKKYTN RGLQFLDLIQ EGNIGLMKAV DKFEYRRGYK FSTYATWWIR QAITRSIADQ ARTIRIPVHM IETINKMNRI SRQHLQETGE EPDSAKLAEL MQMPEDKIRK IMKIAKEPIS METPIGDDDD SHLGDFIEDA NNVAPADAAM YTSLHEVTKE ILESLTPREA KVLRMRFGID MNTDHTLEEV GRQFDVTRER IRQIEAKALR KLRHPTRSDR LRSFLDSEDS KL // ID Q9JZJ9_NEIMB Unreviewed; 378 AA. AC Q9JZJ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; GN Name=purK {ECO:0000256|HAMAP-Rule:MF_01928, GN ECO:0000256|RuleBase:RU361200, ECO:0000313|EMBL:AAF41419.1}; GN OrderedLocusNames=NMB1019 {ECO:0000313|EMBL:AAF41419.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41419.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41419.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41419.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|HAMAP-Rule:MF_01928}. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|RuleBase:RU361200}. CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole CC + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP- CC Rule:MF_01928, ECO:0000256|RuleBase:RU361200, CC ECO:0000256|SAAS:SAAS00575099}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP- CC Rule:MF_01928}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41419.1; -; Genomic_DNA. DR PIR; C81132; C81132. DR RefSeq; NP_274053.1; NC_003112.2. DR RefSeq; WP_002230480.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ9; -. DR STRING; 122586.NMB1019; -. DR PaxDb; Q9JZJ9; -. DR EnsemblBacteria; AAF41419; AAF41419; NMB1019. DR GeneID; 903157; -. DR KEGG; nme:NMB1019; -. DR PATRIC; 20357573; VBINeiMen85645_1303. DR eggNOG; ENOG4105CY8; Bacteria. DR eggNOG; COG0026; LUCA. DR HOGENOM; HOG000034029; -. DR KO; K01589; -. DR OMA; DSPCGQV; -. DR OrthoDB; EOG6QZMX7; -. DR BioCyc; NMEN122586:GHGG-1056-MONOMER; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01928; PurK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR005875; PurK. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01161; purK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513347}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200}; Lyase {ECO:0000313|EMBL:AAF41419.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513347}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513319}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 111 297 ATP-grasp. {ECO:0000256|HAMAP- FT Rule:MF_01928, FT ECO:0000259|PROSITE:PS50975}. FT NP_BIND 151 157 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT NP_BIND 181 184 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT NP_BIND 267 268 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 107 107 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 146 146 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 189 189 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 212 212 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. SQ SEQUENCE 378 AA; 41176 MW; 26286F8F998BE696 CRC64; MKNISLSPPA MLGILGGGQL GRMFTVAAKT MGYKVTVLDP DPDAPAAEFA DRHLCAPFND QAALDELAKC AAVTTEFENV NADAMRFLAK HTNVSPSGDC VAIAQNRIQE KAWIRKAGLQ TAPYQVVCKA EDITEASAQF LPGILKTATL GYDGKGQIRV KTLDELKAAF AEHGGVDCVL EKMVDLRSEI SVIVCRLNND NVQTFDPAEN IHENGILAYS IVPARLSADV QQQARQMAQR LADELDYVGV LAVEMFVVGD THELVVNEIA PRPHNSGHHT IDACAADQFQ QQVRIMCNLP PADTKLLSSC CMANILGDVW QEDGGEPDWL PLQSHPNAHL HLYGKKTAHK GRKMGHFTVL TTDSDTAFQE AKKLHQSL // ID Q7DDC0_NEIMB Unreviewed; 179 AA. AC Q7DDC0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 54. DE SubName: Full=IS1016C2 transposase {ECO:0000313|EMBL:AAF41765.1}; GN OrderedLocusNames=NMB1401 {ECO:0000313|EMBL:AAF41765.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41765.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41765.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41765.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41765.1; -; Genomic_DNA. DR PIR; G81086; G81086. DR PaxDb; Q7DDC0; -. DR EnsemblBacteria; AAF41765; AAF41765; NMB1401. DR PATRIC; 20358491; VBINeiMen85645_1757. DR eggNOG; ENOG4105S1F; Bacteria. DR eggNOG; ENOG4111JFI; LUCA. DR HOGENOM; HOG000218644; -. DR OMA; IVRHEKI; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NMEN122586:GHGG-1439-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. DR SMART; SM01126; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 179 AA; 20443 MW; 43BB0DDD2441522E CRC64; MKITHCKLKK KVQKELLRFF VLEVTARSAA DILGIHPNSA VLFYRKIRMV ISHYLALAAN EVFEGSVELD ESYFGGRRKG KRGRGAAGKV VVFGILKRNG RVYTVVVDNA KSDTLMPVIK QKIMPDSIVY TDSLSSYDKL DVSGFIHYRI NHSKEFADRQ NHINGIENFW NQAKRVLRK // ID Q9JYN7_NEIMB Unreviewed; 186 AA. AC Q9JYN7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887}; GN OrderedLocusNames=NMB1496 {ECO:0000313|EMBL:AAF41852.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41852.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41852.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41852.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family. CC {ECO:0000256|RuleBase:RU003887, ECO:0000256|SAAS:SAAS00545889}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41852.1; -; Genomic_DNA. DR PIR; D81076; D81076. DR RefSeq; NP_274504.1; NC_003112.2. DR RefSeq; WP_002216863.1; NC_003112.2. DR ProteinModelPortal; Q9JYN7; -. DR STRING; 122586.NMB1496; -. DR PaxDb; Q9JYN7; -. DR EnsemblBacteria; AAF41852; AAF41852; NMB1496. DR GeneID; 903918; -. DR KEGG; nme:NMB1496; -. DR PATRIC; 20358758; VBINeiMen85645_1888. DR eggNOG; ENOG4108R99; Bacteria. DR eggNOG; COG1187; LUCA. DR HOGENOM; HOG000044955; -. DR KO; K06181; -. DR OMA; TWIELSI; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; NMEN122586:GHGG-1536-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 150 PseudoU_synth_2. FT {ECO:0000259|Pfam:PF00849}. SQ SEQUENCE 186 AA; 21255 MW; 9FA51AC1686210DE CRC64; MKNLIAFNKP YGVICQFSPH EKHKSLKDFI NLPGFYPAGR LDTDSEGLLL LTDDGRLQAQ ITDPKFKHPK TYWAQLEGVP DESRLESLRK GIDLGGFVTR PASIRILKHG EADSLWERIP PIRVRKTVPD FWIEITISEG KNRQVRRMTA KAGYPCLRLI RVASGRLKLF DLDLKPGEWA YAPFKP // ID Q9JZL8_NEIMB Unreviewed; 227 AA. AC Q9JZL8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN OrderedLocusNames=NMB0995 {ECO:0000313|EMBL:AAF41398.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41398.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41398.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41398.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. CC Required for the reduction of the AhpC active site cysteine CC residues and for the regeneration of the AhpC enzyme activity. CC {ECO:0000256|SAAS:SAAS00088543}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000256|SAAS:SAAS00088505}. CC -!- SIMILARITY: Belongs to the AhpD family. CC {ECO:0000256|SAAS:SAAS00571262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41398.1; -; Genomic_DNA. DR PIR; B81134; B81134. DR RefSeq; NP_274031.2; NC_003112.2. DR ProteinModelPortal; Q9JZL8; -. DR STRING; 122586.NMB0995; -. DR PaxDb; Q9JZL8; -. DR DNASU; 903124; -. DR EnsemblBacteria; AAF41398; AAF41398; NMB0995. DR GeneID; 903124; -. DR KEGG; nme:NMB0995; -. DR PATRIC; 20357503; VBINeiMen85645_1268. DR eggNOG; ENOG4108YE5; Bacteria. DR eggNOG; COG2128; LUCA. DR HOGENOM; HOG000218410; -. DR OMA; INVEHAC; -. DR OrthoDB; EOG6P5ZKB; -. DR BioCyc; NMEN122586:GHGG-1032-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 3: Inferred from homology; KW Antioxidant {ECO:0000256|SAAS:SAAS00461132}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00461175}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00461184}; KW Peroxidase {ECO:0000256|SAAS:SAAS00461184}; KW Redox-active center {ECO:0000256|SAAS:SAAS00461089}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 86 167 CMD. {ECO:0000259|Pfam:PF02627}. SQ SEQUENCE 227 AA; 24170 MW; F6F39FF6C8358602 CRC64; MPSEKCSDGI SYNLLFAAHN QSVFPIPFRN AYHAPVPNIC EQGKKMARLT VHTLETAPEA AKARVEAVLQ NNGFIPNLIG VLSNAPEALA FYQEVGKLNA ANSLTAGEVE VIQIIAARTN QCGFCVAGHT KLATLKKLLS EQSVKAARAL AAGEFDDAKL GALAAFTQAV MAKKGAVSDE ELKAFFDAGY NQQQAVEVVM GVALATLCNY VNNLGQTEIN PELQAYA // ID Q9JXA1_NEIMB Unreviewed; 203 AA. AC Q9JXA1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42461.1}; GN OrderedLocusNames=NMB2153 {ECO:0000313|EMBL:AAF42461.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42461.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42461.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42461.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42461.1; -; Genomic_DNA. DR PIR; G81000; G81000. DR RefSeq; NP_275138.1; NC_003112.2. DR RefSeq; WP_002255036.1; NC_003112.2. DR ProteinModelPortal; Q9JXA1; -. DR STRING; 122586.NMB2153; -. DR PaxDb; Q9JXA1; -. DR DNASU; 903219; -. DR EnsemblBacteria; AAF42461; AAF42461; NMB2153. DR GeneID; 903219; -. DR KEGG; nme:NMB2153; -. DR PATRIC; 20360502; VBINeiMen85645_2747. DR eggNOG; ENOG4108ZK7; Bacteria. DR eggNOG; COG1739; LUCA. DR HOGENOM; HOG000075268; -. DR OMA; ILQSEYA; -. DR OrthoDB; EOG6N685N; -. DR BioCyc; NMEN122586:GHGG-2218-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.230.30; -; 1. DR InterPro; IPR023582; Impact. DR InterPro; IPR001498; Impact_N. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR020569; UPF0029_Impact_CS. DR PANTHER; PTHR16301; PTHR16301; 1. DR Pfam; PF01205; UPF0029; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS00910; UPF0029; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 124 UPF0029. {ECO:0000259|Pfam:PF01205}. SQ SEQUENCE 203 AA; 22871 MW; D48C297EC6B5C8F6 CRC64; MITTYKTITS LTQAEFKDKG SRFIAFAYPI RTLADVKKYL DPLKEEHHKA RHWCYAYRLG VDGVQFRAND DGEPSGSAGR PILGQIDSVG ITDVLVVVVR YFGGTLLGVP GLIHAYKEAT AQALAVAEVV EKNIEKTVWL KCEYPFLNEA IRIAKQYQAD ILERDLQLDC RLTVSLSLVN YEACVAAWKN TRQIEVNTEK PFE // ID Q9K138_NEIMB Unreviewed; 324 AA. AC Q9K138; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Sugar isomerase, KpsF/GutQ family {ECO:0000313|EMBL:AAF40795.1}; GN OrderedLocusNames=NMB0352 {ECO:0000313|EMBL:AAF40795.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40795.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40795.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40795.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily. CC {ECO:0000256|PIRNR:PIRNR004692}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40795.1; -; Genomic_DNA. DR PIR; G81207; G81207. DR RefSeq; NP_273401.1; NC_003112.2. DR RefSeq; WP_002243982.1; NC_003112.2. DR ProteinModelPortal; Q9K138; -. DR STRING; 122586.NMB0352; -. DR PaxDb; Q9K138; -. DR EnsemblBacteria; AAF40795; AAF40795; NMB0352. DR GeneID; 902467; -. DR KEGG; nme:NMB0352; -. DR PATRIC; 20355853; VBINeiMen85645_0445. DR eggNOG; ENOG4105C2X; Bacteria. DR eggNOG; COG0517; LUCA. DR eggNOG; COG0794; LUCA. DR HOGENOM; HOG000264729; -. DR KO; K06041; -. DR OMA; LMACLMR; -. DR OrthoDB; EOG6RFZWS; -. DR BioCyc; NMEN122586:GHGG-373-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR004800; KdsD/KpsF-type. DR InterPro; IPR001347; SIS. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01380; SIS; 1. DR PIRSF; PIRSF004692; KdsD_KpsF; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR00393; kpsF; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF40795.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}. FT DOMAIN 36 179 SIS. {ECO:0000259|PROSITE:PS51464}. FT DOMAIN 205 270 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 272 324 CBS. {ECO:0000259|PROSITE:PS51371}. FT METAL 77 77 Zinc. {ECO:0000256|PIRSR:PIRSR004692-2}. FT SITE 54 54 Catalytically relevant. FT {ECO:0000256|PIRSR:PIRSR004692-3}. FT SITE 106 106 Catalytically relevant. FT {ECO:0000256|PIRSR:PIRSR004692-3}. FT SITE 147 147 Catalytically relevant. FT {ECO:0000256|PIRSR:PIRSR004692-3}. FT SITE 188 188 Catalytically relevant. FT {ECO:0000256|PIRSR:PIRSR004692-3}. SQ SEQUENCE 324 AA; 34156 MW; 03A3A3BD83B553F5 CRC64; MAENGKYLDW AREVLHAEAE GLREIAAELD KNFVLAADAL LHCKGRVVIT GMGKSGHIGR KMAATMASTG TPAFFVHPAE AAHGDLGMIV DNDVVVAISN SGESDEIAAI IPALKRKDIT LVCITARPDS TMARHADIHI TASVSKEACP LGLAPTTSTT AVMALGDALA VVLLRARAFT PDDFALSHPA GSLGKRLLLR VADIMHKGGG LPAVRLGTPL KEAIVSMSEK GLGMLAVTDG QGRLKGVFTD GDLRRLFQEC DNFTGLSIDE VMHTHPKTIS AERLATEALK VMQANHVNGL LVTDADGVLI GALNMHDLLA ARIV // ID Q9JZU1_NEIMB Unreviewed; 305 AA. AC Q9JZU1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41308.1}; GN OrderedLocusNames=NMB0900 {ECO:0000313|EMBL:AAF41308.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41308.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41308.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41308.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41308.1; -; Genomic_DNA. DR PIR; A81144; A81144. DR RefSeq; NP_273940.1; NC_003112.2. DR RefSeq; WP_002219437.1; NC_003112.2. DR STRING; 122586.NMB0900; -. DR PaxDb; Q9JZU1; -. DR EnsemblBacteria; AAF41308; AAF41308; NMB0900. DR GeneID; 903021; -. DR KEGG; nme:NMB0900; -. DR PATRIC; 20357233; VBINeiMen85645_1130. DR eggNOG; ENOG4106498; Bacteria. DR eggNOG; ENOG410Y19Z; LUCA. DR HOGENOM; HOG000220714; -. DR OrthoDB; EOG644ZVD; -. DR BioCyc; NMEN122586:GHGG-938-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR InterPro; IPR017880; KilA_N. DR InterPro; IPR018004; KilA_N/APSES_HTH. DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type. DR Pfam; PF04383; KilA-N; 1. DR SMART; SM01252; KilA-N; 1. DR SUPFAM; SSF54616; SSF54616; 1. DR PROSITE; PS51301; KILA_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 108 KilA-N. {ECO:0000259|PROSITE:PS51301}. SQ SEQUENCE 305 AA; 33465 MW; 9DBBACC4057E7B85 CRC64; MNVSVLNFGN TPVSFRQDGF LNATAIASHF GKLPKDYLKS EQTQQYISAL AENLSVRRKI LTEANQIVIV KRGGSEQGTW LHPKLAIHFA RWLNPKFAVW CDEQIEILLN GKISDGIKTV TPKPTRALPD GLTGEQIEAV KKLHNALTKS APKEAQARIA ITLWSAVKSK FGCSYKEVPA EQFPEVLSVM GRVAVENGVL YGEVLDREPL PAPQPALPIS GNALYDLAVA VRYGAWAIQM GRDVSLPLKQ LGCKQAVTMW TVWAETRSRL KAAANALEAL NAHADAEHAA KIRPMLPEIR NLSSV // ID Q9JXH0_NEIMB Unreviewed; 449 AA. AC Q9JXH0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU003385}; GN Name=petB {ECO:0000313|EMBL:AAF42372.1}; GN OrderedLocusNames=NMB2052 {ECO:0000313|EMBL:AAF42372.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42372.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42372.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42372.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. {ECO:0000256|RuleBase:RU003385}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|RuleBase:RU003385}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU003385}; CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein. CC {ECO:0000256|RuleBase:RU003385}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000256|RuleBase:RU003385}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42372.1; -; Genomic_DNA. DR PIR; E81011; E81011. DR RefSeq; NP_275042.1; NC_003112.2. DR RefSeq; WP_002225698.1; NC_003112.2. DR ProteinModelPortal; Q9JXH0; -. DR STRING; 122586.NMB2052; -. DR PaxDb; Q9JXH0; -. DR EnsemblBacteria; AAF42372; AAF42372; NMB2052. DR GeneID; 904030; -. DR KEGG; nme:NMB2052; -. DR PATRIC; 20360260; VBINeiMen85645_2630. DR eggNOG; ENOG4105DJ5; Bacteria. DR eggNOG; COG1290; LUCA. DR HOGENOM; HOG000255206; -. DR KO; K00412; -. DR OMA; QAPRYAY; -. DR OrthoDB; EOG6P3338; -. DR BioCyc; NMEN122586:GHGG-2115-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR SUPFAM; SSF81648; SSF81648; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|RuleBase:RU003385}; KW Heme {ECO:0000256|RuleBase:RU003385}; KW Iron {ECO:0000256|RuleBase:RU003385}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU003385}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42372.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Respiratory chain {ECO:0000256|RuleBase:RU003385}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003385}. FT TRANSMEM 41 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 178 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 363 382 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 388 408 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 429 446 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 12 231 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 241 418 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. SQ SEQUENCE 449 AA; 50271 MW; EBF0BF0E0067C5B3 CRC64; MANQTNSKAK ALLGWVDARF PLSKMWKEHL SEYYAPKNFN FWYFFGSLSM LVLVIQIVSG IFLTMNYKPD GNLNAYHLPA AFTAVEYIMR DVSGGWIIRY MHSTGASFFF IVVYLHMFRG LIYGSYKKPR ELVWIFGSLI FLALMAEAFM GYLLPWGQMS FWGAQVIINL FSAIPVIGPD LSTWIRGDFN VSDVTLNRFF ALHVIAVPLV LLGLVVAHII ALHEVGSNNP DGVEIKKLKD ENGVPLDGIP FFPYYVVHDI LAVTIFLIVF CAVMFFAPEG GGYFLEAPNF DAANALKTPP HIAPVWYFTP FYAILRAIPS FAGTQVWGVI GMGAAVVLIA LLPWLDKGEV KSVRYRGPIF KTALVLFIIA FIGLGILGAM VATDTRTLVA RILSFVYFAF FLGMPFYTKL DTNKPVPERV TMSTTKQKIM FFVYVGITVV GAYLFATNI // ID Q9JYV8_NEIMB Unreviewed; 217 AA. AC Q9JYV8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=IS1016C2 transposase {ECO:0000313|EMBL:AAF41773.1}; GN OrderedLocusNames=NMB1411 {ECO:0000313|EMBL:AAF41773.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41773.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41773.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41773.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41773.1; -; Genomic_DNA. DR PIR; G81087; G81087. DR RefSeq; NP_274424.1; NC_003112.2. DR RefSeq; WP_010980932.1; NC_003112.2. DR PaxDb; Q9JYV8; -. DR EnsemblBacteria; AAF41773; AAF41773; NMB1411. DR GeneID; 903833; -. DR KEGG; nme:NMB1411; -. DR PATRIC; 20358501; VBINeiMen85645_1762. DR eggNOG; ENOG4105S1F; Bacteria. DR eggNOG; ENOG4111JFI; LUCA. DR HOGENOM; HOG000218644; -. DR KO; K07488; -. DR OMA; IKECEFR; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NMEN122586:GHGG-1449-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. DR SMART; SM01126; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 217 AA; 24833 MW; 775A74BD0513877B CRC64; MKITHCKLKK KVQKELLRFF VLEVTARSAA DILGIHPNSA VLFYRKIRTV INHHLALAAD EVFEGPVEPD ESDFGGRRKG RRGRGAAGKV VVFGILKRNG RGYTVVVDNA KSETLLPVIK KKIMPDSIVY TDSLSSCDKL DVSGFIHYRI NHSKEFADRQ NHINGIENFW NQAKRVLRKY NGIDRKSFPL FLKECEFRFN FGTPSQQLKI LRDWCGI // ID Q9JYG8_NEIMB Unreviewed; 287 AA. AC Q9JYG8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41946.1}; GN OrderedLocusNames=NMB1593 {ECO:0000313|EMBL:AAF41946.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41946.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41946.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41946.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41946.1; -; Genomic_DNA. DR PIR; C81066; C81066. DR RefSeq; NP_274599.1; NC_003112.2. DR RefSeq; WP_002234132.1; NC_003112.2. DR STRING; 122586.NMB1593; -. DR PaxDb; Q9JYG8; -. DR EnsemblBacteria; AAF41946; AAF41946; NMB1593. DR GeneID; 904269; -. DR KEGG; nme:NMB1593; -. DR PATRIC; 20359068; VBINeiMen85645_2046. DR eggNOG; ENOG4105DJP; Bacteria. DR eggNOG; COG0697; LUCA. DR HOGENOM; HOG000271939; -. DR OMA; SIWYYVI; -. DR OrthoDB; EOG6JTC7T; -. DR BioCyc; NMEN122586:GHGG-1641-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 271 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 128 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 148 269 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 287 AA; 31214 MW; 929675B741AB53BB CRC64; MLVAAACFTI MNVLIKEASA KFALGSGELV FWRMLFSTVA LGAAAVLRRD TFRTPHWKNH LNRSMVGTGA MLLLFYAVTH LPLATGVTLS YTSSIFLAVF SFLILKERIS VYTQAVLLLG FAGVVLLLNP SFRSGQETAA LAGLAGGAMS GWAYLKVREL SLAGEPGWRV VFYLSVTGVA MSSVWATLTG WHTLSFPSAV YLSCIGVSAL IAQLSMTRAY KVGDKFTVAS LSYMTVVFSA LSAAFFLGEE LFWQEILGMC IIILSGILSS IRPTAFKQRL QSLFRQR // ID Q9JY75_NEIMB Unreviewed; 354 AA. AC Q9JY75; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Alpha-1,2-N-acetylglucosamine transferase {ECO:0000313|EMBL:AAF42053.1}; GN Name=rfaK {ECO:0000313|EMBL:AAF42053.1}; GN OrderedLocusNames=NMB1705 {ECO:0000313|EMBL:AAF42053.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42053.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42053.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42053.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42053.1; -; Genomic_DNA. DR PIR; C81053; C81053. DR RefSeq; NP_274709.1; NC_003112.2. DR RefSeq; WP_002222112.1; NC_003112.2. DR ProteinModelPortal; Q9JY75; -. DR STRING; 122586.NMB1705; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR PaxDb; Q9JY75; -. DR EnsemblBacteria; AAF42053; AAF42053; NMB1705. DR GeneID; 903397; -. DR KEGG; nme:NMB1705; -. DR PATRIC; 20359367; VBINeiMen85645_2189. DR eggNOG; ENOG4107T8Q; Bacteria. DR eggNOG; COG0438; LUCA. DR HOGENOM; HOG000219076; -. DR OMA; DCTMFTA; -. DR OrthoDB; EOG68DD0W; -. DR BioCyc; NMEN122586:GHGG-1761-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42053.1}. FT DOMAIN 16 167 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13439}. FT DOMAIN 178 333 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 354 AA; 39987 MW; F135478AD95CDE42 CRC64; MEKEFRILNI VSAKIWGGGE QYVYDVSKAL GLRGCTMFTA VNKNNELMHR RFSEVSSVFT TRLHTLNGLF SLYALTRFIR KNRISHLMIH TGKIAALSIL LKKLTGVRLI FVKHNVVANK TDFYHRLIQK NTDRFICVSR LVYDVQTADN PFKEKYRIVH NGIDTGRFPP SQEKPDSRFF TVAYAGRISP EKGLENLIEA CVILHRKYPQ IRLKLAGDGH PDYMCRLKRD VSASGAEPFV SFEGFTEKLA SFYRQSDVVV LPSLVPEAFG LSLCEAMYCR TAVISNTLGA QKEIVEHHQS GILLDRLTPE SLADEIERLV LNPETKNALA TAAHQCVAAR FTINHTADKL LDAI // ID Q9JZW7_NEIMB Unreviewed; 213 AA. AC Q9JZW7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41279.1}; GN OrderedLocusNames=NMB0868 {ECO:0000313|EMBL:AAF41279.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41279.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41279.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41279.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41279.1; -; Genomic_DNA. DR PIR; D81148; D81148. DR RefSeq; NP_273909.1; NC_003112.2. DR RefSeq; WP_002225377.1; NC_003112.2. DR ProteinModelPortal; Q9JZW7; -. DR STRING; 122586.NMB0868; -. DR ESTHER; neime-NMB0868; Atu1826-like. DR PaxDb; Q9JZW7; -. DR EnsemblBacteria; AAF41279; AAF41279; NMB0868. DR GeneID; 902982; -. DR KEGG; nme:NMB0868; -. DR PATRIC; 20357125; VBINeiMen85645_1081. DR eggNOG; ENOG4105DHZ; Bacteria. DR eggNOG; COG2945; LUCA. DR HOGENOM; HOG000265112; -. DR KO; K07018; -. DR OMA; KVAECGH; -. DR OrthoDB; EOG6XDH0P; -. DR BioCyc; NMEN122586:GHGG-899-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 213 AA; 22630 MW; 8A2DDF4E1E2A69F7 CRC64; MLKPETIHIS GPAGILETIH IPSEQVPARG VAVINHPNPL QGGTNTNKVI QTAAKALSKL GFHCYLPNLR GVGGSGGTHD YGRGETQDCL AVIDYARAQH PEAPEFALSG FSFGGYVATF AAQARTPDLL LLIGAAVCHY TDRPEPSAVP NVAKTLMIHG AEDEVVEIGK ALKWAEPQDL PVITIAGSTH FFHGKLIVLR DTILRFAPVC LNG // ID Q9JYD3_NEIMB Unreviewed; 500 AA. AC Q9JYD3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945, GN ECO:0000313|EMBL:AAF41991.1}; GN OrderedLocusNames=NMB1642 {ECO:0000313|EMBL:AAF41991.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41991.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41991.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41991.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates in both transcription termination and CC antitermination. {ECO:0000256|HAMAP-Rule:MF_00945}. CC -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA- CC dependent RNA polymerase and to nascent RNA. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}. CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41991.1; -; Genomic_DNA. DR PIR; B81060; B81060. DR RefSeq; NP_274647.1; NC_003112.2. DR RefSeq; WP_002225001.1; NC_003112.2. DR ProteinModelPortal; Q9JYD3; -. DR SMR; Q9JYD3; 363-426. DR STRING; 122586.NMB1642; -. DR PaxDb; Q9JYD3; -. DR DNASU; 903935; -. DR EnsemblBacteria; AAF41991; AAF41991; NMB1642. DR GeneID; 903935; -. DR KEGG; nme:NMB1642; -. DR PATRIC; 20359204; VBINeiMen85645_2114. DR eggNOG; ENOG4105CHV; Bacteria. DR eggNOG; COG0195; LUCA. DR HOGENOM; HOG000006394; -. DR KO; K02600; -. DR OMA; QLFMDKL; -. DR OrthoDB; EOG6NSGHW; -. DR BioCyc; NMEN122586:GHGG-1691-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1480.10; -; 1. DR Gene3D; 3.30.300.20; -; 2. DR HAMAP; MF_00945_B; NusA_B; 1. DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR025249; KH_dom_NusA-like. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR030842; NusA_bac. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR013735; TF_NusA_N. DR InterPro; IPR010214; Tscrpt_termin_fac_NusA_C_rpt. DR InterPro; IPR010213; Tscrpt_termination_fac_NusA. DR Pfam; PF13184; KH_5; 1. DR Pfam; PF08529; NusA_N; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00322; KH; 3. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF47794; SSF47794; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54814; SSF54814; 2. DR SUPFAM; SSF69705; SSF69705; 1. DR TIGRFAMs; TIGR01953; NusA; 1. DR TIGRFAMs; TIGR01954; nusA_Cterm_rpt; 2. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription antitermination {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription termination {ECO:0000256|HAMAP-Rule:MF_00945}. FT DOMAIN 140 208 S1 motif. {ECO:0000256|HAMAP- FT Rule:MF_00945, FT ECO:0000259|PROSITE:PS50126}. FT DOMAIN 310 346 KH. {ECO:0000259|PROSITE:PS50084}. SQ SEQUENCE 500 AA; 55752 MW; 753FA50DDEF5B774 CRC64; MSREMLQLAE ALASEKNVDA EVVFQALEFA LSTAAKKKAD REHMDVRVQI NRDTGEYQTF RRWLIVADED YTYPDVEKTI EEIQEEIPGT TIQIGEYYEE QLPNEGFGRQ AAQTAKQIIL QRIRDAEREQ NLNEFLAVKE DIVSGTVKRV ERHGIIVEVV AGKLDALIPR DQMIPRENFR SGDRIRALFL RVEEIGNTGR KQVILSRTSG DFLVKLYANE VPEIADGMLE IRAVARDPGQ RAKVAVKAND QRIDPQGTCI GVRGSRVNAV SNELSGERID VVLWSPEPAQ FVMSALSPAE VSRIVIDEDK HAVDVIVAED QLALAIGRGG QNVRLASDLT GWQLNIMTSA EADERNAAED AAIRRLFMDH LNVDEETADV LVQEGFATLE EVAYVPAAEL LAIEGFDEEI VDMLRNRARD AILTMAIAAE EKLGEVSDDM RNLEGIDADM LRSLAEAGIT TRDDLAELAV DELIEITGVN EETAKAVILT AREHWFTEDK // ID Q9K0A3_NEIMB Unreviewed; 290 AA. AC Q9K0A3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=RNA polymerase sigma factor RpoH {ECO:0000256|HAMAP-Rule:MF_00961}; DE AltName: Full=RNA polymerase sigma-32 factor {ECO:0000256|HAMAP-Rule:MF_00961}; GN Name=rpoH {ECO:0000256|HAMAP-Rule:MF_00961, GN ECO:0000313|EMBL:AAF41127.1}; GN OrderedLocusNames=NMB0712 {ECO:0000313|EMBL:AAF41127.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41127.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41127.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41127.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBUNIT: Interacts with the RNA polymerase core enzyme. CC {ECO:0000256|HAMAP-Rule:MF_00961}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00961}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41127.1; -; Genomic_DNA. DR PIR; G81166; G81166. DR RefSeq; NP_273754.1; NC_003112.2. DR RefSeq; WP_010980829.1; NC_003112.2. DR ProteinModelPortal; Q9K0A3; -. DR STRING; 122586.NMB0712; -. DR PaxDb; Q9K0A3; -. DR EnsemblBacteria; AAF41127; AAF41127; NMB0712. DR GeneID; 902824; -. DR KEGG; nme:NMB0712; -. DR PATRIC; 20356773; VBINeiMen85645_0908. DR eggNOG; ENOG4105DEK; Bacteria. DR eggNOG; COG0568; LUCA. DR HOGENOM; HOG000270269; -. DR KO; K03089; -. DR OMA; EIHEYIV; -. DR OrthoDB; EOG6D5G0W; -. DR BioCyc; NMEN122586:GHGG-740-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:InterPro. DR GO; GO:0001123; P:transcription initiation from bacterial-type RNA polymerase promoter; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00961; Sigma70_RpoH; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR009042; RNA_pol_sigma70_r1_2. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR016263; RNA_pol_sigma_factor. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR012759; RNA_pol_sigma_RpoH_proteobac. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00140; Sigma70_r1_2; 1. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PIRSF; PIRSF000770; RNA_pol_sigma-SigE/K; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02392; rpoH_proteo; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS00715; SIGMA70_1; 1. DR PROSITE; PS00716; SIGMA70_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00961}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00961, KW ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Sigma factor {ECO:0000256|HAMAP-Rule:MF_00961, KW ECO:0000256|SAAS:SAAS00458134}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_00961}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00961, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00961, KW ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 80 93 RNA_pol_sigma70. FT {ECO:0000259|PROSITE:PS00715}. FT DOMAIN 253 279 RNA_pol_sigma70. FT {ECO:0000259|PROSITE:PS00716}. FT DNA_BIND 254 273 H-T-H motif. {ECO:0000256|HAMAP- FT Rule:MF_00961}. FT REGION 56 125 Sigma-70 factor domain-2. FT {ECO:0000256|HAMAP-Rule:MF_00961}. FT REGION 229 281 Sigma-70 factor domain-4. FT {ECO:0000256|HAMAP-Rule:MF_00961}. FT MOTIF 80 83 Interaction with polymerase core subunit FT RpoC. {ECO:0000256|HAMAP-Rule:MF_00961}. SQ SEQUENCE 290 AA; 32870 MW; 1EA047D48266FEEF CRC64; MSQMNNAFAL PAIQSGNGSL EQYIHTVNRI PMLTQEEETR LAERQHKGDL NAAKQLILSH LRVVVSIARG YDGYGLNQAD LIQEGNIGLM KAVKRYEPGR GARLFSFAVH WIKAEIHEFI LRNWRLVRVA TTKPQRKLFF NLRSMRKNLN ALSPKEAQDI ADDLGVKLSE VLEMEQRMTG HDIAIMADNS DDEDSFAPID WLADHDSEPS RQLSKQAHYA LQTEGLQNAL AQLDDRSRRI VESRWLQDDG GLTLHQLAAE YGVSAERIRQ IEAKAMQKLR GFLTEEAEAV // ID Q9K0L3_NEIMB Unreviewed; 553 AA. AC Q9K0L3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase {ECO:0000313|EMBL:AAF41009.1}; DE EC=1.5.5.1 {ECO:0000313|EMBL:AAF41009.1}; GN OrderedLocusNames=NMB0581 {ECO:0000313|EMBL:AAF41009.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41009.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41009.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41009.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41009.1; -; Genomic_DNA. DR PIR; G81181; G81181. DR RefSeq; NP_273625.1; NC_003112.2. DR RefSeq; WP_002222867.1; NC_003112.2. DR ProteinModelPortal; Q9K0L3; -. DR SMR; Q9K0L3; 3-553. DR STRING; 122586.NMB0581; -. DR PaxDb; Q9K0L3; -. DR EnsemblBacteria; AAF41009; AAF41009; NMB0581. DR GeneID; 902696; -. DR KEGG; nme:NMB0581; -. DR PATRIC; 20356445; VBINeiMen85645_0742. DR eggNOG; ENOG4105DWH; Bacteria. DR eggNOG; COG0644; LUCA. DR HOGENOM; HOG000259450; -. DR KO; K00311; -. DR OMA; FKLDQNS; -. DR OrthoDB; EOG6ZPSVS; -. DR BioCyc; NMEN122586:GHGG-607-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR007859; ETFD_OxRdtase/FixX. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR PANTHER; PTHR10617:SF107; PTHR10617:SF107; 1. DR Pfam; PF05187; ETF_QO; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41009.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Ubiquinone {ECO:0000313|EMBL:AAF41009.1}. SQ SEQUENCE 553 AA; 61050 MW; 538CC6D5C2DC93D7 CRC64; MTESITRDSM QYDVVIVGAG PSGLSAAIKL KQLAEQNGRE ISVCVVEKGS EVGAHSLAGA VIDPIALNEL ISDWKEKGAP LTRTVTQDKV LFLTEKKAFN LPITPNFDNH GNYIVSLGEV VRWLAEQAEN MGVEIYPGFA AAEVLYHEDG SVKGIATGNM GIGKDGEPTD SFQPGMELWA QQTLFAEGCR GSLSKQIIER FQLDQNSQPQ TYGLGIKEVW EVPSEQHQPG LVVHSAGWPL DSKTYGGAFV YHFDDNKVAV GFVVGLDYQN PYLSPFEEFQ RFKTHPEIRK TFEGGRRIAY GARSLIEGGL QSLPKLSFKG GILVGDAAGF LNMPRIKGIH TAMKSAMLAA EAVFPLLENL EEVEGFDSGK EAADYQQRFE QSWLYQELYA ARNVRPSFKW GVYLGSIYTG IDQMIFRGKA PWTLKHHGKD NEQLKKAAAC KPIDYPKPDG VLTFDRLSSV FLANLAHEEN QPDHLVLNNP QTMIDVNYKE YASPETRYCP AGVYEIVEEN GNPRLQINAA NCVHCKTCDI KDPTQNITWI CPEGASGPNY GGM // ID Q7DDM6_NEIMB Unreviewed; 225 AA. AC Q7DDM6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=DNA-binding response regulator {ECO:0000313|EMBL:AAF41023.1}; GN OrderedLocusNames=NMB0595 {ECO:0000313|EMBL:AAF41023.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41023.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41023.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41023.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains OmpR/PhoB-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00583175}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00122778}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41023.1; -; Genomic_DNA. DR PIR; H81180; H81180. DR RefSeq; NP_273639.1; NC_003112.2. DR RefSeq; WP_002214312.1; NC_003112.2. DR ProteinModelPortal; Q7DDM6; -. DR STRING; 122586.NMB0595; -. DR PaxDb; Q7DDM6; -. DR EnsemblBacteria; AAF41023; AAF41023; NMB0595. DR GeneID; 902710; -. DR KEGG; nme:NMB0595; -. DR PATRIC; 20356475; VBINeiMen85645_0757. DR eggNOG; ENOG4105E3W; Bacteria. DR eggNOG; COG0745; LUCA. DR HOGENOM; HOG000034819; -. DR KO; K02483; -. DR OMA; HAINIET; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NMEN122586:GHGG-621-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919, KW ECO:0000313|EMBL:AAF41023.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00478953}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00478953}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00478431}. FT DOMAIN 3 116 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 129 224 OmpR/PhoB-type DNA-binding. FT {ECO:0000259|PROSITE:PS51755}. SQ SEQUENCE 225 AA; 24780 MW; 02E4E418D047D089 CRC64; MSRVLLVDDD ALLTELLTEY LSAEGLNVRS VPDGEAGVQE ILSGQYDVVV LDSMMPKMNG LDVLKNVRAR STVPIIMLTA KGDDIDRIIG LEMGADDYVP KPCTPRELLA RINAILRRAQ HSGEQNNAPN SISVSDVVLY PAKRQASVKD MPLELTSTEF NLLEVLMRHA GQVVSKETLS VEALDRKLAK FDRSIDVHIS SIRHKLGDAS LIQTVRGLGY LFVKN // ID Q9JXL6_NEIMB Unreviewed; 1457 AA. AC Q9JXL6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Adhesion and penetration protein {ECO:0000313|EMBL:AAF42312.1}; GN Name=hap {ECO:0000313|EMBL:AAF42312.1}; GN OrderedLocusNames=NMB1985 {ECO:0000313|EMBL:AAF42312.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42312.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42312.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42312.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42312.1; -; Genomic_DNA. DR PIR; D81019; D81019. DR RefSeq; NP_274977.1; NC_003112.2. DR RefSeq; WP_002225857.1; NC_003112.2. DR ProteinModelPortal; Q9JXL6; -. DR STRING; 122586.NMB1985; -. DR MEROPS; S06.006; -. DR PaxDb; Q9JXL6; -. DR EnsemblBacteria; AAF42312; AAF42312; NMB1985. DR GeneID; 904147; -. DR KEGG; nme:NMB1985; -. DR PATRIC; 20360055; VBINeiMen85645_2532. DR eggNOG; ENOG4108BMY; Bacteria. DR eggNOG; COG3468; LUCA. DR HOGENOM; HOG000218734; -. DR KO; K01347; -. DR OMA; YFIEREN; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NMEN122586:GHGG-2042-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.160.20.20; -; 3. DR Gene3D; 2.40.128.130; -; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR006315; OM_autotransptr_brl. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR000710; Peptidase_S6. DR InterPro; IPR030396; Peptidase_S6_dom. DR InterPro; IPR004899; Pertactin_central. DR InterPro; IPR033116; TRYPSIN_SER. DR Pfam; PF02395; Peptidase_S6; 1. DR Pfam; PF03212; Pertactin; 1. DR PRINTS; PR00921; IGASERPTASE. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF51126; SSF51126; 3. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS51691; PEPTIDASE_S6; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 43 310 Peptidase S6. FT {ECO:0000259|PROSITE:PS51691}. FT DOMAIN 1204 1457 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. SQ SEQUENCE 1457 AA; 159966 MW; B759529CFD4BD0AF CRC64; MKTTDKRTTE THRKAPKTGR IRFSPAYLAI CLSFGILPQA WAGHTYFGIN YQYYRDFAEN KGKFAVGAKD IEVYNKKGEL VGKSMTKAPM IDFSVVSRNG VAALVGDQYI VSVAHNGGYN NVDFGAEGRN PDQHRFTYKI VKRNNYKAGT KGHPYGGDYH MPRLHKFVTD AEPVEMTSYM DGRKYIDQNN YPDRVRIGAG RQYWRSDEDE PNNRESSYHI ASAYSWLVGG NTFAQNGSGG GTVNLGSEKI KHSPYGFLPT GGSFGDSGSP MFIYDAQKQK WLINGVLQTG NPYIGKSNGF QLVRKDWFYD EIFAGDTHSV FYEPRQNGKY SFNDDNNGTG KINAKHEHNS LPNRLKTRTV QLFNVSLSET AREPVYHAAG GVNSYRPRLN NGENISFIDE GKGELILTSN INQGAGGLYF QGDFTVSPEN NETWQGAGVH ISEDSTVTWK VNGVANDRLS KIGKGTLHVQ AKGENQGSIS VGDGTVILDQ QADDKGKKQA FSEIGLVSGR GTVQLNADNQ FNPDKLYFGF RGGRLDLNGH SLSFHRIQNT DEGAMIVNHN QDKESTVTIT GNKDIATTGN NNSLDSKKEI AYNGWFGEKD TTKTNGRLNL VYQPAAEDRT LLLSGGTNLN GNITQTNGKL FFSGRPTPHA YNHLNDHWSQ KEGIPRGEIV WDNDWINRTF KAENFQIKGG QAVVSRNVAK VKGDWHLSNH AQAVFGVAPH QSHTICTRSD WTGLTNCVEK TITDDKVIAS LTKTDISGNV DLADHAHLNL TGLATLNGNL SANGDTRYTV SHNATQNGNL SLVGNAQATF NQATLNGNTS ASGNASFNLS DHAVQNGSLT LSGNAKANVS HSALNGNVSL ADKAVFHFES SRFTGQISGG KDTALHLKDS EWTLPSGTEL GNLNLDNATI TLNSAYRHDA AGAQTGSATD APRRRSRRSR RSLLSVTPPT SVESRFNTLT VNGKLNGQGT FRFMSELFGY RSDKLKLAES SEGTYTLAVN NTGNEPASLE QLTVVEGKDN KPLSENLNFT LQNEHVDAGA WRYQLIRKDG EFRLHNPVKE QELSDKLGKA EAKKQAEKDN AQSLDALIAA GRDAVEKTES VAEPARQAGG ENVGIMQAEE EKKRVQADKD TALAKQREAE TRPATTAFPR ARRARRDLPQ LQPQPQPQPQ RDLISRYANS GLSEFSATLN SVFAVQDELD RVFAEDRRNA VWTSGIRDTK HYRSQDFRAY RQQTDLRQIG MQKNLGSGRV GILFSHNRTE NTFDDGIGNS ARLAHGAVFG QYGIDRFYIG ISAGAGFSSG SLSDGIGGKI RRRVLHYGIQ ARYRAGFGGF GIEPHIGATR YFVQKADYRY ENVNIATPGL AFNRYRAGIK ADYSFKPAQH ISITPYLSLS YTDAASGKVR TRVNTAVLAQ DFGKTRSAEW GVNAEIKGFT LSLHAAAAKG PQLEAQHSAG IKLGYRW // ID Q9K1J4_NEIMB Unreviewed; 92 AA. AC Q9K1J4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Preprotein translocase SecE subunit {ECO:0000313|EMBL:AAF40584.1}; GN Name=secE {ECO:0000313|EMBL:AAF40584.1}; GN OrderedLocusNames=NMB0125 {ECO:0000313|EMBL:AAF40584.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40584.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40584.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40584.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. CC {ECO:0000256|SAAS:SAAS00569815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40584.1; -; Genomic_DNA. DR PIR; B81235; B81235. DR RefSeq; NP_273183.1; NC_003112.2. DR RefSeq; WP_002215367.1; NC_003112.2. DR STRING; 122586.NMB0125; -. DR PaxDb; Q9K1J4; -. DR EnsemblBacteria; AAF40584; AAF40584; NMB0125. DR GeneID; 902233; -. DR KEGG; nme:NMB0125; -. DR PATRIC; 20355271; VBINeiMen85645_0165. DR eggNOG; COG0690; LUCA. DR HOGENOM; HOG000218664; -. DR KO; K03073; -. DR OMA; FQQGIVQ; -. DR OrthoDB; EOG6DRPR4; -. DR BioCyc; NMEN122586:GHGG-135-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:InterPro. DR HAMAP; MF_00422; SecE; 1. DR InterPro; IPR022943; SecE. DR InterPro; IPR005807; SecE_bac. DR InterPro; IPR001901; Translocase_SecE/Sec61-g. DR Pfam; PF00584; SecE; 1. DR TIGRFAMs; TIGR00964; secE_bact; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00458914, ECO:0000256|SAM:Phobius}; KW Protein transport {ECO:0000256|SAAS:SAAS00458899}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Translocation {ECO:0000256|SAAS:SAAS00458899}; KW Transmembrane {ECO:0000256|SAAS:SAAS00458914, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00458914, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00458899}. FT TRANSMEM 59 84 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 92 AA; 10626 MW; 186EA2A8CE4EF9E7 CRC64; MTEHTPEKKN VKVDQLVVQD KESASNSGKE GFFAYFSNSW SEFKKVVWPK REDAVRMTVF VIVFVAVLSI FIYAADTAIS WLFFDVLLRR EG // ID Q9JXZ3_NEIMB Unreviewed; 123 AA. AC Q9JXZ3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42161.1}; GN OrderedLocusNames=NMB1826 {ECO:0000313|EMBL:AAF42161.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42161.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42161.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42161.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42161.1; -; Genomic_DNA. DR PIR; G81037; G81037. DR RefSeq; NP_274823.2; NC_003112.2. DR ProteinModelPortal; Q9JXZ3; -. DR STRING; 122586.NMB1826; -. DR PaxDb; Q9JXZ3; -. DR EnsemblBacteria; AAF42161; AAF42161; NMB1826. DR GeneID; 903274; -. DR KEGG; nme:NMB1826; -. DR PATRIC; 20359637; VBINeiMen85645_2324. DR eggNOG; ENOG4105WQ3; Bacteria. DR eggNOG; COG2501; LUCA. DR HOGENOM; HOG000074028; -. DR KO; K14761; -. DR OrthoDB; EOG6VB6ZH; -. DR BioCyc; NMEN122586:GHGG-1881-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR002942; S4_RNA-bd. DR PROSITE; PS50889; S4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 59 119 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 123 AA; 13453 MW; 5F4D4B934FD6B126 CRC64; MAAYGVSDGI FTFTEQAVRI HRRFFGNFGY GGGRCYNNGL FLQGNIMEAT VYLEDNEYIA LCDLLKLVGL AESGGQAKAF IAEGLVLRNG ETETRKTAKI RGGEVIEFDG ARLEIADGYD PEV // ID Q7DDS6_NEIMB Unreviewed; 475 AA. AC Q7DDS6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Putative amino acid symporter {ECO:0000313|EMBL:AAF40651.1}; GN OrderedLocusNames=NMB0194 {ECO:0000313|EMBL:AAF40651.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40651.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40651.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40651.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU363064}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363064}. CC -!- SIMILARITY: Belongs to the sodium:alanine (SAF) symporter family. CC {ECO:0000256|RuleBase:RU363064}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40651.1; -; Genomic_DNA. DR PIR; G81227; G81227. DR RefSeq; NP_273252.1; NC_003112.2. DR RefSeq; WP_002215509.1; NC_003112.2. DR STRING; 122586.NMB0194; -. DR PaxDb; Q7DDS6; -. DR EnsemblBacteria; AAF40651; AAF40651; NMB0194. DR GeneID; 902302; -. DR KEGG; nme:NMB0194; -. DR PATRIC; 20355421; VBINeiMen85645_0239. DR eggNOG; ENOG4105BZG; Bacteria. DR eggNOG; COG1115; LUCA. DR HOGENOM; HOG000255107; -. DR KO; K03310; -. DR OMA; AQLFKVK; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NMEN122586:GHGG-205-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR30330; PTHR30330; 1. DR Pfam; PF01235; Na_Ala_symp; 1. DR PRINTS; PR00175; NAALASMPORT. DR TIGRFAMs; TIGR00835; agcS; 1. DR PROSITE; PS00873; NA_ALANINE_SYMP; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU363064}; KW Cell membrane {ECO:0000256|RuleBase:RU363064}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Symport {ECO:0000256|RuleBase:RU363064}; KW Transmembrane {ECO:0000256|RuleBase:RU363064}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363064}; KW Transport {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 20 47 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 151 168 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 188 207 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 216 237 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 243 266 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 308 330 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 350 376 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 388 414 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 420 443 Helical. {ECO:0000256|RuleBase:RU363064}. SQ SEQUENCE 475 AA; 51792 MW; ED2BF9316BBD95F8 CRC64; MNENFTEWLH GWVGAINDPM WSYLVYMLLG TGLFFTVTTG FVQFRLFGRS IKEMLGGRKQ GDDPHGITPF QAFVTGLASR VGVGNIAGVA IAIKVGGPGA VFWMWVTALI GMSSAFVESS LAQLFKVRDY DNHHFRGGPA YYITQGLGQK WLGVLFALSL IFCFGFVFEA VQTNTIADTV KAAWGWEPHY VGVALVILTA PIIFGGIRRI SKAAEIVVPL MAVLYLFIAL FIILTNIPMI PDVFGQIFSG AFKFDAAAGG LLGGLISQTM MMGIKRGLYS NEAGMGSAPN AAAAAEVKHP VSQGMIQMLG VFVDTIIVCS CTAFIILIYQ QPYGDLSGAA LTQAAIVSQV GQWGAGFLAV ILFMFAFSTV IGNYAYAESN VQFIKSHWLI TAVFRMLVLA WVYFGAVANV PLVWDMADMA MGIMAWINLV AILLLSPLAF MLLRDYTAKL KMGKDPEFKL SEHPGLKRRI KSDVW // ID Q9JYS9_NEIMB Unreviewed; 671 AA. AC Q9JYS9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920}; DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01920}; GN Name=rep {ECO:0000256|HAMAP-Rule:MF_01920, GN ECO:0000313|EMBL:AAF41807.1}; GN OrderedLocusNames=NMB1447 {ECO:0000313|EMBL:AAF41807.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41807.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41807.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41807.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase CC involved in DNA replication; it can initiate unwinding at a nick CC in the DNA. It binds to the single-stranded DNA and acts in a CC progressive fashion along the DNA in the 3' to 5' direction. CC {ECO:0000256|HAMAP-Rule:MF_01920}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|SAAS:SAAS00553768}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|SAAS:SAAS00597767}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_01920}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_01920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41807.1; -; Genomic_DNA. DR PIR; H81082; H81082. DR RefSeq; NP_274459.1; NC_003112.2. DR RefSeq; WP_002225110.1; NC_003112.2. DR ProteinModelPortal; Q9JYS9; -. DR STRING; 122586.NMB1447; -. DR PaxDb; Q9JYS9; -. DR EnsemblBacteria; AAF41807; AAF41807; NMB1447. DR GeneID; 903867; -. DR KEGG; nme:NMB1447; -. DR PATRIC; 20358623; VBINeiMen85645_1823. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR HOGENOM; HOG000033015; -. DR KO; K03656; -. DR OMA; EKVLMQN; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; NMEN122586:GHGG-1485-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 4. DR HAMAP; MF_01920; Helicase_Rep; 1. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR005752; Helicase_Rep. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 2. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01074; rep; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAF41807.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_01920}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAF41807.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAF41807.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAF41807.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 278 UvrD-like helicase ATP-binding. FT {ECO:0000256|HAMAP-Rule:MF_01920, FT ECO:0000259|PROSITE:PS51198}. FT DOMAIN 279 557 UvrD-like helicase C-terminal. FT {ECO:0000256|HAMAP-Rule:MF_01920, FT ECO:0000259|PROSITE:PS51217}. FT NP_BIND 23 30 ATP. {ECO:0000256|HAMAP-Rule:MF_01920}. FT BINDING 276 276 ATP. {ECO:0000256|HAMAP-Rule:MF_01920}. SQ SEQUENCE 671 AA; 75616 MW; F0CAD252B39D3848 CRC64; MMKLNPQQLE AVRYLGGPLL VLAGAGSGKT GVITQKIKHL IVNVGYLPHT VAAITFTNKA AAEMQERVAK MLPKPQTRGL TICTFHSLGM KILREEANHI GYKKNFSILD STDSAKIIGE LLGGTGKEAV FKAQHQISLW KNDLKTPEDV VQTASNIWEQ QTARVYASYQ ETLQSYQAVD FDDLIRLPAV LLQQNSEVRN KWQRRLRYLL VDECQDTNTC QFTLMKLLTG AEGMFTAVGD DDQSIYAWRG ANMENLRKMQ ENYPQMKVIK LEQNYRSTAR ILKIANKVIE NNPKLFTKKL WSQLGEGEPV KVVACQNEQH EADWVVSQIV KQKLIGGDKT QYADFAVLYR GKHQARIFEE ALRGARIPYQ LSGGQSFFDK AEIKDVLSYV RLLANPNDDP AFLRAVTTPK RGIGDVTLGK LNTYAHEHEC SLYEAAQNEE ALATLNNTNR QHLQTFMDMF VSYLAKAETS EAGEFINSLL EEIDYENHLM QNEEGKAGEI KWRNVGDLVS WFARKGGEDG KNIIELAQTV ALMTLLEGKD EEETDAVSLS TLHAAKGLEY PYVFLVGCEE GVLPHNDSIE EGNVEEERRL MYVGITRAKR QLTLTHCVKR KKQGTWQFPE PSRFIDEMPQ EDLKILGRKG GEPIVSKEEG RRNLADIIGR LDNLKKSGAA D // ID Q4W573_NEIMB Unreviewed; 766 AA. AC Q4W573; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000256|SAAS:SAAS00088338}; DE EC=3.6.1.41 {ECO:0000256|SAAS:SAAS00088330}; GN OrderedLocusNames=NMB0661 {ECO:0000313|EMBL:AAY52137.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52137.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52137.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52137.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to CC yield ADP. {ECO:0000256|SAAS:SAAS00088333}. CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate + CC H(2)O = 2 ADP. {ECO:0000256|SAAS:SAAS00088336}. CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family. CC {ECO:0000256|SAAS:SAAS00571253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52137.1; -; Genomic_DNA. DR RefSeq; NP_273703.2; NC_003112.2. DR ProteinModelPortal; Q4W573; -. DR STRING; 122586.NMB0661; -. DR PaxDb; Q4W573; -. DR EnsemblBacteria; AAY52137; AAY52137; NMB0661. DR GeneID; 903194; -. DR KEGG; nme:NMB0661; -. DR PATRIC; 20356621; VBINeiMen85645_0829. DR eggNOG; ENOG4105D37; Bacteria. DR eggNOG; COG0168; LUCA. DR eggNOG; COG0639; LUCA. DR OMA; YWIINST; -. DR OrthoDB; EOG63589N; -. DR BioCyc; NMEN122586:GHGG-688-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-EC. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 2. DR InterPro; IPR004617; ApaH. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR003445; Cat_transpt. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF02386; TrkH; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00668; apaH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|SAAS:SAAS00460980}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 291 312 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 339 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 351 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 414 434 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 467 491 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 511 536 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 557 575 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 607 626 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 675 696 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 703 722 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 742 764 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 147 Metallophos. {ECO:0000259|Pfam:PF00149}. SQ SEQUENCE 766 AA; 85382 MW; 834BFC6BC50E50F4 CRC64; MAHYAIGDIQ GCFDELTALL GKIGFNHGTD TLWLTGDIVN RGPKSLETLQ FCIRHENSVQ IVLGNHDLHL LAVGCGEGAP KRSDTIEPIL KHPDGKKMLD WLRAQPLLIR EGSRVMVHAG ILPQWRITKA ESLAREAEAE LRGKKYVKFF SKMYGNKPAA WDEGLKGYAR LRFIVNAFTR MRALTFKNEL DFDYKSTVKK MPPYLRPWFK APDRQNLDAH HLRTLVLAGL HECRQRHLAG HRRAVGRTAD RRQPRNGRNY PSPSRRRHRL EKLRKITDRP TMHKILPIAH VLSRLGMLFS FILLIPAALS YAFSDGAYTA FATTATVTLS GSCIVRLATL RFRRELRPRD GFTLVLMLWL AFAAMAAMPM YLYFPNMGFT DAFFESMSGL TTTGATVIPH VDGLAPSVNF WRHMLNWLGG MGIIVLAVAI LPMLGVGGTQ LFKAEIPGID KESKMSPRIS QVAKKLWFGY TLITILAAAC LHFAGMGWFD AVCHAMATLS LGGFSTHDAS IAYYNSPLIE AVIIVFTIVG GINFANHFAA LNSRSLKTYW KDEECRTMLL LLSGSILAAA LYLWHTGYYA GFTESLRYTA FNFVSIGLAN GLANTDFAQW PLLISLWMFF LANILANSGS TGGGIKTIRA LVLFKFSLRE MMVLLHPKAV RTVKISGKAI PDRLALTVMS FIFIYFMTVV LFSFLLMASG MEFTTAFTAV IACITNAGPG LGEVGPAGNY AGLDVMQKWI CVTAMLLGRL EIFTVFILFT PAYWKK // ID Q9JY98_NEIMB Unreviewed; 141 AA. AC Q9JY98; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42029.1}; GN OrderedLocusNames=NMB1681 {ECO:0000313|EMBL:AAF42029.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42029.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42029.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42029.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3MW6} RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS). RX PubMed=21045552; DOI=10.4161/rna.7.6.13688; RA Chaulk S., Lu J., Tan K., Arthur D.C., Edwards R.A., Frost L.S., RA Joachimiak A., Glover J.N.; RT "N. meningitidis 1681 is a member of the FinO family of RNA RT chaperones."; RL RNA Biol. 7:812-819(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42029.1; -; Genomic_DNA. DR PIR; C81055; C81055. DR RefSeq; NP_274685.1; NC_003112.2. DR RefSeq; WP_002224984.1; NC_003112.2. DR PDB; 3MW6; X-ray; 2.21 A; A/B/C/D/E/F=1-141. DR PDBsum; 3MW6; -. DR ProteinModelPortal; Q9JY98; -. DR SMR; Q9JY98; 1-116. DR STRING; 122586.NMB1681; -. DR PaxDb; Q9JY98; -. DR DNASU; 903426; -. DR EnsemblBacteria; AAF42029; AAF42029; NMB1681. DR GeneID; 903426; -. DR KEGG; nme:NMB1681; -. DR PATRIC; 20359313; VBINeiMen85645_2163. DR eggNOG; ENOG4106FIT; Bacteria. DR eggNOG; ENOG410XXHH; LUCA. DR HOGENOM; HOG000219072; -. DR OMA; TASTKYL; -. DR OrthoDB; EOG6RJV9P; -. DR BioCyc; NMEN122586:GHGG-1736-MONOMER; -. DR EvolutionaryTrace; Q9JY98; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.1710.10; -; 1. DR InterPro; IPR016103; ProQ/FinO. DR Pfam; PF04352; ProQ; 1. DR SMART; SM00945; ProQ; 1. DR SUPFAM; SSF48657; SSF48657; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3MW6}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 141 AA; 15500 MW; ACAEF529775E6063 CRC64; MTQETALGAA LKSAVQTMSK KKQTEMIADH IYGKYDVFKR FKPLALGIDQ DLIAALPQYD AALIARVLAN HCRRPRYLKA LARGGKRFDL NNRFKGEVTP EEQAIAQNHP FVQQALQQQS AQAAAETLSV EAEAAESSAA E // ID Q9K1J6_NEIMB Unreviewed; 189 AA. AC Q9K1J6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40581.1}; GN OrderedLocusNames=NMB0122 {ECO:0000313|EMBL:AAF40581.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40581.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40581.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40581.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40581.1; -; Genomic_DNA. DR PIR; G81234; G81234. DR RefSeq; NP_273180.1; NC_003112.2. DR RefSeq; WP_002224769.1; NC_003112.2. DR ProteinModelPortal; Q9K1J6; -. DR STRING; 122586.NMB0122; -. DR PaxDb; Q9K1J6; -. DR EnsemblBacteria; AAF40581; AAF40581; NMB0122. DR GeneID; 902226; -. DR KEGG; nme:NMB0122; -. DR PATRIC; 20355257; VBINeiMen85645_0162. DR eggNOG; ENOG4106H78; Bacteria. DR eggNOG; COG0742; LUCA. DR HOGENOM; HOG000050676; -. DR OMA; KDYGMTR; -. DR OrthoDB; EOG64XXSX; -. DR BioCyc; NMEN122586:GHGG-128-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0031167; P:rRNA methylation; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004398; RNA_MeTrfase_RsmD. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF004553; CHP00095; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00095; TIGR00095; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 189 AA; 21072 MW; ACCDBD481E78C428 CRC64; MAAGKHTKHS NRVRIIGGQC RGRKLSFTSA DGLRPTPDSV REKLFNWLGQ DLTGKTVLDL FGGSGALGIE AASRNAKRVL ISDNNRQTVQ TLQKNSRELG LGQVQIVFSD GIAYLKTVSE QFDVVFLDPP FAWQDWQILF DALKPCLNPR AFVYLEAGTL PNIPDWLTEY REGKSGQSTF ELRVFQVAE // ID Q9JZ90_NEIMB Unreviewed; 124 AA. AC Q9JZ90; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41620.1}; GN OrderedLocusNames=NMB1239 {ECO:0000313|EMBL:AAF41620.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41620.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41620.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41620.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ArsC family. CC {ECO:0000256|SAAS:SAAS00565471}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41620.1; -; Genomic_DNA. DR PIR; D81105; D81105. DR RefSeq; NP_274263.1; NC_003112.2. DR RefSeq; WP_002225193.1; NC_003112.2. DR ProteinModelPortal; Q9JZ90; -. DR STRING; 122586.NMB1239; -. DR PaxDb; Q9JZ90; -. DR EnsemblBacteria; AAF41620; AAF41620; NMB1239. DR GeneID; 903661; -. DR KEGG; nme:NMB1239; -. DR PATRIC; 20358075; VBINeiMen85645_1550. DR eggNOG; ENOG4105KUZ; Bacteria. DR eggNOG; COG1393; LUCA. DR HOGENOM; HOG000059714; -. DR OMA; FGIKNCD; -. DR OrthoDB; EOG6NSGMX; -. DR BioCyc; NMEN122586:GHGG-1276-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR006660; Arsenate_reductase-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR006504; Tscrpt_reg_Spx/MgsR. DR Pfam; PF03960; ArsC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01617; arsC_related; 1. DR PROSITE; PS51353; ARSC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 124 AA; 13981 MW; 1660997108271B86 CRC64; MIVLHGIPNC DTVKKAKNRL AGYGLEFEFR DFKKQRPSEA EICSWLEQVP LATLLNKRGT SWRKLDAETQ QKVLSSTAEA VKLMSEMPSL IKRPVLECGG KVYAGFSEET YDGIFNRQAP CRQG // ID Q9JYF9_NEIMB Unreviewed; 372 AA. AC Q9JYF9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 71. DE SubName: Full=Putative transposase {ECO:0000313|EMBL:AAF62334.1}; GN OrderedLocusNames=NMB1602 {ECO:0000313|EMBL:AAF62334.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62334.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62334.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62334.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62334.1; -; Genomic_DNA. DR RefSeq; NP_274608.1; NC_003112.2. DR RefSeq; WP_002248744.1; NC_003112.2. DR PaxDb; Q9JYF9; -. DR EnsemblBacteria; AAF62334; AAF62334; NMB1602. DR GeneID; 904293; -. DR KEGG; nme:NMB1602; -. DR PATRIC; 20359084; VBINeiMen85645_2054. DR eggNOG; ENOG4105T1S; Bacteria. DR eggNOG; COG3547; LUCA. DR HOGENOM; HOG000130877; -. DR KO; K07486; -. DR OMA; VAPMAND; -. DR OrthoDB; EOG65F90T; -. DR BioCyc; NMEN122586:GHGG-1650-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR003346; Transposase_20. DR InterPro; IPR002525; Transposase_N. DR Pfam; PF01548; DEDD_Tnp_IS110; 1. DR Pfam; PF02371; Transposase_20; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 151 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. SQ SEQUENCE 372 AA; 41487 MW; A995E7CF7A5DA13B CRC64; MLIHYIDIAK RNFVIAVSSL SKTKTETNNP KGIAHTIEYL KKHKVALVVT ESTGGLEIPA AKAIHRAGIA VIIANPRQTH QFAQSQSLTK TDAKDAKMPA FFAQMKAQKE DWQTMPYHPP TEAEEVLEAL VNRRNQSADM RTAEKNRLHQ VHETQVGSVK QLIAHFDRLI DESDKQIDDH THTHFDGKAQ VAEQIKGIGS ITTATLMAML PELGRLSHKR IASLVGIAPH PRKSGEAKFK SRCFGGRSAV LKALYMATVA ATRFEPLIRD FHQRPLSEGK PYKVAVTACM RKLLETFAKF LSLTTTEIPT QVFGCFRPKY RLILPKHPLN PPRTPDNQAS GLPFRRQRAH LACWRLSTGS NTSPSDGFAH SL // ID Q9JZ95_NEIMB Unreviewed; 820 AA. AC Q9JZ95; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973, GN ECO:0000313|EMBL:AAF41612.1}; GN OrderedLocusNames=NMB1231 {ECO:0000313|EMBL:AAF41612.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41612.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41612.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41612.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: ATP-dependent serine protease that mediates the CC selective degradation of mutant and abnormal proteins as well as CC certain short-lived regulatory proteins. Required for cellular CC homeostasis and for survival from DNA damage and developmental CC changes induced by stress. Degrades polypeptides processively to CC yield small peptide fragments that are 5 to 10 amino acids long. CC Binds to DNA in a double-stranded, site-specific manner. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338846}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00004348}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00536021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004358}. CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00536024}. CC -!- SIMILARITY: Contains 1 Lon N-terminal domain. {ECO:0000256|HAMAP- CC Rule:MF_01973}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. {ECO:0000256|HAMAP- CC Rule:MF_01973}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41612.1; -; Genomic_DNA. DR PIR; H81106; H81106. DR RefSeq; NP_274255.1; NC_003112.2. DR RefSeq; WP_002225200.1; NC_003112.2. DR ProteinModelPortal; Q9JZ95; -. DR SMR; Q9JZ95; 611-792. DR STRING; 122586.NMB1231; -. DR MEROPS; S16.001; -. DR PaxDb; Q9JZ95; -. DR EnsemblBacteria; AAF41612; AAF41612; NMB1231. DR GeneID; 903653; -. DR KEGG; nme:NMB1231; -. DR PATRIC; 20358053; VBINeiMen85645_1539. DR eggNOG; ENOG4105C6P; Bacteria. DR eggNOG; COG0466; LUCA. DR HOGENOM; HOG000261410; -. DR KO; K01338; -. DR OMA; GIKKAGM; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; NMEN122586:GHGG-1268-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-HAMAP. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01973; lon_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027543; Lon_bac. DR InterPro; IPR004815; Lon_bac/euk-typ. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR003111; LON_substr-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR008268; Peptidase_S16_AS. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF02190; LON_substr_bdg; 1. DR PIRSF; PIRSF001174; Lon_proteas; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00763; lon; 1. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2, KW ECO:0000256|SAAS:SAAS00417290}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417288}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2, KW ECO:0000256|SAAS:SAAS00417290}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00417292}. FT DOMAIN 13 206 LON. {ECO:0000259|SMART:SM00464}. FT DOMAIN 351 503 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 359 366 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2}. FT ACT_SITE 696 696 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. FT ACT_SITE 739 739 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. SQ SEQUENCE 820 AA; 90723 MW; 5CF8AB913D83E18D CRC64; MTQKEKHFEE YAALATLPLR DVVVYPHMVL PLFVGRPKSI AALENAITRE EPVFLLAQTD AAVEEPIAAD LYQTGTVAQV LQVLKLPDGT VKVLVEGLYR GRVLTIEDTG GLFVSHIETV VEEDTGGNTD LEAVRRTLLA QFEQYAKLNK KIPAEIIGSI NGIAENSRLT DTVAAHLQLK LAQRQQILEI PEIGKRMEFL LAQLESELDI MQAEKRIRGR VKRQMEKSQR EYYLNEQIKA IHKELGEEDE NGELDALEAD IKKAGMTKEA EEKCLSELKK LKMMPPMSAE STVVRNYIDT LLELPWKKKS RVSKDIAKAG LVLDADHYGL EKVKERILEY LAVQKRMDKL KGPILCLVGP PGVGKTSLGE SIAKATGRKY VRMALGGVRD ESEIRGHRRT YIGSMPGKIL QNMAKAGVKN PLFLLDEIDK LGNDFRGDPA SALLEVLDPE QNNKFADHYA EVDYDLSDVM FIATSNSLNI PTPLLDRMEI IRLSGYTEDE KINIAMQYLV PKQMKRNGVK EGELAIEESA VRDIIRYYTR EAGVRSLDRE IAKICRKVVM QITLDEDKKR LSETKKTSKA KPKAVKVNEK NLHDYLGVRR FDYGVAESEN RIGQVTGLAW TEVGGELLTV EAAALPGKGV IQCTGQLGDV MKESVSAAWS VVRSRAESVG LAPDFYEKKD IHIHVPEGAT PKDGPSAGIA MTLAAVSAFT KIPVRADVAM TGEITLRGEV LPIGGLKEKL LAALRGGIKH VLIPKDNVKD LEEIPENVKT GLTIHPVKWI DEVLALGLES QPEPWAEPSG AEAAAESASK PKPRSRATKH // ID Q9K1H4_NEIMB Unreviewed; 463 AA. AC Q9K1H4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Putative sodium/alanine symporter {ECO:0000313|EMBL:AAF40634.1}; GN OrderedLocusNames=NMB0177 {ECO:0000313|EMBL:AAF40634.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40634.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40634.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40634.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU363064}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363064}. CC -!- SIMILARITY: Belongs to the sodium:alanine (SAF) symporter family. CC {ECO:0000256|RuleBase:RU363064}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40634.1; -; Genomic_DNA. DR PIR; B81228; B81228. DR RefSeq; NP_273235.1; NC_003112.2. DR RefSeq; WP_002216257.1; NC_003112.2. DR STRING; 122586.NMB0177; -. DR PaxDb; Q9K1H4; -. DR EnsemblBacteria; AAF40634; AAF40634; NMB0177. DR GeneID; 902284; -. DR KEGG; nme:NMB0177; -. DR PATRIC; 20355379; VBINeiMen85645_0219. DR eggNOG; ENOG4105BZG; Bacteria. DR eggNOG; COG1115; LUCA. DR HOGENOM; HOG000255106; -. DR KO; K03310; -. DR OMA; FWMWVTG; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NMEN122586:GHGG-187-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR30330; PTHR30330; 1. DR Pfam; PF01235; Na_Ala_symp; 1. DR PRINTS; PR00175; NAALASMPORT. DR TIGRFAMs; TIGR00835; agcS; 1. DR PROSITE; PS00873; NA_ALANINE_SYMP; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU363064}; KW Cell membrane {ECO:0000256|RuleBase:RU363064}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Symport {ECO:0000256|RuleBase:RU363064}; KW Transmembrane {ECO:0000256|RuleBase:RU363064}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363064}; KW Transport {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 20 51 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 71 98 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 156 174 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 194 212 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 219 240 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 252 271 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 313 334 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 360 383 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 404 422 Helical. {ECO:0000256|RuleBase:RU363064}. FT TRANSMEM 428 446 Helical. {ECO:0000256|RuleBase:RU363064}. SQ SEQUENCE 463 AA; 48588 MW; ADD5EDD5EE63C594 CRC64; MQVFLDNPKA FFETVSGWVW GPLMLMLLVG TGILLTVLLK GLQFTMLGYA LKQAFMPPKK HKSGEGHEGD ISHFAALMTA LSATIGTGNI AGVATAVVTG GPGAVFWMWM TAIFGMATKY GEGVLAVKYR VNNSKGEMSG GPMYYIEKGL GKNWKWMAVA FALFGTFASF GIGSSVQSNS VAQAVQTSFG IEPAYTGITL TVLTAVVVLG GIKGIAKAAS FIVPAMAVFY VLGGLSIIAI NSDALMPAVK LIFSDAFSAQ AVAGGAIGTV IRYGVARGVF SNEAGMGSAP IAAAAAKTDH PVRQALVSMT GTFLDTIVVC SITGIVLVMG LLGAGGEFVK PEVSGAALTT VTFQKMLPGI GGWIVTIGLI FFAYSTILGW CYYGEKCAVY VFGEKFAGLY RVGYVSSVML GTVLSLDLVW LASDTFNGLM ALPNLIALLL MAKVIVNETR DFKQKITNGE LPH // ID Q9JXP1_NEIMB Unreviewed; 616 AA. AC Q9JXP1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Putative soluble lytic murein transglycosylase {ECO:0000313|EMBL:AAF42278.1}; GN OrderedLocusNames=NMB1949 {ECO:0000313|EMBL:AAF42278.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42278.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42278.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42278.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42278.1; -; Genomic_DNA. DR PIR; F81023; F81023. DR RefSeq; NP_274943.1; NC_003112.2. DR RefSeq; WP_002225836.1; NC_003112.2. DR ProteinModelPortal; Q9JXP1; -. DR STRING; 122586.NMB1949; -. DR PaxDb; Q9JXP1; -. DR EnsemblBacteria; AAF42278; AAF42278; NMB1949. DR GeneID; 904201; -. DR KEGG; nme:NMB1949; -. DR PATRIC; 20359953; VBINeiMen85645_2481. DR eggNOG; ENOG4107SC1; Bacteria. DR eggNOG; COG0741; LUCA. DR HOGENOM; HOG000265691; -. DR KO; K08309; -. DR OMA; YFRIKPQ; -. DR OrthoDB; EOG6S52QZ; -. DR BioCyc; NMEN122586:GHGG-2006-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR Gene3D; 1.10.1240.20; -; 1. DR Gene3D; 1.25.20.10; -; 1. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR016026; Lytic_TGlyclase_suprhlx_U/L. DR InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L. DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF48435; SSF48435; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 616 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328303. FT DOMAIN 461 564 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 616 AA; 67738 MW; 9647045990C7767B CRC64; MYLPSMKHSL PLLAALVLAA CSSTNTLPAG KTPADNIETA DLSASVPTRP AEPERKTLAD YGGYPSALDA VKQKNDAAVA AYLENAGDSA MAENVRNEWL KSLGARRQWT LFAQEYAKLE PAGRAQEVEC YADSSRNDYT RAAELVKNTG KLPSGCTKLL EQAAASGLLD GNDAWRRVRG LLAGRQTTDA RNLAAALGSP FDGGTQGSRE YALLNVIGKE ARKSPNAAAL LSEMESGLSL EQRSFAWGVL GHYQSQNLNV PAALDYYGKV ADRRQLTDDQ IEWYARAALR ARRWDELASV ISHMPEKLQK SPTWLYWLAR SRAATGNTQE AEKLYKQAAA TGRNFYAVLA GEELGRKIDT RNNVPDAGKN SVRRMAEDGA VKRALVLFQN SQSAGDAKMR RQAQAEWRFA TRGFDEDKLL TAAQTAFDHG FYDMAVNSAE RTDRKLNYTL RYISPFKDTV IRHAQNVNVD PAWVYGLIRQ ESRFVIGAQS RVGAQGLMQV MPATAREIAG KIGMDAAQLY TADGNIRMGT WYMADTKRRL QNNEVLATAG YNAGPGRARR WQADTPLEGA VYAETIPFSE TRDYVKKVMA NAAYYAALFG APHIPLKQRM GIVPAR // ID Q9K0I9_NEIMB Unreviewed; 419 AA. AC Q9K0I9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 122. DE RecName: Full=Polyamine-transporting ATPase {ECO:0000256|SAAS:SAAS00083160}; DE EC=3.6.3.31 {ECO:0000256|SAAS:SAAS00083160}; GN Name=potA-1 {ECO:0000313|EMBL:AAF41037.1}; GN OrderedLocusNames=NMB0610 {ECO:0000313|EMBL:AAF41037.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41037.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41037.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41037.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the ABC transporter complex PotABCD involved in CC spermidine/putrescine import. Responsible for energy coupling to CC the transport system. {ECO:0000256|SAAS:SAAS00083152}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + polyamine(Out) = ADP + phosphate CC + polyamine(In). {ECO:0000256|SAAS:SAAS00083162}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PotA), two transmembrane proteins (PotB and PotC) and a solute- CC binding protein (PotD). {ECO:0000256|SAAS:SAAS00083151}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Spermidine/putrescine importer (TC 3.A.1.11.1) family. CC {ECO:0000256|SAAS:SAAS00569590}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41037.1; -; Genomic_DNA. DR PIR; C81179; C81179. DR RefSeq; NP_273654.1; NC_003112.2. DR RefSeq; WP_002225539.1; NC_003112.2. DR ProteinModelPortal; Q9K0I9; -. DR STRING; 122586.NMB0610; -. DR PaxDb; Q9K0I9; -. DR EnsemblBacteria; AAF41037; AAF41037; NMB0610. DR GeneID; 902724; -. DR KEGG; nme:NMB0610; -. DR PATRIC; 20356509; VBINeiMen85645_0774. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR KO; K11076; -. DR OMA; YVGHGIS; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-636-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015417; F:polyamine-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005893; Sp_pt_ABC_ATP-bd. DR InterPro; IPR013611; Transp-assoc_OB_typ2. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08402; TOBE_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01187; potA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAF41037.1}; KW Cell membrane {ECO:0000256|SAAS:SAAS00458580}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|SAAS:SAAS00458628}; KW Membrane {ECO:0000256|SAAS:SAAS00458580}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAF41037.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|SAAS:SAAS00452289}. FT DOMAIN 58 288 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 419 AA; 47424 MW; CBD9CEE7B640F1BA CRC64; MLPVRFTRVS DGIKRLTPAS NQTAFYHPFE NPFCRYSSFY WSIAIMTATT ASSAKPYLKI QGLVKKFGDN YAVDNIDLDI YQHEIFALLG SSGSGKSTLL RMLAGMESPN QGKIILDGQD ITKLAPYDRP INMMFQSYAL FPHMTVEQNI AFGLKQDKMP KGEIAARVEE MLRLVQMTKF AKRKPHQLSG GQQQRIALAR SLAKRPKILL LDEPLGALDK KLRQQTQLEL VNTLEQVGVT CIMVTHDQEE AMTMATRIAI MSDGQLQQVG TPSDVYDYPN SRFTAEFIGE TNIFDGVVIE DHADYAVIEC EGLENHVRID HGLGGPSEQD LWVSIRPEDI DLYKEKPEYL GDYNWAKGTV KEIAYLGSFA IYHIKLGNGR VVKSQVPAPY WYVRNITPPT WDETVYISWP ENQPTPLFR // ID Q9K0P1_NEIMB Unreviewed; 1161 AA. AC Q9K0P1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN OrderedLocusNames=NMB0545 {ECO:0000313|EMBL:AAF40974.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40974.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40974.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40974.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for chromosome condensation and partitioning. CC {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- DOMAIN: Contains large globular domains required for ATP CC hydrolysis at each terminus and a third globular domain forming a CC flexible hinge near the middle of the molecule. These domains are CC separated by coiled-coil structures. {ECO:0000256|HAMAP- CC Rule:MF_01894}. CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP- CC Rule:MF_01894}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40974.1; -; Genomic_DNA. DR PIR; G81186; G81186. DR RefSeq; NP_273590.1; NC_003112.2. DR RefSeq; WP_002225580.1; NC_003112.2. DR ProteinModelPortal; Q9K0P1; -. DR STRING; 122586.NMB0545; -. DR PaxDb; Q9K0P1; -. DR EnsemblBacteria; AAF40974; AAF40974; NMB0545. DR GeneID; 902660; -. DR KEGG; nme:NMB0545; -. DR PATRIC; 20356349; VBINeiMen85645_0693. DR eggNOG; ENOG4105CDB; Bacteria. DR eggNOG; COG1196; LUCA. DR HOGENOM; HOG000036391; -. DR KO; K03529; -. DR OMA; AFQTASN; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NMEN122586:GHGG-571-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01894; Smc_prok; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR010935; SMC_hinge. DR InterPro; IPR011890; SMC_prok. DR Pfam; PF02463; SMC_N; 2. DR PIRSF; PIRSF005719; SMC; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. DR TIGRFAMs; TIGR02168; SMC_prok_B; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_01894}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 589 SMC_N. {ECO:0000259|Pfam:PF02463}. FT DOMAIN 771 1144 SMC_N. {ECO:0000259|Pfam:PF02463}. FT NP_BIND 32 39 ATP. {ECO:0000256|HAMAP-Rule:MF_01894}. FT COILED 170 485 {ECO:0000256|HAMAP-Rule:MF_01894}. FT COILED 671 879 {ECO:0000256|HAMAP-Rule:MF_01894}. SQ SEQUENCE 1161 AA; 130410 MW; 21764D8C55C6066B CRC64; MRLTHIKLSG FKSFTDPTTI HVPGQLVAVI GPNGCGKSNV IDAVRWVLGE ASAKQLRGES MQDVIFNGAA TRRPAPRASV ELVFDNSDHS LQGAWGQYAE VSIKRQLTRQ GESTYFINNQ TVRRRDITDL FLGTGVGARG YAVIEQGMIS RIIEARPEEL RAYIEEAAGV SKYKERRKET EGRLKDTREH LQRLGDLQNE LARQVEKLEK QAETAERYKS LTAQLNQQQD LLDYAQWRQS LAAADKATAQ HQSLQAQQDE TAAQVQALND EVHALQTAEQ SQQQAVHELS NKRGVLREQI ARLEEQIRHQ QNLHQRIERD KQAAQAQLQR IHQEQQQIRV QLEENELQVE EKQTELAEWA MQVAEHEERL PELEEAQATL NAAFQTQQDE ANRIRRELAL KQQQLAHAEQ TIAKHEERKG RLKQENQALN LPDEAETAAA QEAAALLQSQ QEHYEEQIIA AEEALHAARE AFQTASNRFQ SLKQQHITLQ AQQQALSQIL SQQQEAADFW QATDHAAAPQ LWQHITAPAE WQHALSVILA ERLHARAVPQ GFVPPEPLPQ GQAAWLSDDL SGGIKKSLPV QALLNQIQAQ PPFQTALHYW LDGVLCAPDL SYALAHQNDL GAHQIWLTPE GHQVDKVSVL LYAKPAQESL IAQKARLDGI ASELENLAPE LSAAEAAFKQ AEAAVRSSEV QHKNLMQQQQ QHTRQYSQAQ QRAAELLART NQGQIRREHI ERELAQLAEE QTVLQHTSDG LSDDIVTLQE AAAELEHQQQ TTAHSRQEQQ GRLKQAQLAL LEANRQYGLA EVAVHKLNQQ KQNYRQQIAQ LEQQTLDWQE RQQELALAYE TEFQNDEQHI KLEELSEAVQ TLDEEYIVVQ EKLAQIQEQG REQYAKVQTL QTKLPQLQAA TQTALLQQQE ALINAKRYHQ NLTERAADLD ALEALAKESP KVLNSSIGSL SQQIEALGAV NLAALQELEE ARERDGYYRS QSEDVQAAIT LLEEAIAQID DKTKARFKET FDAVNSKVQT FFPTLFGGGE ATLKMIGDDL LTAGVSIMAR PPGKKNSTIH LLSGGEKALT AMSLVFALFS LNPAPFCLLD EVDAPLDDAN TSRFCRLVKE MSAQTQFLYI SHNRLTMEMA EQLVGVTMQE KGVSRVVAVD IKQALEMAEA V // ID Q9K079_NEIMB Unreviewed; 505 AA. AC Q9K079; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41152.1}; GN OrderedLocusNames=NMB0739 {ECO:0000313|EMBL:AAF41152.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41152.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41152.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41152.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41152.1; -; Genomic_DNA. DR PIR; C81165; C81165. DR RefSeq; NP_273781.1; NC_003112.2. DR RefSeq; WP_010980832.1; NC_003112.2. DR ProteinModelPortal; Q9K079; -. DR STRING; 122586.NMB0739; -. DR PaxDb; Q9K079; -. DR EnsemblBacteria; AAF41152; AAF41152; NMB0739. DR GeneID; 902852; -. DR KEGG; nme:NMB0739; -. DR PATRIC; 20356839; VBINeiMen85645_0940. DR eggNOG; ENOG4105C9W; Bacteria. DR eggNOG; COG1161; LUCA. DR eggNOG; COG1386; LUCA. DR KO; K14540; -. DR OrthoDB; EOG6G4VXH; -. DR BioCyc; NMEN122586:GHGG-768-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0051304; P:chromosome separation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR Gene3D; 1.10.1580.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR023179; GTP-bd_ortho_bundle. DR InterPro; IPR019991; GTP-bd_ribosome_bgen. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005234; ScpB_csome_segregation. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF04079; SMC_ScpB; 1. DR SUPFAM; SSF46785; SSF46785; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03596; GTPase_YlqF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 116 206 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 505 AA; 57253 MW; DB99A4D00B524338 CRC64; MAIQWFPGHM NKAKKAIAER AKSVDMVIEM LDARMPASSE NPLLAQLSKG KPKLKILNKQ DLADPERTKI WLEHYNSRPD TCAIALDSSE TGAHGKITQA CRAMIPHRQG IDKPLRVLIC GIPNVGKSTL INGMIGKKSA KTGNEPGITK AEQRLFLADD FWLYDTPGML WPKIIVEEGG YNLAAGGAVG RNALDEEEVA LELLDYLRRH YLPMLQERYQ ADKDPSSHWD ENVWLEWIAK KRGAVLSGGR INYQKAAENI LTDFREGKIG RITLETPNQW ETWLKKARQK EAELKAIREA RKAERKGQKL RKHKECRLKN IFQAASLYSN RFQTAYPNPC RFSTDTRMTD KISPDALIEA ALLTQTEPLT EKSMRELCVP PLSQDKLIDV LAQLKTRWQD RALQLVHTQE GWRFQIVQTA FERLGSLQEQ RAPRYSRAVM ETLAIIAYQQ PVTRGDIEGI RGVAVSQNVM QTCRIGGGLK SSDIGTHWEN PHCGRQRQRS SAIWV // ID Q9JZY0_NEIMB Unreviewed; 209 AA. AC Q9JZY0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41264.1}; GN OrderedLocusNames=NMB0853 {ECO:0000313|EMBL:AAF41264.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41264.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41264.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41264.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41264.1; -; Genomic_DNA. DR PIR; H81149; H81149. DR RefSeq; NP_273894.1; NC_003112.2. DR RefSeq; WP_002225392.1; NC_003112.2. DR STRING; 122586.NMB0853; -. DR PaxDb; Q9JZY0; -. DR EnsemblBacteria; AAF41264; AAF41264; NMB0853. DR GeneID; 902967; -. DR KEGG; nme:NMB0853; -. DR PATRIC; 20357097; VBINeiMen85645_1067. DR eggNOG; COG2976; LUCA. DR HOGENOM; HOG000261006; -. DR OMA; KASDEGY; -. DR OrthoDB; EOG6MSS1R; -. DR BioCyc; NMEN122586:GHGG-884-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR018704; TPR_21. DR InterPro; IPR019734; TPR_repeat. DR InterPro; IPR026039; UPF0070. DR Pfam; PF09976; TPR_21; 1. DR PIRSF; PIRSF006170; YfgM; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 42 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 161 194 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 209 AA; 23135 MW; 159C7DE9DD133F31 CRC64; MAAHLEEQQE LDNFKYFWKT TGKWLFALLI LAALGYLGYT VYQNRKVSQN QEAAAVLANI VEKAQSKAPQ SEINAELTKL QQSYPHSISA AQATLMAAAT EFDAQRYDVA EGHLKWVLSN QKDSLIQALA AQRLGVVLLQ QKKYDAALAA LDTPVEADFA PLLMETKGDV YAAQGKSQEA LKNYGQALEK MPQDSVGREL VQMKLDSLK // ID Q9JXK3_NEIMB Unreviewed; 1431 AA. AC Q9JXK3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Serine-type peptidase {ECO:0000313|EMBL:AAF42325.1}; GN OrderedLocusNames=NMB1998 {ECO:0000313|EMBL:AAF42325.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42325.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42325.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42325.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42325.1; -; Genomic_DNA. DR PIR; A81018; A81018. DR RefSeq; NP_274990.1; NC_003112.2. DR RefSeq; WP_002225871.1; NC_003112.2. DR ProteinModelPortal; Q9JXK3; -. DR STRING; 122586.NMB1998; -. DR PaxDb; Q9JXK3; -. DR EnsemblBacteria; AAF42325; AAF42325; NMB1998. DR GeneID; 904129; -. DR KEGG; nme:NMB1998; -. DR PATRIC; 20360095; VBINeiMen85645_2552. DR eggNOG; ENOG4108BMY; Bacteria. DR eggNOG; COG3468; LUCA. DR HOGENOM; HOG000152751; -. DR KO; K01347; -. DR OMA; YAHIGIQ; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NMEN122586:GHGG-2055-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.160.20.20; -; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR000710; Peptidase_S6. DR InterPro; IPR030396; Peptidase_S6_dom. DR InterPro; IPR004899; Pertactin_central. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF02395; Peptidase_S6; 2. DR Pfam; PF03212; Pertactin; 1. DR PRINTS; PR00921; IGASERPTASE. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF51126; SSF51126; 2. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS51691; PEPTIDASE_S6; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 1431 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328297. FT DOMAIN 27 284 Peptidase S6. FT {ECO:0000259|PROSITE:PS51691}. FT DOMAIN 1178 1431 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. FT COILED 971 998 {ECO:0000256|SAM:Coils}. FT COILED 1078 1105 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1431 AA; 157646 MW; 6801F0E209C24EFC CRC64; MRFTHTTPFC SVLSTLGLFA VSPAYSSIVR NDVDYQYFRD FAENKGAFTV GASNISIQDK QGKILGRVLN GIPMPDFRVS NRQTAIATLV HPQYVNSVKH NVGYGSIQFG NDTQNPEEQA YTYRLVSRNP HPDYDYHLPR LNKLVTEISP TALSSVPLLG NGQPKANAYL DTDRFPYFVR LGSGTQQVRK ADGTRTRTAP AYQYLTGGTP LKVLGFQNHG LLVGGSLTDQ PLNTYAIAGD SGSPLFAFDK HENRWVLAGV LSTYAGFDNF FNKYIVTQPE FIRSTIRQYE TRLDVGLTTN ELIWRDNGNG NSTLQGLNER ITLPIANPSL APQNDSRHMP SEDAGKTLIL SSRFDNKTLM LADNINQGAG ALQFDSNFTV VGKNHTWQGA GVIVADGKRV FWQVSNPKGD RLSKLGAGTL IANGQGINQG DISIGEGTVV LAQKAASDGS KQAFNQVGIT SGRGTAVLAD SQQIKPENLY FGFRGGRLDL NGNNLAFTHI RHADGGAQIV NHNPDQAATL TLTGNPVLSP EHVEWVQWGN RPQGNAAVYE YINPHRNRRT DYFILKPGGN PREFFPLNMK NSTSWQFIGN NRQQAAEQVA QAENARPDLI TFGGYLGENA QTGKAAPSYS KTNEAAIEKT RHIANAAVYG RPEYRYNGAL NLHYRPKRTD STLLLNGGMN LNGEVLIEGG NMIVSGRPVP HAYDHQAKRE PVLENEWTDG SFKAARFTLR NHARLTAGRN TAHLDGDITA YDLSGIDLGF TQGKTPECYR SYHSGSTHCT PNAVLKAENY RALPATQVRG DITLNDRSEL RLGKAHLYGS IRAGKDTAVR MEADSNWTLS QSSHTGALTL DGAQITLNPD FANNTHNNRF NTLTVNGTLD GFGTFRFLTG IVRKQNAPPL KLEGDSRGAF QIHVKNTGQE PQTTESLALV SLNPKHSHQA RFTLQNGYAD LGAYRYILRK NNNGYSLYNP LKEAELQIEA TRAEHERNQQ AYNQLQATDI SRQVQHDSDA TRQALQAWQN SQTELARIDS QVQYLSAQLK QTDPLTGILT RAQNLCAAQG YSADICRQVA KAADTNDLTL FETELDTYIE RVEMAESELD KARQGGDAQA VETARHAYLN ALNRLSRQIH SLKTGVAGIR MPNLAELISR SANTAVSEQA AYNTGRQQAG RRIDRHLTDP QQQNIWLETG TQQTDYHSGT HRPYQQTTNY AHIGIQTGIT DRLSVGTILT DERTNNRFDE GVSARNRSNG AHLFVKGENG ALFAAADLGY SNSRTRFTDY DGAAVRRHAW DAGINTGIKI DTGINLRPYA GIRINRSNGN RYVLDGAEIN SPAQIQTTWH AGIRLDKTVE LGQAKLTPAF SSDYYHTRQN SGSALSVNDR TLLQQAAHGT LHTLQIDAGY KGWNAKLHAA YGKDSNTARH KQAGIKIGYN W // ID Q9JYB2_NEIMB Unreviewed; 451 AA. AC Q9JYB2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=Putative protease {ECO:0000313|EMBL:AAF42013.1}; GN OrderedLocusNames=NMB1664 {ECO:0000313|EMBL:AAF42013.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42013.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42013.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42013.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42013.1; -; Genomic_DNA. DR PIR; B81056; B81056. DR RefSeq; NP_274669.1; NC_003112.2. DR RefSeq; WP_002222142.1; NC_003112.2. DR STRING; 122586.NMB1664; -. DR PaxDb; Q9JYB2; -. DR EnsemblBacteria; AAF42013; AAF42013; NMB1664. DR GeneID; 903446; -. DR KEGG; nme:NMB1664; -. DR PATRIC; 20359268; VBINeiMen85645_2142. DR eggNOG; ENOG4105CFP; Bacteria. DR eggNOG; COG0826; LUCA. DR HOGENOM; HOG000275241; -. DR KO; K08303; -. DR OMA; DFQVNGE; -. DR OrthoDB; EOG6GJBTC; -. DR BioCyc; NMEN122586:GHGG-1718-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001539; Peptidase_U32. DR InterPro; IPR032525; Peptidase_U32_C. DR Pfam; PF01136; Peptidase_U32; 1. DR Pfam; PF16325; Peptidase_U32_C; 1. DR PROSITE; PS01276; PEPTIDASE_U32; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42013.1}; KW Protease {ECO:0000313|EMBL:AAF42013.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 369 445 Peptidase_U32_C. FT {ECO:0000259|Pfam:PF16325}. SQ SEQUENCE 451 AA; 50833 MW; 1395CD6A4691C301 CRC64; MKAPELLLPA GGLERMRAAY DYGADAVYAG SPRYSLRARN NEFAKLDVLE QGIKEAHERN KKFFLTVNTL PHNSKLKTFV ADMEPLIAMK PDALIMADPG LIMTVREKWP EMPIHLSVQA NTTNYWGVKF WQNIGVERII LSRELSMEEI AEIRQECPDI ELEVFIHGAL CIAYSGRCLL SGYFNHRDPN QGTCTNSCRW DYKVHNATES DAGDAQLLQG FNFEKAQEEA NQNFEGINGQ KRHPYADKVF LIEESNRPGE MMPIMEDEHG TYIMNSKDLR GIEVVEKLAK IGVDSLKVEG RTKSLYYVAR VAQSYRKAID DAVAGRPFDY SLLSELEGLA NRGYTSGFLE RHQTQDYQNY LTGHSTAKQS QYVGHVTEID ENGWATVEVK NRFAVSDSLE IIHPSGNQTI KLEQMTRKGQ PVDVAPGNGI QVKIPNMQGK EKALIARVLN P // ID Q9JZV6_NEIMB Unreviewed; 195 AA. AC Q9JZV6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414}; GN Name=sodB {ECO:0000313|EMBL:AAF41295.1}; GN OrderedLocusNames=NMB0884 {ECO:0000313|EMBL:AAF41295.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41295.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41295.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41295.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000256|RuleBase:RU000414}. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC {ECO:0000256|RuleBase:RU000414}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. {ECO:0000256|RuleBase:RU000414}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41295.1; -; Genomic_DNA. DR PIR; G81147; G81147. DR RefSeq; NP_273925.1; NC_003112.2. DR RefSeq; WP_002220670.1; NC_003112.2. DR ProteinModelPortal; Q9JZV6; -. DR SMR; Q9JZV6; 4-191. DR STRING; 122586.NMB0884; -. DR PaxDb; Q9JZV6; -. DR EnsemblBacteria; AAF41295; AAF41295; NMB0884. DR GeneID; 903003; -. DR KEGG; nme:NMB0884; -. DR PATRIC; 20357175; VBINeiMen85645_1101. DR eggNOG; ENOG4105CK4; Bacteria. DR eggNOG; COG0605; LUCA. DR HOGENOM; HOG000013584; -. DR KO; K04564; -. DR OMA; EPIMAHT; -. DR OrthoDB; EOG63NMNT; -. DR BioCyc; NMEN122586:GHGG-920-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR PANTHER; PTHR11404; PTHR11404; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF46609; SSF46609; 1. DR SUPFAM; SSF54719; SSF54719; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|RuleBase:RU000414}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000414, KW ECO:0000313|EMBL:AAF41295.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 79 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}. FT DOMAIN 89 190 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}. SQ SEQUENCE 195 AA; 21893 MW; FAA8BA67BFF8D0A9 CRC64; MEHKLPQLPY ELDALSPHLS KETLEFHYGK HHQTYITNLN NQIKGTEFEN LPLEEIVKKS SGGVFNNAAQ TWNHTFYWLG FTSKGQGKPA GELAAAIDAK WGSFEKFQEA FNACAAGTFG SGWAWLVKTP AGGLDLVSTS NAATPLTTEN TPLLTCDVWE HAYYIDYRNS RPNYLKGFWE IVNWDEVAKR FAALS // ID Q7DDQ8_NEIMB Unreviewed; 524 AA. AC Q7DDQ8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 63. DE RecName: Full=Phosphate transporter {ECO:0000256|RuleBase:RU363058}; GN OrderedLocusNames=NMB0378 {ECO:0000313|EMBL:AAF40818.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40818.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40818.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40818.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU363058}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363058}. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) CC (TC 2.A.20) family. {ECO:0000256|RuleBase:RU363058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40818.1; -; Genomic_DNA. DR PIR; F81207; F81207. DR RefSeq; NP_273427.1; NC_003112.2. DR RefSeq; WP_002212449.1; NC_003112.2. DR STRING; 122586.NMB0378; -. DR PaxDb; Q7DDQ8; -. DR EnsemblBacteria; AAF40818; AAF40818; NMB0378. DR GeneID; 902493; -. DR KEGG; nme:NMB0378; -. DR PATRIC; 20355917; VBINeiMen85645_0476. DR eggNOG; ENOG4105CJ3; Bacteria. DR eggNOG; COG0306; LUCA. DR HOGENOM; HOG000231892; -. DR KO; K03306; -. DR OMA; WINLATW; -. DR OrthoDB; EOG6NWBS7; -. DR BioCyc; NMEN122586:GHGG-400-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006817; P:phosphate ion transport; IEA:InterPro. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PTHR11101; 2. DR Pfam; PF01384; PHO4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363058}; KW Phosphate transport {ECO:0000256|RuleBase:RU363058}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363058}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363058}; KW Transport {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 12 32 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 38 59 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 71 98 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 118 139 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 151 170 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 182 202 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 294 315 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 327 349 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 409 429 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 465 486 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 498 520 Helical. {ECO:0000256|RuleBase:RU363058}. SQ SEQUENCE 524 AA; 56343 MW; 5DF6906034C4F799 CRC64; MAQIQMSANV KTINAVFAAM LVGTVGYFIY WGLGYTHYNY AALFIIATMF GVFMAFNIGG NDVANSFGTS VGAGTLTIPQ ALLIAAVFEV SGAVIAGGEV TNTIRKGIVD LKGVDFEPIQ FVFIMMSALL AAALWLLFAS KKGLPVSTTH SIIGGIVGSA VCMAVMNDAA SGDLIRWGKL GGIGVSWVLS PVLGGAVSYF LFSRVKKNVL DYNAWAEGTL KGIKQEKKAY KERHRLFFEG LSEAEKVEYA TKMAHDAQIY DEPEFDPQEL QSEYYRGLYA FDNRKNNVDS YKALHSWIPF IASFGAMMIS AMLIFKGLKN LHLGMSNVNS FLTIFMIGAA VWMGTFVFAK SLKRKDLGKS TFQMFSWMQV FTACGFAFSH GANDIANAIG PFAAIMDVLR TNSVAAQNVV PPIAMLTFGI ALIVGLWFVG KEVIKTVGTS LAEMHPASGF TAELSAASVV MGASLMGLPV SSTHILVGAV LGIGLVNRNA NWKLMKPIGL AWVITLPAAA VLSVVCYLVL QAVF // ID Q9K1A9_NEIMB Unreviewed; 498 AA. AC Q9K1A9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 97. DE SubName: Full=NADH dehydrogenase I, M subunit {ECO:0000313|EMBL:AAF40712.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AAF40712.1}; GN Name=nuoM {ECO:0000313|EMBL:AAF40712.1}; GN OrderedLocusNames=NMB0258 {ECO:0000313|EMBL:AAF40712.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40712.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40712.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40712.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40712.1; -; Genomic_DNA. DR PIR; E81220; E81220. DR RefSeq; NP_273314.1; NC_003112.2. DR RefSeq; WP_002224834.1; NC_003112.2. DR STRING; 122586.NMB0258; -. DR PaxDb; Q9K1A9; -. DR EnsemblBacteria; AAF40712; AAF40712; NMB0258. DR GeneID; 902369; -. DR KEGG; nme:NMB0258; -. DR PATRIC; 20355594; VBINeiMen85645_0321. DR eggNOG; ENOG4105C8S; Bacteria. DR eggNOG; COG1008; LUCA. DR HOGENOM; HOG000100683; -. DR KO; K00342; -. DR OMA; TWPILSV; -. DR OrthoDB; EOG647TZ6; -. DR BioCyc; NMEN122586:GHGG-273-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro. DR InterPro; IPR000260; NADH4_N. DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4. DR InterPro; IPR003918; NADH_UbQ_OxRdtase. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF01059; Oxidored_q5_N; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01437; NUOXDRDTASE4. DR TIGRFAMs; TIGR01972; NDH_I_M; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAF40712.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 208 226 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 323 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 335 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 399 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 411 434 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 455 474 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 68 125 Oxidored_q5_N. FT {ECO:0000259|Pfam:PF01059}. FT DOMAIN 132 421 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 498 AA; 54605 MW; A08E24EC41ABA04F CRC64; MFSNYLLSLA IWIPIAAGVL VLATGSDSRA PFARVLAFMG ALAGFLVTLP LFTGFDRLSG GYQFTEFHEW IPLLKINYAL GVDGISVLFI ILNAFITLLV VLAGWEVIQK RPAQYMAAFL IMSGLINGAF AAQDAILFYV FFEGMLIPLY LIIGVWGGPR RVYASVKLFL YTLMGSLLML VAMVYLYYQT GSFSIVDFQN IEQIPLGVQQ LLFVAFFLSF AVKVPMFPVH TWLPDAHVEA PTGGSMVLAA ITLKLGAYGF LRFILPIMPD AARYFAPVII VLSLIAVIYI GMVALVQTDM KKLVAYSSIS HMGFVTLGMF LFVDGQLDDW ALKGAIIQMI SHGFVSAAMF MCIGVMYDRL HTRNIADYGG VVNVMPKFAA FMMLFGMANA GLPATSGFVG EFMVIMGAVK VNFWVGALAA MTLIYGASYT LWMYKRVIFG AIHNPHVAEM QDINCREFAI LAILAVAVLG MGLYPNAFIE VVHQAANDLI AHVAQSKI // ID Q9JZ32_NEIMB Unreviewed; 257 AA. AC Q9JZ32; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41694.1}; GN OrderedLocusNames=NMB1319 {ECO:0000313|EMBL:AAF41694.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41694.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41694.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41694.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363041}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363041}. CC -!- SIMILARITY: Belongs to the UPF0721 family. CC {ECO:0000256|RuleBase:RU363041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41694.1; -; Genomic_DNA. DR PIR; F81096; F81096. DR STRING; 122586.NMB1319; -. DR PaxDb; Q9JZ32; -. DR EnsemblBacteria; AAF41694; AAF41694; NMB1319. DR PATRIC; 20358285; VBINeiMen85645_1654. DR eggNOG; ENOG4105HF0; Bacteria. DR eggNOG; COG0730; LUCA. DR HOGENOM; HOG000068439; -. DR OMA; FKTLHTG; -. DR OrthoDB; EOG6RZB3C; -. DR BioCyc; NMEN122586:GHGG-1357-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU363041}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363041}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363041}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 7 40 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 52 73 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 85 103 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 109 127 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 187 209 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 215 237 Helical. {ECO:0000256|RuleBase:RU363041}. SQ SEQUENCE 257 AA; 26750 MW; 4BA46DB2C389A0A3 CRC64; MWHWDIILIL LAVGSAAGFI AGLFGVGGGT LIVPVVLWVL DLQGLAQHPY AQHLAVGTSF AVMVFTAFSS MLGQHKKQAV DWKTVFTMMP GMIFGVFTGA LSAKYIPAFG LQIFFILFLT AVAFKTLHTD PQTASRPLPG LPGLTAVSTL FGTMSSWVGI GGGSLSVPFL IHCGFPAHKA IGTSSGLAWP IALSGAISYL LNGLNIAGLP EGSLGFLYLP AVAVLSAATI AFAPLGVKTA HKLSSAKLKK SSALCCF // ID Q9JXW3_NEIMB Unreviewed; 453 AA. AC Q9JXW3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 97. DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase {ECO:0000313|EMBL:AAF42195.1}; DE EC=6.3.4.14 {ECO:0000313|EMBL:AAF42195.1}; GN Name=accC {ECO:0000313|EMBL:AAF42195.1}; GN OrderedLocusNames=NMB1861 {ECO:0000313|EMBL:AAF42195.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42195.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42195.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42195.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42195.1; -; Genomic_DNA. DR PIR; F81033; F81033. DR RefSeq; NP_274857.1; NC_003112.2. DR RefSeq; WP_002223021.1; NC_003112.2. DR ProteinModelPortal; Q9JXW3; -. DR SMR; Q9JXW3; 1-444. DR STRING; 122586.NMB1861; -. DR PaxDb; Q9JXW3; -. DR PRIDE; Q9JXW3; -. DR EnsemblBacteria; AAF42195; AAF42195; NMB1861. DR GeneID; 904327; -. DR KEGG; nme:NMB1861; -. DR PATRIC; 20359747; VBINeiMen85645_2379. DR eggNOG; ENOG4105CER; Bacteria. DR eggNOG; COG0439; LUCA. DR HOGENOM; HOG000008988; -. DR KO; K01961; -. DR OMA; EDPYKFI; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; NMEN122586:GHGG-1917-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005481; BC-like_N. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; Biotin_carb_N; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00514; accC; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS50979; BC; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF42195.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 445 Biotin carboxylation. FT {ECO:0000259|PROSITE:PS50979}. FT DOMAIN 120 317 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. SQ SEQUENCE 453 AA; 49599 MW; CDF79D537CB21C0F CRC64; MLKKVLIANR GEIALRVLRA CREMGIATVA VHSEADKDSL HVKLADESVC IGPAASAQSY LNVPAIIAAA EVSCADAVHP GYGFLAENAD FAEQVEQSGF TFIGPKPDTI RLMGDKVSAK HAMIAAGVPC VPGSDGALPD DGEEILKIAD KVGYPVIIKA SGGGGGRGMR VVEKKEDLLQ SVEMTKAEAG AAFGNPMVYM ERYLQRPRHV EIQVIADEHG NAIYLAERDC SLQRRHQKVI EEAPAPFITE KERAKIGNAC ADACKRIGYR GAGTFEFLYE DGEFFFIEMN TRVQVEHPVT ELITGVDIVQ EQLRIAAGLP LQYKQKDIQV EGHAFECRIN AEDPYNFIPS PGLIESCHLP GGFGIRVDSH IYQGYRIPPY YDSLIGKICV HGKTREQAMA KMRVALAELA VTGIKTNTPL HRDLFADAGF QKGGVSIHYL EHWLEDRKAK QDK // ID Q9K084_NEIMB Unreviewed; 158 AA. AC Q9K084; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41147.1}; GN OrderedLocusNames=NMB0734 {ECO:0000313|EMBL:AAF41147.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41147.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41147.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41147.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Removes the pyruvyl group from chorismate, with CC concomitant aromatization of the ring, to provide 4- CC hydroxybenzoate (4HB) for the ubiquinone pathway. CC {ECO:0000256|SAAS:SAAS00005100}. CC -!- CATALYTIC ACTIVITY: Chorismate = 4-hydroxybenzoate + pyruvate. CC {ECO:0000256|SAAS:SAAS00005101}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000256|SAAS:SAAS00005092}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00005108}. CC -!- SIMILARITY: Belongs to the UbiC family. CC {ECO:0000256|SAAS:SAAS00535671}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41147.1; -; Genomic_DNA. DR PIR; F81164; F81164. DR RefSeq; NP_273776.1; NC_003112.2. DR RefSeq; WP_002225453.1; NC_003112.2. DR ProteinModelPortal; Q9K084; -. DR STRING; 122586.NMB0734; -. DR PaxDb; Q9K084; -. DR EnsemblBacteria; AAF41147; AAF41147; NMB0734. DR GeneID; 902847; -. DR KEGG; nme:NMB0734; -. DR PATRIC; 20356827; VBINeiMen85645_0934. DR eggNOG; COG3161; LUCA. DR HOGENOM; HOG000137785; -. DR KO; K03181; -. DR OMA; MEHLFEE; -. DR OrthoDB; EOG6Z0QB1; -. DR BioCyc; NMEN122586:GHGG-763-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008813; F:chorismate lyase activity; IEA:InterPro. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1410.10; -; 1. DR InterPro; IPR007440; Chorismate--pyruvate_lyase. DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom. DR Pfam; PF04345; Chor_lyase; 1. DR SUPFAM; SSF64288; SSF64288; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00417425}; KW Lyase {ECO:0000256|SAAS:SAAS00417426}; KW Pyruvate {ECO:0000256|SAAS:SAAS00417424}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Ubiquinone biosynthesis {ECO:0000256|SAAS:SAAS00417423}. SQ SEQUENCE 158 AA; 17789 MW; 7226803D6BC7E08F CRC64; MEHLFGKWLP DLPAAISDGI SLPMVRLLHT RSLTAALRAL PHTFSVELLK LGELETECGG RLVREVLLKL DRIPVVEARS ECRIGSAFWQ NILDCGTRPL GERLFQADLE GARSAFEFAV AGEGCGRYFA ARRSRFSRHG EEMLLTEYFL PELKRFIG // ID Q9JZ43_NEIMB Unreviewed; 275 AA. AC Q9JZ43; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068}; DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068}; GN OrderedLocusNames=NMB1305 {ECO:0000313|EMBL:AAF41680.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41680.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41680.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41680.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:4B6G} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 3-275. RX PubMed=22937752; DOI=10.1089/ars.2012.4749; RA Chen N.H., Counago R.M., Djoko K.Y., Jennings M.P., Apicella M.A., RA Kobe B., McEwan A.G.; RT "A glutathione-dependent detoxification system is required for RT formaldehyde resistance and optimal survival of Neisseria meningitidis RT in biofilms."; RL Antioxid. Redox Signal. 18:743-755(2013). CC -!- FUNCTION: Serine hydrolase involved in the detoxification of CC formaldehyde. {ECO:0000256|RuleBase:RU363068}. CC -!- CATALYTIC ACTIVITY: S-formylglutathione + H(2)O = glutathione + CC formate. {ECO:0000256|RuleBase:RU363068}. CC -!- SIMILARITY: Belongs to the esterase D family. CC {ECO:0000256|RuleBase:RU363068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41680.1; -; Genomic_DNA. DR PIR; G81097; G81097. DR RefSeq; NP_274324.1; NC_003112.2. DR RefSeq; WP_002225169.1; NC_003112.2. DR PDB; 4B6G; X-ray; 1.40 A; A/B=3-275. DR PDBsum; 4B6G; -. DR ProteinModelPortal; Q9JZ43; -. DR STRING; 122586.NMB1305; -. DR ESTHER; neime-ESD; A85-EsteraseD-FGH. DR PaxDb; Q9JZ43; -. DR EnsemblBacteria; AAF41680; AAF41680; NMB1305. DR GeneID; 903727; -. DR KEGG; nme:NMB1305; -. DR PATRIC; 20358251; VBINeiMen85645_1637. DR eggNOG; ENOG4105C4W; Bacteria. DR eggNOG; COG0627; LUCA. DR HOGENOM; HOG000263929; -. DR KO; K01070; -. DR OMA; TEQPWAT; -. DR OrthoDB; EOG63587Z; -. DR BioCyc; NMEN122586:GHGG-1343-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:InterPro. DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000801; Esterase_put. DR InterPro; IPR014186; S-formylglutathione_hydrol. DR PANTHER; PTHR10061; PTHR10061; 1. DR Pfam; PF00756; Esterase; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR02821; fghA_ester_D; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4B6G}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU363068}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Serine esterase {ECO:0000256|RuleBase:RU363068}. SQ SEQUENCE 275 AA; 31431 MW; 5D3AE8477A35775E CRC64; MKLIEQHQIF GGSQQVWAHH AQTLQCEMKF AVYLPNNPEN RPLGVIYWLS GLTCTEQNFI TKSGFQRYAA EHQVIVVAPD TSPRGEQVPN DDAYDLGQSA GFYLNATEQP WAANYQMYDY ILNELPRLIE KHFPTNGKRS IMGHSMGGHG ALVLALRNQE RYQSVSAFSP ILSPSLVPWG EKAFTAYLGK DREKWQQYDA NSLIQQGYKV QGMRIDQGLE DEFLPTQLRT EDFIETCRAA NQPVDVRFHK GYDHSYYFIA SFIGEHIAYH AAFLK // ID Q9K1M4_NEIMB Unreviewed; 404 AA. AC Q9K1M4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Sodium/glutamate symporter {ECO:0000313|EMBL:AAF40548.1}; GN Name=gltS {ECO:0000313|EMBL:AAF40548.1}; GN OrderedLocusNames=NMB0085 {ECO:0000313|EMBL:AAF40548.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40548.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40548.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40548.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40548.1; -; Genomic_DNA. DR PIR; F81240; F81240. DR RefSeq; NP_273147.1; NC_003112.2. DR RefSeq; WP_002224758.1; NC_003112.2. DR STRING; 122586.NMB0085; -. DR PaxDb; Q9K1M4; -. DR EnsemblBacteria; AAF40548; AAF40548; NMB0085. DR GeneID; 902189; -. DR KEGG; nme:NMB0085; -. DR PATRIC; 20355175; VBINeiMen85645_0121. DR eggNOG; ENOG4105D6U; Bacteria. DR eggNOG; COG0786; LUCA. DR HOGENOM; HOG000282013; -. DR KO; K03312; -. DR OMA; WEISFDM; -. DR OrthoDB; EOG6FRCSX; -. DR BioCyc; NMEN122586:GHGG-91-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015501; F:glutamate:sodium symporter activity; IEA:InterPro. DR InterPro; IPR004445; GltS. DR PANTHER; PTHR36178:SF1; PTHR36178:SF1; 1. DR Pfam; PF03616; Glt_symporter; 1. DR TIGRFAMs; TIGR00210; gltS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 155 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 238 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 299 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 340 363 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 375 402 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 404 AA; 43186 MW; 61BD7302ACC503F4 CRC64; MEWEFNSYYT LIAATLVLLV GKFLVQKIKF LRDFNIPEPV AGGLIAAIVL FALHEAYGVS FKFEKPLQNA FMLIFFTSIG LSADFSRLKA GGLPLVVFTA IVGGFILVQN FVGVGLATAL GLDPLIGLIT GSVSLTGGHG TSGAWGPNFE TQYGLVGATG LGIASATFGL VFGGLIGGPV ARRLINKMGR KPVENKKQDQ DDNADDVFEQ AKRTRLITAE SAVETLAMFA ACLAFAEIMD GFDKEYLFDL PKFVWCLFGG VVIRNILTAA FKVNMFDRAI DVFGNASLSL FLAMALLNLK LWELTGLAGP VTVILAVQTV VMVLYATFVT YVFMGRDYDA AVLAAGHCGF GLGATPTAVA NMQSVTHTFG ASHKAFLIVP MVGAFFVDLI NAAILTGFVN FFKG // ID Q9JY56_NEIMB Unreviewed; 212 AA. AC Q9JY56; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42076.1}; GN OrderedLocusNames=NMB1731 {ECO:0000313|EMBL:AAF42076.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42076.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42076.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42076.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42076.1; -; Genomic_DNA. DR PIR; B81049; B81049. DR RefSeq; NP_274734.1; NC_003112.2. DR RefSeq; WP_002222941.1; NC_003112.2. DR ProteinModelPortal; Q9JY56; -. DR STRING; 122586.NMB1731; -. DR PaxDb; Q9JY56; -. DR EnsemblBacteria; AAF42076; AAF42076; NMB1731. DR GeneID; 903368; -. DR KEGG; nme:NMB1731; -. DR PATRIC; 20359425; VBINeiMen85645_2218. DR eggNOG; ENOG4108Z4T; Bacteria. DR eggNOG; COG1994; LUCA. DR HOGENOM; HOG000077737; -. DR OMA; VEPYGFF; -. DR OrthoDB; EOG6WHNQN; -. DR BioCyc; NMEN122586:GHGG-1786-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 208 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 212 AA; 23602 MW; 264C111A07D7D13D CRC64; MFQNFDLGVF LLAVLPVLLS ITVREVARGY TARYWGDNTA EQYGRLTLNP LPHIDLVGTI IVPLLTLMFT PFLFGWARPI PIDSRNFRNP RLAWRCVAAS GPLSNLAMAV LWGVVLVLTP YVGGAYQMPL AQMANYGILI NAILFALNII PILPWDGGIF IDTFLSAKYS QAFRKIEPYG TWIILLLMLT GVLGAFIAPI VRLVIAFVQM FV // ID Q9JZT1_NEIMB Unreviewed; 238 AA. AC Q9JZT1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAF41318.1}; GN OrderedLocusNames=NMB0910 {ECO:0000313|EMBL:AAF41318.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41318.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41318.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41318.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41318.1; -; Genomic_DNA. DR PIR; C81145; C81145. DR RefSeq; NP_273950.1; NC_003112.2. DR RefSeq; WP_002220696.1; NC_003112.2. DR ProteinModelPortal; Q9JZT1; -. DR STRING; 122586.NMB0910; -. DR PaxDb; Q9JZT1; -. DR EnsemblBacteria; AAF41318; AAF41318; NMB0910. DR GeneID; 903031; -. DR KEGG; nme:NMB0910; -. DR PATRIC; 20357253; VBINeiMen85645_1140. DR eggNOG; ENOG4108XTP; Bacteria. DR eggNOG; COG2932; LUCA. DR HOGENOM; HOG000127685; -. DR OMA; WLTTGNT; -. DR OrthoDB; EOG61KBMJ; -. DR BioCyc; NMEN122586:GHGG-948-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF00717; Peptidase_S24; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51306; SSF51306; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 63 HTH cro/C1-type DNA-binding. FT {ECO:0000259|SMART:SM00530}. SQ SEQUENCE 238 AA; 26564 MW; 39EC28144B2795AE CRC64; MTMHETTDRL FEIAKEQGVL KPADIAERLN ISQQALKNWE SRGIAAKALP EVAKAFGVSE TWLRTGEGSR TAPVLIDPDL PHEVKDIHRP MTWSSNDPLP DDDYVFVPYL KESCFKGGVG TYEIPDYNGY RLPFGKSTLK RKGINPDNVF CCTLTGDSME EKIAEDAAIA VDTGETAIRD GKIYAFAQDG MFRVKYLIRQ PGNSVLIRSH NSGFYGDENA PLDSLTVIGR VFWWSVLD // ID Q9JXA8_NEIMB Unreviewed; 195 AA. AC Q9JXA8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=RNA polymerase sigma factor {ECO:0000256|RuleBase:RU000716}; GN OrderedLocusNames=NMB2144 {ECO:0000313|EMBL:AAF42452.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42452.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42452.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42452.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily. CC {ECO:0000256|RuleBase:RU000716, ECO:0000256|SAAS:SAAS00565917}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42452.1; -; Genomic_DNA. DR PIR; F81002; F81002. DR RefSeq; NP_275129.1; NC_003112.2. DR RefSeq; WP_002220007.1; NC_003112.2. DR ProteinModelPortal; Q9JXA8; -. DR STRING; 122586.NMB2144; -. DR PaxDb; Q9JXA8; -. DR EnsemblBacteria; AAF42452; AAF42452; NMB2144. DR GeneID; 903228; -. DR KEGG; nme:NMB2144; -. DR PATRIC; 20360482; VBINeiMen85645_2737. DR eggNOG; ENOG4108WQI; Bacteria. DR eggNOG; COG1595; LUCA. DR HOGENOM; HOG000220918; -. DR KO; K03088; -. DR OMA; PEEMMEQ; -. DR OrthoDB; EOG6F299N; -. DR BioCyc; NMEN122586:GHGG-2209-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014289; RNA_pol_sigma-24-rel. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF08281; Sigma70_r4_2; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02943; Sig70_famx1; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS01063; SIGMA70_ECF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Sigma factor {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 15 77 Sigma70_r2. {ECO:0000259|Pfam:PF04542}. FT DOMAIN 129 180 Sigma70_r4_2. {ECO:0000259|Pfam:PF08281}. SQ SEQUENCE 195 AA; 22610 MW; D1045617DEDB2339 CRC64; MPLPDLTDAE LIESRKLLLH FARLQLPDHP DLAEDLVQET LLSAYSAGDS FQGRALVNSW LFAILKNKII DALRQIGRQR KVFTTLDDEL LDEAFESHFS QNGHWTQEGQ PQHWNTPEKS LNNNEFQKIL QSCLYNLPEN TARVFTLKEI LGFSSDEIQQ MCGISTSNYH TIMHRARESL RQCLQIKWFN QENPK // ID Q9JY66_NEIMB Unreviewed; 412 AA. AC Q9JY66; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Membrane fusion protein {ECO:0000313|EMBL:AAF42063.1}; GN Name=mtrC {ECO:0000313|EMBL:AAF42063.1}; GN OrderedLocusNames=NMB1716 {ECO:0000313|EMBL:AAF42063.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42063.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42063.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42063.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) CC (TC 8.A.1) family. {ECO:0000256|SAAS:SAAS00568556}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42063.1; -; Genomic_DNA. DR PIR; F81051; F81051. DR RefSeq; NP_274719.1; NC_003112.2. DR RefSeq; WP_002224968.1; NC_003112.2. DR ProteinModelPortal; Q9JY66; -. DR STRING; 122586.NMB1716; -. DR PaxDb; Q9JY66; -. DR EnsemblBacteria; AAF42063; AAF42063; NMB1716. DR GeneID; 903386; -. DR KEGG; nme:NMB1716; -. DR PATRIC; 20359393; VBINeiMen85645_2202. DR eggNOG; ENOG4105C1P; Bacteria. DR eggNOG; ENOG410XNVN; LUCA. DR HOGENOM; HOG000158247; -. DR KO; K03585; -. DR OMA; INVRYTK; -. DR OrthoDB; EOG6GJBSS; -. DR BioCyc; NMEN122586:GHGG-1771-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR032317; HlyD_D23. DR InterPro; IPR006143; RND_pump_MFP. DR Pfam; PF00529; HlyD; 1. DR Pfam; PF16576; HlyD_D23; 1. DR TIGRFAMs; TIGR01730; RND_mfp; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 412 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332242. FT DOMAIN 64 300 HlyD_D23. {ECO:0000259|Pfam:PF16576}. SQ SEQUENCE 412 AA; 42796 MW; 0B7A0DB0E3113E4E CRC64; MAFYAFKAMR AAALAAAVAL VLSSCGKGGD AAQGGQPAGR EAPAPVVGVV TVHPQTVALT VELPGRLESL RTADVRAQVG GIIQKRLFQE GSYVRAGQPL YQIDSSTYEA GLESARAQLA TAQATLAKAD ADLARYKPLV AAEAVSRQEY DAAVTAKRSA EAGVKAAQAA IKSAGISLNR SRITAPISGF IGQSKVSEGT LLNAGDATVL ATIRQTNPMY VNVTQSASEV MKLRRQIAEG KLLAADGVIA VGIKFDDGTV YPEKGRLLFA DPAVNESTGQ ITLRAAVPND QNILMPGLYV RVLMDQVAVD NAFVVPQQAV TRGAKDTVMI VNAQGGMEPR EVTVAQQQGT NWIVTSGLKD GDKVVVEGIS IAGITGAKKV TPKEWASSEN QAAAPQSGVQ TASEAKPASE AK // ID Q9K1K3_NEIMB Unreviewed; 706 AA. AC Q9K1K3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 107. DE SubName: Full=Putative nitrogen regulation protein NtrY {ECO:0000313|EMBL:AAF40573.1}; GN OrderedLocusNames=NMB0114 {ECO:0000313|EMBL:AAF40573.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40573.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40573.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40573.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00577673}. CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00577406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40573.1; -; Genomic_DNA. DR PIR; D81236; D81236. DR RefSeq; NP_273172.1; NC_003112.2. DR RefSeq; WP_002224765.1; NC_003112.2. DR ProteinModelPortal; Q9K1K3; -. DR STRING; 122586.NMB0114; -. DR PaxDb; Q9K1K3; -. DR EnsemblBacteria; AAF40573; AAF40573; NMB0114. DR GeneID; 902218; -. DR KEGG; nme:NMB0114; -. DR PATRIC; 20355241; VBINeiMen85645_0154. DR eggNOG; ENOG4105ES5; Bacteria. DR eggNOG; COG5000; LUCA. DR HOGENOM; HOG000266158; -. DR OMA; VVSYQFV; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NMEN122586:GHGG-120-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR000014; PAS. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR017232; Sig_transdc_His_kinase_NtrY. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PIRSF; PIRSF037532; STHK_NtrY; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55785; SSF55785; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|RuleBase:RU003568, ECO:0000256|SAAS:SAAS00529081}; KW Membrane {ECO:0000256|SAAS:SAAS00577774, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Phosphoprotein {ECO:0000256|RuleBase:RU003568}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00529081}; KW Transmembrane {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 98 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 295 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 296 348 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 360 406 PAS (PER-ARNT-SIM). FT {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 490 702 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 706 AA; 76470 MW; FC4CB2921BE7EA4F CRC64; MRRFLPIAAI CAVVLLYGLT AATGSTSSLA DYFWWIVAFS AMLLLVLSAV LARYVILLLK DRRDGVFGSQ IAKRLSGMFT LVAVLPGVFL FGVSAQFING TINSWFGNDT HEALERSLNL SKSALNLAAD NALGNAVPVQ IDLIGAASLP GDMGRVLEHY AGSGFAQLAL YNAASGKIEK SINPHKLDQP FPGKARWEKI QRAGSVRDLE SIGGVLYAQG WLSAGTHNGR DYALFFRQPV PKGVAEDAVL IEKARAKYAE LSYSKKGLQT FFLATLLIAS LLSIFLALVM ALYFARRFVE PVLSLAEGAK AVAQGDFSQT RPVLRNDEFG RLTKLFNHMT EQLSIAKEAD ERNRRREEAA RHYLECVLEG LTTGVVVFDE QGCLKTFNKA AEQILGMPLT PLWGSSRHGW HGVSAQQSLL AEVFAAIGAA AGTDKPVHVK YAAPDDAKIL LGKATVLPED NGNGVVMVID DITVLIHAQK EAAWGEVAKR LAHEIRNPLT PIQLSAERLA WKLGGKLDEQ DAQILTRSTD TIVKQVAALK EMVEAFRNYA RSPSLKLENQ DLNALIGDVL ALYEAGPCRF AAELAGEPLT VAADTTAMRQ VLHNIFKNAA EAAEEADVPE VRVKSETGQD GRIVLTVCDN GKGFGREMLH NAFEPYVTDK PAGTGLGLPV VKKIIEEHGG RISLSNQDAG GACVRIILPK TVKTYA // ID Q9JYH3_NEIMB Unreviewed; 367 AA. AC Q9JYH3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Putative protease {ECO:0000313|EMBL:AAF41940.1}; GN OrderedLocusNames=NMB1587 {ECO:0000313|EMBL:AAF41940.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41940.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41940.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41940.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41940.1; -; Genomic_DNA. DR PIR; E81065; E81065. DR RefSeq; NP_274593.1; NC_003112.2. DR RefSeq; WP_010980959.1; NC_003112.2. DR ProteinModelPortal; Q9JYH3; -. DR STRING; 122586.NMB1587; -. DR PaxDb; Q9JYH3; -. DR EnsemblBacteria; AAF41940; AAF41940; NMB1587. DR GeneID; 904239; -. DR KEGG; nme:NMB1587; -. DR PATRIC; 20359040; VBINeiMen85645_2038. DR eggNOG; ENOG4105ERU; Bacteria. DR eggNOG; COG0616; LUCA. DR HOGENOM; HOG000281079; -. DR KO; K04774; -. DR OMA; WYGEDAL; -. DR OrthoDB; EOG6P5ZHQ; -. DR BioCyc; NMEN122586:GHGG-1629-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002142; Peptidase_S49. DR InterPro; IPR013703; Peptidase_S49_N_proteobac. DR Pfam; PF01343; Peptidase_S49; 1. DR Pfam; PF08496; Peptidase_S49_N; 1. DR SUPFAM; SSF52096; SSF52096; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41940.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000313|EMBL:AAF41940.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 48 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 21 177 Peptidase_S49_N. FT {ECO:0000259|Pfam:PF08496}. FT DOMAIN 180 329 Peptidase_S49. FT {ECO:0000259|Pfam:PF01343}. FT COILED 80 110 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 367 AA; 41415 MW; 814711B59F2C6684 CRC64; MMDNIDMFMP EQEEIQSMWK EILLNYGIFL LELLTVFGAI ALIVLAIVQS KKQSESGSVV LTDFSENYKK QRQSFEAFFL SGEEAKHQEK EEKKKEKAEA KAEKKRLKEG GEKSAETQKS RLFVLDFDGD LYAHAVESLR HEITAVLLIA KPEDEVLLRL ESPGGVVHGY GLAASQLRRL RERNIPLTVA VDKVAASGGY MMACVADKIA SAPFAIVGSV GVVAEVPNIH RLLKKHDIDV DVMTAGEFKR TVTFMGENTE KGKQKFRQEL EETHQLFKQF VSENRPQLDI EEVATGEHWF GRQALALNLI DEISTSDDLL LKAFENKQVI EVKYQEKQSL IQRIGLQAEA SVEKLFAKLV NRRADVM // ID Q9K0F9_NEIMB Unreviewed; 412 AA. AC Q9K0F9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41068.1}; GN OrderedLocusNames=NMB0647 {ECO:0000313|EMBL:AAF41068.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41068.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41068.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41068.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41068.1; -; Genomic_DNA. DR PIR; B81176; B81176. DR STRING; 122586.NMB0647; -. DR PaxDb; Q9K0F9; -. DR EnsemblBacteria; AAF41068; AAF41068; NMB0647. DR PATRIC; 20356593; VBINeiMen85645_0815. DR eggNOG; ENOG4106HIT; Bacteria. DR eggNOG; ENOG410Y691; LUCA. DR HOGENOM; HOG000027893; -. DR OMA; RCASTGR; -. DR OrthoDB; EOG64R617; -. DR BioCyc; NMEN122586:GHGG-674-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR029501; EndoU_bac. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF14436; EndoU_bacteria; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 32 PT-VENN. {ECO:0000259|Pfam:PF04829}. FT DOMAIN 289 410 EndoU_bacteria. FT {ECO:0000259|Pfam:PF14436}. SQ SEQUENCE 412 AA; 45508 MW; 6B41BAD5323C9052 CRC64; MIASLTGAAV GGTPVDAQTG GAVGQNAVEN NLYLTSEALK KDKQTARKIY SVIKEQVKHE CSSTGRITEC RQNIGRIIEF TQDKRFDSRF KDLKKESLYY LNKHPDLVAS YLKAEYEKLD REDKSILHRY ISPGAEIVSG SLGVVLSGVA GGGSCAETFG LGCAAALVGV TSSYDHVITG TKNFGKKASE QRPTIAVQAL KQLGLSEQAA EYVQFSIDLF SVGKSGGGIP KAKPVFDAKP RWEVDRKLNK LTTREQVEKN VQETRRRSQS SQFKAHAQRE WENKTGLDFN HFIGGDINKK GTVTGGHSLT RGDVRVIQQT SAPDKHGVYQ ATVEIKKPDG SWEVKTKKGG KVMTKHTMFP KDWDEARIRA EVTSAWESRI MLKDNKWQGT SKSGIKIEGF TEPNRTAYPI YE // ID Q9JXH9_NEIMB Unreviewed; 291 AA. AC Q9JXH9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Thiamin pyrophosphokinase-related protein {ECO:0000313|EMBL:AAF42362.1}; GN OrderedLocusNames=NMB2041 {ECO:0000313|EMBL:AAF42362.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42362.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42362.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42362.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42362.1; -; Genomic_DNA. DR PIR; F81012; F81012. DR RefSeq; NP_275032.1; NC_003112.2. DR RefSeq; WP_002244347.1; NC_003112.2. DR ProteinModelPortal; Q9JXH9; -. DR STRING; 122586.NMB2041; -. DR PaxDb; Q9JXH9; -. DR EnsemblBacteria; AAF42362; AAF42362; NMB2041. DR GeneID; 904050; -. DR KEGG; nme:NMB2041; -. DR PATRIC; 20360228; VBINeiMen85645_2614. DR eggNOG; ENOG4108YAT; Bacteria. DR eggNOG; COG0494; LUCA. DR HOGENOM; HOG000218721; -. DR OMA; GPWRDEQ; -. DR OrthoDB; EOG6K9QF5; -. DR BioCyc; NMEN122586:GHGG-2104-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000313|EMBL:AAF42362.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42362.1}. FT DOMAIN 126 267 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 291 AA; 32042 MW; 90BF43C968B8FE26 CRC64; MPTVRFTESV SKQDLDALFE WAKASYGAES CWKTLYLNGL PLGNLSPEWV ERVKKDWEAG CSESSDGIFL NADGWPDMGG RLQHLALGWH CAGLLDGWRN ECFDLTDGGG NPLFTLERAA FRPFGLLSRA VHLNGLTESD GRWHFWIGRR SPHKAVDPNK LDNTAAGGVS GGEMPSEAVC RESSEEAGLD KTLLPLIRPV SQLHSLRSVS RGVHNEILYV FDAVLPETFL PENQDGEVAG FEKMDIGGLL DAMLSGNMMH DAQLVTLDAF CRYGLIDAAH PLSEWLDGIR L // ID Q9JXG0_NEIMB Unreviewed; 480 AA. AC Q9JXG0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=TldD protein {ECO:0000313|EMBL:AAF42385.1}; GN Name=tldD {ECO:0000313|EMBL:AAF42385.1}; GN OrderedLocusNames=NMB2066 {ECO:0000313|EMBL:AAF42385.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42385.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42385.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42385.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42385.1; -; Genomic_DNA. DR PIR; F81010; F81010. DR RefSeq; NP_275056.1; NC_003112.2. DR RefSeq; WP_002240845.1; NC_003112.2. DR STRING; 122586.NMB2066; -. DR PaxDb; Q9JXG0; -. DR EnsemblBacteria; AAF42385; AAF42385; NMB2066. DR GeneID; 904006; -. DR KEGG; nme:NMB2066; -. DR PATRIC; 20360292; VBINeiMen85645_2646. DR eggNOG; ENOG4105D1U; Bacteria. DR eggNOG; COG0312; LUCA. DR HOGENOM; HOG000224929; -. DR KO; K03568; -. DR OMA; MVGNDLS; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; NMEN122586:GHGG-2129-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR InterPro; IPR025502; TldD. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. DR PIRSF; PIRSF004919; TldD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 480 AA; 50753 MW; 75297BDF4F84F7AA CRC64; MHPTYSAVQA RLLEANRLSP ELLAKSLCII GAHHVDYADI YCQRTAYESW HLEEGIVKSG SFQINQGVGV RAVSGDKTAF AYADSLCIDS INRSARAVRA IGAAGGKVSA KMPSETRGKP VCSASDPIAG LDSAAKVALL NKVEAIAKAA DPRIVQVMAG LTCEYDMVYL ARLDGKHAAD IRPMVRLNVT VIAKQGERRE QGSAGGGGRY DLAYFDENLV HRFVDAAVKQ ALTNLESRPA PAGEMTVVLG NGWPGVLLHE AVGHGLEGDF NRKGTSVFSG RIGERVAAKG VTVVDQGDIA GRRGSLNIDD EGNETRRTVL IEDGILVGYM QDETNARLTG TQSTGNGRRE SYASAPMPRM TNTFMENGSY EPEEIIASID KGIYAVNFGG GQVDITSGKF VFSASEAWWV EGGRLQYPVK GATIIGNGPE VLKHVSMIGN DTALDSGVGV CGKEGQSVPV GVGQPTLRID AGLTVGGSAI // ID Q7DDI9_NEIMB Unreviewed; 167 AA. AC Q7DDI9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41413.1}; GN OrderedLocusNames=NMB1012 {ECO:0000313|EMBL:AAF41413.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41413.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41413.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41413.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2IS5} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-165. RA Chang C., Li H., Abdullah J., Joachimiak A.; RT "Crystal structure of 3 residues truncated version of protein NMB1012 RT from Neisseria meningitides."; RL Submitted (OCT-2006) to the PDB data bank. RN [3] {ECO:0000213|PDB:2IKB} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS). RA Zhang R., Li H., Bargassa M., Joachimiak A.; RT "The 1.7 A crystal structure of a hypothetical protein NMB1012 from RT Neisseria meningitidis."; RL Submitted (OCT-2006) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41413.1; -; Genomic_DNA. DR PIR; E81131; E81131. DR RefSeq; NP_274047.1; NC_003112.2. DR RefSeq; WP_002225286.1; NC_003112.2. DR PDB; 2IKB; X-ray; 1.70 A; A/B/C/D=1-167. DR PDB; 2IS5; X-ray; 1.85 A; A/B/C/D=2-165. DR PDBsum; 2IKB; -. DR PDBsum; 2IS5; -. DR ProteinModelPortal; Q7DDI9; -. DR SMR; Q7DDI9; 1-163. DR STRING; 122586.NMB1012; -. DR PaxDb; Q7DDI9; -. DR EnsemblBacteria; AAF41413; AAF41413; NMB1012. DR GeneID; 903150; -. DR KEGG; nme:NMB1012; -. DR PATRIC; 20357553; VBINeiMen85645_1293. DR eggNOG; ENOG41090JY; Bacteria. DR eggNOG; COG3926; LUCA. DR HOGENOM; HOG000013718; -. DR OMA; FDFYVNA; -. DR OrthoDB; EOG6WDSH0; -. DR BioCyc; NMEN122586:GHGG-1049-MONOMER; -. DR EvolutionaryTrace; Q7DDI9; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008565; DUF847. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR018537; Peptidoglycan-bd_3. DR Pfam; PF05838; Glyco_hydro_108; 1. DR Pfam; PF09374; PG_binding_3; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2IKB, ECO:0000213|PDB:2IS5}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 92 154 PG_binding_3. {ECO:0000259|Pfam:PF09374}. SQ SEQUENCE 167 AA; 18667 MW; AB85D27FB2000180 CRC64; MSDKFNQFIN RVLSHEGGYA NHPKDPGGET NWGITKRTAQ ANGYNGSMRA MTREQAISIY RKAFWERYRA DQMPEAVAFQ FFDACVNHGY GNAARMLQRA AGVPDDGVIG AVSLKAINSL PENDLLLRFN AERLVFYTKL GTFTSFGKGW VRRVAQNLIH ASADNTD // ID Q9K040_NEIMB Unreviewed; 459 AA. AC Q9K040; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=DNA repair protein radA {ECO:0000256|RuleBase:RU003555}; GN Name=radA {ECO:0000313|EMBL:AAF41195.1}; GN OrderedLocusNames=NMB0782 {ECO:0000313|EMBL:AAF41195.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41195.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41195.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41195.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: DNA-dependent ATPase involved in processing of CC recombination intermediates, plays a role in repairing DNA breaks. CC Stimulates the branch migration of RecA-mediated strand transfer CC reactions, allowing the 3' invading strand to extend heteroduplex CC DNA faster. Binds ssDNA in the presence of ADP but not other CC nucleotides, has ATPase activity that is stimulated by ssDNA and CC various branched DNA structures, but inhibited by SSB. Does not CC have RecA's homology-searching function. CC {ECO:0000256|RuleBase:RU003555}. CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily. CC {ECO:0000256|RuleBase:RU003555}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41195.1; -; Genomic_DNA. DR PIR; C81158; C81158. DR RefSeq; NP_273824.1; NC_003112.2. DR RefSeq; WP_002235637.1; NC_003112.2. DR ProteinModelPortal; Q9K040; -. DR STRING; 122586.NMB0782; -. DR PaxDb; Q9K040; -. DR EnsemblBacteria; AAF41195; AAF41195; NMB0782. DR GeneID; 902897; -. DR KEGG; nme:NMB0782; -. DR PATRIC; 20356945; VBINeiMen85645_0991. DR eggNOG; ENOG4105DNJ; Bacteria. DR eggNOG; COG1066; LUCA. DR HOGENOM; HOG000218329; -. DR KO; K04485; -. DR OMA; FEGERGH; -. DR OrthoDB; EOG6DRPHC; -. DR BioCyc; NMEN122586:GHGG-813-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PRINTS; PR01874; DNAREPAIRADA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR TIGRFAMs; TIGR00416; sms; 1. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU003555}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|RuleBase:RU003555}; KW DNA repair {ECO:0000256|RuleBase:RU003555}; KW DNA-binding {ECO:0000256|RuleBase:RU003555}; KW Metal-binding {ECO:0000256|RuleBase:RU003555}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003555}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU003555}; KW Zinc-finger {ECO:0000256|RuleBase:RU003555}. FT DOMAIN 68 216 RECA_2. {ECO:0000259|PROSITE:PS50162}. SQ SEQUENCE 459 AA; 49533 MW; 9CA60BCE60FBE166 CRC64; MAKTLKTLYQ CTECGGTSPK WQGKCPHCGE WNTLQESLAA PEPKNARFQS WAADTSTVQS LSAVTATEVP RNPTGMGELD RVLGGGLVDG AVILLGGDPG IGKSTLLLQT IAKMAQSRKV LYVSGEESAQ QVALRAQRLE LPTDGVNLLA EIRMEAIQAA LKQHQPEVVV IDSIQTMYSD QITSAPGSVS QVRECAAQLT RMAKQMGIAM ILVGHVTKDG AIAGPRVLEH MVDTVLYFEG DQHSNYRMIR AIKNRFGAAN ELGVFAMTEN GLKGVSNPSA IFLASYRDDT PGSCVLVTQE GSRPLLVEIQ ALVDDAHGFT PKRLTVGLEQ NRLAMLLAVL NRHGGIACFD QDVFLNAVGG VKIGEPAADL AVILAMLSSF RNRPMPEKTV VFGEIGLSGE VRPVARGQER LKEAEKLGFK RAIVPKANMP RNAKEFPNLK IYGVSSLQEA IDICRDSRE // ID Q9JZ70_NEIMB Unreviewed; 158 AA. AC Q9JZ70; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Putative zinc uptake regulation protein {ECO:0000313|EMBL:AAF41643.1}; GN OrderedLocusNames=NMB1266 {ECO:0000313|EMBL:AAF41643.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41643.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41643.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41643.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41643.1; -; Genomic_DNA. DR PIR; D81102; D81102. DR RefSeq; NP_274287.2; NC_003112.2. DR ProteinModelPortal; Q9JZ70; -. DR STRING; 122586.NMB1266; -. DR PaxDb; Q9JZ70; -. DR EnsemblBacteria; AAF41643; AAF41643; NMB1266. DR GeneID; 903688; -. DR KEGG; nme:NMB1266; -. DR PATRIC; 20358147; VBINeiMen85645_1585. DR eggNOG; COG0735; LUCA. DR HOGENOM; HOG000014146; -. DR KO; K09823; -. DR OMA; DHSHCVH; -. DR OrthoDB; EOG6N6839; -. DR BioCyc; NMEN122586:GHGG-1304-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR CollecTF; EXPREG_000016a0; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 158 AA; 17494 MW; 40ECF38C411AF6B4 CRC64; MKTNFKQKII EQARSEGLQV TALREQVLDI VLQQSGVIKA YNVLSQMQQQ SEGVLAPPTA YRALDFWAEQ GVLHKVAAVN GYILCSHAQH ECDDHCHDHE EAEAHHSAFI LVCTECGTAD EQTLSHEWAA LRAGVAESGF ALKEEHVVLT GICKKCQQ // ID Q9K160_NEIMB Unreviewed; 384 AA. AC Q9K160; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Fatty acid efflux system protein {ECO:0000313|EMBL:AAF40763.1}; GN Name=farA {ECO:0000313|EMBL:AAF40763.1}; GN OrderedLocusNames=NMB0318 {ECO:0000313|EMBL:AAF40763.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40763.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40763.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40763.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40763.1; -; Genomic_DNA. DR PIR; A81212; A81212. DR RefSeq; NP_273367.1; NC_003112.2. DR RefSeq; WP_002224866.1; NC_003112.2. DR ProteinModelPortal; Q9K160; -. DR STRING; 122586.NMB0318; -. DR PaxDb; Q9K160; -. DR EnsemblBacteria; AAF40763; AAF40763; NMB0318. DR GeneID; 902434; -. DR KEGG; nme:NMB0318; -. DR PATRIC; 20355767; VBINeiMen85645_0403. DR eggNOG; ENOG4105CW7; Bacteria. DR eggNOG; COG1566; LUCA. DR HOGENOM; HOG000112072; -. DR KO; K03543; -. DR OMA; RQLMINS; -. DR OrthoDB; EOG6C014B; -. DR BioCyc; NMEN122586:GHGG-338-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 43 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 384 AA; 41323 MW; FD65F80CA67DDFB2 CRC64; MDTHTDETKL QNTQAKRKRR LTALTLLFAL AAAAAGSAFF LWWQHEEETE DAYVAGRVVQ VTPQKGGTVR KVLHDDTDAV KKGDVLAVLD DDNDVLAYER AKNELVQAVR QNRRQNAATS QAGAQVALRR ADLARAQDDL RRRSALAESG AVSAEELAHA RAAVSQAQAA VKAALAEESS ARAALGGQVS LREQPAVQTA IGRLKDAWLN LQRTQIRAPA DGQVAKRSVQ VGQQVAAGAP LMAVVPLSDV WVDANFKETQ LRHMKIGQPA ELVSDLYGKQ IVYRGRVAGF SAGTGSAFSL IPAQNATGNW IKVVQRVPVR IVLNREDVDR HPLRIGLSMT VKVDTSAAGA PVSKTPGAAL PEMESTDWSE VDRTVDEILG QSAP // ID Q9JYH2_NEIMB Unreviewed; 187 AA. AC Q9JYH2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000313|EMBL:AAF41941.1}; DE EC=2.7.8.5 {ECO:0000313|EMBL:AAF41941.1}; GN Name=pgsA {ECO:0000313|EMBL:AAF41941.1}; GN OrderedLocusNames=NMB1588 {ECO:0000313|EMBL:AAF41941.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41941.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41941.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41941.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I family. {ECO:0000256|RuleBase:RU003750, CC ECO:0000256|SAAS:SAAS00571358}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41941.1; -; Genomic_DNA. DR PIR; F81065; F81065. DR RefSeq; NP_274594.1; NC_003112.2. DR RefSeq; WP_002244239.1; NC_003112.2. DR STRING; 122586.NMB1588; -. DR PaxDb; Q9JYH2; -. DR EnsemblBacteria; AAF41941; AAF41941; NMB1588. DR GeneID; 904259; -. DR KEGG; nme:NMB1588; -. DR PATRIC; 20359054; VBINeiMen85645_2039. DR eggNOG; ENOG4105BZQ; Bacteria. DR eggNOG; COG0558; LUCA. DR HOGENOM; HOG000010898; -. DR KO; K00995; -. DR OMA; VQMVAIP; -. DR OrthoDB; EOG6WMJ3D; -. DR BioCyc; NMEN122586:GHGG-1636-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR000462; CDP-OH_P_trans. DR InterPro; IPR004570; Phosphatidylglycerol_P_synth. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1. DR TIGRFAMs; TIGR00560; pgsA; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipid biosynthesis {ECO:0000256|SAAS:SAAS00461556}; KW Lipid metabolism {ECO:0000256|SAAS:SAAS00461556}; KW Membrane {ECO:0000256|SAAS:SAAS00461540, ECO:0000256|SAM:Phobius}; KW Phospholipid biosynthesis {ECO:0000256|SAAS:SAAS00461556}; KW Phospholipid metabolism {ECO:0000256|SAAS:SAAS00461556}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003750, KW ECO:0000256|SAAS:SAAS00461509, ECO:0000313|EMBL:AAF41941.1}; KW Transmembrane {ECO:0000256|SAAS:SAAS00461540, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00461540, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 179 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 187 AA; 21318 MW; 7BD62D935C242CB7 CRC64; MPWNLPIFLT WLRVLLIPVL TALFYLPFPW FAEETINLTA AVIFAVAALT DWFDGFLARL WKQTSDFGAF LDPVADKLMV AVSLLLLVKL DRTYVLFAMI IIGREITISA LREWMAQMGK RNSVAVATVG KFKTAAQMLA IFLLLLNFPD FYGFNLAFIG NVLMFIASLL TVWSMLYYLK MAWKEIA // ID Q9K0B2_NEIMB Unreviewed; 691 AA. AC Q9K0B2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Competence protein ComA {ECO:0000313|EMBL:AAF41119.1}; GN Name=comA {ECO:0000313|EMBL:AAF41119.1}; GN OrderedLocusNames=NMB0702 {ECO:0000313|EMBL:AAF41119.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41119.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41119.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41119.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41119.1; -; Genomic_DNA. DR PIR; G81167; G81167. DR RefSeq; NP_273744.1; NC_003112.2. DR RefSeq; WP_010980828.1; NC_003112.2. DR ProteinModelPortal; Q9K0B2; -. DR STRING; 122586.NMB0702; -. DR PaxDb; Q9K0B2; -. DR EnsemblBacteria; AAF41119; AAF41119; NMB0702. DR GeneID; 902814; -. DR KEGG; nme:NMB0702; -. DR PATRIC; 20356743; VBINeiMen85645_0893. DR eggNOG; ENOG4108EQH; Bacteria. DR eggNOG; COG0658; LUCA. DR eggNOG; COG2333; LUCA. DR HOGENOM; HOG000262043; -. DR KO; K02238; -. DR OMA; EMFPEQS; -. DR OrthoDB; EOG647TTM; -. DR BioCyc; NMEN122586:GHGG-730-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR004477; ComEC_N. DR InterPro; IPR004797; Competence_ComEC/Rec2. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF03772; Competence; 1. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00360; ComEC_N-term; 1. DR TIGRFAMs; TIGR00361; ComEC_Rec2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 179 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 306 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 416 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 455 633 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 691 AA; 74409 MW; 5EC00CE0B166C6FE CRC64; MLCVLAGAAY GVFRTEAALS SQWRAEAVSG VPLTVEVADM PRSDGRRVQF AAKAVDSGGR TFDLLLSDYK RREWAVGSRW RITARVHPVV GELNLRGLNR EAWALSNGIG GAGTVGADRV LLHGGSGWGI AVWRSRISRN WQQADADGGL SDGIGLMRAL SVGEQSALRP ELWQAFRPLG LTHLVSISGL HVTMVAVMFA WLAKRLLACS PRLPARPRVW VLAAGCAGAL FYALLAGFSV PTQRSVLMLA AFAWAWRRGR LSAWATWWQA LAAVLLFDPL AVLGVGTWLS FGLVAALIWA CSGRLHEGKR QTAVRGQWAA SVLSLVLLGY LFASLPLISP LVNAVAIPWF SWVLTPLALL GSVVPFAPLQ QLGAFLAEYT LRFLVWLADV SPEFAVAAAP LPLLVLAVCA ALLLLLPRGL GLRPWAVLLL AGFVFYRSPG VPENEVAVTV WDAGQGLSVS VQTANHHLLF DTGTASAAQT GIVPSLNAAG VRRLDKLVLS HHDSDHDGGF RAVRNIPAGG IYAGQPEFYE GARHCAEQRW QWDGVDFEFL RPSERKNIDD NGKSCVLRVV AGGAALLVTG DLDTKGEESL VGKYGGNLYS QVLVLGHHGS NTSSSGVFLN AVSPEYAVAS SGYANAYKHP TEAVQNRVRA HGIKLLRTDL SGALQFGLGR GGVKAQRLRG YKFYWQKKPF E // ID Q9K0L9_NEIMB Unreviewed; 187 AA. AC Q9K0L9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 107. DE SubName: Full=Transcriptional regulator, AsnC family {ECO:0000313|EMBL:AAF41001.1}; GN OrderedLocusNames=NMB0573 {ECO:0000313|EMBL:AAF41001.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41001.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41001.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41001.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2P5V, ECO:0000213|PDB:2P6S, ECO:0000213|PDB:2P6T} RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-187 IN COMPLEX WITH RP CALCIUM. RX PubMed=17374605; DOI=10.1074/jbc.M701082200; RA Ren J., Sainsbury S., Combs S.E., Capper R.G., Jordan P.W., RA Berrow N.S., Stammers D.K., Saunders N.J., Owens R.J.; RT "The structure and transcriptional analysis of a global regulator from RT Neisseria meningitidis."; RL J. Biol. Chem. 282:14655-14664(2007). CC -!- SIMILARITY: Contains 3 HTH asnC-type DNA-binding domains. CC {ECO:0000256|RuleBase:RU000704}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41001.1; -; Genomic_DNA. DR PIR; H81182; H81182. DR RefSeq; NP_273617.1; NC_003112.2. DR RefSeq; WP_002214348.1; NC_003112.2. DR PDB; 2P5V; X-ray; 1.99 A; A/B/C/D/E/F/G/H=28-187. DR PDB; 2P6S; X-ray; 2.80 A; A/B/C/D/E/F/G/H=28-187. DR PDB; 2P6T; X-ray; 2.90 A; A/B/C/D/E/F/G/H=28-187. DR PDBsum; 2P5V; -. DR PDBsum; 2P6S; -. DR PDBsum; 2P6T; -. DR ProteinModelPortal; Q9K0L9; -. DR SMR; Q9K0L9; 28-185. DR STRING; 122586.NMB0573; -. DR PaxDb; Q9K0L9; -. DR EnsemblBacteria; AAF41001; AAF41001; NMB0573. DR GeneID; 902688; -. DR KEGG; nme:NMB0573; -. DR PATRIC; 20356427; VBINeiMen85645_0733. DR eggNOG; ENOG4105EW9; Bacteria. DR eggNOG; COG1522; LUCA. DR HOGENOM; HOG000115327; -. DR KO; K03719; -. DR OMA; ATHADLF; -. DR OrthoDB; EOG6F29D2; -. DR BioCyc; NMEN122586:GHGG-599-MONOMER; -. DR EvolutionaryTrace; Q9K0L9; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2P5V, ECO:0000213|PDB:2P6S, KW ECO:0000213|PDB:2P6T}; KW Calcium {ECO:0000213|PDB:2P5V, ECO:0000213|PDB:2P6S, KW ECO:0000213|PDB:2P6T}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000704}; KW Metal-binding {ECO:0000213|PDB:2P5V, ECO:0000213|PDB:2P6S, KW ECO:0000213|PDB:2P6T}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000704}; KW Transcription regulation {ECO:0000256|RuleBase:RU000704}. FT DOMAIN 33 96 HTH asnC-type DNA-binding. FT {ECO:0000259|PROSITE:PS50956}. FT METAL 132 132 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:2P6T}. FT METAL 132 132 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:2P6T}. FT METAL 134 134 Calcium 1. {ECO:0000213|PDB:2P6T}. FT METAL 163 163 Calcium 2. {ECO:0000213|PDB:2P6T}. SQ SEQUENCE 187 AA; 21052 MW; 31B3B0538C7F5774 CRC64; MLIWSPSVRI AANIRTDNPN SLKRNANMPQ LTLDKTDIKI LQVLQENGRL TNVELSERVA LSPSPCLRRL KQLEDAGIVR QYAALLSPES VNLGLQAFIR VSIRKAKDAR EDFAASVRKW PEVLSCFALT GETDYLLQAF FTDMNAFSHF VLDTLLSHHG VQDAQSSFVL KEIKHTTSLP LNHLLKE // ID Q9K1J7_NEIMB Unreviewed; 125 AA. AC Q9K1J7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40580.1}; GN OrderedLocusNames=NMB0121 {ECO:0000313|EMBL:AAF40580.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40580.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40580.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40580.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40580.1; -; Genomic_DNA. DR PIR; F81234; F81234. DR RefSeq; NP_273179.1; NC_003112.2. DR RefSeq; WP_002233408.1; NC_003112.2. DR ProteinModelPortal; Q9K1J7; -. DR STRING; 122586.NMB0121; -. DR PaxDb; Q9K1J7; -. DR EnsemblBacteria; AAF40580; AAF40580; NMB0121. DR GeneID; 902225; -. DR KEGG; nme:NMB0121; -. DR PATRIC; 20355255; VBINeiMen85645_0161. DR eggNOG; COG1396; LUCA. DR HOGENOM; HOG000025367; -. DR OMA; HWSQEEM; -. DR OrthoDB; EOG6FV87D; -. DR BioCyc; NMEN122586:GHGG-127-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 61 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. FT COILED 94 124 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 125 AA; 14309 MW; 3EBE6F2E55307F15 CRC64; METHEKIRLM RELNKWSQED MAEKLAMSAG GYAKIERGET QLNIPRLEQL AQIFKIDMWD LLKSGGGGMV FQINEGDSGG DIALYASGDV SMKIEFLKME LKHCKEMLEQ KDKEIELLRK LTETV // ID Q9JZW9_NEIMB Unreviewed; 289 AA. AC Q9JZW9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41277.1}; GN OrderedLocusNames=NMB0866 {ECO:0000313|EMBL:AAF41277.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41277.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41277.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41277.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41277.1; -; Genomic_DNA. DR PIR; B81148; B81148. DR RefSeq; NP_273907.1; NC_003112.2. DR RefSeq; WP_002244513.1; NC_003112.2. DR ProteinModelPortal; Q9JZW9; -. DR STRING; 122586.NMB0866; -. DR PaxDb; Q9JZW9; -. DR EnsemblBacteria; AAF41277; AAF41277; NMB0866. DR GeneID; 902980; -. DR KEGG; nme:NMB0866; -. DR PATRIC; 20357121; VBINeiMen85645_1079. DR eggNOG; ENOG4108V2X; Bacteria. DR eggNOG; ENOG4111J0Z; LUCA. DR HOGENOM; HOG000218890; -. DR OMA; KAGNYWM; -. DR OrthoDB; EOG6SNDQS; -. DR BioCyc; NMEN122586:GHGG-897-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR Gene3D; 2.40.160.20; -; 1. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR025737; Phenol_MetA_deg_put. DR Pfam; PF13557; Phenol_MetA_deg; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 289 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327746. SQ SEQUENCE 289 AA; 31744 MW; EF615CE562D6FFAE CRC64; MKRIFLPALP AILPLSTYAD LPLTIEDIMT DKGKWKLETS LTYLNSENNR AELAAPVYIQ TGATSFIPIP TEIQENGSNT DMLVGTLGLR YGLTGNTDIY GSGSYLWHEE RKLDGNSKTR NKRMSDVSLG ISHTFLKDDK NPALISFLES TVYEKSRNKA SSGKSWLIGA TTYKAIDPIV LSLTAAYRIN GSKTLSDGIR YKSGNYLLLN PNISFAANDR ISLTGGIQWL GRQPDRTDGK RESSRNTSTY AHFGAGFGFT KTTALNASAR FNVSGQSSSE LKFGVQHTF // ID Q9K0J2_NEIMB Unreviewed; 369 AA. AC Q9K0J2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Histone deacetylase family protein {ECO:0000313|EMBL:AAF41032.1}; GN OrderedLocusNames=NMB0605 {ECO:0000313|EMBL:AAF41032.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41032.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41032.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41032.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41032.1; -; Genomic_DNA. DR PIR; F81178; F81178. DR RefSeq; NP_273649.1; NC_003112.2. DR RefSeq; WP_002222843.1; NC_003112.2. DR ProteinModelPortal; Q9K0J2; -. DR STRING; 122586.NMB0605; -. DR PaxDb; Q9K0J2; -. DR EnsemblBacteria; AAF41032; AAF41032; NMB0605. DR GeneID; 902719; -. DR KEGG; nme:NMB0605; -. DR PATRIC; 20356495; VBINeiMen85645_0767. DR eggNOG; ENOG4105DGU; Bacteria. DR eggNOG; COG0123; LUCA. DR HOGENOM; HOG000225183; -. DR OMA; VLYFSTH; -. DR OrthoDB; EOG6TN43P; -. DR BioCyc; NMEN122586:GHGG-631-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.800.20; -; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR PANTHER; PTHR10625; PTHR10625; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 41 327 Hist_deacetyl. FT {ECO:0000259|Pfam:PF00850}. SQ SEQUENCE 369 AA; 40604 MW; 69802796B383210D CRC64; MSLTRLILKF YALLRLFLGK NARTAWISHP ACAGHEPGAN HPDSPDRILC IEQALRRAGI WQHLQTIEAE EISDTRLALV HSSKYLNRLE SCLPQKGKIS RLDNDTAIST GSLSAARFAA GSAVQAVDMV MNRKAWHAFC AARPPGHHAG SGKAGGFCLL NNVAAGVMHA IAEYRLKRIA VIDFDVHYGD GTAEIFKDDP RILFFNLFET DLFPFPENND MPDGGNMVHL PLPPGTGSRT FREAVRRQWL PRLAAFKPEL VLLSAGFDAH RLDESGRLNL HEADFAWLTH KIIQTASGCP GKIISVLEGG YTLEPLAQSA AEHIRVLAGL GKSDAATAYQ KTLDPTKKRF AKPKTGQVRQ PTQSDRYDI // ID Q9JZ12_NEIMB Unreviewed; 887 AA. AC Q9JZ12; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156}; DE EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156}; GN Name=pdhA {ECO:0000313|EMBL:AAF41716.1}; GN OrderedLocusNames=NMB1341 {ECO:0000313|EMBL:AAF41716.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41716.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41716.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41716.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, CC that catalyzes the overall conversion of pyruvate to acetyl-CoA CC and CO(2). {ECO:0000256|PIRNR:PIRNR000156}. CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). CC {ECO:0000256|PIRNR:PIRNR000156}. CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|PIRNR:PIRNR000156}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41716.1; -; Genomic_DNA. DR PIR; E81094; E81094. DR RefSeq; NP_274360.1; NC_003112.2. DR RefSeq; WP_002222352.1; NC_003112.2. DR ProteinModelPortal; Q9JZ12; -. DR SMR; Q9JZ12; 58-880. DR STRING; 122586.NMB1341; -. DR PaxDb; Q9JZ12; -. DR PRIDE; Q9JZ12; -. DR EnsemblBacteria; AAF41716; AAF41716; NMB1341. DR GeneID; 903763; -. DR KEGG; nme:NMB1341; -. DR PATRIC; 20358335; VBINeiMen85645_1679. DR eggNOG; ENOG4105DAQ; Bacteria. DR eggNOG; COG2609; LUCA. DR HOGENOM; HOG000115215; -. DR KO; K00163; -. DR OMA; GFVPQRR; -. DR OrthoDB; EOG6BW4TW; -. DR BioCyc; NMEN122586:GHGG-1379-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR004660; 2-oxoA_DH_E1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 5. DR Pfam; PF00456; Transketolase_N; 1. DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00759; aceE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156, KW ECO:0000313|EMBL:AAF41716.1}; KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:AAF41716.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}. FT DOMAIN 137 292 TRANSKETOLASE_1. FT {ECO:0000259|Pfam:PF00456}. SQ SEQUENCE 887 AA; 99562 MW; BA7BA93E38C5206F CRC64; MSTQLHDVDP IETQEWLDAL SSVLEYEGGE RAQYLLENLV KYCRDKGVRM PHGTTTPYLN TVSVENEKGI PGDQNIEHRI RAFVRWNAAA IVLRAGKKDL ELGGHIASFQ SAATMYEVGF NHFWKAKGEG EEGDLVFFQG HVAPGIYARA FVEGRLTEDQ LNNFRQEVDG HGLPSYPHPH LLPDFWQFPT VSMGLGPIMA IYQARFLKYL ESRGLAKTKG RKVWCFCGDG EMDEPESQGA IALAAREGLD NLIFVINCNL QRLDGPVRGN GKIIQELEGN FAGAGWNVVK VIWGRRWDRL LAKDKDGILR QRMEECLDGD YQTYKSKDGA YVREHFFNTP ELKALVADMT DEQLWALNRG GHDPQKVYNA YDRAANHADG KPTVILAKTI KGYGMGASGE GQNVAHQAKK MDKASLKQFR DRFDIPVTDE QIESGDLPYL TFAPDTEEYK YLHARRDALG GYLPQRKPTQ EVLEVPELSA FDAQLKSSGE REFSTTMAFV RILSTLLKDK KIGKRVVPIV PDESRTFGME GMFRQYGIWN PKGQQYTPQD KDQLMFYKES VDGQILQEGI NEPGAMADWI AAATSYANSN FAMIPFYIYY SMFGFQRIGD LAWAAGDMHA RGFLLGGTAG RTTLNGEGLQ HEDGHSHIQA DLIPNCVSYD PTFQYEVAVI VQDGLRRMYA NNEDVFYYIT LMNENYTHPD MPEGAEQDIL KGMYLLKAGG KGDKKVQLMG SGTILQEVIA GAELLKADFG VEADIWSCPS FNLLHRDAVE VERFNRLHPL EAEKVPFVTS QLQGHDGPVI AATDYIRSYA DRIRAYIPND YHVLGTDGFG RSDSRANLRR FFEVDRYNVA VAALAALAEQ GKVSKETVQQ AIEKYGIKAD SAPSWKR // ID Q9JXY9_NEIMB Unreviewed; 219 AA. AC Q9JXY9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Putative phosphoglycolate phosphatase {ECO:0000313|EMBL:AAF42165.1}; GN OrderedLocusNames=NMB1830 {ECO:0000313|EMBL:AAF42165.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42165.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42165.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42165.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42165.1; -; Genomic_DNA. DR PIR; C81038; C81038. DR RefSeq; NP_274827.1; NC_003112.2. DR RefSeq; WP_002222994.1; NC_003112.2. DR ProteinModelPortal; Q9JXY9; -. DR STRING; 122586.NMB1830; -. DR PaxDb; Q9JXY9; -. DR DNASU; 903270; -. DR EnsemblBacteria; AAF42165; AAF42165; NMB1830. DR GeneID; 903270; -. DR KEGG; nme:NMB1830; -. DR PATRIC; 20359649; VBINeiMen85645_2330. DR eggNOG; ENOG4108UKG; Bacteria. DR eggNOG; COG0546; LUCA. DR HOGENOM; HOG000248344; -. DR KO; K01091; -. DR OMA; LIAFDWD; -. DR OrthoDB; EOG600DR0; -. DR BioCyc; NMEN122586:GHGG-1885-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 185 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 219 AA; 23341 MW; 52C104457BF7EB46 CRC64; MTTPKLIIFD WDGTLADTTQ PIIDTMRRSF AECGFPPPEA ERVRSLIGYS LPEIIRTLLE MPSETAVADI TRTYSAHYLN PNNRNMSLFP DALPCLDKLK AQGYWLAVAT GKGRAGLDNA ISQTATGGYW LATACAGEYP SKPSPEMVFG ICGELGLDPK EALVVGDTAH DLHMAANAGA AAVGVATGAH SREQLLSAPH LAVLDGLSEL PGFLAQHYA // ID Q9JZR1_NEIMB Unreviewed; 239 AA. AC Q9JZR1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=tRNA-specific adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_00972}; DE EC=3.5.4.33 {ECO:0000256|HAMAP-Rule:MF_00972}; GN Name=tadA {ECO:0000256|HAMAP-Rule:MF_00972}; GN OrderedLocusNames=NMB0933 {ECO:0000313|EMBL:AAF41340.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41340.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41340.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41340.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the CC wobble position 34 of tRNA(Arg2). {ECO:0000256|HAMAP- CC Rule:MF_00972}. CC -!- CATALYTIC ACTIVITY: Adenine(34) in tRNA + H(2)O = hypoxanthine(34) CC in tRNA + NH(3). {ECO:0000256|HAMAP-Rule:MF_00972}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00972}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00972}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00972}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000256|HAMAP-Rule:MF_00972}. CC -!- SIMILARITY: Contains 1 CMP/dCMP-type deaminase domain. CC {ECO:0000256|HAMAP-Rule:MF_00972}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41340.1; -; Genomic_DNA. DR PIR; H81141; H81141. DR RefSeq; NP_273972.1; NC_003112.2. DR RefSeq; WP_002225332.1; NC_003112.2. DR ProteinModelPortal; Q9JZR1; -. DR STRING; 122586.NMB0933; -. DR PaxDb; Q9JZR1; -. DR DNASU; 903054; -. DR EnsemblBacteria; AAF41340; AAF41340; NMB0933. DR GeneID; 903054; -. DR KEGG; nme:NMB0933; -. DR PATRIC; 20357335; VBINeiMen85645_1182. DR eggNOG; ENOG4108Z6B; Bacteria. DR eggNOG; COG0590; LUCA. DR eggNOG; COG3070; LUCA. DR HOGENOM; HOG000085050; -. DR OMA; RIGRIFF; -. DR OrthoDB; EOG64FKGZ; -. DR BioCyc; NMEN122586:GHGG-971-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00972; tRNA_aden_deaminase; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR007077; TfoX_C. DR InterPro; IPR028883; tRNA_aden_deaminase. DR Pfam; PF14437; MafB19-deam; 1. DR Pfam; PF04994; TfoX_C; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00972}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00972}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00972}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00972}. FT DOMAIN 90 223 CMP/dCMP-type deaminase. FT {ECO:0000256|HAMAP-Rule:MF_00972, FT ECO:0000259|PROSITE:PS51747}. FT ACT_SITE 143 143 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_00972}. FT METAL 141 141 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00972}. FT METAL 141 141 Zinc; via pros nitrogen; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00972}. FT METAL 171 171 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00972}. FT METAL 174 174 Zinc; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00972}. SQ SEQUENCE 239 AA; 25988 MW; AF3444A8C60438FE CRC64; MLTTPPLAPK TVAALHRLGI RTLEELRQNG SVKAFLLLKA SGLTLTKSTL WQLESLLDGT PPQEMSQAHK ARLLAELKNH PPVAAFPPQE EMEHFMCEAL RQAEQSSADG EIPVGAVIVS DGKIIASAHN TCIADCNVSR HAEINALAQA GREIQNYRLD GCDIYITLEP CAMCASALIQ ARIRRVIYGA AEPKTGAAGS IVNLFADKRL NTHTAIRGGI LQEECRAVLS RFFQNKRKG // ID Q9K0J0_NEIMB Unreviewed; 618 AA. AC Q9K0J0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463, GN ECO:0000313|EMBL:AAF41034.1}; GN OrderedLocusNames=NMB0607 {ECO:0000313|EMBL:AAF41034.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41034.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41034.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41034.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000256|HAMAP- CC Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}. CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF-YajC and YidC. {ECO:0000256|HAMAP- CC Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01463}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01463}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41034.1; -; Genomic_DNA. DR PIR; H81178; H81178. DR RefSeq; NP_273651.1; NC_003112.2. DR RefSeq; WP_010980818.1; NC_003112.2. DR ProteinModelPortal; Q9K0J0; -. DR STRING; 122586.NMB0607; -. DR PaxDb; Q9K0J0; -. DR EnsemblBacteria; AAF41034; AAF41034; NMB0607. DR GeneID; 902721; -. DR KEGG; nme:NMB0607; -. DR PATRIC; 20356499; VBINeiMen85645_0769. DR eggNOG; ENOG4107QN8; Bacteria. DR eggNOG; COG0342; LUCA. DR HOGENOM; HOG000018637; -. DR KO; K03072; -. DR OMA; AAPMEII; -. DR OrthoDB; EOG6N0HJT; -. DR BioCyc; NMEN122586:GHGG-633-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01463_B; SecD_B; 1. DR InterPro; IPR005791; SecD. DR InterPro; IPR027398; SecD-TM. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF13721; SecD-TM1; 1. DR Pfam; PF02355; SecD_SecF; 1. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR01129; secD; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}. FT TRANSMEM 10 30 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 438 458 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 462 482 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 491 511 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 548 568 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 571 591 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT DOMAIN 2 104 SecD-TM1. {ECO:0000259|Pfam:PF13721}. SQ SEQUENCE 618 AA; 66847 MW; F4F805FB28B0AF10 CRC64; MMNRYPLWKY LLIVFTIAVA AVYSLPNLFG ETPAVQVSTN RQAIIINEQT QFKVDAALKN AGIQTDGMFV VDNSLKVRFK DTETQLKARD VIENTLGEGY ITALNLLADS PEWMAKIKAN PMFLGLDLRG GVHFTMQVDM KAAMQKTFER YSGDIRRELR REKIRSGTVR QAGNSLTVPL QDAGDVQKAL PQLRKLFPEA TLNSDGSNIV LTLSEEAVNK VCSDAVKQNI TTLHNRVNEL GVAEPVIQQS GADRIVVQLP GVQDTAKAKD IIGRTATLEL RMVEDDPAKL REALEGNVPS GYELLSSGGD RPEILLISKQ VELTGDNIND AQPSFDQMGA PAVSLSLDSA GGSIFGELTA ANVGKRMAMV LIDQGKSEVV TAPVIRTAIT GGRVEISGSM TTAEANDTSL LLRAGSLAAP MQIVEERTIG PSLGKENIEK GFHSTLWGFA IVAAFMVVYY RLMGFFSTIA LSANILFLIG ILSAMQATLT LPGMAALALT LGMAIDSNVL INERIREELR AGVPPQQAIN LGFQHAWATI VDSNLTSLIA GIALLVFGSG PVRGFAVVHC LGILTSMYSS VVVFRALVNL WYGRRRKLQN ISIGSVWKPK AEMAGGKE // ID Q9JYS0_NEIMB Unreviewed; 659 AA. AC Q9JYS0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996}; DE EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996}; GN Name=tktA {ECO:0000313|EMBL:AAF41816.1}; GN OrderedLocusNames=NMB1457 {ECO:0000313|EMBL:AAF41816.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41816.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41816.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41816.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from CC a ketose donor to an aldose acceptor, via a covalent intermediate CC with the cofactor thiamine pyrophosphate. CC {ECO:0000256|RuleBase:RU004996}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. CC {ECO:0000256|RuleBase:RU004996}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU004996}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU004996}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU004996}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|RuleBase:RU004996}; CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other CC divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). CC {ECO:0000256|RuleBase:RU004996}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|RuleBase:RU004996}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000256|RuleBase:RU004996}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}. CC -!- SIMILARITY: Belongs to the transketolase family. CC {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS00570687}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41816.1; -; Genomic_DNA. DR PIR; B81082; B81082. DR RefSeq; NP_274468.1; NC_003112.2. DR RefSeq; WP_002244175.1; NC_003112.2. DR ProteinModelPortal; Q9JYS0; -. DR SMR; Q9JYS0; 3-659. DR STRING; 122586.NMB1457; -. DR PaxDb; Q9JYS0; -. DR EnsemblBacteria; AAF41816; AAF41816; NMB1457. DR GeneID; 903879; -. DR KEGG; nme:NMB1457; -. DR PATRIC; 20358657; VBINeiMen85645_1838. DR eggNOG; ENOG4105CV1; Bacteria. DR eggNOG; COG0021; LUCA. DR HOGENOM; HOG000225954; -. DR KO; K00615; -. DR OMA; WEVLYVE; -. DR OrthoDB; EOG6N3CRG; -. DR BioCyc; NMEN122586:GHGG-1497-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR005478; Transketolase_bac-like. DR InterPro; IPR020826; Transketolase_BS. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR Pfam; PF00456; Transketolase_N; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00232; tktlase_bact; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU004996}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|RuleBase:RU004996, KW ECO:0000256|SAAS:SAAS00460037}; KW Metal-binding {ECO:0000256|RuleBase:RU004996, KW ECO:0000256|SAAS:SAAS00460052}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996, KW ECO:0000256|SAAS:SAAS00459980}; KW Transferase {ECO:0000256|RuleBase:RU004996, KW ECO:0000256|SAAS:SAAS00460013, ECO:0000313|EMBL:AAF41816.1}. FT DOMAIN 9 29 TRANSKETOLASE_1. FT {ECO:0000259|PROSITE:PS00801}. SQ SEQUENCE 659 AA; 71658 MW; 54C9519D37D171F1 CRC64; MSQLANAIRF LSADAVQKAN SGHPGAPMGM AEMAETLWTK FLNHNPANPK FYNRDRFVLS NGHASMLLYS LLHLTGYNLS IEDLKNFRQL HSKTPGHPEY GYTDGVETTT GPLGQGIANA VGMALAEKIL AAEFNKDGLN IVDHYTYVFM GDGCLMEGVS HEACSLAGTL GLGKLIVLYD DNNISIDGKV DGWFTENIPQ RFESYGWHVV PNVNGHDTAA IQAAIEAARA ETGKPSIICC KTLIGKGSAN KEGSHKTHGA PLGADEIEAT RKHLGWTYPA FEIPQEIYDA WNAKEQGAKL EADWNELFAQ YQAKYPAEAA EFVRRMDKKL PDNFDEYVQA ALKEVCAKAE TIATRKASQN SIEILAKELP ELVGGSADLT PSNLTDWSNS VSVTRDKGGN YIHYGVREFG MGAIMNGLVL HGGVKPFGAT FLMFSEYERN ALRMAALMKI NPVFVFTHDS IGLGEDGPTH QPIEQTATLR LIPNMDVWRP CDTAESLVAW AEAVKAADHP SCLIFSRQNL KFQARSEQQL NDIKRGGYVI SEAQGNAQAV IIATGSEVEL ALEAQKALAA QNIAVRVVSM PSTNVFDRQD AAYQAAVLPE GLPRIAVEAG HADGWYKYVG LNGAVVGINR FGESAPADLL FKAFGFTVDN VVDTVKSVL // ID Q9JXD9_NEIMB Unreviewed; 259 AA. AC Q9JXD9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974}; DE Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974}; DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000256|HAMAP-Rule:MF_01974, GN ECO:0000313|EMBL:AAF42410.1}; GN OrderedLocusNames=NMB2093 {ECO:0000313|EMBL:AAF42410.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42410.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42410.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42410.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. CC The N-terminal methionine is often cleaved when the second residue CC in the primary sequence is small and uncharged (Met-Ala-, Cys, CC Gly, Pro, Ser, Thr, or Val). Requires deformylation of the CC N(alpha)-formylated initiator methionine before it can be CC hydrolyzed. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Note=Binds 2 divalent metal cations per subunit. Has a high- CC affinity and a low affinity metal-binding site. The true nature of CC the physiological cofactor is under debate. The enzyme is active CC with cobalt, zinc, manganese or divalent iron ions. Most likely, CC methionine aminopeptidases function as mononuclear Fe(2+)- CC metalloproteases under physiological conditions, and the CC catalytically relevant metal-binding site has been assigned to the CC histidine-containing high-affinity site. {ECO:0000256|HAMAP- CC Rule:MF_01974}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42410.1; -; Genomic_DNA. DR PIR; C81008; C81008. DR RefSeq; NP_275081.1; NC_003112.2. DR RefSeq; WP_002218216.1; NC_003112.2. DR ProteinModelPortal; Q9JXD9; -. DR SMR; Q9JXD9; 4-256. DR STRING; 122586.NMB2093; -. DR PaxDb; Q9JXD9; -. DR EnsemblBacteria; AAF42410; AAF42410; NMB2093. DR GeneID; 903955; -. DR KEGG; nme:NMB2093; -. DR PATRIC; 20360356; VBINeiMen85645_2675. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR HOGENOM; HOG000030427; -. DR KO; K01265; -. DR OMA; VIKDEYH; -. DR OrthoDB; EOG6MWNDS; -. DR BioCyc; NMEN122586:GHGG-2158-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR002467; Pept_M24A_MAP1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; SSF55920; 1. DR TIGRFAMs; TIGR00500; met_pdase_I; 1. DR PROSITE; PS00680; MAP_1; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAF42410.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAF42410.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAF42410.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 13 244 Peptidase_M24. FT {ECO:0000259|Pfam:PF00557}. FT METAL 99 99 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 110 110 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 110 110 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 173 173 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01974}. FT METAL 206 206 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 237 237 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 237 237 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT BINDING 82 82 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01974}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01974}. SQ SEQUENCE 259 AA; 28246 MW; D2914718F9278398 CRC64; MNGIIIKTPE EIEKMRELGK LVAEALDYIG QFVKPGVTTD EIDKLVYDYH VNVQGGYPAP LHYGNPPYPK SCCTSVNHVI CHGIPDDKPL KEGDIINIDL TIKKDGFHGD SSRMFTVGKV SPIAQRLIDV THASMMAGIE AVKPGATLGD VGYACQQVAE NAGYSVVQEF CGHGIGRGFH EAPQVLHYGK KGQGPVLKPG MIFTVEPMIN QGKRHLRILN DGWTVVTKDR SLSAQWEHEV LVTETGYEIL TVSPASGKP // ID Q9K018_NEIMB Unreviewed; 265 AA. AC Q9K018; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41222.1}; GN OrderedLocusNames=NMB0809 {ECO:0000313|EMBL:AAF41222.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41222.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41222.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41222.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41222.1; -; Genomic_DNA. DR PIR; H81155; H81155. DR RefSeq; NP_273851.1; NC_003112.2. DR RefSeq; WP_002225414.1; NC_003112.2. DR ProteinModelPortal; Q9K018; -. DR STRING; 122586.NMB0809; -. DR PaxDb; Q9K018; -. DR EnsemblBacteria; AAF41222; AAF41222; NMB0809. DR GeneID; 902924; -. DR KEGG; nme:NMB0809; -. DR PATRIC; 20357005; VBINeiMen85645_1021. DR eggNOG; ENOG4107SRH; Bacteria. DR eggNOG; COG0451; LUCA. DR HOGENOM; HOG000218867; -. DR OMA; QPVNLVH; -. DR OrthoDB; EOG6SZ1GS; -. DR BioCyc; NMEN122586:GHGG-840-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 265 AA; 29361 MW; 31318C073865CDD7 CRC64; MRAVPPPHIS ITGLGYLGLP LAQKFYQHGS RVAAVKRSLT SDDINLPIHL DTIDLNQDSA FQSANLARDT SFWRHHANKP VWFCLLPPSS LTHYADTVKQ WAELARACNV QHLIFTSSTS VYGDTARECD EIALPDPQTE SARQILAAEQ HLLDSGVPNI DILRLGGLYC AERHPVGRLV QKQNIPGGNR PINIVHRNIA VESLFQTAFN PGGRRLKNII EPRHPTRREF YTEEAAKLGL PAPDFAPDDS VGKIIRTVCD NGLSL // ID Q9JXR1_NEIMB Unreviewed; 248 AA. AC Q9JXR1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=3-oxoacyl-(Acyl-carrier-protein) reductase {ECO:0000313|EMBL:AAF42251.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AAF42251.1}; GN Name=fabG-2 {ECO:0000313|EMBL:AAF42251.1}; GN OrderedLocusNames=NMB1921 {ECO:0000313|EMBL:AAF42251.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42251.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42251.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42251.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42251.1; -; Genomic_DNA. DR PIR; E81026; E81026. DR RefSeq; NP_274915.1; NC_003112.2. DR RefSeq; WP_002225822.1; NC_003112.2. DR ProteinModelPortal; Q9JXR1; -. DR SMR; Q9JXR1; 5-247. DR STRING; 122586.NMB1921; -. DR PaxDb; Q9JXR1; -. DR EnsemblBacteria; AAF42251; AAF42251; NMB1921. DR GeneID; 904233; -. DR KEGG; nme:NMB1921; -. DR PATRIC; 20359889; VBINeiMen85645_2449. DR eggNOG; ENOG4105CHR; Bacteria. DR eggNOG; ENOG410XNW1; LUCA. DR KO; K00059; -. DR OMA; GMMKRRW; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NMEN122586:GHGG-1978-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011284; 3oxo_ACP_reduc. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42251.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 248 AA; 26068 MW; D5FAC9F11E6FA6D6 CRC64; MSTQDLNGKI ALVTGASRGI GAAIADTLAA AGAKVIGTAT SESGAAAISE RLAQWGGEGR VLNSAEPETI ESLIADIEKA FGKLDILVNN AGITRDNLLM RMKEEEWDDI MQVNLKSVFR ASKAVLRGMM KQRSGRIINI TSVVGVMGNA GQTNYAAAKA GLIGFSKSMA REVGSRGITV NCVAPGFIDT DMTRALPEET RQTFTAQTAL GRFGDAQDIA DAVLFLASDQ AKYITGQTLH VNGGMLMP // ID Q9K1G2_NEIMB Unreviewed; 257 AA. AC Q9K1G2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=ParA family protein {ECO:0000313|EMBL:AAF40648.1}; GN OrderedLocusNames=NMB0191 {ECO:0000313|EMBL:AAF40648.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40648.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40648.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40648.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40648.1; -; Genomic_DNA. DR PIR; D81227; D81227. DR RefSeq; NP_273249.1; NC_003112.2. DR RefSeq; WP_002221868.1; NC_003112.2. DR ProteinModelPortal; Q9K1G2; -. DR STRING; 122586.NMB0191; -. DR PaxDb; Q9K1G2; -. DR EnsemblBacteria; AAF40648; AAF40648; NMB0191. DR GeneID; 902299; -. DR KEGG; nme:NMB0191; -. DR PATRIC; 20355409; VBINeiMen85645_0233. DR eggNOG; ENOG4107QJE; Bacteria. DR eggNOG; COG1192; LUCA. DR HOGENOM; HOG000019422; -. DR KO; K03496; -. DR OMA; GVIVPMQ; -. DR OrthoDB; EOG6D8BCX; -. DR BioCyc; NMEN122586:GHGG-202-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025669; AAA_dom. DR InterPro; IPR000392; Nitogenase_NifH/Reductase_ChlL. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13614; AAA_31; 1. DR PRINTS; PR00091; NITROGNASEII. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 257 AA; 27150 MW; 0630BAF3D73159BD CRC64; MSANILAIAN QKGGVGKTTT TVNLAASLAS RGKRVLVVDL DPQGNATTGS GIDKAGLQSG VYQVLLGDAD VQSAAVRSKE GGYAVLGANR ALAGAEIELV QEIAREVRLK NALKAVEEDY DFILIDCPPS LTLLTLNGLV AAGGVIVPML CEYYALEGIS DLIATVRKIR QAVNPDLDIT GIVRTMYDSR SRLVAEVSEQ LRSHFGDLLF ETVIPRNIRL AEAPSHGMPV MAYDAQAKGT KAYLALADEL AARVSGK // ID Q9JZY3_NEIMB Unreviewed; 138 AA. AC Q9JZY3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41261.1}; GN OrderedLocusNames=NMB0850 {ECO:0000313|EMBL:AAF41261.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41261.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41261.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41261.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41261.1; -; Genomic_DNA. DR PIR; E81149; E81149. DR RefSeq; NP_273891.1; NC_003112.2. DR RefSeq; WP_002225396.1; NC_003112.2. DR ProteinModelPortal; Q9JZY3; -. DR STRING; 122586.NMB0850; -. DR PaxDb; Q9JZY3; -. DR EnsemblBacteria; AAF41261; AAF41261; NMB0850. DR GeneID; 902964; -. DR KEGG; nme:NMB0850; -. DR PATRIC; 20357091; VBINeiMen85645_1064. DR eggNOG; COG4642; LUCA. DR HOGENOM; HOG000218875; -. DR OMA; TYDGDVG; -. DR OrthoDB; EOG6CVVDC; -. DR BioCyc; NMEN122586:GHGG-881-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR003409; MORN. DR Pfam; PF02493; MORN; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 138 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327749. SQ SEQUENCE 138 AA; 15199 MW; A2157570DC828D8E CRC64; MLKHLAFLLP AMMFALPTSA AVLTSYQEPG CTYDGNVGKD GKPAGKGTWR CQDGRNYTGS FKNGKFDGQG VYTVAANREI FIEPFNSDST KFRNMVLSGT FKKGLAHGRF TVSQNGETLF IMKCENGMIK EVKLPKNK // ID Q9K1K0_NEIMB Unreviewed; 768 AA. AC Q9K1K0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000256|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952}; GN Name=topA {ECO:0000256|HAMAP-Rule:MF_00952, GN ECO:0000313|EMBL:AAF40577.1}; GN OrderedLocusNames=NMB0118 {ECO:0000313|EMBL:AAF40577.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40577.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40577.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40577.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000256|HAMAP- CC Rule:MF_00952, ECO:0000256|SAAS:SAAS00046667}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00952}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952, CC ECO:0000256|SAAS:SAAS00535586}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00553561}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP- CC Rule:MF_00952}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40577.1; -; Genomic_DNA. DR PIR; H81236; H81236. DR RefSeq; NP_273176.1; NC_003112.2. DR RefSeq; WP_002224768.1; NC_003112.2. DR ProteinModelPortal; Q9K1K0; -. DR STRING; 122586.NMB0118; -. DR PaxDb; Q9K1K0; -. DR EnsemblBacteria; AAF40577; AAF40577; NMB0118. DR GeneID; 902222; -. DR KEGG; nme:NMB0118; -. DR PATRIC; 20355249; VBINeiMen85645_0158. DR eggNOG; ENOG4105C73; Bacteria. DR eggNOG; COG0550; LUCA. DR eggNOG; COG0551; LUCA. DR HOGENOM; HOG000004018; -. DR KO; K03168; -. DR OMA; RIKYNEI; -. DR OrthoDB; EOG6S7XQ9; -. DR BioCyc; NMEN122586:GHGG-124-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 2.70.20.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 3. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 2. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00440074}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00440015}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00535572}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00535563}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00440015}. FT DOMAIN 3 117 Toprim. {ECO:0000259|PROSITE:PS50880}. FT REGION 167 172 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT COILED 615 642 {ECO:0000256|SAM:Coils}. FT ACT_SITE 304 304 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00952}. FT METAL 9 9 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00952}. FT METAL 82 82 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00952}. FT METAL 82 82 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT METAL 84 84 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 33 33 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 143 143 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 144 144 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 147 147 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 159 159 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 306 306 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 497 497 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 768 AA; 87066 MW; 8F6F77C3F325376E CRC64; MAKNLLIVES PSKAKTLKKY LGGDFEILAS YGHVRDLVPK SGAVDPDNGF AMKYQLISRN GKHVDAIVAG AKEAENIYLA TDPDREGEAI SWHLLEILKS KRGLKNIKPQ RVVFHEITKN AVLDAVAHPR EIEMDLVDAQ QARRALDYLV GFNLSPLLWK KIRRGLSAGR VQSPALRLIC ERENEIRAFE AQEYWTVHLD SHKGRSKFTA KLAQYNGAKL EQFDLPNEAA QADVLKELEG KEAVVTAIEK KKRSRNPAAP FTTSTMQQDA VRKLGFTTDR TMRTAQQLYE GIDVGQGAIG LITYMRTDSV NLADEALTEI RHYIENKIGK EYLPSAAKQY KTKSKNAQEA HEAIRPTSVY RTPESVKPFL SADQFKLYQM IWQRTVACQM TPAKFDQTTV DITVGKGVFR VTGQVQTFAG FLSVYEESSD DEEGEDSKKL PEMSEGDKLP VDKLYGEQHF TTPPPRYNEA TLVKALEEYG IGRPSTYASI ISTLKDREYV TLEQKRFMPT DTGDIVNKFL TEHFAQYVDY HFTAKLEDQL DEIADGKRQW IPLMDKFWKP FIKQVEEKEG IERAKFTTQE LDETCPKCGE HKLQIKFGKM GRFVACAGYP ECSYTRNVNE TAEEAAERIA KAEAEQAELD GRECPKCGGR LVYKYSRTGS KFIGCVNYPK CKHVEPLEKP KDTGVQCPQC KKGNLVERKS RYGKLFYSCS TYPDCNYATW NPPVAEECLN CHWPVLTIKT TKRWGVEKVC PQKECGWKEQ IEPPAPKE // ID Q9JZR7_NEIMB Unreviewed; 148 AA. AC Q9JZR7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Acyl CoA thioester hydrolase family protein {ECO:0000313|EMBL:AAF41333.1}; GN OrderedLocusNames=NMB0925 {ECO:0000313|EMBL:AAF41333.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41333.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41333.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41333.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41333.1; -; Genomic_DNA. DR PIR; A81141; A81141. DR RefSeq; NP_273965.1; NC_003112.2. DR RefSeq; WP_002219418.1; NC_003112.2. DR ProteinModelPortal; Q9JZR7; -. DR SMR; Q9JZR7; 7-141. DR STRING; 122586.NMB0925; -. DR PaxDb; Q9JZR7; -. DR EnsemblBacteria; AAF41333; AAF41333; NMB0925. DR GeneID; 903046; -. DR KEGG; nme:NMB0925; -. DR PATRIC; 20357299; VBINeiMen85645_1163. DR eggNOG; ENOG4105NAU; Bacteria. DR eggNOG; COG1607; LUCA. DR HOGENOM; HOG000044841; -. DR KO; K10806; -. DR OMA; VNVEVWV; -. DR OrthoDB; EOG676Z6F; -. DR BioCyc; NMEN122586:GHGG-963-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR033120; HOTDOG_ACOT. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR006683; Thioestr_dom. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR PROSITE; PS51770; HOTDOG_ACOT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41333.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 127 HotDog ACOT-type. FT {ECO:0000259|PROSITE:PS51770}. SQ SEQUENCE 148 AA; 16332 MW; 28E9B40D502D80B4 CRC64; MQHEEGNRQR PQGELLLRTV AMPRDTNPNQ DIFGGWIMSQ MDLGGGILAA EIARGRIVTV AVQEMNFIRP VKVGNVVCCY GHCVRVGNTS LQLKVDVWVK TLMNDCVTED RYLVTEAVFT YVAIDAEGNP RPIPKEGNPK LAGLLPTP // ID Q9JYZ4_NEIMB Unreviewed; 350 AA. AC Q9JYZ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887}; GN OrderedLocusNames=NMB1361 {ECO:0000313|EMBL:AAF41735.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41735.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41735.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41735.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family. CC {ECO:0000256|RuleBase:RU003887, ECO:0000256|SAAS:SAAS00545889}. CC -!- SIMILARITY: Contains S4 RNA-binding domain. CC {ECO:0000256|SAAS:SAAS00568442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41735.1; -; Genomic_DNA. DR PIR; B81092; B81092. DR RefSeq; NP_274379.1; NC_003112.2. DR RefSeq; WP_010980926.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ4; -. DR STRING; 122586.NMB1361; -. DR PaxDb; Q9JYZ4; -. DR EnsemblBacteria; AAF41735; AAF41735; NMB1361. DR GeneID; 903783; -. DR KEGG; nme:NMB1361; -. DR PATRIC; 20358385; VBINeiMen85645_1704. DR eggNOG; ENOG4105FE9; Bacteria. DR eggNOG; COG1187; LUCA. DR HOGENOM; HOG000044954; -. DR KO; K06178; -. DR OMA; MEEWINN; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; NMEN122586:GHGG-1399-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 98 159 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 350 AA; 39510 MW; BED04AED800D4111 CRC64; MMSKQPTSKR QWRDGAAPSA KKTAKPFKSK ARPKDETGKT ASQPYGQKAS DGIKPQNVPK QRAAKAKKLV VRNPNQKIME HARDLKERRS DLSRMEPERL QKVLAASGVG SRREMEEWIT NGWITVNGKT AQLGDKVTPD DHVTVKGSII KLKWADRLPR IILYYKQEGE IVSRDDPQGR VSIFDRLPQA ASSRWVAIGR LDINTSGLLI LTTSGELVQR FAHPSFEVER EYAVRVLGGL TGEQMRVLTE EGVMLEDGLA KVERIREQGG EGANKWYNVV IKEGRNREVR RIFESQGLTV SRLVRIGFGP IGLPNRLKRG QFYELNPAEV ANIIKWADML LPGERRRKKA // ID Q9JXH7_NEIMB Unreviewed; 591 AA. AC Q9JXH7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|PIRNR:PIRNR000732}; DE EC=2.7.3.9 {ECO:0000256|PIRNR:PIRNR000732}; DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|PIRNR:PIRNR000732}; GN Name=ptsI {ECO:0000313|EMBL:AAF42364.1}; GN OrderedLocusNames=NMB2044 {ECO:0000313|EMBL:AAF42364.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42364.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42364.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42364.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: General (non sugar-specific) component of the CC phosphoenolpyruvate-dependent sugar phosphotransferase system CC (sugar PTS). This major carbohydrate active-transport system CC catalyzes the phosphorylation of incoming sugar substrates CC concomitantly with their translocation across the cell membrane. CC Enzyme I transfers the phosphoryl group from phosphoenolpyruvate CC (PEP) to the phosphoryl carrier protein (HPr). CC {ECO:0000256|PIRNR:PIRNR000732}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine = CC pyruvate + protein N(pi)-phospho-L-histidine. CC {ECO:0000256|PIRNR:PIRNR000732}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000732, CC ECO:0000256|PIRSR:PIRSR000732-3}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000732}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|SAAS:SAAS00563041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42364.1; -; Genomic_DNA. DR PIR; H81012; H81012. DR RefSeq; NP_275034.1; NC_003112.2. DR RefSeq; WP_002225691.1; NC_003112.2. DR ProteinModelPortal; Q9JXH7; -. DR STRING; 122586.NMB2044; -. DR PaxDb; Q9JXH7; -. DR EnsemblBacteria; AAF42364; AAF42364; NMB2044. DR GeneID; 904047; -. DR KEGG; nme:NMB2044; -. DR PATRIC; 20360242; VBINeiMen85645_2621. DR eggNOG; ENOG4105BZ3; Bacteria. DR eggNOG; COG1080; LUCA. DR HOGENOM; HOG000278513; -. DR KO; K08483; -. DR OMA; RSFSMHP; -. DR OrthoDB; EOG657JBQ; -. DR BioCyc; NMEN122586:GHGG-2107-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 1.10.274.10; -; 1. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.50.30.10; -; 1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR024692; PTS_EI. DR InterPro; IPR006318; PTS_EI-like. DR InterPro; IPR008731; PTS_EIN. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF05524; PEP-utilisers_N; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR PIRSF; PIRSF000732; PTS_enzyme_I; 1. DR SUPFAM; SSF47831; SSF47831; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01417; PTS_I_fam; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000732}; KW Kinase {ECO:0000256|PIRNR:PIRNR000732}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000732, KW ECO:0000256|PIRSR:PIRSR000732-3}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000732, KW ECO:0000256|PIRSR:PIRSR000732-3}; KW Phosphotransferase system {ECO:0000256|PIRNR:PIRNR000732}; KW Pyruvate {ECO:0000313|EMBL:AAF42364.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Sugar transport {ECO:0000256|PIRNR:PIRNR000732}; KW Transferase {ECO:0000256|PIRNR:PIRNR000732}; KW Transport {ECO:0000256|PIRNR:PIRNR000732}. FT DOMAIN 6 129 PEP-utilisers_N. FT {ECO:0000259|Pfam:PF05524}. FT DOMAIN 160 230 PEP-utilizers. FT {ECO:0000259|Pfam:PF00391}. FT DOMAIN 257 548 PEP-utilizers_C. FT {ECO:0000259|Pfam:PF02896}. FT ACT_SITE 194 194 Tele-phosphohistidine intermediate. FT {ECO:0000256|PIRSR:PIRSR000732-1}. FT ACT_SITE 510 510 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000732-1}. FT METAL 439 439 Magnesium. FT {ECO:0000256|PIRSR:PIRSR000732-3}. FT METAL 463 463 Magnesium. FT {ECO:0000256|PIRSR:PIRSR000732-3}. FT BINDING 301 301 Substrate. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 337 337 Substrate. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 439 439 Substrate. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 460 460 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 461 461 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 462 462 Substrate. FT {ECO:0000256|PIRSR:PIRSR000732-2}. FT BINDING 463 463 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000732-2}. SQ SEQUENCE 591 AA; 65144 MW; 25BFD965C8A101D9 CRC64; MSIVLHGVAA GKGIAVGCAH LIARGTEEVP QYDVAEADTD AEAERFDAAV KATRKELEQL RSAIPENAPT ELGAFISLHL MLLTDVTLSR EPVDILREQK INAEWALKQQ SDKLAAQFDN MDDAYLRERK QDMLQVVRRI HNNLIGQGNE LEVADNLFDE TVLIANDLSP ADTVLFKEQR IAAFVTDAGG PTGHTAILGR SLDIPSVVGL HNARKLITEG ETVIVDGING VLIIAPDESV LNEYRRRARE YRSHKRDLNK LKKTAAATAD GVCIELVGNI ESAEDVKPLH NLGADGIGLF RSEFLYLNRD TMPSEDEQYE VYSAIVKKMK GKSVTIRTVD LGVDKNPRWF GKNSTPNGSL NPALGMTGIR LCLAEPVMFR TQMRAILRAA VHGPVRMMWP MITSVSEVRQ CLIHLDTAQR QLAERGDAFG KVGIGCMIEI PSAALTVGSI LKLVDFISVG TNDLIQYILS VDRGDDSVSH LYQPGHPAVL KMLQHVIRTA NRMDKDVSVC GEMAGDTAFT RVLLGMGLRR FSMNPNNILP VKNIILHSNV GQLESDIVKV IRCEDEEKSE KLIKQMNSVS VEEEADFKGR K // ID Q9JXN8_NEIMB Unreviewed; 201 AA. AC Q9JXN8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Stringent starvation protein A {ECO:0000313|EMBL:AAF42282.1}; GN Name=sspA {ECO:0000313|EMBL:AAF42282.1}; GN OrderedLocusNames=NMB1953 {ECO:0000313|EMBL:AAF42282.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42282.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42282.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42282.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|RuleBase:RU003494}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42282.1; -; Genomic_DNA. DR PIR; B81024; B81024. DR RefSeq; NP_274947.1; NC_003112.2. DR RefSeq; WP_002214825.1; NC_003112.2. DR ProteinModelPortal; Q9JXN8; -. DR STRING; 122586.NMB1953; -. DR PaxDb; Q9JXN8; -. DR EnsemblBacteria; AAF42282; AAF42282; NMB1953. DR GeneID; 904197; -. DR KEGG; nme:NMB1953; -. DR PATRIC; 20359965; VBINeiMen85645_2487. DR eggNOG; ENOG4107MKT; Bacteria. DR eggNOG; COG0625; LUCA. DR HOGENOM; HOG000255228; -. DR KO; K03599; -. DR OMA; RIVLYEK; -. DR OrthoDB; EOG6MWN8X; -. DR BioCyc; NMEN122586:GHGG-2010-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 78 GST N-terminal. FT {ECO:0000259|PROSITE:PS50404}. FT DOMAIN 83 201 GST C-terminal. FT {ECO:0000259|PROSITE:PS50405}. SQ SEQUENCE 201 AA; 23165 MW; 89E804E4591C36D1 CRC64; MMTLYSGITC PFSHRCRFVL YEKGMDFEIK DVDIYNKPED LAVMNPYNQV PVLVERDLVL HESNIINEYI DERFPHPQLM PGDPVMRGRG RLVLYRMEKE LFNHVQVLEN PAATNKEQAK AREAIGNGLT MLAPSFSKSK YILGEDFSMI DVALAPLLWR LDHYDVKLGK SAAPLLKYAE RIFQREAFIE ALTPAEKAMR K // ID Q9K177_NEIMB Unreviewed; 456 AA. AC Q9K177; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306, GN ECO:0000313|EMBL:AAF40746.1}; GN OrderedLocusNames=NMB0295 {ECO:0000313|EMBL:AAF40746.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40746.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40746.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40746.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic CC signal sequence of the ribosome-nascent chain (RNC) as it emerges CC from the ribosomes. The SRP-RNC complex is then targeted to the CC cytoplasmic membrane where it interacts with the SRP receptor CC FtsY. Interaction with FtsY leads to the transfer of the RNC CC complex to the Sec translocase for insertion into the membrane, CC the hydrolysis of GTP by both Ffh and FtsY, and the dissociation CC of the SRP-FtsY complex into the individual components. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which CC is responsible for interactions with the ribosome, the central G CC domain, which binds GTP, and the C-terminal M domain, which binds CC the RNA and the signal sequence of the RNC. {ECO:0000256|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40746.1; -; Genomic_DNA. DR PIR; F81215; F81215. DR RefSeq; NP_273349.1; NC_003112.2. DR RefSeq; WP_002215706.1; NC_003112.2. DR ProteinModelPortal; Q9K177; -. DR SMR; Q9K177; 2-429. DR STRING; 122586.NMB0295; -. DR PaxDb; Q9K177; -. DR EnsemblBacteria; AAF40746; AAF40746; NMB0295. DR GeneID; 902406; -. DR KEGG; nme:NMB0295; -. DR PATRIC; 20355694; VBINeiMen85645_0371. DR eggNOG; ENOG4105CB9; Bacteria. DR eggNOG; COG0541; LUCA. DR HOGENOM; HOG000036164; -. DR KO; K03106; -. DR OMA; MLPGMGQ; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; NMEN122586:GHGG-310-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW. DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.10.260.30; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR004780; SRP_Ffh. DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47446; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00306}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 269 282 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 107 114 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 190 194 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 248 251 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT COILED 13 40 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 49515 MW; 3E362F1D1F193749 CRC64; MLDNLTGRFS NVFKNIRGQA KLTEDNIKEA LREVRLALLE ADVALPVVKE FINNVKEKAL GQEVAGSLTP DQAFIGVVNK ALTELMGREN KTLDLSVAPP AVVLMAGLQG AGKTTTVGKL ARLLKNDQKK KVLVVSADVY RPAAIEQLRL LAEQVGVDFF PSDTNQKPVE IATAAVDYAK KHFYDVLMVD TAGRLAIDEE MMNEIKALHA AVNPVETLFV IDAMLGQDAV NTAQAFNEAL PLTGVVLTKM DGDSRGGAAL SVRHVTGKPI KFIGVGEKIN GLEPFHPDRL AGRILGMGDV LTLIEDVQKG IDEEAAAKMA KKLHKGKGFD LNDFKEQIQQ MRNMGGLENL MSKMPGELGQ ISKQIPEGTA EKAMGKVEAI INSMTPKERA NPALLKASRK RRIAMGAGTT VQEVNKLLKQ FEQMQQMMKM FSGNGLGKLM RMAKGMRGIK GMFPGL // ID Q9JYH6_NEIMB Unreviewed; 289 AA. AC Q9JYH6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=3-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AAF41937.1}; GN OrderedLocusNames=NMB1584 {ECO:0000313|EMBL:AAF41937.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41937.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41937.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41937.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41937.1; -; Genomic_DNA. DR PIR; B81065; B81065. DR RefSeq; NP_274590.1; NC_003112.2. DR RefSeq; WP_002212808.1; NC_003112.2. DR ProteinModelPortal; Q9JYH6; -. DR STRING; 122586.NMB1584; -. DR PaxDb; Q9JYH6; -. DR EnsemblBacteria; AAF41937; AAF41937; NMB1584. DR GeneID; 904236; -. DR KEGG; nme:NMB1584; -. DR PATRIC; 20359034; VBINeiMen85645_2035. DR eggNOG; ENOG4105CF3; Bacteria. DR eggNOG; COG2084; LUCA. DR HOGENOM; HOG000219608; -. DR KO; K00020; -. DR OMA; CYDIMKA; -. DR OrthoDB; EOG62RS92; -. DR BioCyc; NMEN122586:GHGG-1626-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR015815; HIBADH-related. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029154; NADP-bd. DR Pfam; PF14833; NAD_binding_11; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; HIBADH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 163 NAD_binding_2. FT {ECO:0000259|Pfam:PF03446}. FT DOMAIN 166 283 NAD_binding_11. FT {ECO:0000259|Pfam:PF14833}. FT ACT_SITE 172 172 {ECO:0000256|PIRSR:PIRSR000103-1}. SQ SEQUENCE 289 AA; 30378 MW; 8E8CD33C58C1A32E CRC64; MSANEYAQIG WIGLGQMGLP MVTRLLDGGI EVGVYNRSPD KTAPISAKGA KVYGNTAELV RDYPVIFLMV SDYAAVCDIL NGVRDGLAGK IIVNMSTISP TENLAVKALV EAAGGQFAEA PVSGSVGPAT NGTLLILFGG SEAVLNPLQK IFSLVGKKTF HFGDVGKGSG AKLVLNSLLG IFGEAYSEAM LMARQFGIDT DTIVEAIGGS AMDSPMFQTK KSLWANREFP PAFALKHASK DLNLAVKELE QAGNTLPAVE TVAASYRKAV EAGYGEQDVS GVYLKLAEH // ID Q9K0X4_NEIMB Unreviewed; 262 AA. AC Q9K0X4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40870.1}; GN OrderedLocusNames=NMB0432 {ECO:0000313|EMBL:AAF40870.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40870.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40870.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40870.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363041}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363041}. CC -!- SIMILARITY: Belongs to the UPF0721 family. CC {ECO:0000256|RuleBase:RU363041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40870.1; -; Genomic_DNA. DR PIR; B81200; B81200. DR RefSeq; NP_273480.1; NC_003112.2. DR RefSeq; WP_002216541.1; NC_003112.2. DR STRING; 122586.NMB0432; -. DR PaxDb; Q9K0X4; -. DR EnsemblBacteria; AAF40870; AAF40870; NMB0432. DR GeneID; 902548; -. DR KEGG; nme:NMB0432; -. DR PATRIC; 20356064; VBINeiMen85645_0547. DR eggNOG; ENOG4105EJ9; Bacteria. DR eggNOG; COG0730; LUCA. DR HOGENOM; HOG000114880; -. DR KO; K07090; -. DR OMA; GTNKGQS; -. DR OrthoDB; EOG61VZ6K; -. DR BioCyc; NMEN122586:GHGG-456-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU363041}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363041}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363041}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 6 32 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 76 94 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 100 118 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 130 148 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 154 173 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 194 218 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 230 248 Helical. {ECO:0000256|RuleBase:RU363041}. SQ SEQUENCE 262 AA; 27236 MW; 01A755E718245B56 CRC64; MEDLYIILAL GLVAMIAGFI DAIAGGGGLI TLPALLLAGI PPVSAIATNK LQAAAATFSA TVSFARKGLI DWKKGLPIAA ASFVGGVAGA LSVSLVSKDI LLAVVPVLLI FVALYFVFSP KLDGSKEGKA RMSFFLFGLT VAPLLGFYDG VFGPGVGSFF LIAFIVLLGC KLLNAMSYTK LANVACNLGS LSVFLLHGSI IFPIAATMAV GAFVGANLGA RFAVRFGSKL IKPLLIVISI SMAVKLLIDE RNPLYQMIVS MF // ID Q9K0K8_NEIMB Unreviewed; 304 AA. AC Q9K0K8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Putative adhesin {ECO:0000313|EMBL:AAF41014.1}; GN OrderedLocusNames=NMB0586 {ECO:0000313|EMBL:AAF41014.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41014.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41014.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41014.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 CC family. {ECO:0000256|RuleBase:RU003512}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41014.1; -; Genomic_DNA. DR PIR; D81182; D81182. DR RefSeq; NP_273630.1; NC_003112.2. DR RefSeq; WP_002225548.1; NC_003112.2. DR ProteinModelPortal; Q9K0K8; -. DR STRING; 122586.NMB0586; -. DR PaxDb; Q9K0K8; -. DR PRIDE; Q9K0K8; -. DR EnsemblBacteria; AAF41014; AAF41014; NMB0586. DR GeneID; 902701; -. DR KEGG; nme:NMB0586; -. DR PATRIC; 20356457; VBINeiMen85645_0748. DR eggNOG; ENOG4105DSE; Bacteria. DR eggNOG; COG0803; LUCA. DR HOGENOM; HOG000180308; -. DR KO; K02077; -. DR OMA; HAWQNVA; -. DR OrthoDB; EOG6B3601; -. DR BioCyc; NMEN122586:GHGG-612-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR006129; AdhesinB. DR InterPro; IPR006128; Lipoprotein_4. DR InterPro; IPR006127; ZnuA-like. DR Pfam; PF01297; ZnuA; 1. DR PRINTS; PR00691; ADHESINB. DR PRINTS; PR00690; ADHESNFAMILY. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|RuleBase:RU003512}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 304 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329377. SQ SEQUENCE 304 AA; 33281 MW; 223C2157CBF6AAA3 CRC64; MKHLKLTLIA ALLTASATAA PLPVVTSFSI LGDVAKQIGG ERVSIQSLVG ANQDTHAYHM TSGDIKKIRS AKLVLLNGLG LEAADVQRAV KQSKVSYTEA TKGIQPLKAE EEGGHHHDHD HDHEGHHHDH GEYDPHVWND PVLMSAYAQN VAKALIKADP EGKVYYQQRL GNYQMQLKKL HSDAQAAFNA VPAAKRKVLT GHDAFSYMGK RYHIEFIAPQ GVSSEAEPSA KQVAAIIRQI KREGIKAVFT ENIKDTRMVD RIAKETGVNV SGKLYSDALG NAPADTYIGM YRHNIKALTN AMKQ // ID Q9JYN4_NEIMB Unreviewed; 154 AA. AC Q9JYN4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=Universal stress protein {ECO:0000256|PIRNR:PIRNR006276}; GN OrderedLocusNames=NMB1500 {ECO:0000313|EMBL:AAF41856.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41856.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41856.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41856.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006276}. CC -!- SIMILARITY: Belongs to the universal stress protein A family. CC {ECO:0000256|PIRNR:PIRNR006276, ECO:0000256|SAAS:SAAS00569497}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41856.1; -; Genomic_DNA. DR PIR; H81076; H81076. DR RefSeq; NP_274508.1; NC_003112.2. DR RefSeq; WP_002244191.1; NC_003112.2. DR ProteinModelPortal; Q9JYN4; -. DR STRING; 122586.NMB1500; -. DR PaxDb; Q9JYN4; -. DR EnsemblBacteria; AAF41856; AAF41856; NMB1500. DR GeneID; 903931; -. DR KEGG; nme:NMB1500; -. DR PATRIC; 20358782; VBINeiMen85645_1901. DR eggNOG; ENOG41081P2; Bacteria. DR eggNOG; COG0589; LUCA. DR HOGENOM; HOG000238897; -. DR OMA; LETEANN; -. DR OrthoDB; EOG65BDRM; -. DR BioCyc; NMEN122586:GHGG-1540-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR006015; Universal_stress_UspA. DR InterPro; IPR006016; UspA. DR Pfam; PF00582; Usp; 1. DR PIRSF; PIRSF006276; UspA; 1. DR PRINTS; PR01438; UNVRSLSTRESS. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 148 Usp. {ECO:0000259|Pfam:PF00582}. SQ SEQUENCE 154 AA; 16524 MW; CBAB524DF5221CAB CRC64; MYKHLVVAVD GSETSINALK HAAELAGVNG ARLTLVHVAN PAEYMALAPE FLQHESYEAA AVAQGNEVLD AAERTAQELG VENTVKHLLV ANKGAREMAQ DLVDYADENG ADLLVLGTHG RTGLMHLLMG SFAETVMRQS HLPLLIIRSK AEEA // ID Q9K0T8_NEIMB Unreviewed; 260 AA. AC Q9K0T8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000256|SAAS:SAAS00055581}; DE Short=Malonyl-ACP O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835}; DE EC=2.1.1.197 {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000256|SAAS:SAAS00055581}; DE AltName: Full=Biotin synthesis protein BioC {ECO:0000256|HAMAP-Rule:MF_00835}; GN Name=bioC {ECO:0000256|HAMAP-Rule:MF_00835}; GN OrderedLocusNames=NMB0474 {ECO:0000313|EMBL:AAF40911.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40911.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40911.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40911.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester CC to its methyl ester by transfer of a methyl group from S-adenosyl- CC L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the CC fatty acid synthetic pathway. {ECO:0000256|HAMAP-Rule:MF_00835, CC ECO:0000256|SAAS:SAAS00558123}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + malonyl-[acyl- CC carrier protein] = S-adenosyl-L-homocysteine + malonyl-[acyl- CC carrier protein] methyl ester. {ECO:0000256|HAMAP-Rule:MF_00835, CC ECO:0000256|SAAS:SAAS00055583}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000256|SAAS:SAAS00055597}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000256|HAMAP-Rule:MF_00835, ECO:0000256|SAAS:SAAS00558118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40911.1; -; Genomic_DNA. DR PIR; E81194; E81194. DR RefSeq; NP_273521.1; NC_003112.2. DR RefSeq; WP_002224953.1; NC_003112.2. DR ProteinModelPortal; Q9K0T8; -. DR STRING; 122586.NMB0474; -. DR PaxDb; Q9K0T8; -. DR EnsemblBacteria; AAF40911; AAF40911; NMB0474. DR GeneID; 902590; -. DR KEGG; nme:NMB0474; -. DR PATRIC; 20356200; VBINeiMen85645_0621. DR eggNOG; ENOG41090JN; Bacteria. DR eggNOG; ENOG4111P8N; LUCA. DR HOGENOM; HOG000003262; -. DR KO; K02169; -. DR OMA; SADYWLF; -. DR OrthoDB; EOG6GXTQ5; -. DR BioCyc; NMEN122586:GHGG-498-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00835; BioC; 1. DR InterPro; IPR011814; BioC. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02072; BioC; 1. PE 3: Inferred from homology; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00835, KW ECO:0000256|SAAS:SAAS00444287}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835, KW ECO:0000256|SAAS:SAAS00444274}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835, KW ECO:0000256|SAAS:SAAS00444270}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835, KW ECO:0000256|SAAS:SAAS00444274}. FT DOMAIN 54 146 Methyltransf_11. FT {ECO:0000259|Pfam:PF08241}. SQ SEQUENCE 260 AA; 29691 MW; 0D79B4C59C64FD4C CRC64; MESLTAINKS RIRQAFQKAL NDYDRHALIQ QKMTINLMTH LQDYLPDMPL ENVLELGCGS GMLSALLQKQ ISANYWLFND LCNVQPQLAE KLPQSFDFYC GDAENFPFQR QFDLIASASA VQWFHQPDAF ITHCKTGLKT NGLLAVATFG KDNLKEVRQI TNIGLNYPTL SQWQAWLAKD FELLWCEDFT VILDFDTPSD VLKHLKYTGV TATNQKNWTR KNLNGFIGDY LSAFGMPSGK VRLTYHPLFF IARYSAAGRQ // ID Q9K0D8_NEIMB Unreviewed; 426 AA. AC Q9K0D8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Malate oxidoreductase (NAD) {ECO:0000313|EMBL:AAF41089.1}; DE EC=1.1.1.38 {ECO:0000313|EMBL:AAF41089.1}; GN Name=sfcA {ECO:0000313|EMBL:AAF41089.1}; GN OrderedLocusNames=NMB0671 {ECO:0000313|EMBL:AAF41089.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41089.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41089.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41089.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000256|PIRSR:PIRSR000106-3}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41089.1; -; Genomic_DNA. DR PIR; C81173; C81173. DR RefSeq; NP_273713.1; NC_003112.2. DR RefSeq; WP_002225506.1; NC_003112.2. DR ProteinModelPortal; Q9K0D8; -. DR STRING; 122586.NMB0671; -. DR PaxDb; Q9K0D8; -. DR PRIDE; Q9K0D8; -. DR EnsemblBacteria; AAF41089; AAF41089; NMB0671. DR GeneID; 902782; -. DR KEGG; nme:NMB0671; -. DR PATRIC; 20356643; VBINeiMen85645_0840. DR eggNOG; ENOG4105C6K; Bacteria. DR eggNOG; COG0281; LUCA. DR HOGENOM; HOG000132447; -. DR KO; K00027; -. DR OMA; VYDRTFN; -. DR OrthoDB; EOG6QCD9W; -. DR BioCyc; NMEN122586:GHGG-698-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR SMART; SM01274; malic; 1. DR SMART; SM00919; Malic_M; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41089.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 163 402 Malic_M. {ECO:0000259|SMART:SM00919}. FT ACT_SITE 39 39 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000106-1}. FT ACT_SITE 94 94 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000106-1}. FT METAL 136 136 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 137 137 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 162 162 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. SQ SEQUENCE 426 AA; 46025 MW; 10D412C23824A3F8 CRC64; MENSLKEAAL KFHEFPVPGK ISVTPTKSLA TDKDLALAYS PGVAAPCMEI HADPQNAYKY TAKGNLVAVI SNGTAVLGLG DIGALAGKPV MEGKGVLFKK FAGVDVFDIE IDEKDPQKLV DIIAALEPTF GGINLEDIKA PECFYIEREL RKRCKIPVFH DDQHGTAIIT AAAVLNALRF TGRKIEEATL VCSGAGAAAI ACLNQLLDLG LKRENVTVCD SKGVIYQTRE DKDRMDESKQ FYAIEDNGQR VLADAVKGKD IFLGLSGANL LTPEILNTMN EKPIVFAMAN PNPEILPPLA KETRPDVVIG TGRSDFPNQV NNVLCFPFIF RGALDVGATT INEEMKRACV YALADLAMEE VTEEVVAAYG KKFEFGAEYL IPTPFDSRLL PRVATAAAKA AMESGVATRP IADLEAYAAK LSEWKL // ID Q9JZZ0_NEIMB Unreviewed; 566 AA. AC Q9JZZ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Single-stranded-DNA-specific exonuclease RecJ {ECO:0000313|EMBL:AAF41253.1}; DE EC=3.1.-.- {ECO:0000313|EMBL:AAF41253.1}; GN Name=recJ {ECO:0000313|EMBL:AAF41253.1}; GN OrderedLocusNames=NMB0842 {ECO:0000313|EMBL:AAF41253.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41253.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41253.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41253.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41253.1; -; Genomic_DNA. DR PIR; G81151; G81151. DR RefSeq; NP_273883.1; NC_003112.2. DR RefSeq; WP_002225400.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ0; -. DR STRING; 122586.NMB0842; -. DR PaxDb; Q9JZZ0; -. DR EnsemblBacteria; AAF41253; AAF41253; NMB0842. DR GeneID; 902956; -. DR KEGG; nme:NMB0842; -. DR PATRIC; 20357071; VBINeiMen85645_1054. DR eggNOG; ENOG4105C2R; Bacteria. DR eggNOG; COG0608; LUCA. DR HOGENOM; HOG000018414; -. DR KO; K07462; -. DR OMA; GKHKKAW; -. DR OrthoDB; EOG63C0P5; -. DR BioCyc; NMEN122586:GHGG-873-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR004610; RecJ. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. DR TIGRFAMs; TIGR00644; recJ; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Exonuclease {ECO:0000313|EMBL:AAF41253.1}; KW Hydrolase {ECO:0000313|EMBL:AAF41253.1}; KW Nuclease {ECO:0000313|EMBL:AAF41253.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 74 200 DHH. {ECO:0000259|Pfam:PF01368}. FT DOMAIN 378 446 DHHA1. {ECO:0000259|Pfam:PF02272}. FT COILED 306 333 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 566 AA; 62165 MW; CDFD00CC8DA716B5 CRC64; MSVKIQTRSV NTDVFNHLLT AGADPLIAQL CASRGVQSPA ELDDKLASLL PYQSLTNCEA AARRLADAVG RKEKILIVAD YDADGATACA VGMSGLAAMG AKVDFLVPNR FEHGYGLTPE LAEIAAAQGV DLLITVDNGI ASIAGVARAQ ALGLDVIVTD HHLPAETVPD CIIVNPNQKG CGFPSKSLAG VGVIFYVLMA LRAELRRRNY FSDGIKEPNL GELLDLVALG TVADVVPLDH NNRILVSQGL KRMRSGKMRP GIRALFEVAR RDWRKAQPFD MGFALGPRIN AAGRLDDMSV GIACLLARDD SEAQELAAQL NNLNIERREI EQSMLQDALN DFPETLPSGQ MTLVAYRDDF HQGVVGIVAS RLKDRFYRPT IVFAPADNGE VRGSGRSIPN LHLRDALDLV SKRHPDLILK FGGHAMAAGL SILEHNIPAF QTTFEEAVRE MVCEDDLSQT FITDGSLPAC DITLEQAQNL ARHVWGQGFA PPSFTDEFHV VRQQPLGAEG KHKKVWLQKD GCEFEAMFWR CSEDIPEYIR TVYRPVANEW RNNLELQLYI DYWEAA // ID Q9JYI9_NEIMB Unreviewed; 208 AA. AC Q9JYI9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930}; DE EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; GN Name=purN {ECO:0000256|HAMAP-Rule:MF_01930, GN ECO:0000313|EMBL:AAF41920.1}; GN OrderedLocusNames=NMB1566 {ECO:0000313|EMBL:AAF41920.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41920.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41920.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41920.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10- CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and CC tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + N(1)-(5-phospho-D- CC ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide. {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5- CC phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP- CC Rule:MF_01930}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41920.1; -; Genomic_DNA. DR PIR; B81068; B81068. DR RefSeq; NP_274573.1; NC_003112.2. DR RefSeq; WP_002222210.1; NC_003112.2. DR ProteinModelPortal; Q9JYI9; -. DR SMR; Q9JYI9; 3-196. DR STRING; 122586.NMB1566; -. DR PaxDb; Q9JYI9; -. DR EnsemblBacteria; AAF41920; AAF41920; NMB1566. DR GeneID; 904144; -. DR KEGG; nme:NMB1566; -. DR PATRIC; 20358994; VBINeiMen85645_2016. DR eggNOG; ENOG4108V3E; Bacteria. DR eggNOG; COG0299; LUCA. DR HOGENOM; HOG000033575; -. DR KO; K11175; -. DR OMA; GDSEHGT; -. DR OrthoDB; EOG615VP4; -. DR BioCyc; NMEN122586:GHGG-1607-MONOMER; -. DR UniPathway; UPA00074; UER00126. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR004607; PurN_trans. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01930}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01930, KW ECO:0000256|SAAS:SAAS00476799, ECO:0000313|EMBL:AAF41920.1}. FT DOMAIN 2 179 Formyl_trans_N. FT {ECO:0000259|Pfam:PF00551}. FT REGION 12 14 5'-phosphoribosylglycinamide binding. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT REGION 87 90 10-formyltetrahydrofolate binding. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT ACT_SITE 106 106 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_01930}. FT BINDING 62 62 10-formyltetrahydrofolate. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT BINDING 104 104 10-formyltetrahydrofolate. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT SITE 142 142 Raises pKa of active site His. FT {ECO:0000256|HAMAP-Rule:MF_01930}. SQ SEQUENCE 208 AA; 22451 MW; 53C707AC5316E56A CRC64; MKNIVILISG RGSNMQAIVN AAIHNVRIAA VLSNSETAAG LQWAAERGIP TDSLNHKNFT SRLAFDTAMM EKIDAYQPDL VVLAGFMRIL TPEFCARYEG RLMNIHPSIL PSFTGLHTHE RALEAGCRVA GCTIHFVTAE LDCGPIVSQG VVPILDGDTA DDIAARVLAV EHKLYPKAVA DFAAGRLIIE GNRVRNSENA DAARFLTA // ID Q9K1J5_NEIMB Unreviewed; 83 AA. AC Q9K1J5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Ferredoxin, 4Fe-4S bacterial type {ECO:0000313|EMBL:AAF40582.1}; GN OrderedLocusNames=NMB0123 {ECO:0000313|EMBL:AAF40582.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40582.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40582.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40582.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40582.1; -; Genomic_DNA. DR PIR; H81234; H81234. DR RefSeq; NP_273181.1; NC_003112.2. DR RefSeq; WP_002215364.1; NC_003112.2. DR ProteinModelPortal; Q9K1J5; -. DR SMR; Q9K1J5; 2-79. DR STRING; 122586.NMB0123; -. DR PaxDb; Q9K1J5; -. DR EnsemblBacteria; AAF40582; AAF40582; NMB0123. DR GeneID; 902227; -. DR KEGG; nme:NMB0123; -. DR PATRIC; 20355259; VBINeiMen85645_0163. DR eggNOG; ENOG4105K5D; Bacteria. DR eggNOG; COG1145; LUCA. DR HOGENOM; HOG000044615; -. DR OMA; CPVECII; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; NMEN122586:GHGG-129-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 29 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 31 64 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 83 AA; 9553 MW; 85BD3D2B948FC251 CRC64; MSLFITDECI NCDVCEPECP NDAISQGEEI YEINPNLCTQ CVGHYDEPQC QQVCPVDCIL IDEEHPETHD ELMAKYEKII QFK // ID Q9JZJ0_NEIMB Unreviewed; 187 AA. AC Q9JZJ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41429.1}; GN OrderedLocusNames=NMB1030 {ECO:0000313|EMBL:AAF41429.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41429.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41429.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41429.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the UPF0312 family. CC {ECO:0000256|SAAS:SAAS00564357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41429.1; -; Genomic_DNA. DR PIR; D81130; D81130. DR RefSeq; NP_274064.1; NC_003112.2. DR RefSeq; WP_002217107.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ0; -. DR STRING; 122586.NMB1030; -. DR PaxDb; Q9JZJ0; -. DR EnsemblBacteria; AAF41429; AAF41429; NMB1030. DR GeneID; 903167; -. DR KEGG; nme:NMB1030; -. DR PATRIC; 20357595; VBINeiMen85645_1314. DR eggNOG; ENOG4108YYC; Bacteria. DR eggNOG; COG2353; LUCA. DR HOGENOM; HOG000262660; -. DR OMA; GEFNRDE; -. DR OrthoDB; EOG6QCDB3; -. DR BioCyc; NMEN122586:GHGG-1067-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.40.128.110; -; 1. DR InterPro; IPR007372; Lipid/polyisoprenoid-bd_YceI. DR Pfam; PF04264; YceI; 1. DR SMART; SM00867; YceI; 1. DR SUPFAM; SSF101874; SSF101874; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 187 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329352. FT DOMAIN 21 185 YceI. {ECO:0000259|SMART:SM00867}. SQ SEQUENCE 187 AA; 20531 MW; 4EDFCCA14936DBC8 CRC64; MKKIIFAALA AAAISTASAA TYKVDEYHAN ARFAIDHFNT STNVGGFYGL TGSVEFDQAK RDGKIDITIP IANLQSGSQH FTDHLKSADI FDAAQYPDIR FVSTKFNFNG KKLVSVDGNL TMHGKTAPVK LKAEKFNCYQ SPMEKTEVCG GDFSTTIDRT KWGMDYLVNV GMTKSVRIDI QIEAAKQ // ID Q9K1Q5_NEIMB Unreviewed; 482 AA. AC Q9K1Q5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485}; DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485}; GN Name=gnd {ECO:0000313|EMBL:AAF40494.1}; GN OrderedLocusNames=NMB0015 {ECO:0000313|EMBL:AAF40494.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40494.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40494.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40494.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH. CC {ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. {ECO:0000256|RuleBase:RU000485}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. {ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. {ECO:0000256|RuleBase:RU000485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40494.1; -; Genomic_DNA. DR PIR; E81248; E81248. DR RefSeq; NP_273081.1; NC_003112.2. DR RefSeq; WP_002225759.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q5; -. DR SMR; Q9K1Q5; 3-473. DR STRING; 122586.NMB0015; -. DR PaxDb; Q9K1Q5; -. DR EnsemblBacteria; AAF40494; AAF40494; NMB0015. DR GeneID; 902118; -. DR KEGG; nme:NMB0015; -. DR PATRIC; 20354961; VBINeiMen85645_0016. DR eggNOG; ENOG4105C7Q; Bacteria. DR eggNOG; COG0362; LUCA. DR HOGENOM; HOG000255147; -. DR KO; K00033; -. DR OMA; EGEPCVT; -. DR OrthoDB; EOG6MSS4W; -. DR BioCyc; NMEN122586:GHGG-16-MONOMER; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 1.20.5.320; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR012284; 6PGD_dom_3. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006183; Pgluconate_DH. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Gluconate utilization {ECO:0000256|RuleBase:RU000486}; KW NADP {ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000485, KW ECO:0000313|EMBL:AAF40494.1}; KW Pentose shunt {ECO:0000256|RuleBase:RU000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT NP_BIND 9 14 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 32 34 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 74 76 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT ACT_SITE 183 183 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000109-1}. FT ACT_SITE 190 190 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000109-1}. FT BINDING 102 102 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT BINDING 451 451 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. SQ SEQUENCE 482 AA; 53032 MW; A60532F230BF75EA CRC64; MNGDIGVIGL AVMGQNLILN MNDCGFKVVA YNRTTAKVDE FLNGAAKGTN IIGAYSLQDL VDKLEKPRKI MMMVRAGSVV DEFIEQLLPL LEEGDILIDG GNANYPDTTR RTHYLAEKGI LFVGAGVSGG EEGARRGPSI MPGGDKRAWD AVKPIFQAIA AKTSQGEPCC DWVGKDGAGH FVKMVHNGIE YGDMQLICEA YQFMKDGLGL SYDEMYRVFA EWNKTELDSY LIEITAAILG YKDEGGEPLV EKILDTAGQK GTGKWTGINA LDLGIPLTLI SEAVFARCVS SFKEQRVQTG KLFARTVTPV EGGKQEWVEA LRQALLASKI ISYAQGFMLI REAGESYGWD LDYGNTALLW REGCIIRSAF LSNIRDAYEN NPDLVFLGAD PYFKNILENC LPAWRKVVAK AVECGIPMPC MASAITFLDG YTTERLPANL LQAQRDYFGA HTYERTDKPR GEFFHTNWTG KGGDTASTTY DI // ID Q9JZV1_NEIMB Unreviewed; 197 AA. AC Q9JZV1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41299.1}; GN OrderedLocusNames=NMB0889 {ECO:0000313|EMBL:AAF41299.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41299.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41299.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41299.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41299.1; -; Genomic_DNA. DR PIR; H81145; H81145. DR RefSeq; NP_273930.1; NC_003112.2. DR RefSeq; WP_002244085.1; NC_003112.2. DR STRING; 122586.NMB0889; -. DR PaxDb; Q9JZV1; -. DR EnsemblBacteria; AAF41299; AAF41299; NMB0889. DR GeneID; 903008; -. DR KEGG; nme:NMB0889; -. DR PATRIC; 20357185; VBINeiMen85645_1106. DR eggNOG; COG4726; LUCA. DR HOGENOM; HOG000218896; -. DR KO; K02673; -. DR OMA; DNKGMEY; -. DR OrthoDB; EOG6JX7J7; -. DR BioCyc; NMEN122586:GHGG-925-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR025205; PilX/PilW_C. DR InterPro; IPR025746; PilX_N_dom. DR Pfam; PF13681; PilX; 1. DR Pfam; PF14341; PilX_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 67 PilX_N. {ECO:0000259|Pfam:PF14341}. FT DOMAIN 92 192 PilX. {ECO:0000259|Pfam:PF13681}. SQ SEQUENCE 197 AA; 21700 MW; 541257EE655B2AE9 CRC64; MRKQNTLTGI PTSDGQRGFA LFIVLMVMIV VAFLVVTAAQ SYNTEQRISA NESDRKLALS LAEAALREGE LQVLDLEYDT DSKVTFSENC GKGLCAAVNV RTNNDNEEAF DNIVVQGKPT VEAVKRSCPA NSTDLCIDKK GMEYKKGTRS VSKMPRYIIE YLGVKNGENV YRVTAKAWGK NANTVVVLQS YVSNNDE // ID Q7DD80_NEIMB Unreviewed; 437 AA. AC Q7DD80; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=Citrate transporter {ECO:0000313|EMBL:AAF42132.1}; GN OrderedLocusNames=NMB1794 {ECO:0000313|EMBL:AAF42132.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42132.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42132.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42132.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42132.1; -; Genomic_DNA. DR PIR; H81041; H81041. DR RefSeq; NP_274792.1; NC_003112.2. DR RefSeq; WP_002222940.1; NC_003112.2. DR PaxDb; Q7DD80; -. DR EnsemblBacteria; AAF42132; AAF42132; NMB1794. DR GeneID; 903305; -. DR KEGG; nme:NMB1794; -. DR PATRIC; 20359553; VBINeiMen85645_2282. DR eggNOG; ENOG4105D4T; Bacteria. DR eggNOG; COG2851; LUCA. DR HOGENOM; HOG000241948; -. DR KO; K03300; -. DR OMA; MVDAMAQ; -. DR OrthoDB; EOG65TRSJ; -. DR BioCyc; NMEN122586:GHGG-1849-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015137; F:citrate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR004680; Cit_transptr-like_dom. DR InterPro; IPR014738; Citrate_transporter. DR PANTHER; PTHR10283:SF87; PTHR10283:SF87; 1. DR Pfam; PF03600; CitMHS; 1. DR TIGRFAMs; TIGR00784; citMHS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 94 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 238 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 328 354 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 374 402 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 414 434 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 16 381 CitMHS. {ECO:0000259|Pfam:PF03600}. SQ SEQUENCE 437 AA; 46752 MW; 65DA46384FF651E4 CRC64; MLTFIGLLII GVIVWLLLTE KVSPIIALIL VPLFGALLAG FDVSQLKEFY SGGTKSVMQI VIMFMFSILF FGIMNDVGLF RPMIGGLIKL TRGNIVAVSV GTVLVSVVAQ LDGAGATTFL LVVPALLPLY KRLHMNPYLL FLLLTSSAGL INLLPWGGPT GRVASVLGAD VGELYKPLLT VQIIGVVFIL ALSLLLGVRE KRRIVRELGA LPAVADLIKP VPLSEEEQKL ARPKLFWWNV LLFLAAMSLL FSGIFPPGYV FMLAATAALL LNYRSPQEQM ERIYAHAGGA VMMASIILAA GTFLGILKGA GMLDAISKDI VHILPDALLP YLHIAIGVLG IPLELVLSTD AYYFGLFPIV EQITSQAGVA PEAAGYAMLI GSIVGTFVTP LSPALWMGLG LAKLSMGKHI RYSFFWAWGL SLAILASSIA AGIVPLP // ID Q9K0K1_NEIMB Unreviewed; 468 AA. AC Q9K0K1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 105. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAF41022.1}; GN OrderedLocusNames=NMB0594 {ECO:0000313|EMBL:AAF41022.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41022.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41022.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41022.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00577673}. CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00577406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41022.1; -; Genomic_DNA. DR PIR; G81180; G81180. DR RefSeq; NP_273638.1; NC_003112.2. DR RefSeq; WP_002225546.1; NC_003112.2. DR ProteinModelPortal; Q9K0K1; -. DR STRING; 122586.NMB0594; -. DR PaxDb; Q9K0K1; -. DR EnsemblBacteria; AAF41022; AAF41022; NMB0594. DR GeneID; 902709; -. DR KEGG; nme:NMB0594; -. DR PATRIC; 20356473; VBINeiMen85645_0756. DR eggNOG; ENOG4105E0F; Bacteria. DR eggNOG; ENOG410XTWD; LUCA. DR HOGENOM; HOG000218823; -. DR KO; K02484; -. DR OMA; YANIDEM; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NMEN122586:GHGG-620-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|RuleBase:RU003568, ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAF41022.1}; KW Membrane {ECO:0000256|SAAS:SAAS00577774, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Phosphoprotein {ECO:0000256|RuleBase:RU003568}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAF41022.1}; KW Transmembrane {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00577774, KW ECO:0000256|SAM:Phobius}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00577723}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 179 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 180 235 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 243 458 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 468 AA; 52782 MW; A2DE9A0A587628B2 CRC64; MKLFQRIFAT FCAVIVCAIF VASFSFWLVQ NTLAENQFNQ RRTIETTLMG SIISAFRARG DAGAREILTE WKDSPVSSGV YVIQGDEKKD ILNRYIDSYT IERARLFAAG HPHSNLVHIE YDRFGEEYLF FTKDWDKLQA RRLPSPLLIP GLPLAPIWHE LIILSFIIIV GLLMAYILAG NIAKPIRILG NGMDRVANGE LETRISQQVD DRDDELSHLA IQFDKMVEKL EKLVAKERHL LHHVSHEMRS PLARMQAIVG LIQAQPQKQE QYLKRLEGEL TRMDTLAGEL LTLSRLETSN MALEKESLKL LPFLGNLVED NQSIAQKNGQ TVTLSADGKI PENTTILANE SYLYRAFDNV IRNAVNYSPE GSTILINIGQ DHKHWIIDVT DNGPGVDEMQ LPHIFTAFYR ADSSANKPGT GLGLALTQHI IEQHCGKIIA ENIKPNGLRM RFILPKKKTG SKTEKSAN // ID Q9JY14_NEIMB Unreviewed; 509 AA. AC Q9JY14; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Cytoplasmic axial filament protein {ECO:0000313|EMBL:AAF42130.1}; GN Name=cafA {ECO:0000313|EMBL:AAF42130.1}; GN OrderedLocusNames=NMB1791 {ECO:0000313|EMBL:AAF42130.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42130.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42130.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42130.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42130.1; -; Genomic_DNA. DR PIR; F81041; F81041. DR RefSeq; NP_274790.1; NC_003112.2. DR RefSeq; WP_010980991.1; NC_003112.2. DR ProteinModelPortal; Q9JY14; -. DR STRING; 122586.NMB1791; -. DR PaxDb; Q9JY14; -. DR EnsemblBacteria; AAF42130; AAF42130; NMB1791. DR GeneID; 903308; -. DR KEGG; nme:NMB1791; -. DR PATRIC; 20359547; VBINeiMen85645_2279. DR eggNOG; ENOG4105C03; Bacteria. DR eggNOG; COG1530; LUCA. DR HOGENOM; HOG000258025; -. DR KO; K08301; -. DR OMA; QVDSREN; -. DR OrthoDB; EOG6PCPTH; -. DR BioCyc; NMEN122586:GHGG-1846-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF10150; RNase_E_G; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00757; RNaseEG; 1. DR PROSITE; PS50126; S1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 64 140 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 509 AA; 57904 MW; 86880AD4C5CF0FC3 CRC64; MQNIFITFSG KTMLSGLPIP KDIARPPETI LVNITPAETR VAVLEENNIC ELHIERNSEH SLVGNIYLGV VRRVLPGMQS AFIDIGLERA AFLHIVDVLE QRRNPEETQR IEHMLFEGQS VLVQVIKDPI NTKGARLSTQ ISLAGRFLVH LPQEDHIGVS QRIEDDAERS SLRERLDKLL PENACRGYII RTNAENATDE QLQSDIDYLT KVWEHIQEQA KIRPPETLLY QDLPLSLRVL RDMVGCDTQK ILVDSTVNHG RMTRFAEQYV HGALGRIELF KGERPLFETH NVEQEISRAL QPRVNLNFGS YLIIESTEAM TTIDVNTGGF VGARNFDETI FRTNLEACHT IARELRLRNL GGIIIIDFID MAQESHREAV LQELAKALAF DRTRVTLHGF TSLGLVELTR KRSRENLNQV LCEPCPSCQG RGRLKTPQTV CYEIQREIVR EARRYDAESF RILAAPNVID LFLDEESQSL AMLIDFIGKP ISLAVETAYT QEQYDIVLM // ID Q9JXL7_NEIMB Unreviewed; 938 AA. AC Q9JXL7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 113. DE SubName: Full=DNA polymerase I {ECO:0000313|EMBL:AAF42310.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAF42310.1}; GN Name=polA {ECO:0000313|EMBL:AAF42310.1}; GN OrderedLocusNames=NMB1982 {ECO:0000313|EMBL:AAF42310.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42310.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42310.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42310.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. CC {ECO:0000256|RuleBase:RU004459}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42310.1; -; Genomic_DNA. DR PIR; G81020; G81020. DR RefSeq; NP_274975.1; NC_003112.2. DR RefSeq; WP_010981015.1; NC_003112.2. DR ProteinModelPortal; Q9JXL7; -. DR SMR; Q9JXL7; 330-938. DR STRING; 122586.NMB1982; -. DR PaxDb; Q9JXL7; -. DR EnsemblBacteria; AAF42310; AAF42310; NMB1982. DR GeneID; 904155; -. DR KEGG; nme:NMB1982; -. DR PATRIC; 20360041; VBINeiMen85645_2525. DR eggNOG; ENOG4105C2M; Bacteria. DR eggNOG; COG0258; LUCA. DR eggNOG; COG0749; LUCA. DR HOGENOM; HOG000020999; -. DR KO; K02335; -. DR OMA; CFDTETT; -. DR OrthoDB; EOG6SJJH7; -. DR BioCyc; NMEN122586:GHGG-2039-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR002562; 3'-5'_exonuclease_dom. DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N. DR InterPro; IPR020045; 5-3_exonuclease_C. DR InterPro; IPR002421; 5-3_exonuclease_N. DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS. DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom. DR InterPro; IPR018320; DNA_polymerase_1. DR InterPro; IPR002298; DNA_polymerase_A. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR Pfam; PF00476; DNA_pol_A; 1. DR Pfam; PF01612; DNA_pol_A_exo1; 1. DR PRINTS; PR00868; DNAPOLI. DR SMART; SM00474; 35EXOc; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SMART; SM00482; POLAc; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR TIGRFAMs; TIGR00593; pola; 1. DR PROSITE; PS00447; DNA_POLYMERASE_A; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|SAAS:SAAS00427491}; KW Nuclease {ECO:0000256|SAAS:SAAS00427491}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAF42310.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42310.1}. FT DOMAIN 3 264 53EXOc. {ECO:0000259|SMART:SM00475}. FT DOMAIN 332 518 3'-5' exonuclease. FT {ECO:0000259|SMART:SM00474}. FT DOMAIN 687 900 POLAc. {ECO:0000259|SMART:SM00482}. SQ SEQUENCE 938 AA; 103183 MW; 6E149C08A8CD24A5 CRC64; MSNRPTLLLV DGSSYLYRAY HAMGQNLTAP DGAPTGALYG VLNMLRRLRS EYPHDYCAVV FDAKGKNFRH QMFEEYKATR PPMPDDLRPQ AEALPDLVRL TGWPVLVIGQ VEADDVIGTL AKQGAEHGLR VIVSTGDKDM AQLVDERVTL VNTMSSETLD IEGVKAKFGV RPDQIRDYLA LMGDKVDNVP GVEKCGPKTA VKWLEAYGSL AGVMEHASEI KGKVGENLQA ALPQLPLSYD LVTIKTDVDL HAELSDGIES LRRTTPKWAQ LVVDFKRWGF RTWLKEAESN MNTGSTDDLF GSDSIGEQAA LNAEMPFEKQ AEKATAPEKL DYQAVTTEAQ FAALLDKLSR ADTIGIDTET TSLDAMNASL VGISIAFQAG EAVYIPVGHS LTAAPEQLDL QDVLGRLKPH LGNPALKKIG QNLKYDQHVF ANYGIALNGI AGDAMLASYI IESHLGHGLD ELSERWLGLE TITYESLCGK GAKQIGFADV AIGQATEYAA QDADFALRLE AHLRAQMDEK QLEMYEKMEL PVAQVLFEME RNGVQIDRAE LARQSAELGA ELMKLEQEAY AAAGQPFNLN SPKQLQEILF DKMGIPTKGL KKTAKGGIST NEAVLEQLAP DYPLPKIILQ NRSLAKLKST YTDKLPEMIS PKDGRVHTTY AQAVAITGRL ASNNPNLQNI PIRTEEGRKV RRAFTAPQGS VIVSADYSQI ELRIMAHLSG DKTLIAAFQN GEDVHRRTAA EVFGTAPENV SSEQRRYAKS INFGLIYGMG QYGLAKSLGI DNLSAKNFID RYFARYPGVA EYMQRTKEQA AAQGYVETLF GRRLYLPDIR NKNANARAGA ERAAINAPMQ GTASDLIKRA MIDVSRWLSE CEASPWDELL QSKLIMQVHD ELVLEVVETE LDFVKEKLPQ IMAKVDGGLL DVPLVAEVGV GENWEEAH // ID Q9JZ02_NEIMB Unreviewed; 447 AA. AC Q9JZ02; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 93. DE SubName: Full=Aldehyde dehydrogenase family protein {ECO:0000313|EMBL:AAF41727.1}; GN OrderedLocusNames=NMB1353 {ECO:0000313|EMBL:AAF41727.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41727.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41727.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41727.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41727.1; -; Genomic_DNA. DR PIR; D81093; D81093. DR RefSeq; NP_274371.1; NC_003112.2. DR RefSeq; WP_002222345.1; NC_003112.2. DR ProteinModelPortal; Q9JZ02; -. DR STRING; 122586.NMB1353; -. DR PaxDb; Q9JZ02; -. DR EnsemblBacteria; AAF41727; AAF41727; NMB1353. DR GeneID; 903775; -. DR KEGG; nme:NMB1353; -. DR PATRIC; 20358363; VBINeiMen85645_1693. DR eggNOG; ENOG4105C26; Bacteria. DR eggNOG; COG1012; LUCA. DR HOGENOM; HOG000271513; -. DR KO; K08324; -. DR OMA; EFTNAQT; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NMEN122586:GHGG-1391-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003344}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 443 Aldedh. {ECO:0000259|Pfam:PF00171}. SQ SEQUENCE 447 AA; 49207 MW; 722353C3E7D31E56 CRC64; MFHSVNVFTG ETLYRRPAQD YAEFERRLAD LKMRGGAFAQ LGVTERAARL QKFADRLEAE KERFAEMVCE EVGRCLHECR AEIGKSIELI RYYARLAPEL LAHKTIATQA SLSQVRFEPL GVVFAVMPWN YPVWQVLRFA VPAMCAGNAC AVKPAPSVAR VSQALFDLAS DGIPLAGVWL DEAGTLKAVE DTDAMAFTGS THTGRILAAH AGANLKKTVL ELGGSNAFIV MPDADLERAA AEACYSRFRD AGQSCNAAKR IIVTEAAADR FITLFLAECA KLKMGDPKHP DTTLAPLHRE DLRDRVHGQV EDAVSNGAVC LTGGKIPQGR GWFYPATVLD RVNPACRVWR EEVFGPAALI LRAENEEHAI ALANDSPFGL GACIYTADTE RAWRFAEKIQ AGSVFINRHT SSDLRLPFGG VKDSGYGREL SEFGLYEFVN VKTYWQK // ID Q7DD70_NEIMB Unreviewed; 146 AA. AC Q7DD70; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Transcriptional regulator, MarR family {ECO:0000313|EMBL:AAF42178.1}; GN OrderedLocusNames=NMB1843 {ECO:0000313|EMBL:AAF42178.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42178.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42178.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42178.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:5AIP, ECO:0000213|PDB:5AIQ} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RA Liguori A., Malito E., Lo Surdo P., Fagnocchi L., Brier S., Pizza M., RA Delany I., Bottomley M.J.; RT "Crystal Structures Reveal the Molecular Basis of Ligand-Dependent RT Regulation of Nadr, the Transcriptional Repressor of Meningococcal RT Virulence Factor and Bexsero Vaccine Antigen Nada."; RL Submitted (FEB-2015) to the PDB data bank. CC -!- SIMILARITY: Contains 2 HTH marR-type DNA-binding domains. CC {ECO:0000256|RuleBase:RU000702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42178.1; -; Genomic_DNA. DR PIR; C81036; C81036. DR RefSeq; NP_274840.1; NC_003112.2. DR RefSeq; WP_002214596.1; NC_003112.2. DR PDB; 5AIP; X-ray; 2.30 A; A/B=1-146. DR PDB; 5AIQ; X-ray; 2.72 A; A/B/C/D=1-146. DR PDBsum; 5AIP; -. DR PDBsum; 5AIQ; -. DR ProteinModelPortal; Q7DD70; -. DR STRING; 122586.NMB1843; -. DR PaxDb; Q7DD70; -. DR EnsemblBacteria; AAF42178; AAF42178; NMB1843. DR GeneID; 903256; -. DR KEGG; nme:NMB1843; -. DR PATRIC; 20359693; VBINeiMen85645_2352. DR eggNOG; ENOG4108V8F; Bacteria. DR eggNOG; COG1846; LUCA. DR HOGENOM; HOG000221451; -. DR OMA; RMESMEL; -. DR OrthoDB; EOG6TN46N; -. DR BioCyc; NMEN122586:GHGG-1898-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR012712; HpaR. DR InterPro; IPR000835; HTH_MarR-typ. DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR SMART; SM00347; HTH_MARR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR02337; HpaR; 1. DR PROSITE; PS01117; HTH_MARR_1; 1. DR PROSITE; PS50995; HTH_MARR_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5AIP, ECO:0000213|PDB:5AIQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}; KW Transcription regulation {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}. FT DOMAIN 7 139 HTH marR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50995}. SQ SEQUENCE 146 AA; 16583 MW; 54AB8DC5486E162A CRC64; MPTQSKHASI NIGLIQAREA LMTQFRPILN QANITDQQWR IIRLLAENGT LDFQDLANQA CILRPSLTGI LTRLEKAGLV VRLKPSNDQR RVFLKLTAEG EKLYEEIGEE VDERYDAIEE VLGREKMLLL KDLLAELAKI EDALNS // ID Q9K000_NEIMB Unreviewed; 380 AA. AC Q9K000; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=Anticodon nuclease {ECO:0000313|EMBL:AAF41243.1}; GN Name=prrC {ECO:0000313|EMBL:AAF41243.1}; GN OrderedLocusNames=NMB0832 {ECO:0000313|EMBL:AAF41243.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41243.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41243.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41243.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41243.1; -; Genomic_DNA. DR PIR; H81152; H81152. DR RefSeq; NP_273873.1; NC_003112.2. DR RefSeq; WP_002217540.1; NC_003112.2. DR STRING; 122586.NMB0832; -. DR PaxDb; Q9K000; -. DR EnsemblBacteria; AAF41243; AAF41243; NMB0832. DR GeneID; 902946; -. DR KEGG; nme:NMB0832; -. DR PATRIC; 20357051; VBINeiMen85645_1044. DR eggNOG; ENOG41075ZK; Bacteria. DR eggNOG; ENOG410Y2DX; LUCA. DR HOGENOM; HOG000003475; -. DR OMA; DTPFFHH; -. DR OrthoDB; EOG69D38S; -. DR BioCyc; NMEN122586:GHGG-863-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR026866; CR006/PrrC. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13166; AAA_13; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 380 AA; 44656 MW; 4BFBE9DF6AE6432C CRC64; MGKSLTEIAE ELKGNDKKVQ LIYAFNGTGK TRLSREFKNL IAPTSSEEPD GEPTRRKFLY YNAFTEDLFF WDNDLLANEA PRLKIQKNSF TDWLLRDNGL DGAVIKNFQY YTDDKLTPDF NDDFSEIAFY FARGNDEQIE NIKISKGEES NFIWSIFYVL IRQVIAELNI PEDSEEGRST DQFDDLEYIF IDDPVSSLDE NHLIQQAVDL ADLIKLSKPR LKFIITTHNV LFYNVLYNEL KKLEKEKKSY LLLKNEDGSF DILEKQGDSN KSFSYHLHLK GVIEKAIENQ QVERFHFMLL RNLYEKTANF LGYKQRSDIL PEDSRRNYFQ RIINFTSHST LSNEAFAEPT PQEQETVKLL LQHLLDNYNF FQDDEQRDKP // ID Q9JYH0_NEIMB Unreviewed; 111 AA. AC Q9JYH0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN OrderedLocusNames=NMB1590 {ECO:0000313|EMBL:AAF41943.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41943.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41943.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41943.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. CC Required for the reduction of the AhpC active site cysteine CC residues and for the regeneration of the AhpC enzyme activity. CC {ECO:0000256|SAAS:SAAS00088543}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000256|SAAS:SAAS00088505}. CC -!- SIMILARITY: Belongs to the AhpD family. CC {ECO:0000256|SAAS:SAAS00571262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41943.1; -; Genomic_DNA. DR PIR; H81065; H81065. DR RefSeq; NP_274596.1; NC_003112.2. DR RefSeq; WP_002225024.1; NC_003112.2. DR ProteinModelPortal; Q9JYH0; -. DR STRING; 122586.NMB1590; -. DR PaxDb; Q9JYH0; -. DR EnsemblBacteria; AAF41943; AAF41943; NMB1590. DR GeneID; 904263; -. DR KEGG; nme:NMB1590; -. DR PATRIC; 20359062; VBINeiMen85645_2043. DR eggNOG; ENOG4105X1V; Bacteria. DR eggNOG; COG0599; LUCA. DR HOGENOM; HOG000252431; -. DR OMA; QWCIALH; -. DR OrthoDB; EOG6W45V8; -. DR BioCyc; NMEN122586:GHGG-1638-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 3: Inferred from homology; KW Antioxidant {ECO:0000256|SAAS:SAAS00461132}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00461175}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00461184}; KW Peroxidase {ECO:0000256|SAAS:SAAS00461184}; KW Redox-active center {ECO:0000256|SAAS:SAAS00461089}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 24 106 CMD. {ECO:0000259|Pfam:PF02627}. SQ SEQUENCE 111 AA; 11533 MW; BC3CF83FDB241B07 CRC64; MFKDWKEHTA LVKKSFGELG KAHPKMLQAY GALEQAAAAE ALDAKTRELI AIAVAITTRC ESCISVHAAA ATKAGATDSE IAGALATAIA LNAGAAYTYA LRALEAVETQ K // ID Q9JYL4_NEIMB Unreviewed; 269 AA. AC Q9JYL4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Putative methylated-DNA--protein-cysteine methyltransferase {ECO:0000313|EMBL:AAF41883.1}; GN OrderedLocusNames=NMB1528 {ECO:0000313|EMBL:AAF41883.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41883.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41883.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41883.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41883.1; -; Genomic_DNA. DR PIR; D81073; D81073. DR RefSeq; NP_274535.1; NC_003112.2. DR RefSeq; WP_002225060.1; NC_003112.2. DR ProteinModelPortal; Q9JYL4; -. DR STRING; 122586.NMB1528; -. DR PaxDb; Q9JYL4; -. DR EnsemblBacteria; AAF41883; AAF41883; NMB1528. DR GeneID; 904039; -. DR KEGG; nme:NMB1528; -. DR PATRIC; 20358856; VBINeiMen85645_1937. DR eggNOG; ENOG4105K85; Bacteria. DR eggNOG; COG0350; LUCA. DR HOGENOM; HOG000244137; -. DR KO; K00567; -. DR OMA; RMITLPS; -. DR OrthoDB; EOG6T1WR0; -. DR BioCyc; NMEN122586:GHGG-1569-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS. DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd. DR InterPro; IPR008332; MethylG_MeTrfase_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01035; DNA_binding_1; 1. DR Pfam; PF02870; Methyltransf_1N; 1. DR SUPFAM; SSF46767; SSF46767; 1. DR SUPFAM; SSF53155; SSF53155; 1. DR TIGRFAMs; TIGR00589; ogt; 1. DR PROSITE; PS00374; MGMT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF41883.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41883.1}. FT DOMAIN 99 178 Methyltransf_1N. FT {ECO:0000259|Pfam:PF02870}. FT DOMAIN 182 260 DNA_binding_1. FT {ECO:0000259|Pfam:PF01035}. SQ SEQUENCE 269 AA; 30418 MW; B341B0EBC3ECD0C4 CRC64; MAKIGDFAVK SMIGIRSKQM ITLPSLNNLP SKWDEIRHWL ESRVFECGVM PHPNLTECEA KQFERDFWDN IGCAPEEYVR IRRAIRLLEA RYPDSLNELV CAAIATPLGE MLAVFGSRGL CLLEFVGQKH LEQEIAAVQK ALRGRFVFRE DERTQLLRQE LDLYFKGRLK TFATPLEQIG TEFQKQAWDA LLAIPYGETR SYKEQAQRLG NPKAVRAVAA ANGQNKVSIL IPCHRVIGSD GKLTGYAGGL NRKQFLLALE HGEVQTALF // ID Q9JYX8_NEIMB Unreviewed; 126 AA. AC Q9JYX8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=HesB/YadR/YfhF family protein {ECO:0000313|EMBL:AAF41749.1}; GN OrderedLocusNames=NMB1381 {ECO:0000313|EMBL:AAF41749.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41749.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41749.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41749.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the HesB/IscA family. CC {ECO:0000256|SAAS:SAAS00595214}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41749.1; -; Genomic_DNA. DR PIR; H81089; H81089. DR RefSeq; NP_274397.1; NC_003112.2. DR RefSeq; WP_009348588.1; NC_003112.2. DR ProteinModelPortal; Q9JYX8; -. DR SMR; Q9JYX8; 22-116. DR STRING; 122586.NMB1381; -. DR PaxDb; Q9JYX8; -. DR EnsemblBacteria; AAF41749; AAF41749; NMB1381. DR GeneID; 903803; -. DR KEGG; nme:NMB1381; -. DR PATRIC; 20358441; VBINeiMen85645_1732. DR eggNOG; ENOG4108Z4V; Bacteria. DR eggNOG; COG0316; LUCA. DR HOGENOM; HOG000228314; -. DR KO; K13628; -. DR OMA; LAYSVDY; -. DR OrthoDB; EOG6VXF8J; -. DR BioCyc; NMEN122586:GHGG-1419-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR Gene3D; 2.60.300.12; -; 1. DR InterPro; IPR000361; FeS_biogenesis. DR InterPro; IPR016092; FeS_cluster_insertion. DR InterPro; IPR017870; FeS_cluster_insertion_CS. DR InterPro; IPR031108; ISCA-like. DR InterPro; IPR011302; IscA_proteobacteria. DR PANTHER; PTHR10072:SF48; PTHR10072:SF48; 1. DR Pfam; PF01521; Fe-S_biosyn; 1. DR SUPFAM; SSF89360; SSF89360; 1. DR TIGRFAMs; TIGR02011; IscA; 1. DR TIGRFAMs; TIGR00049; TIGR00049; 1. DR PROSITE; PS01152; HESB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 22 122 Fe-S_biosyn. {ECO:0000259|Pfam:PF01521}. SQ SEQUENCE 126 AA; 13501 MW; D6874F72E910F4FB CRC64; MPSEPPAASG PSGAVQQGRN MITLTENAAK HINDYLAKRG KGLGVRLGVK TSGCSGMAYN LEFVDEADGD DLIFEGHGAR IYIDPKSLVY LDGTQVDYTK EGLQEGFKFE NPNVKDSCGC GESFHV // ID Q9K0N8_NEIMB Unreviewed; 392 AA. AC Q9K0N8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=AcrA/AcrE family protein {ECO:0000313|EMBL:AAF40977.1}; GN OrderedLocusNames=NMB0548 {ECO:0000313|EMBL:AAF40977.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40977.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40977.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40977.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) CC (TC 8.A.1) family. {ECO:0000256|SAAS:SAAS00568556}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40977.1; -; Genomic_DNA. DR PIR; B81187; B81187. DR RefSeq; NP_273593.1; NC_003112.2. DR RefSeq; WP_010980813.1; NC_003112.2. DR ProteinModelPortal; Q9K0N8; -. DR STRING; 122586.NMB0548; -. DR PaxDb; Q9K0N8; -. DR EnsemblBacteria; AAF40977; AAF40977; NMB0548. DR GeneID; 902663; -. DR KEGG; nme:NMB0548; -. DR PATRIC; 20356359; VBINeiMen85645_0698. DR eggNOG; ENOG4105DJY; Bacteria. DR eggNOG; COG0845; LUCA. DR HOGENOM; HOG000216993; -. DR KO; K13888; -. DR OMA; EINVDSA; -. DR OrthoDB; EOG6DNT5K; -. DR BioCyc; NMEN122586:GHGG-574-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR032317; HlyD_D23. DR InterPro; IPR006143; RND_pump_MFP. DR Pfam; PF16576; HlyD_D23; 1. DR TIGRFAMs; TIGR01730; RND_mfp; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 43 265 HlyD_D23. {ECO:0000259|Pfam:PF16576}. FT COILED 143 177 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 41743 MW; BE38F3EDEA2CCDD4 CRC64; MAKMMKWAAV AAVAAAAVWG GWSYLKPEPQ AAYITETVRR GDISRTVSAT GEISPSNLVS VGAQASGQIK ILYVKLGQQV KKGDLIAEIN STSQTNTLNT EKSKLETYQA KLVSAQIALG SAEKKYKRQA ALWKENATSK EDLESAQDAF AAAKANVAEL KALIRQSKIS INTAESELGY TRITATMDGT VVAILVEEGQ TVNAAQSTPT IVQLANLDMM LNKMQIAEGD ITKVKAGQDI SFTILSEPDT PIKAKLDSVD PGLTTMSSGG YNSSTDTASN AVYYYARSFV PNPDGKLATG MTTQNTVEID GVKNVLIIPS LTVKNRGGKA FVRVLGADGK AAEREIRTGM RDSMNTEVKS GLKEGDKVVI SEITAAEQQE SGERALGGPP RR // ID Q9K134_NEIMB Unreviewed; 472 AA. AC Q9K134; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356}; GN Name=glnA {ECO:0000313|EMBL:AAF40802.1}; GN OrderedLocusNames=NMB0359 {ECO:0000313|EMBL:AAF40802.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40802.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40802.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40802.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. {ECO:0000256|RuleBase:RU004356}. CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two CC hexagons. {ECO:0000256|RuleBase:RU000387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000387}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000256|RuleBase:RU000384}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40802.1; -; Genomic_DNA. DR PIR; F81208; F81208. DR RefSeq; NP_273408.1; NC_003112.2. DR RefSeq; WP_002226993.1; NC_003112.2. DR ProteinModelPortal; Q9K134; -. DR SMR; Q9K134; 2-472. DR STRING; 122586.NMB0359; -. DR PaxDb; Q9K134; -. DR EnsemblBacteria; AAF40802; AAF40802; NMB0359. DR GeneID; 902475; -. DR KEGG; nme:NMB0359; -. DR PATRIC; 20355873; VBINeiMen85645_0454. DR eggNOG; ENOG4105C5F; Bacteria. DR eggNOG; COG0174; LUCA. DR HOGENOM; HOG000005157; -. DR KO; K01915; -. DR OMA; KVLNQVG; -. DR OrthoDB; EOG6B360N; -. DR BioCyc; NMEN122586:GHGG-381-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR Gene3D; 3.10.20.70; -; 1. DR Gene3D; 3.30.590.10; -; 1. DR InterPro; IPR008147; Gln_synt_b-grasp. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR InterPro; IPR008146; Gln_synth_cat_dom. DR InterPro; IPR027303; Gln_synth_gly_rich_site. DR InterPro; IPR004809; Gln_synth_I. DR InterPro; IPR001637; Gln_synth_I_adenylation_site. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; SSF54368; 1. DR TIGRFAMs; TIGR00653; GlnA; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00182; GLNA_ADENYLATION; 1. DR PROSITE; PS00181; GLNA_ATP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004356}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:AAF40802.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004356}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT MOD_RES 401 401 O-AMP-tyrosine. FT {ECO:0000256|PIRSR:PIRSR604809-50}. SQ SEQUENCE 472 AA; 52137 MW; BCD2E0E5EBBDC73D CRC64; MSIKNAVKLI EESEARFVDL RFTDTKGKQH HFTVPARIVL EDPEEWFENG QAFDGSSIGG WKGIQASDMQ LRPDASTAFV DPFYDDATVV LTCDVIDPAD GQGYDRDPRS IARRAEAYLK SSGIGETAYF GPEPEFFVFD GIEFETDMHK TRYEITSESG AWASGLHMDG QNTGHRPTVK GGYAPVAPID CGQDLRSAMV NILEELGIEV EVHHSEVGTG SQMEIGTRFA TLVKRADQTQ DMKYVIQNVA HNFGKTATFM PKPIMGDNGS GMHVHQSIWK DGQNLFAGDG YAGLSDTALY YIGGIIKHAK ALNAITNPST NSYKRLVPHF EAPTKLAYSA KNRSASIRIP SVNSSKARRI EARFPDPTAN PYLAFAALLM AGLDGIQNKI HPGDPADKNL YDLPPEEDAL VPTVCASLEE ALAALKADHE FLLRGGVFSK DWIDSYIAFK EEDVRRIRMA PHPLEFEMYY SL // ID Q9JYI4_NEIMB Unreviewed; 861 AA. AC Q9JYI4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Aconitate hydratase B {ECO:0000256|PIRNR:PIRNR036687}; DE EC=4.2.1.3 {ECO:0000256|PIRNR:PIRNR036687}; DE EC=4.2.1.99 {ECO:0000256|PIRNR:PIRNR036687}; DE AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687}; GN Name=acnB {ECO:0000313|EMBL:AAF41925.1}; GN OrderedLocusNames=NMB1572 {ECO:0000313|EMBL:AAF41925.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41925.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41925.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41925.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = CC (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O. CC {ECO:0000256|PIRNR:PIRNR036687}. CC -!- CATALYTIC ACTIVITY: Citrate = isocitrate. CC {ECO:0000256|PIRNR:PIRNR036687}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRSR:PIRSR036687-1}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|PIRSR:PIRSR036687-1}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC isocitrate from oxaloacetate: step 2/2. CC {ECO:0000256|PIRNR:PIRNR036687}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|PIRNR:PIRNR036687}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41925.1; -; Genomic_DNA. DR PIR; G81068; G81068. DR RefSeq; NP_274578.1; NC_003112.2. DR RefSeq; WP_002222205.1; NC_003112.2. DR ProteinModelPortal; Q9JYI4; -. DR SMR; Q9JYI4; 1-859. DR STRING; 122586.NMB1572; -. DR PaxDb; Q9JYI4; -. DR PRIDE; Q9JYI4; -. DR EnsemblBacteria; AAF41925; AAF41925; NMB1572. DR GeneID; 904159; -. DR KEGG; nme:NMB1572; -. DR PATRIC; 20359008; VBINeiMen85645_2023. DR eggNOG; ENOG4107QIJ; Bacteria. DR eggNOG; COG1049; LUCA. DR HOGENOM; HOG000205991; -. DR KO; K01682; -. DR OMA; HATTRPD; -. DR OrthoDB; EOG6N944W; -. DR BioCyc; NMEN122586:GHGG-1613-MONOMER; -. DR UniPathway; UPA00223; UER00718. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR004406; Aconitase_B. DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom. DR InterPro; IPR015929; Aconitase_B_N. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF06434; Aconitase_2_N; 1. DR Pfam; PF11791; Aconitase_B_N; 1. DR PIRSF; PIRSF036687; AcnB; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR SUPFAM; SSF53732; SSF53732; 1. DR SUPFAM; SSF74778; SSF74778; 1. DR TIGRFAMs; TIGR00117; acnB; 1. DR PROSITE; PS00450; ACONITASE_1; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1, KW ECO:0000256|SAAS:SAAS00436230}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|PIRSR:PIRSR036687-1, ECO:0000256|SAAS:SAAS00436230}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR036687-1, KW ECO:0000256|SAAS:SAAS00436230}; KW Lyase {ECO:0000256|PIRNR:PIRNR036687, ECO:0000256|SAAS:SAAS00432333, KW ECO:0000313|EMBL:AAF41925.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1, KW ECO:0000256|SAAS:SAAS00436230}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR036687}. FT DOMAIN 4 156 Aconitase_B_N. FT {ECO:0000259|Pfam:PF11791}. FT DOMAIN 168 380 Aconitase_2_N. FT {ECO:0000259|Pfam:PF06434}. FT DOMAIN 473 814 Aconitase. {ECO:0000259|Pfam:PF00330}. FT REGION 244 246 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR036687-2}. FT REGION 415 417 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR036687-2}. FT METAL 711 711 Iron-sulfur (4Fe-4S). FT {ECO:0000256|PIRSR:PIRSR036687-1}. FT METAL 769 769 Iron-sulfur (4Fe-4S). FT {ECO:0000256|PIRSR:PIRSR036687-1}. FT METAL 772 772 Iron-sulfur (4Fe-4S). FT {ECO:0000256|PIRSR:PIRSR036687-1}. FT BINDING 191 191 Substrate. FT {ECO:0000256|PIRSR:PIRSR036687-2}. FT BINDING 499 499 Substrate. FT {ECO:0000256|PIRSR:PIRSR036687-2}. FT BINDING 791 791 Substrate. FT {ECO:0000256|PIRSR:PIRSR036687-2}. FT BINDING 796 796 Substrate. FT {ECO:0000256|PIRSR:PIRSR036687-2}. SQ SEQUENCE 861 AA; 92715 MW; 74F2101C65AF0ECF CRC64; MLEAYRKAAA ERAALGIPAL PLNAQQTADL VELLKSPPAG EGEFLVELLA HRVPPGVDDA AKVKASFLAA VAEGSASSPL ISPEYATELL GTMLGGYNIH ALIELLDDDK LASIAAKGLK HTLLMFDSFH DVQEKAEKGN KYAQEVLQSW ADAEWFASRA KVPEKITVTV FKVDGETNTD DLSPAPDAWS RPDIPLHALA MLKNPRDGIT PDKPGEVGPI KLLEELKAKG HPVAYVGDVV GTGSSRKSAT NSVIWHTGED IPFVPNKRFG GVCLGGKIAP IFFNTQEDSG ALPIEVDVSA LKMGDVVDIL PYEGKIVKNG ETVAEFELKS QVLLDEVQAG GRINLIIGRG LTAKAREALK LPASTAFRLP QAPAESKAGF TLAQKMVGRA CGLPEGQGVR PGTYCEPRMT TVGSQDTTGP MTRDELKDLA CLGFSADMVM QSFCHTAAYP KPVDVKTHKE LPAFISTRGG VSLRPGDGVI HSWLNRLLLP DTVGTGGDSH TRFPIGISFP AGSGLVAFAA ATGVMPLDMP ESVLVRFSGK LQPGVTLRDL VNAIPLYAIK QGLLTVAKAG KKNIFSGRIL EIEGLPDLKV EQAFELTDAS AERSAAGCTV KLNKEPIIEY MKSNVVLMKN MIANGYQDPR TLERRIKAME KWLANPELLE ADKDAEYAAV IEINMDDIKE PIIACPNDPD DVCFMSERSG TKIDEVFIGS CMTNIGHFRA ASKLLEGKAD TPVRLWIAPP TKMDAKQLSD EGHYGVLGRA GARMEMPGCS LCMGNQAQVR EGATVMSTST RNFPNRLGKN TFVYLGSAEL AAICSKLGKI PTVEEYQANI GIINEQGDKI YRYMNFNEID SYNEVAETVN V // ID Q9K0Z9_NEIMB Unreviewed; 1201 AA. AC Q9K0Z9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197}; GN Name=putA {ECO:0000313|EMBL:AAF40840.1}; GN OrderedLocusNames=NMB0401 {ECO:0000313|EMBL:AAF40840.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40840.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40840.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40840.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and CC nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRNR:PIRNR000197}; CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 1/2. CC {ECO:0000256|PIRNR:PIRNR000197}. CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L- CC glutamate; L-glutamate from L-proline: step 2/2. CC {ECO:0000256|PIRNR:PIRNR000197}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}. CC -!- SIMILARITY: In the N-terminal section; belongs to the proline CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40840.1; -; Genomic_DNA. DR PIR; F81202; F81202. DR RefSeq; NP_273450.1; NC_003112.2. DR RefSeq; WP_002224912.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z9; -. DR SMR; Q9K0Z9; 9-516. DR STRING; 122586.NMB0401; -. DR PaxDb; Q9K0Z9; -. DR EnsemblBacteria; AAF40840; AAF40840; NMB0401. DR GeneID; 902515; -. DR KEGG; nme:NMB0401; -. DR PATRIC; 20355983; VBINeiMen85645_0509. DR eggNOG; ENOG4105C26; Bacteria. DR eggNOG; COG0506; LUCA. DR eggNOG; COG4230; LUCA. DR HOGENOM; HOG000253911; -. DR KO; K13821; -. DR OMA; YSLDTQE; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NMEN122586:GHGG-423-MONOMER; -. DR UniPathway; UPA00261; UER00373. DR UniPathway; UPA00261; UER00374. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.2060.10; -; 1. DR Gene3D; 1.20.5.550; -; 1. DR Gene3D; 3.20.20.220; -; 1. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR025703; Bifunct_PutA. DR InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR024090; PRODH_PutA_dom_I. DR InterPro; IPR024089; PRODH_PutA_dom_I/II. DR InterPro; IPR024082; PRODH_PutA_dom_II. DR InterPro; IPR002872; Proline_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR Pfam; PF01619; Pro_dh; 1. DR Pfam; PF14850; Pro_dh-DNA_bdg; 1. DR PIRSF; PIRSF000197; Bifunct_PutA; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR SUPFAM; SSF81935; SSF81935; 1. DR TIGRFAMs; TIGR01238; D1pyr5carbox3; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|PIRNR:PIRNR000197}; KW FAD {ECO:0000256|PIRNR:PIRNR000197}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000197}; KW NAD {ECO:0000256|PIRNR:PIRNR000197}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000197, KW ECO:0000313|EMBL:AAF40840.1}; KW Proline metabolism {ECO:0000256|PIRNR:PIRNR000197}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Repressor {ECO:0000256|PIRNR:PIRNR000197}; KW Transcription {ECO:0000256|PIRNR:PIRNR000197}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}. FT DOMAIN 66 176 Pro_dh-DNA_bdg. FT {ECO:0000259|Pfam:PF14850}. FT DOMAIN 187 479 Pro_dh. {ECO:0000259|Pfam:PF01619}. FT DOMAIN 566 1007 Aldedh. {ECO:0000259|Pfam:PF00171}. FT ACT_SITE 782 782 {ECO:0000256|PIRSR:PIRSR000197-1}. FT ACT_SITE 816 816 {ECO:0000256|PIRSR:PIRSR000197-1}. SQ SEQUENCE 1201 AA; 129951 MW; DDEF5443DF017EEF CRC64; MFHFAFPAQT ALRQAITDAY RRNEIEAVQD MLQRAQMSDE ERNAASELAR RLVTQVRAGR TKAGGVDALM HEFSLSSEEG IALMCLAEAL LRIPDNATRD RLIADKISDG NWKSHLNNSP SLFVNAAAWG LLITGKLTAT NDKQMSSALS RLISKGGAPL IRQGVNYAMR LLGKQFVTGQ TIEEALQNGK EREKMGYRFS FDMLGEAAYT QADADRYYRD YVEAIHAIGK DAAGQGVYEG NGISVKLSAI HPRYSRTQHG RVMGELLPRL KELFLLGKKY DIGINIDAEE ANRLELSLDL MEALVSDPDL AGYKGIGFVV QAYQKRCPFV IDYLIDLARR NNQKLMIRLV KGAYWDSEIK WAQVDGLNGY PTYTRKVHTD ISYLACARKL LSAQDAVFPQ FATHNAYTLG AIYQMGKGKD FEHQCLHGMG ETLYDQVVGP QNLGRRVRVY APVGTHETLL AYLVRRLLEN GANSSFVNQI VDENISIDTL IRSPFDTIAE QGIHLHNALP LPRDLYGKCR LNSQGVDLSN ENVLQQLQEQ MNKAAAQDFH AASIVNGKAR DVGEAQPIKN PADHDDIVGT VSFADAALAQ EAVGAAVAAF PEWSATPAAE RAACLRRFAD LLEQHTPALM MLAVREAGKT LNNAIAEVRE AVDFCRYYAN EAEHTLPQDA KAVGAIVAIS PWNFPLAIFT GEVVSALAAG NTVIAKPAEQ TSLIAGYAVS LMHEAGIPTS ALQLVLGAGD VGAALTNDAR IGGVIFTGST EVARLINKAL AKRGDNPVLI AETGGQNAMI VDSTALAEQV CADVLNSAFD SAGQRCSALR ILCVQEDVAD RMLDMIKGAM DELVVGKPIQ LTTDVGPVID AEAQQNLLNH INKMKGVAKS YHEVKTAADV DSKKSTFVRP ILFELNNLNE LQREVFGPVL HVVRYRADEL DNVIDQINSK GYALTHGVHS RIEGTVRHIR SRIEAGNVYV NRNIVGAVVG VQPFGGHGLS GTGPKAGGSF YLQKLTRAGE WVAPTLSQIG QADEAALKRL EALVHKLPFN AEEKKAAAAA LGHARIRTLR RAETVLTGPT GERNSISWHA PKRVWIHGGS TVQAFAALTE LAASGIQAVV EPDSPLASYT ADLEGLLLVN GKPETAGISH VAALSPLDSA RKQELAAHDG ALIRILPSEN GLDILQVFEE ISCSVNTTAA GGNASLMAVA D // ID Q9JY58_NEIMB Unreviewed; 582 AA. AC Q9JY58; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42071.1}; GN OrderedLocusNames=NMB1726 {ECO:0000313|EMBL:AAF42071.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42071.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42071.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42071.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42071.1; -; Genomic_DNA. DR PIR; E81048; E81048. DR RefSeq; NP_274729.1; NC_003112.2. DR RefSeq; WP_002212594.1; NC_003112.2. DR ProteinModelPortal; Q9JY58; -. DR STRING; 122586.NMB1726; -. DR PaxDb; Q9JY58; -. DR EnsemblBacteria; AAF42071; AAF42071; NMB1726. DR GeneID; 903375; -. DR KEGG; nme:NMB1726; -. DR PATRIC; 20359415; VBINeiMen85645_2213. DR eggNOG; ENOG4105DFV; Bacteria. DR eggNOG; COG3975; LUCA. DR HOGENOM; HOG000255783; -. DR OMA; TTSYYDL; -. DR OrthoDB; EOG6V4G82; -. DR BioCyc; NMEN122586:GHGG-1781-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR024191; Peptidase_M61. DR InterPro; IPR007963; Peptidase_M61_catalytic. DR Pfam; PF05299; Peptidase_M61; 1. DR PIRSF; PIRSF016493; Glycyl_aminpptds; 1. DR SUPFAM; SSF50156; SSF50156; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 262 377 Peptidase_M61. FT {ECO:0000259|Pfam:PF05299}. SQ SEQUENCE 582 AA; 65824 MW; 295D4FF4A4291B7C CRC64; MIHYKITPSP LDHEWHILLT FTQDDDLPIE ISLPNWVPGS YLIRDFSRHI TSIHASCNGT SMPLEQIAKN RWHAAAVRGE WQIRYTVYAF DLSVRGSFLT TERGFFDGSC LFLKVEGTET LPHRLELTGI PSEWRIATTL PETGRFVFQA ASYAELIDRP VEMGLIEFLD FEAAGIPHTI ALSGIYPDFD RNRLVSDIKK ICETELAVFS SPAPFQKYLF LLHVGDHIYG GLEHTDSTAL LADRHSLPPY GMTDADDTYT TLLGLFSHEY FHAWNVKSIK PAAFVPYDLD KENYTEQLWA FEGITSYYDD LFLARSRTIS PESYLNLLAQ GITRVQQTRG RLRQTLAESS FTAWNKFYKP DENSPNAIVS YYQKGALAAL CLDLIIRNRS NGRHSLDTLM DKLYREWRDT HSGIPEKHWQ IRCQEITGLD LEDFFQKALY STEDLPLAEC LATAGVGLTF LPLPRQHGGG YAEHICPVPS AGDFGARFKQ NTDHIVLTHV FNGGSAESAA LCPQDKIIAL DGYACTDFTA QWARYHVNAK INIHFFRAGI LRQTVLTVQA AAADTAILHI TDRNLLDNWL FG // ID Q9JZB6_NEIMB Unreviewed; 791 AA. AC Q9JZB6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895}; DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895}; DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895}; GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895}; GN OrderedLocusNames=NMB1200 {ECO:0000313|EMBL:AAF41582.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41582.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41582.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41582.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside CC monophosphates and is involved in maturation of structured RNAs. CC {ECO:0000256|HAMAP-Rule:MF_01895}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. {ECO:0000256|HAMAP- CC Rule:MF_01895, ECO:0000256|SAAS:SAAS00089937}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895, CC ECO:0000256|SAAS:SAAS00089931}. CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP- CC Rule:MF_01895}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41582.1; -; Genomic_DNA. DR PIR; G81109; G81109. DR RefSeq; NP_274225.1; NC_003112.2. DR RefSeq; WP_002225208.1; NC_003112.2. DR ProteinModelPortal; Q9JZB6; -. DR STRING; 122586.NMB1200; -. DR PaxDb; Q9JZB6; -. DR EnsemblBacteria; AAF41582; AAF41582; NMB1200. DR GeneID; 903622; -. DR KEGG; nme:NMB1200; -. DR PATRIC; 20357989; VBINeiMen85645_1507. DR eggNOG; ENOG4105C40; Bacteria. DR eggNOG; COG0557; LUCA. DR HOGENOM; HOG000071120; -. DR KO; K12573; -. DR OMA; YRVHEGP; -. DR OrthoDB; EOG6Q5NRD; -. DR BioCyc; NMEN122586:GHGG-1237-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01895; RNase_R; 1. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013223; RNase_B_OB_dom. DR InterPro; IPR022966; RNase_II/R_CS. DR InterPro; IPR004476; RNase_II/RNase_R. DR InterPro; IPR011805; RNase_R. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF08206; OB_RNB; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 4. DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1. DR TIGRFAMs; TIGR02063; RNase_R; 1. DR PROSITE; PS01175; RIBONUCLEASE_II; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462075}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462115}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462115}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462115}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462035}. FT DOMAIN 639 720 S1 motif. {ECO:0000256|HAMAP- FT Rule:MF_01895, FT ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 791 AA; 88987 MW; 5B61C2FAC853489A CRC64; MNKNIKSLNL REKDPFLSRE KQRYEHPLPS REWIIELLER KGVPSKIESL ARELSITEDE YVFFERRLKA MARDGQVLIN RRGAVCAADK LDLVKCRVEA HKDGFGFAVP LTPAKDGDFV LYERQMRGIM HGDIVTVRPA GMDRRGRREG TVLDIVERAQ SKVVGRFYMD RGVAILEPED KRLNQSIVLE PDGVARFKPE SGQVIVGEIE VYPEQNRPAV AKIIEVLGDY ADSGMEIEIA VRKHHLPHQF SEACAKAAKK IPVHVRKSDL KGRVDLRDLP LVTIDGETAR DFDDAVFAEK VGRNYRLVVA IADVSHYVRP DDVIDADAQE RSTSVYFPRR VIPMLPENLS NGICSLNPDV ERLCMVCDMV VTYAGNIKEY RFYPAVMRSH ARLTYNQVWK WISDGIDHPY KAQIDTLYKL FKILQKKRFE RGAVEFESVE TQMIFDDNGK IEKIVPVVRN DAHKLIEECM LAANVCAADF LLKNKHTALF RNHLGPTPEK LATLREQLGL LGLQLGGGDN PSPKDYAALV EQFKGRPDAE LLQVMMLRSM QQAVYEPHCD GHFGLAYEAY AHFTSPIRRY PDLTVHRAIK AVLNQQTYTP KKSWQALGVH TSFCERRADD ASRDVENWLK TYYMRDKVGE VFEGKISGMT SFGIFVTLDG IHIDGLVHIS DLGEDYFNFR PEIMAIEGER SGIRFNMGDR VAVRVARADL DDGKIDFVLI AGGSGRGRKV KSSASAKPAG TAGKGKPKTA AEKKTARGGK VRGRGASAAA ESRKKAKKPV PIKVKKRKGK S // ID Q9JY83_NEIMB Unreviewed; 86 AA. AC Q9JY83; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Putative acyl carrier protein {ECO:0000313|EMBL:AAF42045.1}; GN OrderedLocusNames=NMB1697 {ECO:0000313|EMBL:AAF42045.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42045.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42045.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42045.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42045.1; -; Genomic_DNA. DR PIR; C81052; C81052. DR RefSeq; NP_274701.1; NC_003112.2. DR RefSeq; WP_002222118.1; NC_003112.2. DR ProteinModelPortal; Q9JY83; -. DR STRING; 122586.NMB1697; -. DR PaxDb; Q9JY83; -. DR EnsemblBacteria; AAF42045; AAF42045; NMB1697. DR GeneID; 903406; -. DR KEGG; nme:NMB1697; -. DR PATRIC; 20359351; VBINeiMen85645_2182. DR eggNOG; ENOG4105VME; Bacteria. DR eggNOG; COG0236; LUCA. DR HOGENOM; HOG000178185; -. DR KO; K02078; -. DR OMA; HFRSINT; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; NMEN122586:GHGG-1752-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.1200.10; -; 1. DR InterPro; IPR009081; PP-bd_ACP. DR Pfam; PF00550; PP-binding; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 61 Acyl carrier. FT {ECO:0000259|PROSITE:PS50075}. SQ SEQUENCE 86 AA; 9328 MW; DDCC730CCA078D0F CRC64; MNDLENQIKQ LIIDSLALED ITAADIGSED ALFGDGGLGL DSVDALELGL AVQKHFGFRL DGEQENLREH FANVKTLAAF VKSRQA // ID Q9JXL0_NEIMB Unreviewed; 324 AA. AC Q9JXL0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Iron(III) ABC transporter, permease protein {ECO:0000313|EMBL:AAF42318.1}; GN OrderedLocusNames=NMB1991 {ECO:0000313|EMBL:AAF42318.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42318.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42318.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42318.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. CC {ECO:0000256|SAAS:SAAS00535775}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42318.1; -; Genomic_DNA. DR PIR; F81018; F81018. DR RefSeq; NP_274983.1; NC_003112.2. DR RefSeq; WP_002221668.1; NC_003112.2. DR ProteinModelPortal; Q9JXL0; -. DR STRING; 122586.NMB1991; -. DR PaxDb; Q9JXL0; -. DR EnsemblBacteria; AAF42318; AAF42318; NMB1991. DR GeneID; 904139; -. DR KEGG; nme:NMB1991; -. DR PATRIC; 20360079; VBINeiMen85645_2544. DR eggNOG; ENOG4105CM4; Bacteria. DR eggNOG; COG4605; LUCA. DR HOGENOM; HOG000099129; -. DR KO; K02015; -. DR OMA; FMTLNVK; -. DR OrthoDB; EOG6WMJ1X; -. DR BioCyc; NMEN122586:GHGG-2048-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00417415}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00417415, KW ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417373}. FT TRANSMEM 17 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 185 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 261 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 320 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 324 AA; 35234 MW; 7B76BB84A7160698 CRC64; MPSEKNIGFM AGSSRPLWVA FALLLVSCVL FMTLNVKGDW DFVLQLRLTK LAALLMVAYA VGVSTQLFQT LTNNPILTPS ILGFDSLYVF LQTLLVFTFG GVGYASLPLT GKFGFELVVM MGGSLLLFYT LIKQGGRDLS RMILIGVIFG ILFRSLSSLL SRMIDPEEFT AAQANMFAGF NTVHSELLGI GALILLVSAA VVWRERYRLD VYLLGRDQAV NLGISYTRNT LWILLWIAAL VATATAVVGP VSFFGLLAAS LANHFSPSVK HSVRLPMTVC IGGILLVGGQ TVFEHLLGMQ AVLSVVVEFA GGLVFLYLVL KHKK // ID Q9K0S9_NEIMB Unreviewed; 327 AA. AC Q9K0S9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Replication protein {ECO:0000313|EMBL:AAF40928.1}; GN OrderedLocusNames=NMB0495 {ECO:0000313|EMBL:AAF40928.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40928.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40928.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40928.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40928.1; -; Genomic_DNA. DR PIR; A81192; A81192. DR RefSeq; NP_273541.1; NC_003112.2. DR RefSeq; WP_002219732.1; NC_003112.2. DR ProteinModelPortal; Q9K0S9; -. DR STRING; 122586.NMB0495; -. DR PaxDb; Q9K0S9; -. DR EnsemblBacteria; AAF40928; AAF40928; NMB0495. DR GeneID; 902611; -. DR KEGG; nme:NMB0495; -. DR PATRIC; 20356240; VBINeiMen85645_0640. DR eggNOG; ENOG41063CS; Bacteria. DR eggNOG; COG5527; LUCA. DR HOGENOM; HOG000152761; -. DR OMA; ETNRWIA; -. DR OrthoDB; EOG6G7R0W; -. DR BioCyc; NMEN122586:GHGG-520-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005727; C:extrachromosomal circular DNA; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR InterPro; IPR000525; Initiator_Rep_prot. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01051; Rep_3; 1. DR SUPFAM; SSF46785; SSF46785; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 184 Rep_3. {ECO:0000259|Pfam:PF01051}. SQ SEQUENCE 327 AA; 37432 MW; 82E132128B1941BE CRC64; MLLTLHGTDK FCIVNNFHTN RNTAYKALKD ACNNLFERQF SFIEKTPKGE KVVRTRWVSQ VAYIEQQATV ELVFAPNVAP LITMLEKNFT SYELDQVSSL SSKYAVRLYE IIISWRAAGK TPMFSTMELR ERLGMMPDEY QKMELFKRKV LDFAVKQIND KTDISITYEQ HKEGRKIVGF TFSILHKIGS KDIPLENQSE LFAGMTDLEA GTIRVRAEAY IASLIAKGQN VTKAHRLNIL KKAVEERWGF EDVAKDNGAK NPENKNAKVV LNEWEKISNG TRFKDKDGTI WVKDSGMLRT EGTNRWIADS QIAKLFPMLT VMVEEGI // ID Q9JY77_NEIMB Unreviewed; 416 AA. AC Q9JY77; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=3-oxoacyl-(Acyl-carrier-protein) synthase II {ECO:0000313|EMBL:AAF42051.1}; DE EC=2.3.1.41 {ECO:0000313|EMBL:AAF42051.1}; GN Name=fabF-2 {ECO:0000313|EMBL:AAF42051.1}; GN OrderedLocusNames=NMB1703 {ECO:0000313|EMBL:AAF42051.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42051.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42051.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42051.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. CC {ECO:0000256|RuleBase:RU003694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42051.1; -; Genomic_DNA. DR PIR; A81053; A81053. DR RefSeq; NP_274707.1; NC_003112.2. DR RefSeq; WP_002257271.1; NC_003112.2. DR ProteinModelPortal; Q9JY77; -. DR STRING; 122586.NMB1703; -. DR PaxDb; Q9JY77; -. DR EnsemblBacteria; AAF42051; AAF42051; NMB1703. DR GeneID; 903400; -. DR KEGG; nme:NMB1703; -. DR PATRIC; 20359361; VBINeiMen85645_2187. DR eggNOG; COG0304; LUCA. DR HOGENOM; HOG000060165; -. DR KO; K09458; -. DR OMA; FFPSEVY; -. DR OrthoDB; EOG6DG2SR; -. DR BioCyc; NMEN122586:GHGG-1758-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:AAF42051.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42051.1}. SQ SEQUENCE 416 AA; 44525 MW; F1C4CC76112E1B8C CRC64; MLNTRRVAVT GIGGITAFGR DWQSIQAAFK AEKNAVKYMD WHERFPELEA QLGAPIENYA PPKHWTRKQL RSMGRVSYLC VDAAEQALAD AGLLGDESIT DGRMGVACGS SSGSTKDIGD VGELLLTGTS RNFSANTYVR MMPHTTAANI GIFFGLKGRI IPTSSACSSG SQGIGYAYEA IKYGLTDMML AGGGEEFFPS EVYVFDSLYA ASRRNGEPEK TPRPYDANRD GLVIGEGAGI FVLEELEHAK RRGAIIYAEL VGYGANSDAY HISTPRPDAQ GAILAFQTAL QHANLAPEDI GWINLHGTGT HHNDNMESRA VAAVFGNNTP CTSTKPQTGH TLGAADAIEA AFAWGIADRQ SNPEGKLPPR LWDGQNDPNL PAINLTGSGS RWETEKRITA SSSFAFGGSN CVLIIG // ID Q9JYX5_NEIMB Unreviewed; 916 AA. AC Q9JYX5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897, GN ECO:0000313|EMBL:AAF41750.1}; GN OrderedLocusNames=NMB1384 {ECO:0000313|EMBL:AAF41750.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41750.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41750.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41750.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01897, CC ECO:0000256|SAAS:SAAS00075911}. CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP- CC Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming CC negative supercoils. Not all organisms have 2 type II CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. {ECO:0000256|SAAS:SAAS00565436}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41750.1; -; Genomic_DNA. DR PIR; A81089; A81089. DR RefSeq; NP_274400.1; NC_003112.2. DR RefSeq; WP_002216981.1; NC_003112.2. DR ProteinModelPortal; Q9JYX5; -. DR SMR; Q9JYX5; 38-533. DR STRING; 122586.NMB1384; -. DR PaxDb; Q9JYX5; -. DR EnsemblBacteria; AAF41750; AAF41750; NMB1384. DR GeneID; 903806; -. DR KEGG; nme:NMB1384; -. DR PATRIC; 20358447; VBINeiMen85645_1735. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR HOGENOM; HOG000076278; -. DR KO; K02469; -. DR OMA; ETVDWVP; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; NMEN122586:GHGG-1422-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.268.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 1. DR HAMAP; MF_01897; GyrA; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR005743; GyrA. DR InterPro; IPR006691; GyrA/parC_pinwhl. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013757; Topo_IIA_A_a. DR Pfam; PF03989; DNA_gyraseA_C; 7. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00440775}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00454525}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00454388}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00440775}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897, KW ECO:0000256|SAAS:SAAS00454388}. FT DOMAIN 19 510 TOP4c. {ECO:0000259|SMART:SM00434}. FT MOTIF 571 577 GyrA-box. {ECO:0000256|HAMAP- FT Rule:MF_01897}. FT ACT_SITE 130 130 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01897}. SQ SEQUENCE 916 AA; 101371 MW; D5DFE651B804782F CRC64; MTDATIRHDH KFALETLPVS LEDEMRKSYL DYAMSVIVGR ALPDVRDGLK PVHRRVLYAM HELKNNWNAA YKKSARIVGD VIGKYHPHGD TAVYDTIVRM AQNFAMRYVL IDGQGNFGSV DGLAAAAMRY TEIRMAKISH EMLADIEEET VNFGPNYDGS EHEPLVLPTR FPTLLVNGSS GIAVGMATNI PPHNLSDTVN ACLRLLDAPD TEIDELIDII QAPDFPTGAT IYGLSGVREG YKTGRGRVVM RGKTHIEPIG RNGEREAIVI DEIPYQVNKA KLVEKIGDLV REKTLEGISE LRDESDKSGM RVVIELKRNE NAEVVLNQLY KLTPLQDSFG INMVVLVDGQ PRLLNLKQIL SEFLRHRREV VTRRTLFRLK KARHEGHIAE GKAVALSNID EIIKLIKESP NAAEAKDKLL ARPWRSSLVE EMLTRSGLDL EMMRPEGLAA NIGLKEQGYY LSEIQADAIL RMSLRNLTGL DQEEIVESYK NLMGKIIDFV DILSKPERIT QIIRDELEEI KTNYGDERRS EINPFGGDIA DEDLIPQREM VVTLTHGGYI KTQPTTDYQA QRRGGRGKQA AATKDEDFIE TLFVANTHDY LMCFTNLGKC HWIKVYKLPE GGRNSRGRPI NNVIQLEEGE KVSAILAVRE FPEDQYVFFA TAQGMVKKVQ LSAFKNVRAQ GIKAIALKEG DYLVGAAQTG GADDIMLFSN LGKAIRFNEY WEKSGNDEAE DADIETEISD GIEDETADSE NALPSGKHGV RPSGRGSGGL RGMRLPADGK IVSLITFAPE TEESGLQVLT ATANGYGKRT PIADYSRKNK GGQGNIAINT GERNGDLVAA TLVGETDDLM LITSGGVLIR TKVEQIRETG RAAAGVKLIN LDEGETLVSL ERVAEDESEL SDASVISNVT EPEVEN // ID Q9K024_NEIMB Unreviewed; 385 AA. AC Q9K024; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AAF41215.1}; DE EC=2.5.1.48 {ECO:0000313|EMBL:AAF41215.1}; GN Name=metB {ECO:0000313|EMBL:AAF41215.1}; GN OrderedLocusNames=NMB0802 {ECO:0000313|EMBL:AAF41215.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41215.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41215.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41215.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU362118}; CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. CC {ECO:0000256|RuleBase:RU362118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41215.1; -; Genomic_DNA. DR PIR; A81158; A81158. DR RefSeq; NP_273844.1; NC_003112.2. DR RefSeq; WP_002219510.1; NC_003112.2. DR ProteinModelPortal; Q9K024; -. DR STRING; 122586.NMB0802; -. DR PaxDb; Q9K024; -. DR EnsemblBacteria; AAF41215; AAF41215; NMB0802. DR GeneID; 902917; -. DR KEGG; nme:NMB0802; -. DR PATRIC; 20356991; VBINeiMen85645_1014. DR eggNOG; ENOG4105C28; Bacteria. DR eggNOG; COG0626; LUCA. DR HOGENOM; HOG000246415; -. DR KO; K01739; -. DR OMA; PPIYQVS; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; NMEN122586:GHGG-833-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00868; CYS_MET_METAB_PP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41215.1}. FT MOD_RES 197 197 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 385 AA; 42169 MW; 90317574C8B39F85 CRC64; MKFATKAIHS SYDCDEHNRA LMPPIYQNSM FALHEIGENV PYRYSRLSNP TRQILEDTVA DLEHGAAGFA FSSGMAGIDA VWRTFLRPGD TIVAVADIYG GAYDLLVDVY QKWGVNVVFA DLGNPDNLDE LLKAHKVKLV WLETPSNPLL RLVDIKVLAA KAKAAGALVG IDNTFATPYL QQPLDMGCDF VFHSATKYLC GHSDVLMGIV VAKTKELAQP LHDMMVHTGA VAGPLDCWLV LRGIKTLALR MNAHCQNALE IARRLEAHPA IEKVFHPGLP SHEHYELAKT QMPKGIGGVV TVYLKNDTRE AANSVIKNMK LVKMASSLGG VESLVNHCYS QSHSGVPHDV KMEMGIKVGL LRFSIGIEDA DDIWNDISAA LDTTL // ID Q9K0E9_NEIMB Unreviewed; 86 AA. AC Q9K0E9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62315.1}; GN OrderedLocusNames=NMB0658 {ECO:0000313|EMBL:AAF62315.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62315.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62315.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62315.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62315.1; -; Genomic_DNA. DR STRING; 122586.NMB0658; -. DR PaxDb; Q9K0E9; -. DR EnsemblBacteria; AAF62315; AAF62315; NMB0658. DR HOGENOM; HOG000220707; -. DR OrthoDB; EOG6130KG; -. DR BioCyc; NMEN122586:GHGG-685-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 86 AA; 9933 MW; 6CEB3DF0A5F8D0E5 CRC64; MLLPRQHLGQ NGRRLKSKHR PSCCRLRMST GQPQCRRNRR SRLQHCRRQS RKVGKNGKTG EIKADGRKVN VRIDSTEADL LYPAGQ // ID Q9K1K7_NEIMB Unreviewed; 443 AA. AC Q9K1K7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40568.1}; GN OrderedLocusNames=NMB0109 {ECO:0000313|EMBL:AAF40568.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40568.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40568.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40568.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40568.1; -; Genomic_DNA. DR PIR; D81238; D81238. DR RefSeq; NP_273167.1; NC_003112.2. DR RefSeq; WP_009344949.1; NC_003112.2. DR ProteinModelPortal; Q9K1K7; -. DR STRING; 122586.NMB0109; -. DR PaxDb; Q9K1K7; -. DR EnsemblBacteria; AAF40568; AAF40568; NMB0109. DR GeneID; 902213; -. DR KEGG; nme:NMB0109; -. DR PATRIC; 20355231; VBINeiMen85645_0149. DR eggNOG; ENOG4105D8S; Bacteria. DR eggNOG; COG1652; LUCA. DR HOGENOM; HOG000270067; -. DR OMA; PELWGMN; -. DR OrthoDB; EOG6F55N6; -. DR BioCyc; NMEN122586:GHGG-115-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR018392; LysM_dom. DR Pfam; PF01476; LysM; 1. DR SMART; SM00257; LysM; 1. DR SUPFAM; SSF54106; SSF54106; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 72 121 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 443 AA; 50120 MW; 05309C2B9C0C27E9 CRC64; MLKCGTFFIT RHIPRGCRRF FQPNQARQTE IYQIRGTVMQ RRIITLLCAA GMAFSTQTLA ANLEVRPNAP ERYTVKQGDT LWGISGKYLY SPWQWGRLWD ANRDQIHNPD LIYPDQVLVL RHVDGEPRLG LEQTDGIPVV KMSPDKEVSG YGIPAIDVNF YRIFMRHPQI VSRKETAAAP RLLSGPEGRL LYTKGTRVYT KGLKEPGRYL TYRINKNITD PDTGKFLGQE VAFSGIVRSL DYTDSVLEQR SKQAGERPKD NEYHTRTHPL ITPLRTPSIQ PLVVETAISE IQQGDYLMKM PEDTDRFNMM PHEPSRPVQA KIVSVFEGTR IAGQFQTITI DKGEADGLDK GTVLSLYKRK KTMQVDLSNN FKSRDTVELI STPAEEVGLA MVYRTSEHLS SAIILENISD ISVGDTAANP GRDLDNIPDQ GRSRVKFGFN RSE // ID Q9JXJ3_NEIMB Unreviewed; 89 AA. AC Q9JXJ3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42339.1}; GN OrderedLocusNames=NMB2015 {ECO:0000313|EMBL:AAF42339.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42339.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42339.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42339.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42339.1; -; Genomic_DNA. DR PIR; D81016; D81016. DR RefSeq; NP_275007.1; NC_003112.2. DR RefSeq; WP_002236220.1; NC_003112.2. DR STRING; 122586.NMB2015; -. DR PaxDb; Q9JXJ3; -. DR EnsemblBacteria; AAF42339; AAF42339; NMB2015. DR GeneID; 904107; -. DR KEGG; nme:NMB2015; -. DR PATRIC; 20360133; VBINeiMen85645_2571. DR HOGENOM; HOG000218725; -. DR OMA; DTIFATM; -. DR OrthoDB; EOG6ZSPB7; -. DR BioCyc; NMEN122586:GHGG-2072-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 89 AA; 10313 MW; 776BCDD973C5533B CRC64; MSNVHPYTIF ATMPHKSTAK DILIMSYDLS KRLVIGLASS ALFDLSESDN IFRMEGAETY RQYQREKQNH PLKKALSFHL LKNFCQSMK // ID Q9JY19_NEIMB Unreviewed; 384 AA. AC Q9JY19; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42125.1}; GN OrderedLocusNames=NMB1786 {ECO:0000313|EMBL:AAF42125.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42125.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42125.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42125.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42125.1; -; Genomic_DNA. DR PIR; C81043; C81043. DR RefSeq; NP_274785.1; NC_003112.2. DR RefSeq; WP_002225636.1; NC_003112.2. DR ProteinModelPortal; Q9JY19; -. DR STRING; 122586.NMB1786; -. DR PaxDb; Q9JY19; -. DR EnsemblBacteria; AAF42125; AAF42125; NMB1786. DR GeneID; 903313; -. DR KEGG; nme:NMB1786; -. DR PATRIC; 20359531; VBINeiMen85645_2271. DR eggNOG; ENOG4105TGR; Bacteria. DR eggNOG; COG2850; LUCA. DR HOGENOM; HOG000220698; -. DR OMA; HWDIRDV; -. DR OrthoDB; EOG676Z13; -. DR BioCyc; NMEN122586:GHGG-1841-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR003347; JmjC_dom. DR Pfam; PF08007; Cupin_4; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 95 238 JmjC. {ECO:0000259|PROSITE:PS51184}. SQ SEQUENCE 384 AA; 44499 MW; C88B1D63C661F0E4 CRC64; MSIHLDFGIS PKTFRQTYLY QKPKLFKGAV RNLESASWKD INEIYQRADP TAPLFHLRKK GAIVPKEEYV ESFDDLGKTR YRFIKSVIYE HMKNGASLVY NHINNEPFSD HIARQVARFA GAHTIVSGYL AFGSDESYKN HWDPRDVYAI QLFGKKRWQL TAPDFPMPLY MQQTKDTDIS IPEHIDMDII LEAGDVLYIP RGWWHRPIPL GCETFHFAVG TFPPNGYNYL EWLMKKFPTI ESLRHSFSDW EQDRTRINDT AAQIAAMIAD PVNYEAFSED FLGKERTDTA FHLEQFANPN ATPLSDDVRL RLNANNLDTL EKGYLIGNGM KISVDELGKK VLEHIGKNEP LLLKNLLVNF NQGKYEEVRK LIYQLIELDF LEIL // ID Q7DD72_NEIMB Unreviewed; 623 AA. AC Q7DD72; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Putative lipopolysaccharide biosynthesis protein WbpC {ECO:0000313|EMBL:AAF42171.1}; GN OrderedLocusNames=NMB1836 {ECO:0000313|EMBL:AAF42171.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42171.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42171.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42171.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42171.1; -; Genomic_DNA. DR RefSeq; NP_274833.1; NC_003112.2. DR RefSeq; WP_002261325.1; NC_003112.2. DR STRING; 122586.NMB1836; -. DR PaxDb; Q7DD72; -. DR EnsemblBacteria; AAF42171; AAF42171; NMB1836. DR GeneID; 903263; -. DR KEGG; nme:NMB1836; -. DR PATRIC; 20359677; VBINeiMen85645_2344. DR eggNOG; ENOG4105EXC; Bacteria. DR eggNOG; COG1835; LUCA. DR HOGENOM; HOG000218768; -. DR OMA; LFSYHCI; -. DR OrthoDB; EOG6HB9KQ; -. DR BioCyc; NMEN122586:GHGG-1891-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR InterPro; IPR002656; Acyl_transf_3. DR Pfam; PF01757; Acyl_transf_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 308 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 334 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 346 369 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 9 330 Acyl_transf_3. FT {ECO:0000259|Pfam:PF01757}. SQ SEQUENCE 623 AA; 70380 MW; DC3A386BB1A4278C CRC64; MSQALPYRPD IDTLRAAAVL SVIVFHIEKD WLPGGFLGVD IFFVISGFLM TTILHREMSG GGGRFSLKAF YIRRIKRILP AFFAVLAATL AGGFFLFTKD DFFLLWKSAL TALGFASNLY FARGKDYFDP AQEEKPLLHI WSLSVEEQFY FVFPILLLLV ARKSLRVQFG FLAALCALSL AASFIPSALD KYYLPHLRAC ELLIGSLTAV WMRCRQPAVG RRCAAVGALF AVCILSTCLF SYSEQTAYFP GPAALIPCLA VAALIYFNHY EHPLKKFFQS KITVAAGLIS YSLYLWHWPI LAFMRYIGPD NLPPYSPAAA VVLILLLSLF SYHCIEKPFK KWQGSFAQSV LWIYALPMLI LGAGSFFAMR LPFMAQYDRL GLTRSNTSCH NNTGKQCLWG DTEKQPELLV LGDSHADHYK TFFDAVGKKE KWSATMVSAD ACAYVEGYAS RVFQNWAACR AVYRYAEEHL PRYSKVVLAM RWGSQMPENS RSLAYDAGFF QKFDRMLHKL SSEKQAVYLM ADNLASSYNV QRAYILSSRI PGYRQALRPD DESTLKANAR IRELAAKYPN VYIIDAAAYI PADFQIGGLP VYSDKDHINP YGGTELAKRF SEKQRFLDTR HNH // ID Q9K0J3_NEIMB Unreviewed; 354 AA. AC Q9K0J3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 104. DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:AAF41031.1}; GN OrderedLocusNames=NMB0604 {ECO:0000313|EMBL:AAF41031.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41031.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41031.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41031.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361277}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|RuleBase:RU361277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41031.1; -; Genomic_DNA. DR PIR; E81178; E81178. DR RefSeq; NP_273648.1; NC_003112.2. DR RefSeq; WP_010980817.1; NC_003112.2. DR ProteinModelPortal; Q9K0J3; -. DR STRING; 122586.NMB0604; -. DR PaxDb; Q9K0J3; -. DR EnsemblBacteria; AAF41031; AAF41031; NMB0604. DR GeneID; 902718; -. DR KEGG; nme:NMB0604; -. DR PATRIC; 20356493; VBINeiMen85645_0766. DR eggNOG; ENOG4105CPQ; Bacteria. DR eggNOG; COG1063; LUCA. DR HOGENOM; HOG000294670; -. DR KO; K00004; -. DR OMA; MIVSIFE; -. DR OrthoDB; EOG6N949Q; -. DR BioCyc; NMEN122586:GHGG-630-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU361277}. SQ SEQUENCE 354 AA; 37921 MW; 2EF4DBACF877C35E CRC64; MKAARFYDKG DIRIEDIPEP TVAPGTVGIN VAWCGICGTD LHEFMEGPIF IPPCGHPHPI SGESAPVTMG HEFSGVVYAV GEGVDDIKVG QHVVVEPYII RDDVPTGEGS NYHLSKDMNF IGLGGCGGGL SEKIAVKRRW VHPISDKIPL DQAALIEPLS VGHHAYVRSG AKEGDVALVG GAGPIGLLLA AVLKAKGIKV IITELSKARK DKARESGVAD YILDPSEVDV VAEVKKLTNG EGVDVAFECT SVNKVLDTLV EACKPAANLV IVSIWSHPAT INVHSVVMKE LDVRGTIAYC NDHAETIKLV EEGKINLEPF ITQRIKLDEL VSKGFERLIH NNESAVKIIV SPNL // ID Q7DD52_NEIMB Unreviewed; 172 AA. AC Q7DD52; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=Gluconokinase {ECO:0000256|RuleBase:RU363066}; DE EC=2.7.1.12 {ECO:0000256|RuleBase:RU363066}; GN Name=gntK {ECO:0000313|EMBL:AAF42351.1}; GN OrderedLocusNames=NMB2028 {ECO:0000313|EMBL:AAF42351.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42351.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42351.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42351.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + D-gluconate = ADP + 6-phospho-D- CC gluconate. {ECO:0000256|RuleBase:RU363066}. CC -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family. CC {ECO:0000256|RuleBase:RU363066}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42351.1; -; Genomic_DNA. DR PIR; G81015; G81015. DR RefSeq; NP_275020.1; NC_003112.2. DR RefSeq; WP_002221692.1; NC_003112.2. DR ProteinModelPortal; Q7DD52; -. DR STRING; 122586.NMB2028; -. DR PaxDb; Q7DD52; -. DR EnsemblBacteria; AAF42351; AAF42351; NMB2028. DR GeneID; 904075; -. DR KEGG; nme:NMB2028; -. DR PATRIC; 20360171; VBINeiMen85645_2585. DR eggNOG; ENOG4108Z67; Bacteria. DR eggNOG; COG3265; LUCA. DR HOGENOM; HOG000032567; -. DR KO; K00851; -. DR OMA; MGVCASG; -. DR OrthoDB; EOG6XHC8K; -. DR BioCyc; NMEN122586:GHGG-2090-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR006001; Therm_gnt_kin. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01313; therm_gnt_kin; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363066}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|RuleBase:RU363066, ECO:0000313|EMBL:AAF42351.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363066}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU363066, KW ECO:0000313|EMBL:AAF42351.1}. SQ SEQUENCE 172 AA; 18947 MW; 248DC962CD121353 CRC64; MTTHFVVMGV CGCGKTTAAL SLQKHLGQCP YAEGDEFHTQ ANRDKMGAGI PLTDEDRYPW LGNLRDWMTQ QAQNGANHTI VTCSALKRGY RDILRGAEGK AAFIHLSPPQ DINLERMMSR KGHYMKAGML DSQLEILEEL GEGEYGVKIA NPGTPEAVEA DILNWVASEN LL // ID Q9JXA0_NEIMB Unreviewed; 311 AA. AC Q9JXA0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Electron transfer flavoprotein, alpha subunit {ECO:0000313|EMBL:AAF42462.1}; GN Name=etfA {ECO:0000313|EMBL:AAF42462.1}; GN OrderedLocusNames=NMB2154 {ECO:0000313|EMBL:AAF42462.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42462.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42462.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42462.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42462.1; -; Genomic_DNA. DR PIR; H81000; H81000. DR RefSeq; NP_275139.1; NC_003112.2. DR RefSeq; WP_002225744.1; NC_003112.2. DR ProteinModelPortal; Q9JXA0; -. DR SMR; Q9JXA0; 2-309. DR STRING; 122586.NMB2154; -. DR PaxDb; Q9JXA0; -. DR PRIDE; Q9JXA0; -. DR EnsemblBacteria; AAF42462; AAF42462; NMB2154. DR GeneID; 903218; -. DR KEGG; nme:NMB2154; -. DR PATRIC; 20360504; VBINeiMen85645_2748. DR eggNOG; ENOG4105C10; Bacteria. DR eggNOG; COG2025; LUCA. DR HOGENOM; HOG000247865; -. DR KO; K03522; -. DR OMA; QIGSDVH; -. DR OrthoDB; EOG6M6JV6; -. DR BioCyc; NMEN122586:GHGG-2219-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR014730; ETF_a/b_N. DR InterPro; IPR001308; ETF_a/FixB. DR InterPro; IPR014731; ETF_asu_C. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01012; ETF; 1. DR Pfam; PF00766; ETF_alpha; 1. DR PIRSF; PIRSF000089; Electra_flavoP_a; 1. DR SMART; SM00893; ETF; 1. DR SUPFAM; SSF52467; SSF52467; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 181 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 311 AA; 32579 MW; B8A5A312252EFB47 CRC64; MSVLIIVEHD NKQLNPTTLH AVTAAAKLGK VDLLVAGNGA SAVVEFAKQV AGVKKVLVAD AAHYAEGLAE ELAPLVVKLA ADYRYVAATA TTFGKNLLPR VAALLDVPQI SDLTEIVDNT TFVRPIYAGN AFETVQADSE KLVLTFRATV FDAVAAQGGN AEVINVEATP AQNLSRFVNR QLSHSDRPEL TQAKVIVSGG RALGSAEKFN EVLTPLADVL GAAIGASRAA VDAEYAPNDA QVGQTGKVVA PQLYFAIGIS GAIQHVAGMQ DSKVIVAINK DADAPIFNVA DYGLVGDLFE IVPQLTEVLK N // ID Q9K0W6_NEIMB Unreviewed; 290 AA. AC Q9K0W6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Putative prephenate dehydrogenase {ECO:0000313|EMBL:AAF40878.1}; GN OrderedLocusNames=NMB0440 {ECO:0000313|EMBL:AAF40878.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40878.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40878.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40878.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40878.1; -; Genomic_DNA. DR PIR; A81199; A81199. DR RefSeq; NP_273488.1; NC_003112.2. DR RefSeq; WP_002222047.1; NC_003112.2. DR ProteinModelPortal; Q9K0W6; -. DR STRING; 122586.NMB0440; -. DR PaxDb; Q9K0W6; -. DR EnsemblBacteria; AAF40878; AAF40878; NMB0440. DR GeneID; 902556; -. DR KEGG; nme:NMB0440; -. DR PATRIC; 20356086; VBINeiMen85645_0558. DR eggNOG; ENOG4105EVN; Bacteria. DR eggNOG; COG0287; LUCA. DR HOGENOM; HOG000043493; -. DR KO; K00210; -. DR OMA; MWRDICL; -. DR OrthoDB; EOG6B8XMB; -. DR BioCyc; NMEN122586:GHGG-464-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro. DR GO; GO:0008977; F:prephenate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003099; Prephen_DH. DR Pfam; PF02153; PDH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51176; PDH_ADH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 290 Prephenate/arogenate dehydrogenase. FT {ECO:0000259|PROSITE:PS51176}. SQ SEQUENCE 290 AA; 31636 MW; 2FA8C864A85A3A00 CRC64; MPILNHIALI GVGLIGGSFV LDLKRQGLVR TVTGIDTDRD NLERALERGV IDQASVAIDA DSIGGADLVL IATPVATVPA ILTALRPVLP EHTWISDVGS TKSSVIEAFR RCLPDRLHHC IAAHPIAGSD RSGAQAAQFG LFRHRKLIIT PHGGEHSDGI ALVENLWHAV GAEIYTMDAQ RHDAVFAAVS HMPHLTAFAY VHQILDHPDG QEYLKFAATG FRDFTRIASG HPAVWADICL ANKDSLLQLV QGLGKQLDVL ANILTTDDRE ALYRYFEEAK TTRDRWLDGN // ID Q7DDL3_NEIMB Unreviewed; 169 AA. AC Q7DDL3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019}; DE Short=PPIase {ECO:0000256|RuleBase:RU363019}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019}; GN OrderedLocusNames=NMB0791 {ECO:0000313|EMBL:AAF41204.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41204.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41204.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41204.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. {ECO:0000256|RuleBase:RU363019}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363019}. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC {ECO:0000256|RuleBase:RU363019}. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC {ECO:0000256|RuleBase:RU363019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41204.1; -; Genomic_DNA. DR PIR; F81156; F81156. DR RefSeq; NP_273833.1; NC_003112.2. DR RefSeq; WP_002213981.1; NC_003112.2. DR ProteinModelPortal; Q7DDL3; -. DR SMR; Q7DDL3; 1-167. DR STRING; 122586.NMB0791; -. DR PaxDb; Q7DDL3; -. DR PRIDE; Q7DDL3; -. DR EnsemblBacteria; AAF41204; AAF41204; NMB0791. DR GeneID; 902906; -. DR KEGG; nme:NMB0791; -. DR PATRIC; 20356969; VBINeiMen85645_1003. DR eggNOG; ENOG4108R5K; Bacteria. DR eggNOG; COG0652; LUCA. DR HOGENOM; HOG000065978; -. DR KO; K03768; -. DR OMA; EIPDEFT; -. DR OrthoDB; EOG6S26C3; -. DR BioCyc; NMEN122586:GHGG-822-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PTHR11071; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; SSF50891; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU363019}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Rotamase {ECO:0000256|RuleBase:RU363019}. FT DOMAIN 1 168 PPIase cyclophilin-type. FT {ECO:0000259|PROSITE:PS50072}. SQ SEQUENCE 169 AA; 18852 MW; D5FF01BB4AE6BDBA CRC64; MIILHTNKGD IKIELDFDKA PVTAKNFEQY VKDGFYDGVI FHRVIKGFMI QGGGMDENMN EKETRDPIQN EASNGLPNDK YTIAMARTSD PHSASAQFFI NTADNAFLNF RSKELYGKTV VQDWGYAVFG KVVDGFDVVD AIEGVSTKRH GYHDDVPSEP VVIIKAEAV // ID Q9JZ97_NEIMB Unreviewed; 131 AA. AC Q9JZ97; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41608.1}; GN OrderedLocusNames=NMB1227 {ECO:0000313|EMBL:AAF41608.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41608.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41608.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41608.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41608.1; -; Genomic_DNA. DR PIR; D81108; D81108. DR RefSeq; NP_274251.1; NC_003112.2. DR RefSeq; WP_002222432.1; NC_003112.2. DR ProteinModelPortal; Q9JZ97; -. DR STRING; 122586.NMB1227; -. DR PaxDb; Q9JZ97; -. DR EnsemblBacteria; AAF41608; AAF41608; NMB1227. DR GeneID; 903649; -. DR KEGG; nme:NMB1227; -. DR PATRIC; 20358045; VBINeiMen85645_1535. DR eggNOG; COG3737; LUCA. DR HOGENOM; HOG000218960; -. DR OMA; SAGLSKW; -. DR OrthoDB; EOG6G20P3; -. DR BioCyc; NMEN122586:GHGG-1264-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1230.10; -; 1. DR InterPro; IPR007523; NDUFAF3/AAMDC. DR PANTHER; PTHR21192; PTHR21192; 1. DR Pfam; PF04430; DUF498; 1. DR SUPFAM; SSF64076; SSF64076; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 131 AA; 14711 MW; 3580E385B630A580 CRC64; MMRQRGKKML FEENPIDGQF AEYECGAGGI RLAGQSFHKP VLVHKDSVCL SQCRTLSDLT PENLLSDVKP VDYPEILIIG TGAAQEFIHP KIMADFSRIG ISVECMNTDS AFRTLVFLHS EGRRAWAWLQ P // ID Q9K0R5_NEIMB Unreviewed; 127 AA. AC Q9K0R5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40947.1}; GN OrderedLocusNames=NMB0515 {ECO:0000313|EMBL:AAF40947.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40947.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40947.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40947.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40947.1; -; Genomic_DNA. DR PIR; E81188; E81188. DR STRING; 122586.NMB0515; -. DR PaxDb; Q9K0R5; -. DR EnsemblBacteria; AAF40947; AAF40947; NMB0515. DR PATRIC; 20356274; VBINeiMen85645_0657. DR OrthoDB; EOG6WMJ06; -. DR BioCyc; NMEN122586:GHGG-540-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 127 AA; 13607 MW; 43DE2008859B7D18 CRC64; MTEQLFDSLA KQNGFRVLSG GKYGGNNGFD HVWQAADGSV VLIVESKQIR NGTVQLNPNG AGGYTQMSRE WIKQVVKSLP DGSPAKAVVL KANQNGKLKT AIAGVDRQTG KAVILSVKVP SKTNIRR // ID Q9K0X7_NEIMB Unreviewed; 436 AA. AC Q9K0X7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40866.1}; GN OrderedLocusNames=NMB0428 {ECO:0000313|EMBL:AAF40866.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40866.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40866.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40866.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40866.1; -; Genomic_DNA. DR PIR; F81199; F81199. DR RefSeq; NP_273476.1; NC_003112.2. DR RefSeq; WP_002212503.1; NC_003112.2. DR STRING; 122586.NMB0428; -. DR PaxDb; Q9K0X7; -. DR EnsemblBacteria; AAF40866; AAF40866; NMB0428. DR GeneID; 902544; -. DR KEGG; nme:NMB0428; -. DR PATRIC; 20356054; VBINeiMen85645_0542. DR eggNOG; ENOG4105C7N; Bacteria. DR eggNOG; COG2252; LUCA. DR HOGENOM; HOG000244362; -. DR KO; K06901; -. DR OMA; MVDFFDT; -. DR OrthoDB; EOG6DNT97; -. DR BioCyc; NMEN122586:GHGG-452-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR029940; AzgA. DR InterPro; IPR026033; Pur_Permease_PbuG-like. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR PANTHER; PTHR11119:SF9; PTHR11119:SF9; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR PIRSF; PIRSF005353; PbuG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 46 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 82 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 241 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 310 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 339 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 407 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 419 435 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 436 AA; 46067 MW; 2719E4D66901C0E4 CRC64; MDTSKQTLLD GIFKLKANGT TVRTELMAGL TTFLTMCYIV IVNPLILGET GMDMGAVFVA TCIASAIGCF VMGFVGNYPI ALAPGMGLNA YFTFAVVKGM GVPWQVALGA VFISGLIFIL FSFFKVREML VNALPMGLKM SIAAGIGLFL ALISLKGAGI IVANPATLVG LGDIHQPSAL LALFGFAMVV VLGHFRVQGA IIITILTITV IASLMGLNEF HGIIGEVPSI APTFMQMDFE GLFTVSMVSV IFVFFLVDLF DSTGTLVGIS HRAGLLVDGK LPRLKRALLA DSTAIVAGAA LGTSSTTPYV ESAAGVSAGG RTGLTAVTVG VLMLACLMFS PLAKSVPAFA TAPALLYVGT QMLRSARDID WDDMTEAAPA FLTIVFMPFT YSIADGIAFG FISYAVVKLL CRRTKDVPPM VWIVAVLWAL KFWYLG // ID Q9JXV5_NEIMB Unreviewed; 354 AA. AC Q9JXV5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:AAF42203.1}; DE EC=4.1.2.13 {ECO:0000313|EMBL:AAF42203.1}; GN Name=cbbA {ECO:0000313|EMBL:AAF42203.1}; GN OrderedLocusNames=NMB1869 {ECO:0000313|EMBL:AAF42203.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42203.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42203.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42203.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000256|SAAS:SAAS00591215}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42203.1; -; Genomic_DNA. DR PIR; C81032; C81032. DR RefSeq; NP_274865.1; NC_003112.2. DR RefSeq; WP_002225784.1; NC_003112.2. DR ProteinModelPortal; Q9JXV5; -. DR STRING; 122586.NMB1869; -. DR PaxDb; Q9JXV5; -. DR EnsemblBacteria; AAF42203; AAF42203; NMB1869. DR GeneID; 904319; -. DR KEGG; nme:NMB1869; -. DR PATRIC; 20359767; VBINeiMen85645_2389. DR eggNOG; ENOG4105D2N; Bacteria. DR eggNOG; COG0191; LUCA. DR HOGENOM; HOG000227792; -. DR KO; K01624; -. DR OMA; VNTREMF; -. DR OrthoDB; EOG6HXJ7B; -. DR BioCyc; NMEN122586:GHGG-1925-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006412; Fruct_bisP_Calv. DR InterPro; IPR000771; Ketose_bisP_aldolase_II. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR TIGRFAMs; TIGR01521; FruBisAldo_II_B; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|SAAS:SAAS00485079, ECO:0000313|EMBL:AAF42203.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00485111}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|SAAS:SAAS00485107}. FT ACT_SITE 83 83 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001359-1}. FT BINDING 199 199 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000256|PIRSR:PIRSR001359- FT 2}. SQ SEQUENCE 354 AA; 38337 MW; 4440D691E7C83EEF CRC64; MALVSMRQLL DHAAENSYGL PAFNVNNLEQ MRAIMEAADQ VDAPVIVQAS AGARKYAGAP FLRHLILAAV EEFPHIPVVM HQDHGASPDV CQRSIQLGFS SVMMDGSLME DGKTPSSYEY NVNATRTVVN FSHACGVSVE GEIGVLGNLE TGEAGEEDGV GAVGKLSHDQ MLTSVEDAVC FVKDTGVDAL AIAVGTSHGA YKFTRPPTGD VLRIDRIKEI HQALPNTHIV MHGSSSVPQE WLKVINEYGG NIGETYGVPV EEIVEGIKHG VRKVNIDTDL RLASTGAVRR YLAENPSDFD PRKYLSKTIE AMKQICLDRY LAFGCEGQAG KIKPVSLEKM ASRYAKGELN QIVK // ID Q7DDM1_NEIMB Unreviewed; 195 AA. AC Q7DDM1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-MAY-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41091.1}; GN OrderedLocusNames=NMB0673 {ECO:0000313|EMBL:AAF41091.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41091.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41091.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41091.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41091.1; -; Genomic_DNA. DR PIR; G81170; G81170. DR RefSeq; NP_273715.1; NC_003112.2. DR RefSeq; WP_002225505.1; NC_003112.2. DR STRING; 122586.NMB0673; -. DR PaxDb; Q7DDM1; -. DR EnsemblBacteria; AAF41091; AAF41091; NMB0673. DR GeneID; 902784; -. DR KEGG; nme:NMB0673; -. DR PATRIC; 20356649; VBINeiMen85645_0843. DR eggNOG; ENOG4107NPI; Bacteria. DR eggNOG; COG3184; LUCA. DR HOGENOM; HOG000218833; -. DR KO; K09924; -. DR OMA; RIICGGI; -. DR OrthoDB; EOG6CZQK7; -. DR BioCyc; NMEN122586:GHGG-700-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018637; DUF2059. DR Pfam; PF09832; DUF2059; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 195 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004288460. FT DOMAIN 105 148 DUF2059. {ECO:0000259|Pfam:PF09832}. SQ SEQUENCE 195 AA; 21704 MW; B8D3062DE366D345 CRC64; MNIKLKTLLL PFATLALCTN AFAAPPSDAS LARWLDTQNF DRDIEKNMIE GFNAGFKPYA DKALAEMPEA KKDQAAEAFN RYRENVLKDL ITPEVKQAVR NTLLKNAREI YTQEEIDGMI AFYGSPVGQS VVAKNPRLIK KSMSEIAVSW TALSGKIAQH HLPEFTEELR RIICGGKNPD AGCKQAGQVG KRHQK // ID Q9JXR9_NEIMB Unreviewed; 175 AA. AC Q9JXR9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42242.1}; GN OrderedLocusNames=NMB1912 {ECO:0000313|EMBL:AAF42242.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42242.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42242.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42242.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42242.1; -; Genomic_DNA. DR PIR; G81028; G81028. DR RefSeq; NP_274906.1; NC_003112.2. DR RefSeq; WP_002244314.1; NC_003112.2. DR ProteinModelPortal; Q9JXR9; -. DR STRING; 122586.NMB1912; -. DR PaxDb; Q9JXR9; -. DR EnsemblBacteria; AAF42242; AAF42242; NMB1912. DR GeneID; 904252; -. DR KEGG; nme:NMB1912; -. DR PATRIC; 20359869; VBINeiMen85645_2439. DR eggNOG; ENOG4108WXJ; Bacteria. DR eggNOG; COG2236; LUCA. DR HOGENOM; HOG000170387; -. DR KO; K07101; -. DR OMA; RTQWLGP; -. DR OrthoDB; EOG6H1Q23; -. DR BioCyc; NMEN122586:GHGG-1969-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU000395}. FT DOMAIN 14 131 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 175 AA; 19921 MW; 1FF2D76CFF900F2D CRC64; MKQKIWYTYD DIHRVIKALA EKIRNADIKY DAMIAIGGGG FIPARMLRCF LEIPIYAVTT AYYDSDNEGQ VTEEVKKVQW LDPVPEALRG KNVLVVDEVD DSRVTMEFCL KELLKEDFGT IGVAVLHEKI KAKAGKIPEG IPYFSGITVE DWWINYPWDA LDIDEHNRLA EAGRG // ID Q9JZK1_NEIMB Unreviewed; 351 AA. AC Q9JZK1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Sulfate ABC transporter, periplasmic sulfate-binding protein {ECO:0000313|EMBL:AAF41417.1}; GN Name=sbp {ECO:0000313|EMBL:AAF41417.1}; GN OrderedLocusNames=NMB1017 {ECO:0000313|EMBL:AAF41417.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41417.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41417.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41417.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41417.1; -; Genomic_DNA. DR PIR; A81132; A81132. DR RefSeq; NP_274051.1; NC_003112.2. DR RefSeq; WP_002225284.1; NC_003112.2. DR ProteinModelPortal; Q9JZK1; -. DR STRING; 122586.NMB1017; -. DR PaxDb; Q9JZK1; -. DR EnsemblBacteria; AAF41417; AAF41417; NMB1017. DR GeneID; 903155; -. DR KEGG; nme:NMB1017; -. DR PATRIC; 20357569; VBINeiMen85645_1301. DR eggNOG; ENOG4105DE7; Bacteria. DR eggNOG; COG1613; LUCA. DR HOGENOM; HOG000260057; -. DR KO; K02048; -. DR OMA; KVHFNDG; -. DR OrthoDB; EOG6PGK2K; -. DR BioCyc; NMEN122586:GHGG-1054-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015419; F:sulfate transmembrane-transporting ATPase activity; IEA:InterPro. DR InterPro; IPR005669; Thiosulph/SO4-bd. DR PANTHER; PTHR30368; PTHR30368; 1. DR TIGRFAMs; TIGR00971; 3a0106s03; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 351 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327858. SQ SEQUENCE 351 AA; 38456 MW; 07EE3A81073FDBA9 CRC64; MKTYAPALYT AALLTACSPA ADSNHPSGQN APANTESDGK NITLLNASYD VARDFYKEYN PLFIKTYQSE HPGTSVSIQQ SHGGSSKQAL SVANGLQADV VTMNQSSDID LLEKKGLVEK GWQQALPDHA APYTSTMVFL VRKNNPKQIR DWNDLAKDGV NIVIANPKTS GNGRYAFLGA YGYGLKTTNG NEQEAQKLVA SILKNTPVFE NGGRAATTTF TQRNIGDVLI TFENEANYVS KKLTQGQFEI VYPSYTISAE SPVAVVNSVV AKKGTQKTAR AYLEYLWSEP AQELAASLYL RPRNPEVLAR HKADFPDLDT FSPEKKFGGW DNIMKTYFAD GGIFDRLTAQ K // ID Q9K035_NEIMB Unreviewed; 275 AA. AC Q9K035; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Amino acid ABC transporter, periplasmic amino acid-binding protein {ECO:0000313|EMBL:AAF41200.1}; GN OrderedLocusNames=NMB0787 {ECO:0000313|EMBL:AAF41200.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41200.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41200.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41200.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 CC family. {ECO:0000256|RuleBase:RU003744}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41200.1; -; Genomic_DNA. DR PIR; H81158; H81158. DR RefSeq; NP_273829.1; NC_003112.2. DR RefSeq; WP_010980844.1; NC_003112.2. DR ProteinModelPortal; Q9K035; -. DR STRING; 122586.NMB0787; -. DR PaxDb; Q9K035; -. DR EnsemblBacteria; AAF41200; AAF41200; NMB0787. DR GeneID; 902902; -. DR KEGG; nme:NMB0787; -. DR PATRIC; 20356961; VBINeiMen85645_0999. DR eggNOG; ENOG4105EAB; Bacteria. DR eggNOG; COG0834; LUCA. DR HOGENOM; HOG000031895; -. DR KO; K02424; -. DR OMA; ANEIDCA; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; NMEN122586:GHGG-818-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR018313; SBP_3_CS. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00062; PBPb; 1. DR PROSITE; PS01039; SBP_BACTERIAL_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 275 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332284. FT DOMAIN 50 271 PBPb. {ECO:0000259|SMART:SM00062}. SQ SEQUENCE 275 AA; 28824 MW; F94F547A2D91A11A CRC64; MMLKKFVLGG IAALVLAACG GSEGGSGASS APAQSAVSGS LIERINNKGT VTVGTEGTYA PFTYHDKDGK LTGYDVEVTR AVAEKLGVKV EFKETQWDSM MAGLKAGRFD VVANQVGLTS PERQATFDKS DPYSWSGAVL VVRNDSNIKS IADIKGVKTA QSLTSNYGEK AKAAGADLVA VDGLAQSLTL IEQKRADATL NDELAVLDYL KKNPNAGVKI VWSAPADEKV GSGLIVNKGN DEAVAKFSTA INELKADGTL KKLGEQFFGK DISVQ // ID Q9JZU0_NEIMB Unreviewed; 94 AA. AC Q9JZU0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=D-lactate dehydrogenase-related protein {ECO:0000313|EMBL:AAF41309.1}; GN OrderedLocusNames=NMB0901 {ECO:0000313|EMBL:AAF41309.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41309.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41309.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41309.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41309.1; -; Genomic_DNA. DR PIR; B81144; B81144. DR STRING; 122586.NMB0901; -. DR PaxDb; Q9JZU0; -. DR EnsemblBacteria; AAF41309; AAF41309; NMB0901. DR PATRIC; 20357235; VBINeiMen85645_1131. DR OrthoDB; EOG6T7NB3; -. DR BioCyc; NMEN122586:GHGG-939-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 94 AA; 10841 MW; 0C97DA1712C5321B CRC64; MAFHHGRRCR ITPLPETESL QESKKMNINE LGARIDRPTI RELIAYATCR NRPISNSTLL RMEKDGRIPC RLKTPLTSPV WDTREVLEAL GLQQ // ID Q9K0K6_NEIMB Unreviewed; 251 AA. AC Q9K0K6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41016.1}; GN OrderedLocusNames=NMB0588 {ECO:0000313|EMBL:AAF41016.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41016.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41016.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41016.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41016.1; -; Genomic_DNA. DR PIR; A81180; A81180. DR RefSeq; NP_273632.1; NC_003112.2. DR RefSeq; WP_002225547.1; NC_003112.2. DR ProteinModelPortal; Q9K0K6; -. DR STRING; 122586.NMB0588; -. DR PaxDb; Q9K0K6; -. DR PRIDE; Q9K0K6; -. DR EnsemblBacteria; AAF41016; AAF41016; NMB0588. DR GeneID; 902703; -. DR KEGG; nme:NMB0588; -. DR PATRIC; 20356461; VBINeiMen85645_0750. DR eggNOG; ENOG4105DIK; Bacteria. DR eggNOG; COG1121; LUCA. DR KO; K02074; -. DR OMA; RGWHREG; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NMEN122586:GHGG-614-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAF41016.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000313|EMBL:AAF41016.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 13 241 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 251 AA; 28349 MW; 7B9488123EE1A621 CRC64; MGRLLLGSIR MSIIVENLTV SYRRRPAVHH VDITFEEHSM WAVFGPNGAG KSTFLKSLMG LQPIDTGSIR LDGLTRQNIA YLPQQSDIDR SQPMTVFDLA AMGLWYEIGF FKGINTAQKQ RVHEALERVG MQRFADRQIA YLSNGQFQRV LFARMLVQNA KFLLLDEPFN AVDARTTYEL LDVLQKCHCG GHAIIAVLHD YEQVRAYFPN TLLLAREKIA AGATETILTE PYLAQANAKM QQQESPDWCA S // ID Q9K176_NEIMB Unreviewed; 268 AA. AC Q9K176; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=CcsA-related protein {ECO:0000313|EMBL:AAF40747.1}; GN OrderedLocusNames=NMB0296 {ECO:0000313|EMBL:AAF40747.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40747.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40747.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40747.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40747.1; -; Genomic_DNA. DR PIR; G81215; G81215. DR RefSeq; NP_273350.1; NC_003112.2. DR RefSeq; WP_002221947.1; NC_003112.2. DR STRING; 122586.NMB0296; -. DR PaxDb; Q9K176; -. DR EnsemblBacteria; AAF40747; AAF40747; NMB0296. DR GeneID; 902407; -. DR KEGG; nme:NMB0296; -. DR PATRIC; 20355696; VBINeiMen85645_0372. DR eggNOG; ENOG4106KVJ; Bacteria. DR eggNOG; COG4137; LUCA. DR HOGENOM; HOG000255939; -. DR OMA; FTLAAFH; -. DR OrthoDB; EOG69SKBK; -. DR BioCyc; NMEN122586:GHGG-311-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro. DR InterPro; IPR002541; Cyt_c_assembly. DR Pfam; PF01578; Cytochrom_C_asm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 82 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 94 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 258 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 43 265 Cytochrom_C_asm. FT {ECO:0000259|Pfam:PF01578}. SQ SEQUENCE 268 AA; 29719 MW; 48725D654A40DCE2 CRC64; MPTVFIFLTA VYAGLGAFAW HCQQQGCGRD YPWKTELPVL GAALTVHGAA LLMPVIQDKI IIMGFGYSGS LIVWMMLFIY FAGSFFYPLR GVQLLLYPCA ALMLLSGLVF PGKFSGYEIT DLPFMLHIGT SLLAYGLFGI ATLLSVLTLL LNRSLHRRSF SKLAGFLPSL LSLEKLMFQA MWAGFILLTY SVVSGTFFAE AVFGKPMTFT HKTVFGILSW LIYGGLLLKH SMTAWRGKKA AVWTIIGFVS LMIAYMGSKF VLEIILKR // ID Q9K0C0_NEIMB Unreviewed; 148 AA. AC Q9K0C0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=FolI protein {ECO:0000313|EMBL:AAF41111.1}; GN Name=folI {ECO:0000313|EMBL:AAF41111.1}; GN OrderedLocusNames=NMB0694 {ECO:0000313|EMBL:AAF41111.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41111.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41111.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41111.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41111.1; -; Genomic_DNA. DR PIR; D81170; D81170. DR RefSeq; NP_273736.1; NC_003112.2. DR RefSeq; WP_002225489.1; NC_003112.2. DR STRING; 122586.NMB0694; -. DR PaxDb; Q9K0C0; -. DR EnsemblBacteria; AAF41111; AAF41111; NMB0694. DR GeneID; 902806; -. DR KEGG; nme:NMB0694; -. DR PATRIC; 20356717; VBINeiMen85645_0880. DR HOGENOM; HOG000218844; -. DR OMA; CIMPDMT; -. DR OrthoDB; EOG679TD5; -. DR BioCyc; NMEN122586:GHGG-722-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 56 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 148 AA; 16615 MW; 498B445B26BFC78D CRC64; MRAFQTALRP SRILNILTVS LHAASLAVCL TWFYGRMMWF GLAALVASYA YSLRITNLKH RHAITAITID RDGQAEIVSG KDKTAKAAAL SGSSMVTPYA LFLQWDTGGK TVRQCIMPDM TDKESYRKLK VWVLWRQPKK TAETDTSD // ID Q9JZU3_NEIMB Unreviewed; 62 AA. AC Q9JZU3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41306.1}; GN OrderedLocusNames=NMB0898 {ECO:0000313|EMBL:AAF41306.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41306.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41306.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41306.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41306.1; -; Genomic_DNA. DR PIR; G81143; G81143. DR STRING; 122586.NMB0898; -. DR PaxDb; Q9JZU3; -. DR EnsemblBacteria; AAF41306; AAF41306; NMB0898. DR OMA; WLSLCTP; -. DR OrthoDB; EOG6FZ4K2; -. DR BioCyc; NMEN122586:GHGG-936-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 62 AA; 6862 MW; 03657997CC267C52 CRC64; MGSRARATGD DKPSVRVMGR GMRPLSYLQT PTNPQSAFQS RLFWTNPPLP PPVPVWLSLC PP // ID Q9JZT6_NEIMB Unreviewed; 71 AA. AC Q9JZT6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41313.1}; GN OrderedLocusNames=NMB0905 {ECO:0000313|EMBL:AAF41313.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41313.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41313.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41313.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41313.1; -; Genomic_DNA. DR PIR; F81144; F81144. DR RefSeq; NP_273945.1; NC_003112.2. DR RefSeq; WP_002219434.1; NC_003112.2. DR STRING; 122586.NMB0905; -. DR PaxDb; Q9JZT6; -. DR EnsemblBacteria; AAF41313; AAF41313; NMB0905. DR GeneID; 903026; -. DR KEGG; nme:NMB0905; -. DR PATRIC; 20357245; VBINeiMen85645_1136. DR HOGENOM; HOG000220716; -. DR OMA; VKQALIC; -. DR OrthoDB; EOG689HWP; -. DR BioCyc; NMEN122586:GHGG-943-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 71 AA; 7961 MW; A1172CEE04DB6E0F CRC64; MTITEEYSID IRVTSEQGKN DYGYPTERYG CDIINTDGEL LVGIEPEYKT PFAAVRKALI CLTKDNLKNA A // ID Q9JYG9_NEIMB Unreviewed; 162 AA. AC Q9JYG9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 2. DT 16-MAR-2016, entry version 53. DE SubName: Full=Putative lipoprotein {ECO:0000313|EMBL:AAF41945.2}; GN OrderedLocusNames=NMB1592 {ECO:0000313|EMBL:AAF41945.2}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41945.2, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41945.2, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41945.2, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41945.2; -; Genomic_DNA. DR PIR; B81066; B81066. DR RefSeq; NP_274598.2; NC_003112.2. DR RefSeq; WP_002231880.1; NC_003112.2. DR STRING; 122586.NMB1592; -. DR PaxDb; Q9JYG9; -. DR EnsemblBacteria; AAF41945; AAF41945; NMB1592. DR GeneID; 904266; -. DR KEGG; nme:NMB1592; -. DR PATRIC; 20359066; VBINeiMen85645_2045. DR HOGENOM; HOG000219036; -. DR OMA; APSHWAD; -. DR OrthoDB; EOG6M9DVZ; -. DR BioCyc; NMEN122586:GHGG-1640-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000313|EMBL:AAF41945.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 162 AA; 18355 MW; 11DA8FC0DBC4F0AA CRC64; MKKYLIPLSI AAVLSGCQSI YVPTLTEIPV NPINTVKTEA PAKGFRLASS HWTDVAKISD EATRLGYQVG IGKMTKVQAA QYLNNFRKRL VGRNAVDDSM YEIYLRSAID SQRGAINTEQ SKLYIQNALR GWQQRWKNMD VKPNNPAFTN FLMEVMKMQP LK // ID Q9K1L6_NEIMB Unreviewed; 50 AA. AC Q9K1L6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40557.1}; GN OrderedLocusNames=NMB0095 {ECO:0000313|EMBL:AAF40557.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40557.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40557.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40557.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40557.1; -; Genomic_DNA. DR PIR; G81239; G81239. DR STRING; 122586.NMB0095; -. DR PaxDb; Q9K1L6; -. DR EnsemblBacteria; AAF40557; AAF40557; NMB0095. DR HOGENOM; HOG000220682; -. DR OMA; VAQRNKW; -. DR OrthoDB; EOG6FV8F9; -. DR BioCyc; NMEN122586:GHGG-101-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 44 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 50 AA; 5474 MW; 55DD2BCEB31960ED CRC64; MSNNHSFFRP EVFVAQRNKW TGPVGWVDAM GAGIFSVAGG YNIGRGMMKP // ID Q9JXH5_NEIMB Unreviewed; 187 AA. AC Q9JXH5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Putative hypoxanthine-guanine phosphoribosyltransferase {ECO:0000313|EMBL:AAF42367.1}; GN OrderedLocusNames=NMB2047 {ECO:0000313|EMBL:AAF42367.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42367.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42367.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42367.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42367.1; -; Genomic_DNA. DR PIR; C81013; C81013. DR RefSeq; NP_275037.1; NC_003112.2. DR RefSeq; WP_002242054.1; NC_003112.2. DR ProteinModelPortal; Q9JXH5; -. DR STRING; 122586.NMB2047; -. DR PaxDb; Q9JXH5; -. DR EnsemblBacteria; AAF42367; AAF42367; NMB2047. DR GeneID; 904042; -. DR KEGG; nme:NMB2047; -. DR PATRIC; 20360248; VBINeiMen85645_2624. DR eggNOG; ENOG4108UGV; Bacteria. DR eggNOG; COG0634; LUCA. DR HOGENOM; HOG000236519; -. DR KO; K00760; -. DR OMA; TMDWMAV; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; NMEN122586:GHGG-2110-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosyltransferase {ECO:0000313|EMBL:AAF42367.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42367.1}. FT DOMAIN 19 159 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 187 AA; 20705 MW; 3DB6D17AF06F0FFF CRC64; MTDLETKRLE TQAMLENADL LFDQGQCRAA LQKVADEITR DLGGKYPLLL PVMGGAVVFT GQLLPLLRFP LDFDYVHVSR YGDKLEGGAF NWKRMPDAEQ IRGRHVVVLD DILDEGHTMS AIQAKLLEMG AASCRAAVFA NKLIDKPKPI RADYVGLDVP NRYVFGYGMD AAGCWRNLGE IYALGGK // ID Q9JYB6_NEIMB Unreviewed; 718 AA. AC Q9JYB6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Guanosine-3`,5`-bis(Diphosphate) 3`-pyrophosphohydrolase {ECO:0000313|EMBL:AAF42008.1}; DE EC=3.1.7.2 {ECO:0000313|EMBL:AAF42008.1}; GN Name=spoT {ECO:0000313|EMBL:AAF42008.1}; GN OrderedLocusNames=NMB1659 {ECO:0000313|EMBL:AAF42008.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42008.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42008.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42008.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5-' CC diphosphate) is a mediator of the stringent response that CC coordinates a variety of cellular activities in response to CC changes in nutritional abundance. {ECO:0000256|RuleBase:RU003847}. CC -!- SIMILARITY: Belongs to the relA/spoT family. CC {ECO:0000256|RuleBase:RU003847}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42008.1; -; Genomic_DNA. DR PIR; B81058; B81058. DR RefSeq; NP_274664.1; NC_003112.2. DR RefSeq; WP_002222147.1; NC_003112.2. DR ProteinModelPortal; Q9JYB6; -. DR STRING; 122586.NMB1659; -. DR PaxDb; Q9JYB6; -. DR DNASU; 903452; -. DR EnsemblBacteria; AAF42008; AAF42008; NMB1659. DR GeneID; 903452; -. DR KEGG; nme:NMB1659; -. DR PATRIC; 20359256; VBINeiMen85645_2136. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR HOGENOM; HOG000018299; -. DR KO; K01139; -. DR OMA; GIYKKMR; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; NMEN122586:GHGG-1713-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42008.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 642 718 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 718 AA; 80134 MW; DF318281B8F5D449 CRC64; MPAPQPSAPY DPLTAEARAL LFHTASYLKP EEQAELEKAV AYAFRAHDGQ TRKSGEPYIT HPIAVATQLA LWHMDIQGLC AGVMHDVLED TGVTKGEMAA VFGNTIAEMV DGLSKLEKLK FEDHAEHQAE SFRKLILAMT KDVRVIVVKL ADRLHNMRTL GSMRPDKRRR IARETLEIYA QIANRIGLNN AYQELQDLSF QNLHPNRYET LKKAMDKSRK NRQDVVGKVL RAFGQRLVGA NIEAKIKGRE KNLYGIHQKM MAKKLRFAEV MDIYGFRVIV NSIPACYAAL GALHTLYQPK PGRFKDYIAI PKSNGYQSLH TTLVGPYGLP IEVQIRTKEM DAVAEGGIAG HWSYKSYSKT VDQAVLHTNR WLKNILDLQA SSANAIEFLE HVKVDLFPNE IYILTPKGKI LTLPKGATPV DFAYAVHTDI GHKTVAARIN NIMMPLRTKL KTGDSVEIIT SEHAKPNPAW LNFAVSGRAR SAIRQYIKNL NRHDAVVLGE SLLQKALSSL LPKDVLLSDG IKEKYLADLN DKQTSFEEVL YNVGMGHTLP VYVAMHIAEL AGEHFGSEVR LSSIKVDGQE SGHIHFAECC HPVPGDSIRL LLVKGKGMII HRDTCPTLLK SDPEQQLDAD WENMNGQNYR VGLQVQSEDS HGLLALMAQA ISDSGADIES VETPSKSQSG TEGFVEFKFL LKVKNLNQLN QIIQNLHSIP YIRKVIRS // ID Q9JZK0_NEIMB Unreviewed; 160 AA. AC Q9JZK0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41418.1}; GN OrderedLocusNames=NMB1018 {ECO:0000313|EMBL:AAF41418.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41418.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41418.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41418.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41418.1; -; Genomic_DNA. DR PIR; B81132; B81132. DR RefSeq; NP_274052.1; NC_003112.2. DR RefSeq; WP_002224566.1; NC_003112.2. DR ProteinModelPortal; Q9JZK0; -. DR STRING; 122586.NMB1018; -. DR PaxDb; Q9JZK0; -. DR EnsemblBacteria; AAF41418; AAF41418; NMB1018. DR GeneID; 903156; -. DR KEGG; nme:NMB1018; -. DR PATRIC; 20357571; VBINeiMen85645_1302. DR eggNOG; ENOG41062MN; Bacteria. DR eggNOG; COG0454; LUCA. DR HOGENOM; HOG000218926; -. DR OMA; PAKESDR; -. DR OrthoDB; EOG65XN44; -. DR BioCyc; NMEN122586:GHGG-1055-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF13673; Acetyltransf_10; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 160 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 160 AA; 18146 MW; 88BEF01AD8AA44C3 CRC64; MSLLTLLRPA TVQDCKDIFK VHLHSVQYTC ILSYNEHALK VWEGLLNTES YLPTISDPDK ALWVAEYKGN IQGFFQIDCQ EAQLDALYVH PLFHNLGLGT ALLHQAETIA HKSGLSFLKL YASLNSVPFY LLNRYESLGS AVLQLDPSIK IKCELMRKHL // ID Q9JYD6_NEIMB Unreviewed; 402 AA. AC Q9JYD6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41984.1}; GN OrderedLocusNames=NMB1634 {ECO:0000313|EMBL:AAF41984.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41984.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41984.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41984.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41984.1; -; Genomic_DNA. DR PIR; D81061; D81061. DR RefSeq; NP_274640.1; NC_003112.2. DR RefSeq; WP_002212532.1; NC_003112.2. DR STRING; 122586.NMB1634; -. DR PaxDb; Q9JYD6; -. DR EnsemblBacteria; AAF41984; AAF41984; NMB1634. DR GeneID; 903969; -. DR KEGG; nme:NMB1634; -. DR PATRIC; 20359172; VBINeiMen85645_2097. DR eggNOG; ENOG4105HKQ; Bacteria. DR eggNOG; COG2946; LUCA. DR HOGENOM; HOG000218820; -. DR KO; K07467; -. DR OMA; LARWYAN; -. DR OrthoDB; EOG6HB9T6; -. DR BioCyc; NMEN122586:GHGG-1683-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR InterPro; IPR003491; Rep_trans. DR Pfam; PF02486; Rep_trans; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 402 AA; 46768 MW; D03EA26B3608C709 CRC64; MSEAEYFSHF ISNGNGKLLE IPQRRGRQDG VFIDWLSFTL HEDSLLKVSG CPLVSDAEYM FVLSKKLEEI LGFGITSRCK SKGNKFYDSM FRLGSEEVDY GEVHYGGQRN TVLIELKGVG CNIANPGWEL RLKQFLEDSL RPRITRVDLA LDFFDGEYTP EQALLDHDNG FFDNSNMRPK SEMVGTAWRR EDGSGKTFYV GRKKNSRFVR VYEKGRQLGD KESKWVRFEI QFNHGDMEIP LDILINQGSY FSGAFPICQK FKNMPNPERF DYRKKVANLT FQHKLRYAKN AVGKLINFMF DMGFDSDEIV RYLKADLGYP KGLEPEKYSL AGLKESLKFG FIHEQPDVDL EVELEELGII KFKQSDKFDP DKRLFDPHHD VESERQYQLY LDRMYDLHAN QN // ID Q9K194_NEIMB Unreviewed; 141 AA. AC Q9K194; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40727.1}; GN OrderedLocusNames=NMB0273 {ECO:0000313|EMBL:AAF40727.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40727.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40727.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40727.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40727.1; -; Genomic_DNA. DR PIR; B81219; B81219. DR RefSeq; NP_273329.1; NC_003112.2. DR RefSeq; WP_002221589.1; NC_003112.2. DR PaxDb; Q9K194; -. DR EnsemblBacteria; AAF40727; AAF40727; NMB0273. DR GeneID; 902384; -. DR KEGG; nme:NMB0273; -. DR PATRIC; 20355632; VBINeiMen85645_0340. DR HOGENOM; HOG000219126; -. DR OMA; PMYADAG; -. DR OrthoDB; EOG615VF4; -. DR BioCyc; NMEN122586:GHGG-288-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 141 AA; 16299 MW; FEF80242B6090978 CRC64; MYWERGLHMY KASAVVPTGY VRVGNTAPLV GEDTQRYASF WGDGYDVYRQ LRWQQIPEKQ RKAFKKAAKS KKTVMFAGRE YGISKQNLSD VWDDFEDAME LKAFPCLSSL FLTKWHKNLY DSGLTKTSTA LPRLSSKRTI L // ID Q9JYP9_NEIMB Unreviewed; 415 AA. AC Q9JYP9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Putative lipoprotein NlpD {ECO:0000313|EMBL:AAF41839.1}; GN OrderedLocusNames=NMB1483 {ECO:0000313|EMBL:AAF41839.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41839.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41839.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41839.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41839.1; -; Genomic_DNA. DR PIR; H81079; H81079. DR RefSeq; NP_274491.1; NC_003112.2. DR RefSeq; WP_002225087.1; NC_003112.2. DR ProteinModelPortal; Q9JYP9; -. DR STRING; 122586.NMB1483; -. DR MEROPS; M23.011; -. DR PaxDb; Q9JYP9; -. DR EnsemblBacteria; AAF41839; AAF41839; NMB1483. DR GeneID; 903905; -. DR KEGG; nme:NMB1483; -. DR PATRIC; 20358732; VBINeiMen85645_1875. DR eggNOG; ENOG4108K5P; Bacteria. DR eggNOG; COG0739; LUCA. DR HOGENOM; HOG000159026; -. DR KO; K06194; -. DR OMA; NTMPAGM; -. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; NMEN122586:GHGG-1523-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.350.10; -; 2. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01476; LysM; 2. DR Pfam; PF01551; Peptidase_M23; 1. DR SMART; SM00257; LysM; 2. DR SUPFAM; SSF51261; SSF51261; 1. DR SUPFAM; SSF54106; SSF54106; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000313|EMBL:AAF41839.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 415 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329342. FT DOMAIN 104 147 LysM. {ECO:0000259|SMART:SM00257}. FT DOMAIN 184 227 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 415 AA; 42875 MW; 7704BF7F0DF54DF5 CRC64; MLKQTTLLAA CTAVAALLGG CATQQPAPVI AGNSGMQDAP SSAVYNNPYG ATPYSPAPAG DAPYVPPVQS APVYTPPAYV PPSAPAVSGT YVPSYAPVDI NAATHTIVRG DTVYNISKRY HISQDDFRAW NGMTDNTLSI GQIVKVKPAG YAAPKAAAVK SRPAVPAAAQ PPVQSAPVDI NAATHTIVRG DTVYNISKRY HISQDDFRAW NGMTDNMLSI GQIVKVKPAG YAAPKTAAVE SRPAVPAAVQ TPVKPAAQPP VQSAPQPAAP AAENKAVPAP APQSPAASPS GTRSVGGIVW QRPTQGKVVA DFGGNNKGVD IAGNAGQPVL AAADGKVVYA GSGLRGYGNL VIIQHNSSFL TAYGHNQKLL VGEGQQVKRG QQVALMGNTD ASRTQLHFEV RQNGKPVNPN SYIAF // ID Q9K0X6_NEIMB Unreviewed; 34 AA. AC Q9K0X6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40867.1}; GN OrderedLocusNames=NMB0429 {ECO:0000313|EMBL:AAF40867.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40867.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40867.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40867.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40867.1; -; Genomic_DNA. DR PIR; G81199; G81199. DR RefSeq; NP_273477.1; NC_003112.2. DR RefSeq; WP_010980793.1; NC_003112.2. DR STRING; 122586.NMB0429; -. DR PaxDb; Q9K0X6; -. DR EnsemblBacteria; AAF40867; AAF40867; NMB0429. DR GeneID; 902545; -. DR KEGG; nme:NMB0429; -. DR BioCyc; NMEN122586:GHGG-453-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 3893 MW; 95380D12648B2D07 CRC64; MKPIQMFSPF LNNPLVFFLS AVLPHNSERS AVFL // ID Q9JYU2_NEIMB Unreviewed; 83 AA. AC Q9JYU2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41792.1}; GN OrderedLocusNames=NMB1431 {ECO:0000313|EMBL:AAF41792.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41792.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41792.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41792.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41792.1; -; Genomic_DNA. DR PIR; H81084; H81084. DR STRING; 122586.NMB1431; -. DR PaxDb; Q9JYU2; -. DR EnsemblBacteria; AAF41792; AAF41792; NMB1431. DR OMA; NFIEFGR; -. DR BioCyc; NMEN122586:GHGG-1469-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 83 AA; 9900 MW; C0E43E88F8826420 CRC64; MKNLRLGIFG FKVRKCGFLC RKLIIFKFFV SKISLSAYFQ LLLRTWRVCR RRGTIANFIE FGRIAAVQRQ TSRRFSGRLV FLF // ID Q7DD89_NEIMB Unreviewed; 266 AA. AC Q7DD89; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Putative transporter {ECO:0000313|EMBL:AAF42077.1}; GN OrderedLocusNames=NMB1732 {ECO:0000313|EMBL:AAF42077.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42077.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42077.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42077.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42077.1; -; Genomic_DNA. DR PIR; C81049; C81049. DR RefSeq; NP_274735.1; NC_003112.2. DR RefSeq; WP_002212588.1; NC_003112.2. DR ProteinModelPortal; Q7DD89; -. DR STRING; 122586.NMB1732; -. DR PaxDb; Q7DD89; -. DR EnsemblBacteria; AAF42077; AAF42077; NMB1732. DR GeneID; 903367; -. DR KEGG; nme:NMB1732; -. DR PATRIC; 20359427; VBINeiMen85645_2219. DR eggNOG; ENOG4105D04; Bacteria. DR eggNOG; COG1230; LUCA. DR HOGENOM; HOG000002625; -. DR OMA; ISLWLIN; -. DR OrthoDB; EOG6B360K; -. DR BioCyc; NMEN122586:GHGG-1787-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR Gene3D; 1.20.1510.10; -; 1. DR InterPro; IPR002524; Cation_efflux. DR InterPro; IPR027469; Cation_efflux_TMD. DR InterPro; IPR006121; HMA_dom. DR PANTHER; PTHR11562; PTHR11562; 1. DR Pfam; PF01545; Cation_efflux; 1. DR SUPFAM; SSF55008; SSF55008; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 167 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 179 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 238 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 262 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 266 AA; 29957 MW; 4536ABAA0C058B7F CRC64; MKKTIFNITK MDCPSEEQLI RMRLKDVSDI YELQFDIAGR CLTVYHDNQD TTILQVLEPL NFDSHIISTE VIVDKIVFNK PDEHLEKRLL YQVLMINFVF FIIECSVGIF ANSMGLIADS LDMLADSFVY ILALSAIGMT LAYKKRVAFL AGITQIILAL FGVIEVIRRF IGAEQLPNYQ LMIGTAFLAL IANWLCLYLL SKNQNKEIHI KASMIFTSND IIINIGVIAA GALTLLTHSS YPDLIIGMIV FVIVLFGARN ILKLAK // ID Q7DDD6_NEIMB Unreviewed; 435 AA. AC Q7DDD6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579}; DE EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579}; GN Name=metM {ECO:0000313|EMBL:AAF41609.1}; GN OrderedLocusNames=NMB1228 {ECO:0000313|EMBL:AAF41609.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41609.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41609.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41609.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. {ECO:0000256|RuleBase:RU000579}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC {ECO:0000256|RuleBase:RU000579}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC {ECO:0000256|RuleBase:RU000579}. CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family. CC {ECO:0000256|RuleBase:RU004171}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41609.1; -; Genomic_DNA. DR PIR; E81106; E81106. DR RefSeq; NP_274252.1; NC_003112.2. DR RefSeq; WP_002222431.1; NC_003112.2. DR ProteinModelPortal; Q7DDD6; -. DR STRING; 122586.NMB1228; -. DR PaxDb; Q7DDD6; -. DR EnsemblBacteria; AAF41609; AAF41609; NMB1228. DR GeneID; 903650; -. DR KEGG; nme:NMB1228; -. DR PATRIC; 20358047; VBINeiMen85645_1536. DR eggNOG; ENOG4105D6E; Bacteria. DR eggNOG; COG0460; LUCA. DR HOGENOM; HOG000076615; -. DR KO; K00003; -. DR OMA; EWIAGII; -. DR OrthoDB; EOG6XM7CQ; -. DR BioCyc; NMEN122586:GHGG-1265-MONOMER; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR016204; HDH. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000098; Homoser_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|RuleBase:RU000579}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579}; KW Methionine biosynthesis {ECO:0000256|RuleBase:RU000579}; KW NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000579, KW ECO:0000313|EMBL:AAF41609.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}. FT DOMAIN 354 429 ACT. {ECO:0000259|PROSITE:PS51671}. FT NP_BIND 9 16 NADP. {ECO:0000256|PIRSR:PIRSR000098-2}. FT ACT_SITE 204 204 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000098-1}. FT BINDING 104 104 NADP. {ECO:0000256|PIRSR:PIRSR000098-2}. FT BINDING 189 189 Substrate. FT {ECO:0000256|PIRSR:PIRSR000098-2}. SQ SEQUENCE 435 AA; 46546 MW; 4F583AA747DA80CA CRC64; MKPVNIGLLG LGTVGGGTAA VLRDNAEEIS RRLGREIRIS AVCDLSEEKA RQTCPSAAFV KDPFELVARE DVDVVVELFG GTGIAKDAVL KAIENGKHIV TANKKLLAEY GNEIFPLAEK QNVIVQFEAA VAGGIPIIKA LREGLAANRI KSIAGIINGT SNFILSEMRE KGSAFADVLK EAQALGYAEA DPTFDIEGND AGHKITIMSA LAFGTPMNFS ACYLEGISKL DSRDIKYAEE LGYRIKLLGI TRKTGKGIEL RVHPTLIPES RLLANVNGVM NAVRVNADMV GETLYYGAGA GALPTASAVV ADIIDIARLV EADTAHRVPH LAFQPAQVQA QTILPMDEIT SSYYLRVQAK DEPGTLGQIA ALLAQENVSI EALIQKGVID QTTAEIVILT HSTVEKHIKS AIAAIEALDC VEKPITMIRM ESLHD // ID Q9JXC3_NEIMB Unreviewed; 328 AA. AC Q9JXC3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Putative protease {ECO:0000313|EMBL:AAF42435.1}; GN OrderedLocusNames=NMB2127 {ECO:0000313|EMBL:AAF42435.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42435.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42435.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42435.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42435.1; -; Genomic_DNA. DR PIR; F81005; F81005. DR RefSeq; NP_275112.1; NC_003112.2. DR RefSeq; WP_002218229.1; NC_003112.2. DR ProteinModelPortal; Q9JXC3; -. DR STRING; 122586.NMB2127; -. DR PaxDb; Q9JXC3; -. DR EnsemblBacteria; AAF42435; AAF42435; NMB2127. DR GeneID; 903411; -. DR KEGG; nme:NMB2127; -. DR PATRIC; 20360430; VBINeiMen85645_2711. DR eggNOG; ENOG4105D07; Bacteria. DR eggNOG; COG0616; LUCA. DR HOGENOM; HOG000022574; -. DR KO; K04773; -. DR OMA; QIFVDKA; -. DR OrthoDB; EOG6GFGG4; -. DR BioCyc; NMEN122586:GHGG-2192-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002142; Peptidase_S49. DR Pfam; PF01343; Peptidase_S49; 1. DR SUPFAM; SSF52096; SSF52096; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42435.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000313|EMBL:AAF42435.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 64 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 143 287 Peptidase_S49. FT {ECO:0000259|Pfam:PF01343}. SQ SEQUENCE 328 AA; 36005 MW; 36CF59A4D7459DD0 CRC64; MQYRIRRENE APEAKNAGET LWERDIMREV LLSAYQDRRR ERMWKNIWRA VSTLILVALI AGIFRKDEAA LQLAGNTPHT AVVNLYGEIG NGVEDQVKKL KDGMEAAYKN PQAKAIVIRA NSPGGSPVVS NTAFEEIRRL KAQHPGIPVY LVAEDMCASG CYYIAAAADK IYADPSSIVG SIGVIGSSFD ATGLMEKIGV KRRVKIAGSN KGMGDPFSPE TPEQSKIWEE MLTGIHGEFI KAVKTGRGGR LKFRQYPDVF SGRVYTGADA LKVGLVDGLG NIYSVARDVV KAPDVVDYTP KDDFGRILGR RFGAELKASV REALQAVR // ID Q9JYE8_NEIMB Unreviewed; 87 AA. AC Q9JYE8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41967.1}; GN OrderedLocusNames=NMB1615 {ECO:0000313|EMBL:AAF41967.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41967.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41967.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41967.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41967.1; -; Genomic_DNA. DR PIR; E81063; E81063. DR PaxDb; Q9JYE8; -. DR EnsemblBacteria; AAF41967; AAF41967; NMB1615. DR PATRIC; 20359124; VBINeiMen85645_2074. DR OrthoDB; EOG6D8BFN; -. DR BioCyc; NMEN122586:GHGG-1663-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 87 AA; 9993 MW; 23EDEA778C527279 CRC64; MFSGESAASE HTAHAHIDLP SLAHRVHRRP LRLKIKLPSV VGITTQKNEL LDIPMFFICF YIVMRSDKRP PDICLDGIVL LNFYKYV // ID Q9JZ63_NEIMB Unreviewed; 327 AA. AC Q9JZ63; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41651.1}; GN OrderedLocusNames=NMB1274 {ECO:0000313|EMBL:AAF41651.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41651.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41651.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41651.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41651.1; -; Genomic_DNA. DR PIR; D81103; D81103. DR RefSeq; NP_274295.1; NC_003112.2. DR RefSeq; WP_002225181.1; NC_003112.2. DR ProteinModelPortal; Q9JZ63; -. DR STRING; 122586.NMB1274; -. DR PaxDb; Q9JZ63; -. DR EnsemblBacteria; AAF41651; AAF41651; NMB1274. DR GeneID; 903696; -. DR KEGG; nme:NMB1274; -. DR PATRIC; 20358167; VBINeiMen85645_1595. DR eggNOG; ENOG4108Q0S; Bacteria. DR eggNOG; COG2845; LUCA. DR HOGENOM; HOG000218983; -. DR KO; K09795; -. DR OMA; QENAYAF; -. DR OrthoDB; EOG62NX13; -. DR BioCyc; NMEN122586:GHGG-1312-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.1110; -; 1. DR InterPro; IPR007407; DUF459. DR InterPro; IPR013830; SGNH_hydro. DR Pfam; PF04311; DUF459; 1. DR SUPFAM; SSF52266; SSF52266; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 327 AA; 36463 MW; 737DC22A75A33B7F CRC64; MKNFLSLFSS ILMSALIAVW FSQNPINAYW QQTYHRNSPL EPLAAYGWWR SGAALQENAY ALSDGIKAFL SGETPPTAQD GGSADMPSEA AASEAVPQTG ETEWKQDTEA AAVRSGDKVF FVGDSLMQGV APFVQKSLKQ QYGIESVNLS KQSTGLSYPS FFDWPKTIEE TLQKHPEISV LAVFLGPNDP WDFPVGKLYL KFASDEWAQE YLKRVDRILE AAHTHRVQVV WLGIPYMKKA KLDGQMRYLD KLLSEHLKGK IILIPTTHTL SGGKDRYTDS VNVNGKPVRY RSKDGIHFTA EGQKLLAAKI MEKIVFEPST QPSSTQP // ID Q7DD37_NEIMB Unreviewed; 488 AA. AC Q7DD37; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Transferrin-binding protein-related protein {ECO:0000313|EMBL:AAF42440.1}; GN OrderedLocusNames=NMB2132 {ECO:0000313|EMBL:AAF42440.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42440.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42440.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42440.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42440.1; -; Genomic_DNA. DR RefSeq; NP_275117.1; NC_003112.2. DR RefSeq; WP_002248796.1; NC_003112.2. DR ProteinModelPortal; Q7DD37; -. DR STRING; 122586.NMB2132; -. DR PaxDb; Q7DD37; -. DR EnsemblBacteria; AAF42440; AAF42440; NMB2132. DR GeneID; 903357; -. DR KEGG; nme:NMB2132; -. DR PATRIC; 20360440; VBINeiMen85645_2716. DR HOGENOM; HOG000218697; -. DR OMA; ANQTGNN; -. DR OrthoDB; EOG6W45NK; -. DR BioCyc; NMEN122586:GHGG-2197-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR001677; Solute-bd_prot_TBP-like. DR Pfam; PF01298; Lipoprotein_5; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 488 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287252. SQ SEQUENCE 488 AA; 50554 MW; B38DD93CA81E4C65 CRC64; MFKRSVIAMA CIFALSACGG GGGGSPDVKS ADTLSKPAAP VVSEKETEAK EDAPQAGSQG QGAPSAQGSQ DMAAVSEENT GNGGAVTADN PKNEDEVAQN DMPQNAAGTD SSTPNHTPDP NMLAGNMENQ ATDAGESSQP ANQPDMANAA DGMQGDDPSA GGQNAGNTAA QGANQAGNNQ AAGSSDPIPA SNPAPANGGS NFGRVDLANG VLIDGPSQNI TLTHCKGDSC SGNNFLDEEV QLKSEFEKLS DADKISNYKK DGKNDKFVGL VADSVQMKGI NQYIIFYKPK PTSFARFRRS ARSRRSLPAE MPLIPVNQAD TLIVDGEAVS LTGHSGNIFA PEGNYRYLTY GAEKLPGGSY ALRVQGEPAK GEMLAGAAVY NGEVLHFHTE NGRPYPTRGR FAAKVDFGSK SVDGIIDSGD DLHMGTQKFK AAIDGNGFKG TWTENGSGDV SGKFYGPAGE EVAGKYSYRP TDAEKGGFGV FAGKKEQD // ID Q9JZE2_NEIMB Unreviewed; 522 AA. AC Q9JZE2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41487.1}; GN OrderedLocusNames=NMB1095 {ECO:0000313|EMBL:AAF41487.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41487.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41487.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41487.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41487.1; -; Genomic_DNA. DR PIR; A81124; A81124. DR RefSeq; NP_274127.1; NC_003112.2. DR RefSeq; WP_002244120.1; NC_003112.2. DR STRING; 122586.NMB1095; -. DR PaxDb; Q9JZE2; -. DR EnsemblBacteria; AAF41487; AAF41487; NMB1095. DR GeneID; 903516; -. DR KEGG; nme:NMB1095; -. DR PATRIC; 20357751; VBINeiMen85645_1392. DR eggNOG; ENOG4105QIB; Bacteria. DR eggNOG; COG4383; LUCA. DR HOGENOM; HOG000013741; -. DR OMA; VDIGFRI; -. DR OrthoDB; EOG6PP9Q8; -. DR BioCyc; NMEN122586:GHGG-1131-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009279; DUF935. DR Pfam; PF06074; DUF935; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 522 AA; 58076 MW; 4BCCE3570FE56670 CRC64; MAKKNNKTKI QKPEAALQTD VAQITATGRV IAEHPSNFIT PQKMRALFED AESGDIRAQH ELFADIEERD SDIAANMGTR KRALLTLNWR VAPPRNATPE EEKLSDQAYE MMDSLPTLED LIMDLMDAVG HGFSALEVEW VFSDGLYLPR NFIHRPQSWF KWDKDNGLLL RTRENPEGEA LWPLGWVVHT QKSRSVQQAR NGLFRTLSWL YMFKHYAVHD FAEFLELYGM PIRIGKYGAG ATKEEKNTLL RAVAEIGHNA AGIMPEGMEI ELHNAANGTT ATSNPFLQMA DWCEKSAARL ILGQTLTSGA DGKSSTNALG NIHNEVRRDL LVSDAKQVAQ TITSQIIGPF LQINYPHADP NRVPKFEFDT REPKDIAVFA DAIPKLVDVG VQIPESWVRD KLVIPDVQEG EAVLVRQVPD NPVNRTALAA LSAHTVPSKA TGRHQEILDG ALDDALVEPD FNSQLNPMVR QAVAALNACN SYEEADAALN ALYPNLDNAK LRTYMQQALF ISDILGQDHA RA // ID Q9K1Q2_NEIMB Unreviewed; 72 AA. AC Q9K1Q2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40499.1}; GN OrderedLocusNames=NMB0028 {ECO:0000313|EMBL:AAF40499.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40499.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40499.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40499.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40499.1; -; Genomic_DNA. DR PIR; G81245; G81245. DR RefSeq; NP_273094.1; NC_003112.2. DR RefSeq; WP_002221786.1; NC_003112.2. DR STRING; 122586.NMB0028; -. DR PaxDb; Q9K1Q2; -. DR EnsemblBacteria; AAF40499; AAF40499; NMB0028. DR GeneID; 902131; -. DR KEGG; nme:NMB0028; -. DR PATRIC; 20355005; VBINeiMen85645_0039. DR eggNOG; ENOG4105VCV; Bacteria. DR eggNOG; COG3205; LUCA. DR HOGENOM; HOG000002413; -. DR OMA; IEPLCNS; -. DR OrthoDB; EOG64R69Q; -. DR BioCyc; NMEN122586:GHGG-29-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018638; DUF2061_membrane. DR Pfam; PF09834; DUF2061; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 52 DUF2061. {ECO:0000259|Pfam:PF09834}. SQ SEQUENCE 72 AA; 8092 MW; 1F02E065D67DD103 CRC64; MLKTLTFAAL HFSVAFSVTY VLTGSIGVSG AVALVEPLIN TVVFYFHEKA WNLYEKNKTV KQTQPFQLHR CS // ID Q9JZI4_NEIMB Unreviewed; 449 AA. AC Q9JZI4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Glutamate--cysteine ligase {ECO:0000313|EMBL:AAF41436.1}; DE EC=6.3.2.2 {ECO:0000313|EMBL:AAF41436.1}; GN Name=gshA {ECO:0000313|EMBL:AAF41436.1}; GN OrderedLocusNames=NMB1037 {ECO:0000313|EMBL:AAF41436.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41436.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41436.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41436.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41436.1; -; Genomic_DNA. DR PIR; H81128; H81128. DR RefSeq; NP_274071.1; NC_003112.2. DR RefSeq; WP_002223737.1; NC_003112.2. DR STRING; 122586.NMB1037; -. DR PaxDb; Q9JZI4; -. DR EnsemblBacteria; AAF41436; AAF41436; NMB1037. DR GeneID; 903174; -. DR KEGG; nme:NMB1037; -. DR PATRIC; 20357609; VBINeiMen85645_1321. DR eggNOG; ENOG41070NA; Bacteria. DR eggNOG; ENOG410XSH9; LUCA. DR HOGENOM; HOG000265033; -. DR KO; K01919; -. DR OMA; GMHFVPL; -. DR OrthoDB; EOG69WFG3; -. DR BioCyc; NMEN122586:GHGG-1074-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC. DR InterPro; IPR011718; GshA. DR Pfam; PF08886; GshA; 1. DR TIGRFAMs; TIGR02049; gshA_ferroox; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF41436.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 449 AA; 49688 MW; 72E179E98CAD7AC1 CRC64; MKLPVMSPEH SAQLQAFEAK ILSNHAKIEA WFRTQWSVHR PPFYGSVDIR NAGYKISSID MNLFPGGFNN LNPNFIPLAA VAAQDAVQRA CETAKSVLII PENHTRNTFY LQNVYALGEI LRSAGYEVRL GSLNPEVTEP TEFETALGDK ILLEPLLRTR DRVHLADGFS PCVVLLNNDL SAGIPDILKG ISQTVLPPLH GGWTTRRKTN HFGAYNQVTA EFAKLIGIDE WQINPYFEKI GGLDFQGREG EDALAEAVER VLAKIQAKYD ESGITDKPFV IVKADAGTYG MGVMSVKSAD EVRGLNRKNR NKMAKVKEGL EVSEVIVQEG IYTYETLNGA VCEPVVYMMD RFVIGGFFRV HEGRGADENL NAGGMVFVPL SNSIPTGNGD NSQEAPEACK RVFEQWDSLG MPRSEKDCDV DNEHNRLYVY GVMARLSLLA ASIELEETA // ID Q9JZI1_NEIMB Unreviewed; 426 AA. AC Q9JZI1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41439.1}; GN OrderedLocusNames=NMB1040 {ECO:0000313|EMBL:AAF41439.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41439.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41439.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41439.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41439.1; -; Genomic_DNA. DR PIR; C81129; C81129. DR RefSeq; NP_274074.1; NC_003112.2. DR RefSeq; WP_002219224.1; NC_003112.2. DR STRING; 122586.NMB1040; -. DR PaxDb; Q9JZI1; -. DR EnsemblBacteria; AAF41439; AAF41439; NMB1040. DR GeneID; 903177; -. DR KEGG; nme:NMB1040; -. DR PATRIC; 20357617; VBINeiMen85645_1325. DR eggNOG; ENOG4108XGF; Bacteria. DR eggNOG; ENOG4111MPB; LUCA. DR HOGENOM; HOG000218976; -. DR OMA; GSFERAC; -. DR OrthoDB; EOG67DPJ4; -. DR BioCyc; NMEN122586:GHGG-1077-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014044; CAP_domain. DR Pfam; PF00188; CAP; 1. DR SUPFAM; SSF55797; SSF55797; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 46 173 SCP. {ECO:0000259|Pfam:PF00188}. SQ SEQUENCE 426 AA; 47911 MW; 8DDD576C4B13D3CB CRC64; MKSLFIRLLL LGSAAGVFYH TQNQSLPAGE LVYPSAPQIR DGGDALHYLN RIRAQIGLHK LAHAPVLENS ARRHASYLTL NPEDGHGEHH PDNPHYTAQK LTERTRLAGY LYNGVHENIS TEEEAAESSD SDIRTQQRQV DGLMSAIYHR LSLLDRHTDE AGAAFVRENG KTVLVFNQGN GRFERHCAQG RNQPEAGRKY YRNACHNGAV VYTDEAMPAQ ELLYTAYPVG SGALPYFHGE RPDPVPEYEI TGNPASIDFS EAAGKITMKS FKLYQGKNEI RPVRVLTAGN DPNGRLTAYQ FALFPLKPLE YGTLYTAVFD YVRNGRRAQA KWQFRTRKPD YPYFEVNGGE TLAVRKGEKY FIHWRGRWCL EACTRYTYRQ RPGSRLSIGR HEAGGIVFSV DGMAGSRITL APEGETERGV TLYLQD // ID Q9JZZ4_NEIMB Unreviewed; 67 AA. AC Q9JZZ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Cold-shock domain family protein {ECO:0000313|EMBL:AAF41249.1}; GN OrderedLocusNames=NMB0838 {ECO:0000313|EMBL:AAF41249.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41249.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41249.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41249.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3CAM} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS). RX PubMed=18391418; DOI=10.1107/S1744309108005411; RA Ren J., Nettleship J.E., Sainsbury S., Saunders N.J., Owens R.J.; RT "Structure of the cold-shock domain protein from Neisseria RT meningitidis reveals a strand-exchanged dimer."; RL Acta Crystallogr. F 64:247-251(2008). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000408, CC ECO:0000256|SAAS:SAAS00557911}. CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain. CC {ECO:0000256|RuleBase:RU000407}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41249.1; -; Genomic_DNA. DR PIR; C81151; C81151. DR RefSeq; NP_273879.1; NC_003112.2. DR RefSeq; WP_002217533.1; NC_003112.2. DR PDB; 3CAM; X-ray; 2.60 A; A/B=1-67. DR PDBsum; 3CAM; -. DR ProteinModelPortal; Q9JZZ4; -. DR SMR; Q9JZZ4; 1-67. DR STRING; 122586.NMB0838; -. DR PaxDb; Q9JZZ4; -. DR EnsemblBacteria; AAF41249; AAF41249; NMB0838. DR GeneID; 25047475; -. DR GeneID; 902952; -. DR KEGG; nme:NMB0838; -. DR PATRIC; 20357063; VBINeiMen85645_1050. DR eggNOG; ENOG4105VEQ; Bacteria. DR eggNOG; COG1278; LUCA. DR HOGENOM; HOG000070674; -. DR KO; K03704; -. DR OMA; NDKVEFT; -. DR OrthoDB; EOG618R0J; -. DR BioCyc; NMEN122586:GHGG-869-MONOMER; -. DR EvolutionaryTrace; Q9JZZ4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR019844; Cold-shock_CS. DR InterPro; IPR012156; Cold_shock_CspA. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF00313; CSD; 1. DR PIRSF; PIRSF002599; Cold_shock_A; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00352; COLD_SHOCK; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3CAM}; KW Activator {ECO:0000256|SAAS:SAAS00444396}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00444364}; KW DNA-binding {ECO:0000256|SAAS:SAAS00444440}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00444462}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00444462}. FT DOMAIN 3 67 CSP. {ECO:0000259|SMART:SM00357}. SQ SEQUENCE 67 AA; 7195 MW; 85FB87B505525460 CRC64; MATGIVKWFN DAKGFGFITP DEGGEDLFAH FSAINMEGFK TLKEGQRVSF DVTTGPKGKQ AANIQAA // ID Q9JZ41_NEIMB Unreviewed; 253 AA. AC Q9JZ41; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Putative fimbrial biogenesis and twitching motility protein {ECO:0000313|EMBL:AAF41684.1}; GN OrderedLocusNames=NMB1309 {ECO:0000313|EMBL:AAF41684.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41684.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41684.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41684.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2VQ2} RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 29-253, AND DISULFIDE BONDS. RX PubMed=18433773; DOI=10.1016/j.jmb.2008.03.028; RA Trindade M.B., Job V., Contreras-Martel C., Pelicic V., Dessen A.; RT "Structure of a widely conserved type IV pilus biogenesis factor that RT affects the stability of secretin multimers."; RL J. Mol. Biol. 378:1031-1039(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41684.1; -; Genomic_DNA. DR PIR; C81098; C81098. DR RefSeq; NP_274328.1; NC_003112.2. DR RefSeq; WP_002227268.1; NC_003112.2. DR PDB; 2VQ2; X-ray; 1.54 A; A=29-253. DR PDBsum; 2VQ2; -. DR ProteinModelPortal; Q9JZ41; -. DR SMR; Q9JZ41; 32-251. DR STRING; 122586.NMB1309; -. DR PaxDb; Q9JZ41; -. DR EnsemblBacteria; AAF41684; AAF41684; NMB1309. DR GeneID; 903731; -. DR KEGG; nme:NMB1309; -. DR PATRIC; 20358263; VBINeiMen85645_1643. DR eggNOG; ENOG41090FY; Bacteria. DR eggNOG; COG3063; LUCA. DR HOGENOM; HOG000218990; -. DR KO; K02656; -. DR OMA; RAQFYIR; -. DR OrthoDB; EOG6Q2SH3; -. DR BioCyc; NMEN122586:GHGG-1347-MONOMER; -. DR EvolutionaryTrace; Q9JZ41; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR013360; Pilus_4_PilW. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR02521; type_IV_pilW; 1. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2VQ2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 36 174 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. FT DISULFID 115 150 {ECO:0000213|PDB:2VQ2}. SQ SEQUENCE 253 AA; 28424 MW; 6BCB1314D61A74DA CRC64; MPFKPSKRIS LLLVLALGAC STSYRPSRAE KANQVSNIKT QLAMEYMRGQ DYRQATASIE DALKSDPKNE LAWLVRAEIY QYLKVNDKAQ ESFRQALSIK PDSAEINNNY GWFLCGRLNR PAESMAYFDK ALADPTYPTP YIANLNKGIC SAKQGQFGLA EAYLKRSLAA QPQFPPAFKE LARTKMLAGQ LGDADYYFKK YQSRVEVLQA DDLLLGWKIA KALGNAQAAY EYEAQLQANF PYSEELQTVL TGQ // ID Q9JXG4_NEIMB Unreviewed; 256 AA. AC Q9JXG4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=ThiF protein {ECO:0000313|EMBL:AAF42381.1}; GN Name=thiF {ECO:0000313|EMBL:AAF42381.1}; GN OrderedLocusNames=NMB2062 {ECO:0000313|EMBL:AAF42381.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42381.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42381.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42381.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42381.1; -; Genomic_DNA. DR PIR; B81010; B81010. DR RefSeq; NP_275052.1; NC_003112.2. DR RefSeq; WP_002225703.1; NC_003112.2. DR ProteinModelPortal; Q9JXG4; -. DR STRING; 122586.NMB2062; -. DR PaxDb; Q9JXG4; -. DR EnsemblBacteria; AAF42381; AAF42381; NMB2062. DR GeneID; 904016; -. DR KEGG; nme:NMB2062; -. DR PATRIC; 20360282; VBINeiMen85645_2641. DR eggNOG; ENOG4105D06; Bacteria. DR eggNOG; COG0476; LUCA. DR HOGENOM; HOG000281217; -. DR OMA; EVACATM; -. DR OrthoDB; EOG628F8J; -. DR BioCyc; NMEN122586:GHGG-2125-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR Pfam; PF00899; ThiF; 1. DR SUPFAM; SSF69572; SSF69572; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 249 ThiF. {ECO:0000259|Pfam:PF00899}. SQ SEQUENCE 256 AA; 27200 MW; 0AAD7E2C9FCD01C7 CRC64; MTTTEHDNDD AFLLRYSRHI LLDEIGIEGQ QKLSAAHILV VGCGGLGAAA LPYLAASGVG TLTIADSDTV ELHNLQRQVA FDEGDVGKLK TEALAGRLKR INHTVNVRAV NEKLDGCRLT GLVQAADIVL DCCDNYATRQ AVNRACVQTK TPLVSGAAVR FEGQLAVYRP DLPDSPCYAC LFDGGSASDG ICSLFGVFSP LVGIIGSTQA AEALKILLDA GEPSHGRLAV YRALEGGWQY FDLPRNPECP VCGTAR // ID Q7DDI4_NEIMB Unreviewed; 214 AA. AC Q7DDI4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=DedA protein {ECO:0000313|EMBL:AAF41450.1}; GN Name=dedA {ECO:0000313|EMBL:AAF41450.1}; GN OrderedLocusNames=NMB1052 {ECO:0000313|EMBL:AAF41450.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41450.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41450.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41450.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41450.1; -; Genomic_DNA. DR PIR; D81128; D81128. DR RefSeq; NP_274086.1; NC_003112.2. DR RefSeq; WP_002219343.1; NC_003112.2. DR STRING; 122586.NMB1052; -. DR PaxDb; Q7DDI4; -. DR DNASU; 903189; -. DR EnsemblBacteria; AAF41450; AAF41450; NMB1052. DR GeneID; 903189; -. DR KEGG; nme:NMB1052; -. DR PATRIC; 20357641; VBINeiMen85645_1337. DR eggNOG; ENOG4105DQR; Bacteria. DR eggNOG; COG0586; LUCA. DR HOGENOM; HOG000105368; -. DR KO; K03975; -. DR OMA; YLDKTHE; -. DR OrthoDB; EOG6D2KZK; -. DR BioCyc; NMEN122586:GHGG-1089-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 204 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 214 AA; 23486 MW; 2E247A942686B9B8 CRC64; MLASAIDFIL HIDQHLLALS AQYGVWIYAI LFLIVFCETG LIVTPLLPGD SLLFAAGGIA ALGGMDIHLM VALLSLAAIL GDALNFTVGK YFGGRLFANP DSKIFRREYL DKTHRFYEKH GGKTIIIARF MPIVRTFAPF VAGMGKMHYA KFIRYNIIGG LLWVILFSYA GYFFANFPVV KNNLGLVMGG IIIVSVLPGA VEIARAKLAV KSKR // ID Q9JYP7_NEIMB Unreviewed; 518 AA. AC Q9JYP7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41841.1}; GN OrderedLocusNames=NMB1485 {ECO:0000313|EMBL:AAF41841.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41841.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41841.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41841.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2O3G} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 428-516. RA Tan K., Volkart L., Gu M., Joachimiak A.; RT "The crystal structure of a conserved putative domain from Neisseria RT meningitidis MC58."; RL Submitted (DEC-2006) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41841.1; -; Genomic_DNA. DR PIR; C81077; C81077. DR RefSeq; NP_274493.1; NC_003112.2. DR RefSeq; WP_002244180.1; NC_003112.2. DR PDB; 2O3G; X-ray; 2.55 A; A=428-516. DR PDBsum; 2O3G; -. DR ProteinModelPortal; Q9JYP7; -. DR SMR; Q9JYP7; 441-516. DR STRING; 122586.NMB1485; -. DR PaxDb; Q9JYP7; -. DR EnsemblBacteria; AAF41841; AAF41841; NMB1485. DR GeneID; 903907; -. DR KEGG; nme:NMB1485; -. DR PATRIC; 20358736; VBINeiMen85645_1877. DR eggNOG; ENOG4105EE5; Bacteria. DR eggNOG; COG0861; LUCA. DR eggNOG; COG1253; LUCA. DR HOGENOM; HOG000279402; -. DR OMA; MVMRLLL; -. DR OrthoDB; EOG6F297P; -. DR BioCyc; NMEN122586:GHGG-1525-MONOMER; -. DR EvolutionaryTrace; Q9JYP7; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005496; Integral_membrane_TerC. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 1. DR Pfam; PF03471; CorC_HlyC; 1. DR Pfam; PF03741; TerC; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2O3G}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00460213, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00460213, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00460213, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 304 366 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 369 425 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 518 AA; 57342 MW; CFD9324DA672DC96 CRC64; MDFSWLAEPH TWIGFATLLV LEVVLGIDNL VFVAILANKV QPARRDRARI IGLGLAVVIR IIMLAFMAHI ITLTEPLFQI GGLAVSGKDM IMLAGGIFLL YKATTELHER LEGHNRFTVA DSQKKHAPFW GVVAQILILD AVFSIDSVIT AVAMVDHIVV AMGAVVVAMA VMISASKLLT EFVDRHPTVV MLCLGFLLMI GFSLIAEAFH FHIPKGYLYA AIGFSILIEL FNQISQRNSR KNDYIGSSWR KRTAENVLGM MGIRESVLAD AGGESGDDAH FEENEKSMIR SVLTLAERPI MGVMIPRRDI ERLDISQSRE EQCAQLQNTP YSRLLVVGKA GVDEPLGYIN KKDLLSQLLE TGGLDIQTAL RQPLVLPDST TALGAIELFR QSSADYALVV DEFGAVLGMV TMKDLLETIA GEFPEEFERE EEPAVQGNPD ESLTVEGALE YVELAPQLNL PQQEEDADFH TVAGLIMEEL QTIPDVGDFA DFHGWRFEVV EKEGQRIERV KITKLPEE // ID Q7DDR7_NEIMB Unreviewed; 703 AA. AC Q7DDR7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Putative TonB-dependent receptor {ECO:0000313|EMBL:AAF40744.1}; GN OrderedLocusNames=NMB0293 {ECO:0000313|EMBL:AAF40744.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40744.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40744.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40744.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU003357}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000256|RuleBase:RU003357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40744.1; -; Genomic_DNA. DR RefSeq; NP_273347.1; NC_003112.2. DR RefSeq; WP_002256351.1; NC_003112.2. DR ProteinModelPortal; Q7DDR7; -. DR STRING; 122586.NMB0293; -. DR PaxDb; Q7DDR7; -. DR EnsemblBacteria; AAF40744; AAF40744; NMB0293. DR GeneID; 902404; -. DR KEGG; nme:NMB0293; -. DR PATRIC; 20355688; VBINeiMen85645_0368. DR eggNOG; ENOG4105E0K; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000130432; -. DR KO; K02014; -. DR OMA; YNSRNKE; -. DR OrthoDB; EOG6DJXWN; -. DR BioCyc; NMEN122586:GHGG-308-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Receptor {ECO:0000313|EMBL:AAF40744.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 703 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004288408. FT DOMAIN 69 164 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 462 702 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 703 AA; 78861 MW; 392CD05997AAF2FA CRC64; MKISFHLALL PTLIIASFPV AAADTQDNGE HYTATLPTVS VVGQSDTSVL KGYINYDEAA VTRNGQLIKE TPQTIDTLNI QKNKNYGTND LSSILEGNAG IDAAYDMRGE SIFLRGFQAD ASDIYRDGVR ESGQVRRSTA NIERVEILKG PSSVLYGRTN GGGVINMVSK YANFKQSRNI GAVYGSWANR SLNMDINEVL NKNVAIRLTG EVGRANSFRS GIDSKNVMVS PSITVKLDNG LKWTGQYTYD NVERTPDRSP TKSVYDRFGL PYRMGFAHRN DFVKDKLQVW RSDLEYAFND KWRAQWQLAH RTAAQDFDHF YAGSENGNLI KRNYAWQQTD NKTLSSNLTL NGDYTIGRFE NHLTVGMDYS REHRNPTLGF SSAFSASINP YDRASWPASG RLQPILTQNR HKADSYGIFV QNIFSATPDL KFVLGGRYDK YTFNSENKLT GSSRQYSGHS FSPNIGAVWN INPVHTLYAS YNKGFAPYGG RGGYLSIDTL SSAVFNADPE YTRQYETGVK SSWLDDRLST TLSAYQIERF NIRYRPDPKN NPYIYAVSGK HRSRGVELSA IGQIIPKKLY LRGSLGVMQA KVVEDKENPD RVGIHLNNTS NVTGNLFFRY TPTENLYGEI GVTGTGKRYG YNSRNKEVTT LPGFARVDAM LGWNHKNVNV TFAAANLLNQ KYWRSDSMPG NPRGYTARVN YRF // ID Q4W560_NEIMB Unreviewed; 47 AA. AC Q4W560; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=DNA adenine methylase, truncation {ECO:0000313|EMBL:AAY52162.1}; GN OrderedLocusNames=NMB1895 {ECO:0000313|EMBL:AAY52162.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52162.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52162.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52162.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52162.1; -; Genomic_DNA. DR STRING; 122586.NMB1895; -. DR PaxDb; Q4W560; -. DR EnsemblBacteria; AAY52162; AAY52162; NMB1895. DR PATRIC; 20359827; VBINeiMen85645_2418. DR eggNOG; COG0338; LUCA. DR HOGENOM; HOG000027863; -. DR OrthoDB; EOG6CS08V; -. DR BioCyc; NMEN122586:GHGG-1952-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAY52162.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAY52162.1}. SQ SEQUENCE 47 AA; 5213 MW; 32268F597EDB23A0 CRC64; MISNHDTEFT RDIYSSAILK TVEVQRNIAA KGSSSRKKVG ELLAIYA // ID Q9K0S3_NEIMB Unreviewed; 94 AA. AC Q9K0S3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40937.1}; GN OrderedLocusNames=NMB0505 {ECO:0000313|EMBL:AAF40937.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40937.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40937.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40937.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40937.1; -; Genomic_DNA. DR PIR; H81190; H81190. DR STRING; 122586.NMB0505; -. DR PaxDb; Q9K0S3; -. DR EnsemblBacteria; AAF40937; AAF40937; NMB0505. DR BioCyc; NMEN122586:GHGG-530-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 94 AA; 10054 MW; 327890B8A2D42E02 CRC64; MLLPRPACFC HRVDLLLLTV SVWMLLLIPS RIILASARAC SPTPARMVAP PSVVSNCVPC SLVSQPDCRL ADSATTLEGS AVFMTWVVVS CALL // ID Q7DD97_NEIMB Unreviewed; 155 AA. AC Q7DD97; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Sigma-54 dependent response regulator {ECO:0000313|EMBL:AAF41959.1}; GN OrderedLocusNames=NMB1607 {ECO:0000313|EMBL:AAF41959.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41959.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41959.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41959.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41959.1; -; Genomic_DNA. DR PIR; A81065; A81065. DR RefSeq; NP_274613.1; NC_003112.2. DR RefSeq; WP_002212784.1; NC_003112.2. DR ProteinModelPortal; Q7DD97; -. DR STRING; 122586.NMB1607; -. DR PaxDb; Q7DD97; -. DR EnsemblBacteria; AAF41959; AAF41959; NMB1607. DR GeneID; 904304; -. DR KEGG; nme:NMB1607; -. DR PATRIC; 20359094; VBINeiMen85645_2059. DR eggNOG; COG2204; LUCA. DR HOGENOM; HOG000219044; -. DR OMA; IRSAHEH; -. DR OrthoDB; EOG67Q9BH; -. DR BioCyc; NMEN122586:GHGG-1655-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF02954; HTH_8; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR01590; HTHFIS. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 121 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. SQ SEQUENCE 155 AA; 17512 MW; 50CA9704516D48A6 CRC64; MTELQHPVLV VDDETDILDL MEMTLMKMGL RVHTASGVAE AKNKLDSQRY SLVLTDMRMP DGSGLEVVQH INSRLLDTPV AVITAFGNAD QAQEALRCGA FDPDTMQIQD YLDQIERDII EQTLKQTEGN RTQAAKRLGI SFRSMRYRME RLNIG // ID Q9JYC9_NEIMB Unreviewed; 208 AA. AC Q9JYC9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Putative hemolysin {ECO:0000313|EMBL:AAF41995.1}; GN OrderedLocusNames=NMB1646 {ECO:0000313|EMBL:AAF41995.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41995.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41995.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41995.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41995.1; -; Genomic_DNA. DR PIR; E81058; E81058. DR RefSeq; NP_274651.1; NC_003112.2. DR RefSeq; WP_002216724.1; NC_003112.2. DR STRING; 122586.NMB1646; -. DR PaxDb; Q9JYC9; -. DR EnsemblBacteria; AAF41995; AAF41995; NMB1646. DR GeneID; 903470; -. DR KEGG; nme:NMB1646; -. DR PATRIC; 20359212; VBINeiMen85645_2118. DR eggNOG; ENOG4108UT2; Bacteria. DR eggNOG; COG1272; LUCA. DR HOGENOM; HOG000039438; -. DR KO; K11068; -. DR OMA; MSHEKPL; -. DR OrthoDB; EOG6QG8NQ; -. DR BioCyc; NMEN122586:GHGG-1695-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019835; P:cytolysis; IEA:InterPro. DR InterPro; IPR004254; AdipoR/HlyIII-related. DR InterPro; IPR005744; Hy-lIII. DR PANTHER; PTHR20855; PTHR20855; 1. DR PANTHER; PTHR20855:SF3; PTHR20855:SF3; 1. DR Pfam; PF03006; HlyIII; 1. DR TIGRFAMs; TIGR01065; hlyIII; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 101 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 207 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 208 AA; 22629 MW; 8B096A4A9BAB12B0 CRC64; MYTGERFNTY SHLSGLILAA AGLALMLLKT IGHGDGYRIF SVSVYGISLL LLYLSSSLYH GIAAGKLKSI LKKTDHCMIY VLIAGSYTPF ALVSLRNGPG WTVFSLSWLL AAAGIAQELT IGRKSEKRLL SIVIYVVMGW MVLAVMKSLT ASLPSAGLAW LAAGGMLYSV GIYWFVNDEK IRHGHGIWHL FVLGGSITQF VSVYGYVI // ID Q9K1P0_NEIMB Unreviewed; 333 AA. AC Q9K1P0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=ABC transporter, periplasmic solute-binding protein {ECO:0000313|EMBL:AAF40512.1}; GN OrderedLocusNames=NMB0041 {ECO:0000313|EMBL:AAF40512.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40512.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40512.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40512.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40512.1; -; Genomic_DNA. DR PIR; C81245; C81245. DR RefSeq; NP_273107.1; NC_003112.2. DR RefSeq; WP_002243927.1; NC_003112.2. DR ProteinModelPortal; Q9K1P0; -. DR STRING; 122586.NMB0041; -. DR PaxDb; Q9K1P0; -. DR EnsemblBacteria; AAF40512; AAF40512; NMB0041. DR GeneID; 902144; -. DR KEGG; nme:NMB0041; -. DR PATRIC; 20355039; VBINeiMen85645_0056. DR eggNOG; ENOG4105DP9; Bacteria. DR eggNOG; COG4143; LUCA. DR HOGENOM; HOG000272498; -. DR KO; K02064; -. DR OMA; DICVNYD; -. DR OrthoDB; EOG6D8BCG; -. DR BioCyc; NMEN122586:GHGG-42-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0030975; F:thiamine binding; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0015888; P:thiamine transport; IEA:InterPro. DR InterPro; IPR005948; Thi_ABC_peri-bd. DR TIGRFAMs; TIGR01254; sfuA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 333 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327791. SQ SEQUENCE 333 AA; 36472 MW; 8B989AB5F4549FC7 CRC64; MKRKIWLLPL LAVSAYLQAQ TEVRLAVHKS FSLPKGLIAR FERANDAKVS IIQAGGANEM LNKLILSRAN PIADAVYGLD NANIGKAREM GILAAAQPES APVAVGLPSA LAVDYGYVSI NYDKKWFEGK KLPLPQTLQD LTRPEYKNLL VVPSPATSSP GLGFLMANIS GLGEESAFKW WAQMRQNGVK VAKGWSEAYY TDFSHNGGAY PLVVGYAASP AAEVYFSKGK YSEPPTGNLF LKGGVFRQVE GAAVLKGAKQ PELAAKLVQW LQSREVQQAV PSEMWVYPAV KNTRLPDVFR FAQAPTHTTA PAQRDIDANQ RGWVSRWIRT VLK // ID Q9JX99_NEIMB Unreviewed; 249 AA. AC Q9JX99; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Electron transfer flavoprotein, beta subunit {ECO:0000313|EMBL:AAF42463.1}; GN Name=etfB {ECO:0000313|EMBL:AAF42463.1}; GN OrderedLocusNames=NMB2155 {ECO:0000313|EMBL:AAF42463.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42463.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42463.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42463.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42463.1; -; Genomic_DNA. DR PIR; A81001; A81001. DR RefSeq; NP_275140.1; NC_003112.2. DR RefSeq; WP_002218263.1; NC_003112.2. DR ProteinModelPortal; Q9JX99; -. DR SMR; Q9JX99; 1-242. DR STRING; 122586.NMB2155; -. DR PaxDb; Q9JX99; -. DR EnsemblBacteria; AAF42463; AAF42463; NMB2155. DR GeneID; 903217; -. DR KEGG; nme:NMB2155; -. DR PATRIC; 20360506; VBINeiMen85645_2749. DR eggNOG; ENOG4105BZJ; Bacteria. DR eggNOG; COG2086; LUCA. DR HOGENOM; HOG000247877; -. DR KO; K03521; -. DR OMA; KGQDKAY; -. DR OrthoDB; EOG65TRQZ; -. DR BioCyc; NMEN122586:GHGG-2220-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS. DR InterPro; IPR014730; ETF_a/b_N. DR InterPro; IPR012255; ETF_b. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21294; PTHR21294; 1. DR Pfam; PF01012; ETF; 1. DR PIRSF; PIRSF000090; Beta-ETF; 1. DR SMART; SM00893; ETF; 1. DR PROSITE; PS01065; ETF_BETA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 23 211 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 249 AA; 26947 MW; EC57EE5F35B65CE8 CRC64; MKALVAVKRV VDYNVKVRVK ADGSDVDIGN VKMSMNPFDE IAVEEAVRLK EAGKVSEIVA VSLGEKKCEE TLRTALAMGA DRAIHVETDT KLESLAVAKL LKAVADKENP QIFFLGKQAI DDDANQVAQM LAALLNAAQG TFASKVQIEG DEVQIVREID GGEETIALKL PAVISADLRL NEPRFVKLPN IMAAKKKPLE KLTPDDLVAD ISPRLKTVKF AEPKARQAGV KVASVAELVE KLKNEAKVI // ID Q7DDH8_NEIMB Unreviewed; 222 AA. AC Q7DDH8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Putative baseplate assembly protein V {ECO:0000313|EMBL:AAF41502.1}; GN OrderedLocusNames=NMB1111 {ECO:0000313|EMBL:AAF41502.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41502.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41502.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41502.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41502.1; -; Genomic_DNA. DR PIR; D81122; D81122. DR RefSeq; NP_274142.1; NC_003112.2. DR RefSeq; WP_002217230.1; NC_003112.2. DR STRING; 122586.NMB1111; -. DR PaxDb; Q7DDH8; -. DR EnsemblBacteria; AAF41502; AAF41502; NMB1111. DR GeneID; 903533; -. DR KEGG; nme:NMB1111; -. DR PATRIC; 20357788; VBINeiMen85645_1410. DR eggNOG; ENOG4108X7Q; Bacteria. DR eggNOG; COG4384; LUCA. DR HOGENOM; HOG000123669; -. DR OMA; TEHGAYR; -. DR OrthoDB; EOG651SVZ; -. DR BioCyc; NMEN122586:GHGG-1147-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR013046; GpV/Gp45. DR InterPro; IPR014462; Phage_Mu_Gp45. DR Pfam; PF06890; Phage_Mu_Gp45; 1. DR PIRSF; PIRSF012337; gp45; 1. DR TIGRFAMs; TIGR01644; phage_P2_V; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 222 AA; 23251 MW; E0AFE240175C90DF CRC64; MSLSKLAKKT AQTAKNIGET LRAAFRGKIT LVVSSEPIQR VQLSGLADET LQDLEHLQEY GFASHPPDGS EAVVIPLGGN TSHGVIVCSQ HGSYRIKNLK PGETAIFNHE GAKIVIKQGK IIEADCDVYR VNCKQYEVNA ATDAKFNAPL VETSAVLTAQ GQINGNGGMA VEGGDGATFS GDVNQTGGSF NTDGDVVAGN ISLRQHPHTD SIGGKTLPAE PA // ID Q9K0G0_NEIMB Unreviewed; 95 AA. AC Q9K0G0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Ribonuclease inhibitor barstar {ECO:0000313|EMBL:AAF41067.1}; GN OrderedLocusNames=NMB0646 {ECO:0000313|EMBL:AAF41067.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41067.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41067.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41067.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41067.1; -; Genomic_DNA. DR PIR; A81176; A81176. DR RefSeq; NP_273688.1; NC_003112.2. DR RefSeq; WP_002217738.1; NC_003112.2. DR ProteinModelPortal; Q9K0G0; -. DR STRING; 122586.NMB0646; -. DR PaxDb; Q9K0G0; -. DR EnsemblBacteria; AAF41067; AAF41067; NMB0646. DR GeneID; 902758; -. DR KEGG; nme:NMB0646; -. DR PATRIC; 20356591; VBINeiMen85645_0814. DR eggNOG; ENOG41063PQ; Bacteria. DR eggNOG; COG2732; LUCA. DR HOGENOM; HOG000125272; -. DR KO; K03623; -. DR OMA; CDITIIL; -. DR OrthoDB; EOG6KWZ46; -. DR BioCyc; NMEN122586:GHGG-673-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.370.10; -; 1. DR InterPro; IPR000468; Barstar. DR Pfam; PF01337; Barstar; 1. DR SUPFAM; SSF52038; SSF52038; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 83 Barstar. {ECO:0000259|Pfam:PF01337}. SQ SEQUENCE 95 AA; 11385 MW; D79ABA9C84DD77B3 CRC64; MQLEIIGSKI YTEQDFHNQI SKIFSIQDYY GNNLDALWDL LSTNVERPIT LVWKDAMFSK NQLENIFIEI VNVLERVKKQ DEDYGFEEKF NYILE // ID Q7DDR0_NEIMB Unreviewed; 288 AA. AC Q7DDR0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE RecName: Full=Peptidylprolyl isomerase {ECO:0000256|RuleBase:RU363014, ECO:0000256|SAAS:SAAS00523066}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014, ECO:0000256|SAAS:SAAS00523066}; GN OrderedLocusNames=NMB0345 {ECO:0000313|EMBL:AAF40788.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40788.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40788.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40788.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363014, CC ECO:0000256|SAAS:SAAS00523013}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40788.1; -; Genomic_DNA. DR PIR; G81209; G81209. DR RefSeq; NP_273394.1; NC_003112.2. DR RefSeq; WP_002212350.1; NC_003112.2. DR ProteinModelPortal; Q7DDR0; -. DR STRING; 122586.NMB0345; -. DR PaxDb; Q7DDR0; -. DR EnsemblBacteria; AAF40788; AAF40788; NMB0345. DR GeneID; 902460; -. DR KEGG; nme:NMB0345; -. DR PATRIC; 20355837; VBINeiMen85645_0437. DR eggNOG; COG0760; LUCA. DR HOGENOM; HOG000219115; -. DR OMA; MGDQNWQ; -. DR OrthoDB; EOG62G5KP; -. DR BioCyc; NMEN122586:GHGG-366-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF13145; Rotamase_2; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Rotamase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Signal {ECO:0000256|RuleBase:RU363014}. FT SIGNAL 1 20 {ECO:0000256|RuleBase:RU363014}. FT CHAIN 21 288 Peptidylprolyl isomerase. FT {ECO:0000256|RuleBase:RU363014}. FT /FTId=PRO_5006529245. FT DOMAIN 152 246 PpiC. {ECO:0000259|PROSITE:PS50198}. SQ SEQUENCE 288 AA; 31455 MW; 535D61C427416805 CRC64; MKAKILTSVA LLACSGSLFA QTLATVNGQK IDSSVIDAQV AAFRAENSRA EDTPQLRQSL LENEVVNTVV AQEVKRLKLD RSAEFKNALA KLRAEAKKSG DDKKPSFKTV WQAVKYGLNG EAYALHIAKT QPVSEQEVKA AYDNISGFYK GTQEVQLGEI LTDKEENAKK AVADLKAKKG FDAVLKQYSL NDRTKQTGAP VGYVPLKDLE QGVPPLYQAI KDLKKGEFTA TPLKNGDFYG VYYVNDSREV KVPSFDEMKG QIAGNLQAER IDRAVGALLG KANIKPAK // ID Q7DDK2_NEIMB Unreviewed; 235 AA. AC Q7DDK2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237}; GN Name=sdhB {ECO:0000313|EMBL:AAF41357.1}; GN OrderedLocusNames=NMB0951 {ECO:0000313|EMBL:AAF41357.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41357.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41357.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41357.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC {ECO:0000256|RuleBase:RU361237}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|RuleBase:RU361237}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237}; CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. CC {ECO:0000256|RuleBase:RU361237}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000256|RuleBase:RU361237}. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000256|RuleBase:RU361237}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41357.1; -; Genomic_DNA. DR PIR; G81138; G81138. DR RefSeq; NP_273989.1; NC_003112.2. DR RefSeq; WP_002221124.1; NC_003112.2. DR ProteinModelPortal; Q7DDK2; -. DR SMR; Q7DDK2; 3-233. DR STRING; 122586.NMB0951; -. DR PaxDb; Q7DDK2; -. DR EnsemblBacteria; AAF41357; AAF41357; NMB0951. DR GeneID; 903071; -. DR KEGG; nme:NMB0951; -. DR PATRIC; 20357385; VBINeiMen85645_1207. DR eggNOG; ENOG4105E33; Bacteria. DR eggNOG; COG0479; LUCA. DR HOGENOM; HOG000160590; -. DR KO; K00240; -. DR OMA; DGQYFGP; -. DR OrthoDB; EOG6CK7MG; -. DR BioCyc; NMEN122586:GHGG-988-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR Pfam; PF13085; Fer2_3; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|RuleBase:RU361237}; KW 3Fe-4S {ECO:0000256|RuleBase:RU361237}; KW 4Fe-4S {ECO:0000256|RuleBase:RU361237}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU361237}; KW Iron-sulfur {ECO:0000256|RuleBase:RU361237}; KW Metal-binding {ECO:0000256|RuleBase:RU361237}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41357.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 13 94 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 136 166 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 235 AA; 27086 MW; 810C95825FF8090F CRC64; MEKMSFEIYR YNPDVDAKPY MQRYELELEP TDVKLLDALV RLKAQDDTLS FRRSCREGIC GSDGMNINGK NGLACLTDLR GLKQPVKIRP LPGLPVIRDL IVDMTQFFKQ YHSVKPYVVN DNPIDADKER LQTQEERKEL DGLYECILCA CCSTACPSFW WNPDKFVGPS GLLNAYRFIA DSRDTITNER LDNLNDPYRL FRCHTIMNCV DVCPKHLNPT RAIGKIKEIM LKRAV // ID Q9JXY1_NEIMB Unreviewed; 143 AA. AC Q9JXY1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42175.1}; GN OrderedLocusNames=NMB1840 {ECO:0000313|EMBL:AAF42175.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42175.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42175.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42175.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42175.1; -; Genomic_DNA. DR PIR; H81035; H81035. DR RefSeq; NP_274837.1; NC_003112.2. DR RefSeq; WP_002217944.1; NC_003112.2. DR STRING; 122586.NMB1840; -. DR PaxDb; Q9JXY1; -. DR EnsemblBacteria; AAF42175; AAF42175; NMB1840. DR GeneID; 903259; -. DR KEGG; nme:NMB1840; -. DR PATRIC; 20359687; VBINeiMen85645_2349. DR eggNOG; ENOG4108VHV; Bacteria. DR eggNOG; COG2510; LUCA. DR HOGENOM; HOG000083000; -. DR KO; K08978; -. DR OMA; WICYFRA; -. DR OrthoDB; EOG6358JF; -. DR BioCyc; NMEN122586:GHGG-1895-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 117 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 141 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 140 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 143 AA; 15404 MW; 1F7A8B16FE8BE92B CRC64; MGSNAWLFWA LASAGFASLT AIFAKMGLQG IDSDFATFIR TLVILAALLL FLTYTGKWQG VNGFTGRNWT FLILSGLATG ASWLAYFKAL QLGNASQVAP IDKFSLVLVA LMAVVFLDER PNTQEWIGLG LVTAGVLVLA LKR // ID Q9K0V8_NEIMB Unreviewed; 74 AA. AC Q9K0V8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40886.1}; GN OrderedLocusNames=NMB0449 {ECO:0000313|EMBL:AAF40886.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40886.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40886.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40886.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40886.1; -; Genomic_DNA. DR PIR; C81197; C81197. DR STRING; 122586.NMB0449; -. DR PaxDb; Q9K0V8; -. DR EnsemblBacteria; AAF40886; AAF40886; NMB0449. DR PATRIC; 20356112; VBINeiMen85645_0572. DR BioCyc; NMEN122586:GHGG-473-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 74 AA; 8574 MW; E5CFE6A53F348AEE CRC64; MNQKYILSAN NNSLIEEIHN TVQSIGYCIV RGLNLNHLDG SRRNKKLFDF LSQLGMLTNH KGDGFKSIFW DIKY // ID Q9JYL9_NEIMB Unreviewed; 173 AA. AC Q9JYL9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41876.1}; GN OrderedLocusNames=NMB1520 {ECO:0000313|EMBL:AAF41876.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41876.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41876.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41876.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41876.1; -; Genomic_DNA. DR PIR; G81074; G81074. DR STRING; 122586.NMB1520; -. DR PaxDb; Q9JYL9; -. DR EnsemblBacteria; AAF41876; AAF41876; NMB1520. DR BioCyc; NMEN122586:GHGG-1560-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 173 AA; 19062 MW; F785AADA660AC72E CRC64; MRVQSGLIFC TQADEFAQSG HVEIDIQTGA VALRRPQCFR QCLHHFVFGF QPAAFGAQGV VDCAYAVRLV YARLFLDGQM QRHMQEGVAF AVFGQPVGVQ MVFDAFEITV VFGMGFDNAE GFLFQCAQLQ RIEPLLPHAG EKAADIVGID IVHGGFDKMF MEIGSDNGGF YIN // ID Q9JZX7_NEIMB Unreviewed; 155 AA. AC Q9JZX7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41267.1}; GN OrderedLocusNames=NMB0856 {ECO:0000313|EMBL:AAF41267.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41267.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41267.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41267.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41267.1; -; Genomic_DNA. DR PIR; C81150; C81150. DR RefSeq; NP_273897.1; NC_003112.2. DR RefSeq; WP_010980861.1; NC_003112.2. DR STRING; 122586.NMB0856; -. DR PaxDb; Q9JZX7; -. DR EnsemblBacteria; AAF41267; AAF41267; NMB0856. DR GeneID; 902970; -. DR KEGG; nme:NMB0856; -. DR PATRIC; 20357105; VBINeiMen85645_1071. DR HOGENOM; HOG000218876; -. DR OMA; MQINNIS; -. DR OrthoDB; EOG6QCD90; -. DR BioCyc; NMEN122586:GHGG-887-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 155 AA; 18574 MW; B0D7C140F404C54C CRC64; MQIDNISDEQ VVIVRMSCYL KKDEIFKNIE RYGYQSSDIK KISPPFPLNI LPVPKPYYFY LYDTHLNQIY DLAWSCNDFL MFEIFILDRE SIKYIDKDKL FKSRETLYSN FKSIKNQCKN YFFCGFDFDA PYFKSGVSQV ADYNFVPDAF SLFFI // ID Q9K0U6_NEIMB Unreviewed; 233 AA. AC Q9K0U6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40902.1}; GN OrderedLocusNames=NMB0465 {ECO:0000313|EMBL:AAF40902.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40902.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40902.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40902.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40902.1; -; Genomic_DNA. DR PIR; F81195; F81195. DR RefSeq; NP_273512.1; NC_003112.2. DR RefSeq; WP_002224946.1; NC_003112.2. DR STRING; 122586.NMB0465; -. DR PaxDb; Q9K0U6; -. DR EnsemblBacteria; AAF40902; AAF40902; NMB0465. DR GeneID; 902581; -. DR KEGG; nme:NMB0465; -. DR PATRIC; 20356178; VBINeiMen85645_0610. DR eggNOG; ENOG4107N3Y; Bacteria. DR eggNOG; COG2928; LUCA. DR HOGENOM; HOG000264416; -. DR OMA; GTMDQSL; -. DR OrthoDB; EOG61308T; -. DR BioCyc; NMEN122586:GHGG-489-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007462; DUF502. DR Pfam; PF04367; DUF502; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 84 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 233 AA; 25100 MW; A2278F306FCB0464 CRC64; MTEPAAEGGK AAKALKKYLI TGILVWLPIA VTVWVVSYIV SASDQLVNLL PKQWRPQYVL GFNIPGLGVI VAIAVLFVTG LFAANVLGRQ ILAAWDSLLG RIPVVKSIYS SVKKVSESLL SDSSRSFKTP VLVPFPQPGI WTIAFVSGQV SNAVKAALPK DGDYLSVYVP TTPNPTGGYY IMVKKSDVRE LDMSVDEALK YVISLGMVIP DDLPVKTLAG PMPSEKADLP EQQ // ID Q9K1E5_NEIMB Unreviewed; 461 AA. AC Q9K1E5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=L-serine dehydratase {ECO:0000313|EMBL:AAF40667.1}; DE EC=4.3.1.17 {ECO:0000313|EMBL:AAF40667.1}; GN Name=sdaA {ECO:0000313|EMBL:AAF40667.1}; GN OrderedLocusNames=NMB0211 {ECO:0000313|EMBL:AAF40667.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40667.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40667.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40667.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40667.1; -; Genomic_DNA. DR PIR; C81225; C81225. DR RefSeq; NP_273268.1; NC_003112.2. DR RefSeq; WP_002243959.1; NC_003112.2. DR ProteinModelPortal; Q9K1E5; -. DR STRING; 122586.NMB0211; -. DR PaxDb; Q9K1E5; -. DR EnsemblBacteria; AAF40667; AAF40667; NMB0211. DR GeneID; 902323; -. DR KEGG; nme:NMB0211; -. DR PATRIC; 20355476; VBINeiMen85645_0262. DR eggNOG; ENOG4105EJQ; Bacteria. DR eggNOG; COG1760; LUCA. DR HOGENOM; HOG000036732; -. DR KO; K01752; -. DR OMA; LENELTW; -. DR OrthoDB; EOG64V2GZ; -. DR BioCyc; NMEN122586:GHGG-226-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro. DR Gene3D; 3.30.1330.90; -; 1. DR InterPro; IPR029009; ASB_dom. DR InterPro; IPR004644; Fe-S_L-Ser_mono. DR InterPro; IPR005130; Ser_deHydtase-like_asu. DR InterPro; IPR005131; Ser_deHydtase_bsu. DR Pfam; PF03313; SDH_alpha; 1. DR Pfam; PF03315; SDH_beta; 1. DR SUPFAM; SSF143548; SSF143548; 1. DR TIGRFAMs; TIGR00720; sda_mono; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF40667.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 150 SDH_beta. {ECO:0000259|Pfam:PF03315}. FT DOMAIN 180 444 SDH_alpha. {ECO:0000259|Pfam:PF03313}. SQ SEQUENCE 461 AA; 49159 MW; CB1CBB08803E7DB1 CRC64; MISIFDIFKI GIGPSSSHTV GPMKAAAAFA AGLDAQAVRI VIDIYGSLAL TGYGHGTFDA LMLGLEGSLP HDIPLAGIPE RLERIRTQHI LRLNGQEIRF IPDRDLNILG NQVLPKHPNS LRFTAYASDG TVLNEQVYYS VGGGFVVTEE DFDRQAETEK AVPYPYTSCA ELLARCRLNR LDISEVVLAN EAALAGCGEA EIRRRAAAVA EVMEGCIKRG LGADGELPSG LNVRRRAPQL AAKLKVLRET EIVNTQLWPM VYAMAVNEEN AAGGRVVTAP TNGAAGIIPA VLHYFRKFNP HATQERVENF LLTAGAIGIL YKTNASISGA DVGCQGEVGV ACSMAAGAYA EVIGGTPKQV ENAAEMAMEH HLGLTCDPVG GLVQIPCIER NGIAAEKALK LGTLALLEDG TDKKVSLDEV IRTMLQTGRD MKATYKETSL AGLAATLRKK AVPVSVRVVE C // ID Q9JXN7_NEIMB Unreviewed; 553 AA. AC Q9JXN7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42283.1}; GN OrderedLocusNames=NMB1954 {ECO:0000313|EMBL:AAF42283.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42283.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42283.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42283.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42283.1; -; Genomic_DNA. DR PIR; C81024; C81024. DR RefSeq; NP_274948.1; NC_003112.2. DR RefSeq; WP_002225838.1; NC_003112.2. DR STRING; 122586.NMB1954; -. DR PaxDb; Q9JXN7; -. DR EnsemblBacteria; AAF42283; AAF42283; NMB1954. DR GeneID; 904196; -. DR KEGG; nme:NMB1954; -. DR PATRIC; 20359967; VBINeiMen85645_2488. DR eggNOG; COG1807; LUCA. DR HOGENOM; HOG000261088; -. DR OMA; LPYWLGA; -. DR OrthoDB; EOG6Z9B0S; -. DR BioCyc; NMEN122586:GHGG-2011-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 321 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 352 378 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 398 416 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 428 450 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 553 AA; 61323 MW; ABDA912D4554B36C CRC64; MLTYTPPDAR PPAKTHEKPW LLLLMAFAWL WPGVFSHDLW NPDEPAVYTA VEALAGSPTP LVAHLFGQTD FGIPPVYLWV AAAFKHLLSP WAADSYDAAR FAGVFFAVIG LTSCGFAGFN FLGRHHGRSV VLILIGCIGL IPVAHFLNPA AAAFAAAGLV LHGYSLARRR VIAASFLLGT GWTLMSLAAA YPAAFALMLP LPVLMFFRPW QSRRLMLTAV ASLAFALPLM TVYPLLLAKT QPALFAQWLD YHVFGTFGGV RHVQTAFSLF YYLKNLLWFA LPALPLAVWT VCRTRLFSTD WGILGVVWML AVLVLLAVNP QRFQDNLVWL LPPLALFGAA QLDSLRRGAA AFVNWFGIMA FGLFAVFLWT GFFAMNYGWP AKLAERAAYF SPYYVPDIDP IPMAVAVLFT PLWLWAITRK NIRGRQAVTN WAAGVTLTWA LLMTLFLPWL DAAKSHAPVV RSMEASLSPE LKRELSDGIE CIGIGGGDLH TRIVWTQYGT LPHRVGDVQC RYRIVLLPQN ADAPQGWQTV WQGARPRNKD SKFALIRKIG ENI // ID Q9JZC2_NEIMB Unreviewed; 95 AA. AC Q9JZC2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41508.1}; GN OrderedLocusNames=NMB1118 {ECO:0000313|EMBL:AAF41508.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41508.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41508.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41508.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41508.1; -; Genomic_DNA. DR PIR; H81119; H81119. DR RefSeq; NP_274148.1; NC_003112.2. DR RefSeq; WP_002213585.1; NC_003112.2. DR STRING; 122586.NMB1118; -. DR PaxDb; Q9JZC2; -. DR EnsemblBacteria; AAF41508; AAF41508; NMB1118. DR GeneID; 903540; -. DR KEGG; nme:NMB1118; -. DR PATRIC; 20357805; VBINeiMen85645_1418. DR eggNOG; ENOG4105ZTN; Bacteria. DR eggNOG; COG2929; LUCA. DR HOGENOM; HOG000218368; -. DR KO; K09803; -. DR OMA; HVLCFTP; -. DR OrthoDB; EOG6K13W7; -. DR BioCyc; NMEN122586:GHGG-1154-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007460; BrnT_toxin. DR Pfam; PF04365; BrnT_toxin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 95 AA; 11187 MW; 1621CBD310670872 CRC64; MKIEFDSEKN QRNIEERNLP FESVGQIRWT TAVIVPDVRF DYPEPRYVAA AYLGDTQRLH IVCFTPIKDG IRVISFRKAN KREVKKYATS ILNKR // ID Q9K180_NEIMB Unreviewed; 76 AA. AC Q9K180; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40740.1}; GN OrderedLocusNames=NMB0288 {ECO:0000313|EMBL:AAF40740.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40740.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40740.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40740.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40740.1; -; Genomic_DNA. DR PIR; H81214; H81214. DR STRING; 122586.NMB0288; -. DR PaxDb; Q9K180; -. DR EnsemblBacteria; AAF40740; AAF40740; NMB0288. DR HOGENOM; HOG000219124; -. DR OMA; GRRGNRM; -. DR OrthoDB; EOG6ZH2PT; -. DR BioCyc; NMEN122586:GHGG-303-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 76 AA; 7589 MW; 39EE6BFB188E1442 CRC64; MGGEVNRADV VGFLVAAFEI PVVALDCGYV AVPVVGRRGN RMRPLPCAAD DGLAAFFAGD GNGVGLGGGD LGIPDD // ID Q7DDR5_NEIMB Unreviewed; 81 AA. AC Q7DDR5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40757.1}; GN OrderedLocusNames=NMB0311 {ECO:0000313|EMBL:AAF40757.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40757.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40757.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40757.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40757.1; -; Genomic_DNA. DR PIR; F81213; F81213. DR RefSeq; NP_273361.1; NC_003112.2. DR RefSeq; WP_002212272.1; NC_003112.2. DR STRING; 122586.NMB0311; -. DR PaxDb; Q7DDR5; -. DR EnsemblBacteria; AAF40757; AAF40757; NMB0311. DR GeneID; 902427; -. DR KEGG; nme:NMB0311; -. DR PATRIC; 20355737; VBINeiMen85645_0388. DR HOGENOM; HOG000219119; -. DR OMA; IADYISH; -. DR OrthoDB; EOG6ND0N9; -. DR BioCyc; NMEN122586:GHGG-331-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 81 AA; 9574 MW; 3EE536247796DC5F CRC64; MLKSIELNSH IRNRLAEYLK GRGMDFQTAM QEEKGNKEIA AIVHSGLPTL VRKLYSEQKM QKFFWEKRDL IADYISRRMQ G // ID Q9JXZ8_NEIMB Unreviewed; 369 AA. AC Q9JXZ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769}; GN Name=ribD {ECO:0000313|EMBL:AAF42152.1}; GN OrderedLocusNames=NMB1817 {ECO:0000313|EMBL:AAF42152.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42152.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42152.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42152.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone CC 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- CC pyrimidinedione 5'-phosphate. {ECO:0000256|PIRNR:PIRNR006769}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 2/4. CC {ECO:0000256|PIRNR:PIRNR006769}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 3/4. CC {ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP CC reductase family. {ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and CC deoxycytidylate deaminase family. {ECO:0000256|PIRNR:PIRNR006769}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42152.1; -; Genomic_DNA. DR PIR; B81039; B81039. DR RefSeq; NP_274814.1; NC_003112.2. DR RefSeq; WP_002225654.1; NC_003112.2. DR ProteinModelPortal; Q9JXZ8; -. DR STRING; 122586.NMB1817; -. DR PaxDb; Q9JXZ8; -. DR EnsemblBacteria; AAF42152; AAF42152; NMB1817. DR GeneID; 903283; -. DR KEGG; nme:NMB1817; -. DR PATRIC; 20359619; VBINeiMen85645_2315. DR eggNOG; ENOG4105D1W; Bacteria. DR eggNOG; COG0117; LUCA. DR eggNOG; COG1985; LUCA. DR HOGENOM; HOG000257442; -. DR KO; K11752; -. DR OMA; YRAGEPH; -. DR OrthoDB; EOG66F07R; -. DR BioCyc; NMEN122586:GHGG-1872-MONOMER; -. DR UniPathway; UPA00275; UER00401. DR UniPathway; UPA00275; UER00402. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro. DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR004794; Eubact_RibD. DR InterPro; IPR011549; RibD_C. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF01872; RibD_C; 1. DR PIRSF; PIRSF006769; RibD; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00326; eubact_ribD; 1. DR TIGRFAMs; TIGR00227; ribD_Cterm; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000313|EMBL:AAF42152.1}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000256|PIRSR:PIRSR006769-3}; KW NADP {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000313|EMBL:AAF42152.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Riboflavin biosynthesis {ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}. FT DOMAIN 4 117 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. FT NP_BIND 299 305 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT ACT_SITE 55 55 Proton donor. FT {ECO:0000256|PIRSR:PIRSR006769-1}. FT METAL 53 53 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT METAL 78 78 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT METAL 87 87 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT BINDING 157 157 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR006769- FT 2}. FT BINDING 171 171 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 173 173 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 187 187 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 199 199 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 203 203 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 207 207 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 210 210 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 225 225 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 297 297 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. SQ SEQUENCE 369 AA; 40083 MW; D41F08D5B9C35EC8 CRC64; MFSDTDISMM ENALRLAALG RFSTSPNPRV GCVIAHGSQI VGQGFHVKAG EPHAEVHALR QAGEMAQGAT AFVTLEPCSH YGRTPPCAEA LVRAGVSRVV AAMRDPNPLV AGKGLALLEA AGIKTECGLL EHQARELNRG FLSRIERRRP FVRLKCAVSL DGKTALSDGS SFWITGEDAR ADVQVLRAES CAVLTGIGTV LADNPRLNVR AFPTLRQPAR IVLDSRLRLP PNSHLVTDGQ SPTYIATLER NEDRLHPYRE HAHVRILMPS ETADSKIDLH HLMRLLADEG FGEIMVEAGS ELTSAFLAEN LADEIVLYRS PKILGSGKDL FSLLENRAAL SAPPLWTPVS SEILGHNIKT VFRKNGNAF // ID Q9K025_NEIMB Unreviewed; 333 AA. AC Q9K025; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515}; DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515}; GN Name=hemB {ECO:0000313|EMBL:AAF41214.1}; GN OrderedLocusNames=NMB0801 {ECO:0000313|EMBL:AAF41214.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41214.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41214.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41214.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 CC H(2)O. {ECO:0000256|RuleBase:RU000515}. CC -!- SUBUNIT: Homooctamer. {ECO:0000256|RuleBase:RU000515}. CC -!- SIMILARITY: Belongs to the ALAD family. CC {ECO:0000256|RuleBase:RU004161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41214.1; -; Genomic_DNA. DR PIR; H81157; H81157. DR RefSeq; NP_273843.1; NC_003112.2. DR RefSeq; WP_002225417.1; NC_003112.2. DR ProteinModelPortal; Q9K025; -. DR SMR; Q9K025; 9-333. DR STRING; 122586.NMB0801; -. DR PaxDb; Q9K025; -. DR EnsemblBacteria; AAF41214; AAF41214; NMB0801. DR GeneID; 902916; -. DR KEGG; nme:NMB0801; -. DR PATRIC; 20356989; VBINeiMen85645_1013. DR eggNOG; ENOG4105D52; Bacteria. DR eggNOG; COG0113; LUCA. DR HOGENOM; HOG000020323; -. DR KO; K01698; -. DR OMA; MDPANSN; -. DR OrthoDB; EOG6VXFCB; -. DR BioCyc; NMEN122586:GHGG-832-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR001731; ALAD. DR InterPro; IPR030656; ALAD_AS. DR InterPro; IPR013785; Aldolase_TIM. DR PANTHER; PTHR11458; PTHR11458; 1. DR Pfam; PF00490; ALAD; 1. DR PIRSF; PIRSF001415; Porphbilin_synth; 1. DR PRINTS; PR00144; DALDHYDRTASE. DR SMART; SM01004; ALAD; 1. DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|RuleBase:RU000515, ECO:0000313|EMBL:AAF41214.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-5}; KW Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT ACT_SITE 202 202 Schiff-base intermediate with substrate. FT {ECO:0000256|PIRSR:PIRSR001415-1}. FT ACT_SITE 257 257 Schiff-base intermediate with substrate. FT {ECO:0000256|PIRSR:PIRSR001415-1}. FT METAL 242 242 Magnesium. FT {ECO:0000256|PIRSR:PIRSR001415-5}. SQ SEQUENCE 333 AA; 36830 MW; A88EF90C3F163F1D CRC64; MQFPYRNVPA SRMRRMRRDD FSRRLMREHT LTADDLIYPV FVLEGSAREE DVPSMPGVKR QSLDRLLFTA EEAVKLGIPM LALFPVVTAN KTERAQEAYN PEGLVPSTVR ALRERFPELG IMTDVALDPY TVHGQDGLTD ENGYVMNDET VEVLVKQALC HAEAGAQVVA PSDMMDGRIG AIREALEDAG HIHTRIMAYS AKYASAFYGP FRDAVGSSGN LGKADKKTYQ MDPANTDEAL HEVALDIQEG ADMVMVKPGL PYLDVVRRVK DEFGVPTYAY QVSGEYAMLQ AAIANGWLDG GKVVLESLLA FKRAGADGIL TYYAIEAAKM LKR // ID Q9JZL9_NEIMB Unreviewed; 363 AA. AC Q9JZL9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:AAF41397.1}; GN OrderedLocusNames=NMB0994 {ECO:0000313|EMBL:AAF41397.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41397.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41397.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41397.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41397.1; -; Genomic_DNA. DR PIR; A81134; A81134. DR RefSeq; NP_274030.1; NC_003112.2. DR RefSeq; WP_002222585.1; NC_003112.2. DR ProteinModelPortal; Q9JZL9; -. DR STRING; 122586.NMB0994; -. DR PaxDb; Q9JZL9; -. DR EnsemblBacteria; AAF41397; AAF41397; NMB0994. DR GeneID; 903120; -. DR KEGG; nme:NMB0994; -. DR PATRIC; 20357501; VBINeiMen85645_1267. DR eggNOG; ENOG4106N9T; Bacteria. DR eggNOG; ENOG410ZM68; LUCA. DR HOGENOM; HOG000102082; -. DR KO; K00257; -. DR OMA; YYTLFAR; -. DR OrthoDB; EOG6KMB49; -. DR BioCyc; NMEN122586:GHGG-1031-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF56645; SSF56645; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 110 Acyl-CoA_dh_N. FT {ECO:0000259|Pfam:PF02771}. SQ SEQUENCE 363 AA; 38926 MW; ED7914E0CB3D569C CRC64; MNAQTLIANV AEFVKTKLKP IVDDIDRKGY YPEAFMRELG AIGGFGAVGT EAEGGNGLGL ATQIAVLREI GKECGATSFS AWCQAACAWY LHQTPNRAVK DKYLADILQG KVLAGTGMSN TVKHLADIEK HNLQAERVEG GYTVNGALPW VSNIGEDHIW ANTAQIGDGY VMFITGGQWE GVSLQNCPEF CALEGTRTFS LNFKDVFIPD EDIIAAPEQF ADYIQSIKAG FILLQIGIGA GVIDGSLGII RLANVVNAEV NNYLNDGYDS LKTRLDGAWA ETERLAGLAW SGTPDNLATL KLREAAAVLA LAAAQSAALH SGAKGYLMRS PAQRRVREAM FVAIVTPAIK HLRKEIAAIE AAK // ID Q7DDI0_NEIMB Unreviewed; 112 AA. AC Q7DDI0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41481.1}; GN OrderedLocusNames=NMB1089 {ECO:0000313|EMBL:AAF41481.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41481.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41481.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41481.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41481.1; -; Genomic_DNA. DR PIR; C81123; C81123. DR RefSeq; NP_274121.1; NC_003112.2. DR RefSeq; WP_002222592.1; NC_003112.2. DR STRING; 122586.NMB1089; -. DR PaxDb; Q7DDI0; -. DR EnsemblBacteria; AAF41481; AAF41481; NMB1089. DR GeneID; 903506; -. DR KEGG; nme:NMB1089; -. DR PATRIC; 20357741; VBINeiMen85645_1387. DR HOGENOM; HOG000218912; -. DR OMA; PFVIHIS; -. DR OrthoDB; EOG6SZ1KD; -. DR BioCyc; NMEN122586:GHGG-1125-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 112 AA; 12875 MW; 0BA31101D2086673 CRC64; MTYRELVERQ LAVRHADLEL GLSRAREQEP FVIHVSDLLD KAGIEYAVRM DKDFQTTFHL EYPITNYDTF KRAVWQTLGA YYCVCNDGDG LEIASNRPDG YAVRIVFGDV PV // ID Q9JYL7_NEIMB Unreviewed; 98 AA. AC Q9JYL7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41879.1}; GN OrderedLocusNames=NMB1523 {ECO:0000313|EMBL:AAF41879.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41879.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41879.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41879.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41879.1; -; Genomic_DNA. DR PIR; H81072; H81072. DR RefSeq; NP_274531.1; NC_003112.2. DR RefSeq; WP_002244194.1; NC_003112.2. DR STRING; 122586.NMB1523; -. DR PaxDb; Q9JYL7; -. DR EnsemblBacteria; AAF41879; AAF41879; NMB1523. DR GeneID; 904013; -. DR KEGG; nme:NMB1523; -. DR PATRIC; 20358844; VBINeiMen85645_1932. DR BioCyc; NMEN122586:GHGG-1563-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 98 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327713. SQ SEQUENCE 98 AA; 8958 MW; 060C9FD73764141E CRC64; MKKSLFAAAL LSLVLAACGG EKAAEAPAAE APAAEAPATE APAAEAPAAE APAAEAPAAE AAATEAPAAE AAATEAPAAE AAATEAPAAE APAAEAAK // ID Q9K0C2_NEIMB Unreviewed; 332 AA. AC Q9K0C2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Tpc protein {ECO:0000313|EMBL:AAF41109.1}; GN Name=tpc {ECO:0000313|EMBL:AAF41109.1}; GN OrderedLocusNames=NMB0692 {ECO:0000313|EMBL:AAF41109.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41109.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41109.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41109.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41109.1; -; Genomic_DNA. DR PIR; B81170; B81170. DR RefSeq; NP_273734.1; NC_003112.2. DR RefSeq; WP_002219588.1; NC_003112.2. DR STRING; 122586.NMB0692; -. DR PaxDb; Q9K0C2; -. DR EnsemblBacteria; AAF41109; AAF41109; NMB0692. DR GeneID; 902804; -. DR KEGG; nme:NMB0692; -. DR PATRIC; 20356713; VBINeiMen85645_0878. DR HOGENOM; HOG000218843; -. DR OMA; NTKSDET; -. DR OrthoDB; EOG6ZPSZ5; -. DR BioCyc; NMEN122586:GHGG-720-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR Gene3D; 3.30.70.1070; -; 1. DR InterPro; IPR011930; FtsN. DR InterPro; IPR007730; SPOR_dom. DR Pfam; PF05036; SPOR; 1. DR SUPFAM; SSF110997; SSF110997; 1. DR TIGRFAMs; TIGR02223; ftsN; 1. DR PROSITE; PS51724; SPOR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 39 {ECO:0000256|SAM:SignalP}. FT CHAIN 40 332 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328361. FT DOMAIN 254 332 SPOR. {ECO:0000259|PROSITE:PS51724}. SQ SEQUENCE 332 AA; 35535 MW; 11E99B488AAF0EF2 CRC64; MSENKQNEVL SGYEQLKRRN RRRLVTASCL VAASCILLAA ALSSGPAEQT AGETSGVENK AAGAAQTPAL KSAADKPQDL AGEDKPSAAD SEISEPENVG APLVLINERL EDSNIKGLEA SEKLQQAETA KTAPKQAKQR AAEKVPATAD STDTVAVEKP KRTAETKPQK AERTAKAKPK AKETKTAEKV ADKPKTAAEK TKPDTAKSDS AVKEAKKADK AESKKTAEKD RSDGKKHETA QKTDKADKTK TAEKEKSGKK AAIQAGYAEK ERALSLQRKM KAAGIDSTIT EIMTDNGKVY RVKSSNYKNA RDAERDLNKL RVHGIAGQVT NE // ID Q9JXP3_NEIMB Unreviewed; 228 AA. AC Q9JXP3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=ABC transporter, permease protein {ECO:0000313|EMBL:AAF42276.1}; GN OrderedLocusNames=NMB1947 {ECO:0000313|EMBL:AAF42276.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42276.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42276.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42276.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42276.1; -; Genomic_DNA. DR PIR; D81023; D81023. DR RefSeq; NP_274941.1; NC_003112.2. DR RefSeq; WP_002225834.1; NC_003112.2. DR ProteinModelPortal; Q9JXP3; -. DR STRING; 122586.NMB1947; -. DR PaxDb; Q9JXP3; -. DR EnsemblBacteria; AAF42276; AAF42276; NMB1947. DR GeneID; 904203; -. DR KEGG; nme:NMB1947; -. DR PATRIC; 20359947; VBINeiMen85645_2478. DR eggNOG; ENOG4108UMI; Bacteria. DR eggNOG; COG2011; LUCA. DR HOGENOM; HOG000222815; -. DR KO; K02072; -. DR OMA; RYQTEVM; -. DR OrthoDB; EOG6P073X; -. DR BioCyc; NMEN122586:GHGG-2004-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 28 51 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 63 87 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 93 115 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 157 179 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 199 222 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 24 215 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 228 AA; 24345 MW; 836949DC8496528E CRC64; MADLTFQQAV STIVGMKDEI FRALGETFVM VGLSTTFAVI FGTLLGVLLF VTSSRQLHYN KLVNFLLDNL VNLMRAFPFV ILMIAMIPAT RAIVGSTIGP VAASLVLSVS GLFYFARLVE QNLREVPKGV IEAAAAMGAP PIAIVCKVLL NEARAGMVSS ITVLAIGLLS YSAAAGMIGG GGLGDLAIRY GYYRYQTEVI IFIVALLVLL VILIQSTGNA LARKLDKR // ID Q9K0N5_NEIMB Unreviewed; 357 AA. AC Q9K0N5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40981.1}; GN OrderedLocusNames=NMB0552 {ECO:0000313|EMBL:AAF40981.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40981.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40981.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40981.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40981.1; -; Genomic_DNA. DR PIR; G81185; G81185. DR RefSeq; NP_273597.1; NC_003112.2. DR RefSeq; WP_002244024.1; NC_003112.2. DR STRING; 122586.NMB0552; -. DR PaxDb; Q9K0N5; -. DR EnsemblBacteria; AAF40981; AAF40981; NMB0552. DR GeneID; 902667; -. DR KEGG; nme:NMB0552; -. DR PATRIC; 20356367; VBINeiMen85645_0702. DR eggNOG; ENOG4105N09; Bacteria. DR eggNOG; COG3213; LUCA. DR HOGENOM; HOG000218803; -. DR OMA; FFTHPMR; -. DR OrthoDB; EOG6BGNXW; -. DR BioCyc; NMEN122586:GHGG-578-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010266; NnrS. DR Pfam; PF05940; NnrS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 106 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 195 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 286 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298 316 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 341 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 357 AA; 39220 MW; 7D362109F25DF4A6 CRC64; MRPFFVGAAV LAILGALVFF INPGAIVLHR QIFLELMLPA AYGGFLTAAL LDWTGFSGNL KPVATLMAAL LLAASAILPF SPQTASFFVA AYWLVLLLFC ARLIWLDRNT DNFALLMLLA AFTVFQTAYA VSGDLNLLRA QVHLNMAAVM FVSVRVSILL GAEALKECRL KDPVFIPNIV YKNIAITFLL LHAAAELWLP AQTAGFTALA VGFILLAKLR ELHHHELLRK HYVRTYYLLQ LFAAAGYLWT GAAKLQNLPA SAPLHLITLG GMMGGVMMVW LTAGLWHSGF TKLDYPKLCR IAVPILFAAA VSRAFLMNVN PIFFITVPAI LTAAVFVLYL FTFIPIFRAN AFTDDPE // ID Q9K185_NEIMB Unreviewed; 626 AA. AC Q9K185; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Ribonuclease II-related protein {ECO:0000313|EMBL:AAF62306.1}; GN OrderedLocusNames=NMB0282 {ECO:0000313|EMBL:AAF62306.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62306.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62306.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62306.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62306.1; -; Genomic_DNA. DR RefSeq; NP_273338.1; NC_003112.2. DR RefSeq; WP_002224849.1; NC_003112.2. DR ProteinModelPortal; Q9K185; -. DR STRING; 122586.NMB0282; -. DR PaxDb; Q9K185; -. DR EnsemblBacteria; AAF62306; AAF62306; NMB0282. DR GeneID; 902393; -. DR KEGG; nme:NMB0282; -. DR PATRIC; 20355658; VBINeiMen85645_0353. DR eggNOG; ENOG4106QXU; Bacteria. DR eggNOG; COG0557; LUCA. DR HOGENOM; HOG000256055; -. DR KO; K01147; -. DR OMA; QGDKMEK; -. DR OrthoDB; EOG6DRPCH; -. DR BioCyc; NMEN122586:GHGG-297-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR012340; NA-bd_OB-fold. DR SUPFAM; SSF50249; SSF50249; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 626 AA; 69312 MW; 49A51E7636DC934D CRC64; MNIFYEESGQ FKIAAIIQKN DATYQVDTPH GKRTKVKANN VFAEFDGDMA AFLENAQAQA ADIDTDLLWE VCGEEEFTAE AIAEEYYGHA PTKTELAATL IALYAAPMYF YKKAKGVFKA APEETLKQAL AAIERKKQQD AQIDAWAEAL KRGEMPSEIA ADLKTILHAP DKQSLTYKAF TKAADALKTS AYELAKKTGG ITSIPQYLQD GFEIKYFPKG TGFPDLALPE MPDLPKADVT AFSIDDESTT EVDDALSLTD LDNGTKRVGI HIAAPSLAVK PGDKMEKNIM ERLSTVYFPG GKITMLPENW IAAFSLDAGA HRPAVSIYFD VDGEFNVGAP TCKIEAVNIA TNLRIQAIEP HFNAETGLDE AGEMMFAHHQ DLIWFYQFAT ALQKARGKYE PDRAPQYDYS IELDEEGKVS VVRRERGSPI DTLVSEMMIL ANSTWAQMLH DNDLPGLFRV QPTGKVRMST KSEPHIGMGV QHYGWFTSPL RRAADYINQK QLISLIDDTA EPLYQNSDAE LFAALRDFDA AYTAYADFQR QMEAYWSLVY LQQQGTSELT ATILKEDLVR IEGLPLVTRA TGIPFDALPK SQALFKITEL DAEKQFVSLN YIKAVAPAGT TAGNAV // ID Q9K1N3_NEIMB Unreviewed; 228 AA. AC Q9K1N3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40522.1}; GN OrderedLocusNames=NMB0053 {ECO:0000313|EMBL:AAF40522.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40522.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40522.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40522.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|PIRSR:PIRSR004848-1}; CC -!- SIMILARITY: Belongs to the UPF0001 family. CC {ECO:0000256|RuleBase:RU004514}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40522.1; -; Genomic_DNA. DR PIR; C81243; C81243. DR RefSeq; NP_273118.1; NC_003112.2. DR RefSeq; WP_002243931.1; NC_003112.2. DR ProteinModelPortal; Q9K1N3; -. DR STRING; 122586.NMB0053; -. DR PaxDb; Q9K1N3; -. DR EnsemblBacteria; AAF40522; AAF40522; NMB0053. DR GeneID; 902155; -. DR KEGG; nme:NMB0053; -. DR PATRIC; 20355099; VBINeiMen85645_0087. DR eggNOG; ENOG4105DFA; Bacteria. DR eggNOG; COG0325; LUCA. DR HOGENOM; HOG000048983; -. DR KO; K06997; -. DR OMA; HGSTMVR; -. DR OrthoDB; EOG6G7R84; -. DR BioCyc; NMEN122586:GHGG-54-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.20.20.10; -; 1. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR029066; PLP-binding_barrel. DR InterPro; IPR011078; UPF0001. DR PANTHER; PTHR10146; PTHR10146; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR00044; TIGR00044; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR004848-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 28 226 Ala_racemase_N. FT {ECO:0000259|Pfam:PF01168}. FT MOD_RES 36 36 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR004848-1}. SQ SEQUENCE 228 AA; 24785 MW; 8F5BB8D4F42FAE5A CRC64; MTVLQERYCE VSDRIGKLVL QAGREPHSVS LIAVGKTFPS DGIREVYAAG QRDFGENYIQ EWYGKTEELA DLTDIVWHVI GDVQSNKTKF VAERAHWVHT VCRLKTAVRL SGQRPSSMPP LQVCIEVNIA GEAVKHGVAP EEAVALAVEV AKLPNIVVRG LMCVAKANSS ETELKVQFQT MRKLLADLNA AGVKADVLSM GMSDDMPAAI ECGATHVRIG SAIFGKRG // ID Q9JZ49_NEIMB Unreviewed; 62 AA. AC Q9JZ49; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41668.1}; GN OrderedLocusNames=NMB1292 {ECO:0000313|EMBL:AAF41668.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41668.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41668.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41668.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41668.1; -; Genomic_DNA. DR PIR; C81101; C81101. DR RefSeq; NP_274312.1; NC_003112.2. DR RefSeq; WP_010980916.1; NC_003112.2. DR STRING; 122586.NMB1292; -. DR PaxDb; Q9JZ49; -. DR EnsemblBacteria; AAF41668; AAF41668; NMB1292. DR GeneID; 903714; -. DR KEGG; nme:NMB1292; -. DR OrthoDB; EOG6HXJF1; -. DR BioCyc; NMEN122586:GHGG-1330-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 62 AA; 7266 MW; 7BFEE84AB8882E57 CRC64; MSAAARQNHT LQNLTICRGR KQEAFLFRRK ILISPPCSRS RSKGKKFTRF LSVKNYQIKQ IL // ID Q7DD93_NEIMB Unreviewed; 553 AA. AC Q7DD93; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=PqiB protein {ECO:0000313|EMBL:AAF42020.1}; GN Name=pqiB {ECO:0000313|EMBL:AAF42020.1}; GN OrderedLocusNames=NMB1671 {ECO:0000313|EMBL:AAF42020.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42020.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42020.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42020.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42020.1; -; Genomic_DNA. DR PIR; A81057; A81057. DR RefSeq; NP_274676.1; NC_003112.2. DR RefSeq; WP_002222140.1; NC_003112.2. DR STRING; 122586.NMB1671; -. DR PaxDb; Q7DD93; -. DR EnsemblBacteria; AAF42020; AAF42020; NMB1671. DR GeneID; 903439; -. DR KEGG; nme:NMB1671; -. DR PATRIC; 20359284; VBINeiMen85645_2150. DR eggNOG; ENOG4105DY2; Bacteria. DR eggNOG; COG3008; LUCA. DR HOGENOM; HOG000256423; -. DR KO; K06192; -. DR OMA; HHVEIKA; -. DR OrthoDB; EOG69WFM1; -. DR BioCyc; NMEN122586:GHGG-1725-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003399; Mce/MlaD. DR Pfam; PF02470; MlaD; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 42 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 50 140 MlaD. {ECO:0000259|Pfam:PF02470}. FT DOMAIN 292 395 MlaD. {ECO:0000259|Pfam:PF02470}. SQ SEQUENCE 553 AA; 60501 MW; 2D92902B7C0E186F CRC64; MTDNSPPPNG HAQARVRKNN TFLSAVWLVP LIALIAGGWL WVKEIRNRGP VVTLLMDSAE GIEVNNTVIK VLSIDVGRVT RIKLRDDQKG VEVTAQLNAD VSGLIRSDTQ FWVVKPRIDQ SGVTGLGTLL SGSYIAFTPG KSDEAKDVFQ VQDIPPVTAI GQSGLRLNLI GKNDRILNVN SPVLYENFMV GQVESAHFDP SDQSVHYTIF IQSPNDKLIH SASRFWLESG INIETTGSGI KLNSAPLPAL LSGAISFDSP KTKNSKNVKS EDSFTLYDSR SEVANLPDDR SLYYTAFFKQ SVRGLTVGSP VEYKGLNVGV VSDVPYFDRN DSLHLFENGW IPVRIRIEPS RLEINADEQS KEHWKQQFQT ALNKGLTATI SSNNLLTGSK MIELNDQPSA SPKLRPHTVY AGDTVIATQG GGLDDLQVKL ADLLDKFDKL PLDKTVAELN GSLAELKSTL KSANAALSSI DKLVGKPQTQ NIPNELNQTL KELRTTLQGV SPQSPIYGDV QNTLQSLDKT LKDVQPVINT LKEKPNALIF NSSSKDPIPK GSR // ID Q9JY37_NEIMB Unreviewed; 417 AA. AC Q9JY37; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42102.1}; GN OrderedLocusNames=NMB1761 {ECO:0000313|EMBL:AAF42102.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42102.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42102.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42102.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42102.1; -; Genomic_DNA. DR PIR; H81046; H81046. DR RefSeq; NP_274761.1; NC_003112.2. DR RefSeq; WP_002232961.1; NC_003112.2. DR STRING; 122586.NMB1761; -. DR PaxDb; Q9JY37; -. DR EnsemblBacteria; AAF42102; AAF42102; NMB1761. DR GeneID; 903337; -. DR KEGG; nme:NMB1761; -. DR PATRIC; 20359487; VBINeiMen85645_2249. DR eggNOG; ENOG410874Z; Bacteria. DR eggNOG; COG3550; LUCA. DR HOGENOM; HOG000152753; -. DR KO; K07154; -. DR OMA; VYDMLTI; -. DR OrthoDB; EOG6Q2SGF; -. DR BioCyc; NMEN122586:GHGG-1816-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR012893; HipA-like_C. DR InterPro; IPR017508; HipA_N1. DR InterPro; IPR012894; HipA_N2. DR Pfam; PF13657; Couple_hipA; 1. DR Pfam; PF07804; HipA_C; 1. DR Pfam; PF07805; HipA_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 104 Couple_hipA. {ECO:0000259|Pfam:PF13657}. FT DOMAIN 155 227 HipA_N. {ECO:0000259|Pfam:PF07805}. FT DOMAIN 235 383 HipA_C. {ECO:0000259|Pfam:PF07804}. SQ SEQUENCE 417 AA; 48110 MW; F8A385BD524245C4 CRC64; MRKPRITYLD VWANDERIGT LEKGAMYRFA YDNPNSSLLG LHYQDRSKVY ISNNMPHIFA QYFPEGFLDA HITSKYAFHD APFEDNEMLR LAILCRETLG RIHVRCNDPL FNEWIDGLEM KNPRILTERD LLGINARQVF QQYMAEIFHH GRFVSVSGIQ QKMSLDAIRR NTKQTASYIA KGFDASEYPC LAANEFLCMQ TIKQAGIAVA QTSLSEDSSV LLVRRFDVSE QGYFLGMEDF TSLRQYSVED KYKGSYAAIA QIIRQISGRP DEDLIHFFNQ LAASCILKNG DAHLKNFSVL YHDEYDVRLA PVYDVLDTSI YRVGTQGIFD AYDDTLALNL TNHGKKTYPS KNTLLDFAEK YCDLGREDAS FMIDTIVQAK EQVLVKYSDV LRENEWLAQK WHFIPDENEE GLPFTFR // ID Q9K109_NEIMB Unreviewed; 752 AA. AC Q9K109; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Maltose phosphorylase {ECO:0000313|EMBL:AAF40830.1}; DE EC=2.4.1.8 {ECO:0000313|EMBL:AAF40830.1}; GN Name=mapA {ECO:0000313|EMBL:AAF40830.1}; GN OrderedLocusNames=NMB0390 {ECO:0000313|EMBL:AAF40830.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40830.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40830.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40830.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40830.1; -; Genomic_DNA. DR PIR; F81203; F81203. DR RefSeq; NP_273439.1; NC_003112.2. DR RefSeq; WP_002224908.1; NC_003112.2. DR ProteinModelPortal; Q9K109; -. DR SMR; Q9K109; 3-743. DR STRING; 122586.NMB0390; -. DR PaxDb; Q9K109; -. DR EnsemblBacteria; AAF40830; AAF40830; NMB0390. DR GeneID; 902505; -. DR KEGG; nme:NMB0390; -. DR PATRIC; 20355943; VBINeiMen85645_0489. DR eggNOG; ENOG4105C71; Bacteria. DR eggNOG; COG1554; LUCA. DR HOGENOM; HOG000055023; -. DR KO; K00691; -. DR OMA; LNMKEGW; -. DR OrthoDB; EOG65XMZ3; -. DR BioCyc; NMEN122586:GHGG-412-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0050082; F:maltose phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.50.10.10; -; 1. DR Gene3D; 2.70.98.40; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR012341; 6hp_glycosidase. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR005194; Glyco_hydro_65_C. DR InterPro; IPR005195; Glyco_hydro_65_M. DR InterPro; IPR005196; Glyco_hydro_65_N. DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase. DR Pfam; PF03633; Glyco_hydro_65C; 1. DR Pfam; PF03632; Glyco_hydro_65m; 1. DR Pfam; PF03636; Glyco_hydro_65N; 1. DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1. DR SUPFAM; SSF48208; SSF48208; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosyltransferase {ECO:0000313|EMBL:AAF40830.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40830.1}. FT DOMAIN 17 261 Glyco_hydro_65N. FT {ECO:0000259|Pfam:PF03636}. FT DOMAIN 318 688 Glyco_hydro_65m. FT {ECO:0000259|Pfam:PF03632}. FT DOMAIN 692 742 Glyco_hydro_65C. FT {ECO:0000259|Pfam:PF03633}. SQ SEQUENCE 752 AA; 85489 MW; 1020224B31BF87F7 CRC64; MYTRIMEISP WTLRSAKLEK EHKRLQESLT SLGNGYMGMR GSFEETYSAD SHLGTYIAGV WFPDKTRVGW WKNGYPKYFG KAINAFNFSK VKIFVDGQEV DLAKNDVAGF SVELDMQHGV LRRSFTVFGV RFNVCKFLSV AQKELAVIRW EAVSVDGKTH QVRIDSIIDA DVKNEDSNYE EKFWQVLDKG VSDSLSYIAA QTVANPFGVE QFIVNAEQTF AGSFKALGGS QTDWQVSNSF ESEVGSTPET FEKRVIVTTS RDYQSLEAVK AAGRALSEKI AGVAFETLLD AHKAGWLHRW EIADVVIEGS DEAQQGIRFN LFQLFSTYYG EDARLNIGPK GFTGEKYGGA TYWDTEAYAV PLYLALAEPE VTRNLLQYRR NQLPQAQHNA REQGLAGALY PMVTFTGIEC HNEWEITFEE IHRNGAIPYA IYNYTNYTGD EGYLAKEGLE VLVEVSRFWA DRVHFSKRNG KYMIHGVTGP NEYENNINNN WYTNTLAAWV LDYTREALAK YPRPDLNVRA DELEKWADIS ANMYRPHDEE LGVFVQHDGF LDKDIRPVSA LSPDDLPLNQ KWSWDKILRS PFIKQADVLQ GIYFFSDRFN IDEKRRNFDF YEPMTVHESS LSPCIHSILA AELGKEEKAV EMYQRTARLD LDNYNNDTED GLHITSMTGS WLAIVQGFAQ MKTWGGKLSF APFLPSAWTG YAFHINYRGR LIKVAVGKEN VVFTLLKGES LDLQVYGKDI TLDGSHTVAL EK // ID Q9K0G5_NEIMB Unreviewed; 77 AA. AC Q9K0G5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41063.1}; GN OrderedLocusNames=NMB0640 {ECO:0000313|EMBL:AAF41063.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41063.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41063.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41063.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41063.1; -; Genomic_DNA. DR PIR; E81175; E81175. DR RefSeq; NP_273683.1; NC_003112.2. DR RefSeq; WP_002225518.1; NC_003112.2. DR STRING; 122586.NMB0640; -. DR PaxDb; Q9K0G5; -. DR EnsemblBacteria; AAF41063; AAF41063; NMB0640. DR GeneID; 902751; -. DR KEGG; nme:NMB0640; -. DR PATRIC; 20356579; VBINeiMen85645_0809. DR HOGENOM; HOG000218827; -. DR OMA; FRPNAMN; -. DR OrthoDB; EOG600DWR; -. DR BioCyc; NMEN122586:GHGG-666-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 59 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 77 AA; 8504 MW; DF4E52B1F21BF9C0 CRC64; MNRRKIYLLS VALFTLAFML LVLLGAYLLT VGSKAFAVAS FLFAFGALFG QIGSLALYLR HKSLRAAQSA TKENRYV // ID Q7DDQ2_NEIMB Unreviewed; 140 AA. AC Q7DDQ2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40891.1}; GN OrderedLocusNames=NMB0454 {ECO:0000313|EMBL:AAF40891.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40891.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40891.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40891.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40891.1; -; Genomic_DNA. DR RefSeq; NP_273501.1; NC_003112.2. DR RefSeq; WP_002216567.1; NC_003112.2. DR STRING; 122586.NMB0454; -. DR PaxDb; Q7DDQ2; -. DR EnsemblBacteria; AAF40891; AAF40891; NMB0454. DR GeneID; 902570; -. DR KEGG; nme:NMB0454; -. DR PATRIC; 20356122; VBINeiMen85645_0577. DR HOGENOM; HOG000219092; -. DR OMA; WQAARIR; -. DR OrthoDB; EOG6BPDPM; -. DR BioCyc; NMEN122586:GHGG-478-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15655 MW; C7F403202DC3D593 CRC64; MNKNRKLLLA ALLLIAFAAV KLVLLQWWQA QQPQAVAAQC DLTEGCTLPD GSRVRAAAVS TKKPFDIYIE HAPAGTEQVS ISFSMKNMDM GFNRYMFERQ PSGTWQAVRI RLPICVEGRR DFTADITIGS RTFQTAFTAE // ID Q9JXE9_NEIMB Unreviewed; 193 AA. AC Q9JXE9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42396.1}; GN OrderedLocusNames=NMB2078 {ECO:0000313|EMBL:AAF42396.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42396.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42396.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42396.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42396.1; -; Genomic_DNA. DR PIR; D81009; D81009. DR RefSeq; NP_275067.1; NC_003112.2. DR RefSeq; WP_002225713.1; NC_003112.2. DR STRING; 122586.NMB2078; -. DR PaxDb; Q9JXE9; -. DR EnsemblBacteria; AAF42396; AAF42396; NMB2078. DR GeneID; 903978; -. DR KEGG; nme:NMB2078; -. DR PATRIC; 20360324; VBINeiMen85645_2659. DR eggNOG; COG1714; LUCA. DR HOGENOM; HOG000218717; -. DR OMA; QNDRRCL; -. DR OrthoDB; EOG6VXFB9; -. DR BioCyc; NMEN122586:GHGG-2144-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010432; RDD. DR Pfam; PF06271; RDD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 172 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 25 184 RDD. {ECO:0000259|Pfam:PF06271}. SQ SEQUENCE 193 AA; 20993 MW; D6D390EE5889EA22 CRC64; MEEKNDYTDA ASDNRNGQEI EVGIAGAGDR ILAALLNQLF TFLVLLVPFA GLIAFAIKNE GRIGSGEEIF GLLLGMTSFW VGLAGILAYT VIQIYYMSRD GQSLGKKIMR IRVLKTDGRN PGFVGTVLVR EIAWSVLVAI IAAVIGLAVG DNGENAINLL AFLANFVLLF MVKRDRRTLY DILADTVVVK LPK // ID Q9JZM6_NEIMB Unreviewed; 165 AA. AC Q9JZM6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=E16-related protein {ECO:0000313|EMBL:AAF41388.1}; GN OrderedLocusNames=NMB0985 {ECO:0000313|EMBL:AAF41388.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41388.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41388.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41388.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41388.1; -; Genomic_DNA. DR PIR; B81135; B81135. DR RefSeq; NP_274021.1; NC_003112.2. DR RefSeq; WP_010980882.1; NC_003112.2. DR STRING; 122586.NMB0985; -. DR PaxDb; Q9JZM6; -. DR EnsemblBacteria; AAF41388; AAF41388; NMB0985. DR GeneID; 903105; -. DR KEGG; nme:NMB0985; -. DR PATRIC; 20357467; VBINeiMen85645_1248. DR eggNOG; ENOG4106FQ3; Bacteria. DR eggNOG; COG4382; LUCA. DR HOGENOM; HOG000218904; -. DR OMA; YGFEMRR; -. DR OrthoDB; EOG67T5NH; -. DR BioCyc; NMEN122586:GHGG-1022-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009363; Phage_Mu_Gp16. DR Pfam; PF06252; DUF1018; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 165 AA; 18430 MW; 142719CF0D184EAF CRC64; MSVRFAKNIG LILYIVFYGF EMRRALIAKI KIAQKELGLD DGTYRAVLER VTGKRSCADM DVSELESVVA DMRSHGFKPK AKGNPHGKPH LRRTSSAAML DKVEALLTVG GKHWNYAHAM ARRMFGKDKV EYLDDTQLHK LVAALQIAEN RKTEKAGGDD GVRKS // ID Q9K0K0_NEIMB Unreviewed; 604 AA. AC Q9K0K0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41024.1}; GN OrderedLocusNames=NMB0596 {ECO:0000313|EMBL:AAF41024.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41024.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41024.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41024.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41024.1; -; Genomic_DNA. DR PIR; A81181; A81181. DR RefSeq; NP_273640.1; NC_003112.2. DR RefSeq; WP_002244038.1; NC_003112.2. DR STRING; 122586.NMB0596; -. DR PaxDb; Q9K0K0; -. DR EnsemblBacteria; AAF41024; AAF41024; NMB0596. DR GeneID; 902711; -. DR KEGG; nme:NMB0596; -. DR PATRIC; 20356477; VBINeiMen85645_0758. DR eggNOG; ENOG4105GU8; Bacteria. DR eggNOG; COG3307; LUCA. DR HOGENOM; HOG000218824; -. DR OMA; LQNIIVY; -. DR OrthoDB; EOG65QWDS; -. DR BioCyc; NMEN122586:GHGG-622-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007016; O-antigen_ligase-related. DR InterPro; IPR031726; PglL_A. DR InterPro; IPR021797; Wzy_C_2. DR Pfam; PF15864; PglL_A; 1. DR Pfam; PF04932; Wzy_C; 1. DR Pfam; PF11846; Wzy_C_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 121 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 220 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 254 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 351 379 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 386 403 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 409 427 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 439 459 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 173 196 PglL_A. {ECO:0000259|Pfam:PF15864}. FT DOMAIN 389 562 Wzy_C_2. {ECO:0000259|Pfam:PF11846}. SQ SEQUENCE 604 AA; 67156 MW; A743C07A4C48E45F CRC64; MPAETTVSGA HPAAKLPIYI LPCFLWIGIV PFTFALKLKP SPDFYHDAAA AAGLIVLLFL TAGKKLFDVK IPAISFLLFA MAAFWYLQAR LMNLIYPGMN DIVSWIFILL AVSAWACRSL VAHFGQERIV TLFAWSLLIG SLLQSCIVVI QFAGWEDTPL FQNIIVYSGQ GVIGHIGQRN NLGHYLMWGI LAAAYLNGQR KIPAALGVIC LIMQTAVLGL VNSRTILTYI AAIALILPFW YFRSDKSNRR TMLGIAAAVF LTALFQFSMN TILETFTGIR YETAVERVAN GGFTDLPRQI EWNKALAAFQ SAPIFGHGWN SFAQQTFLIN AEQHNIYDNL LSNLFTHSHN IVLQLLAEMG ISGTLLVAAT LLTGIAGLLK RPLTPASLFL ICTLAVSMCH SMLEYPLWYV YFLIPFGLML FLSPAEASDG IAFKKAANLG ILTASAAIFA GLLHLDWTYT RLVNAFSPAT DDSAKTLNRK INELRYISAN SPMLSFYADF SLVNFALPEY PETQTWAEEA TLKSLKYRPH SATYRIALYL MRQGKVAEAK QWMRATQSYY PYLMPRYADE IRKLPVWAPL LPELLKDCKA FAAAPGHPEA KPCK // ID Q9JYP2_NEIMB Unreviewed; 143 AA. AC Q9JYP2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41846.1}; GN OrderedLocusNames=NMB1490 {ECO:0000313|EMBL:AAF41846.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41846.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41846.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41846.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41846.1; -; Genomic_DNA. DR PIR; H81077; H81077. DR STRING; 122586.NMB1490; -. DR PaxDb; Q9JYP2; -. DR EnsemblBacteria; AAF41846; AAF41846; NMB1490. DR BioCyc; NMEN122586:GHGG-1530-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 143 AA; 15250 MW; 2EB7AEE571996369 CRC64; MMTADAGICR PFKTKPARTI FGRFPARTVC LCASAIWTAA KSRCGWTAGV PSSLPTLPHP ANAIPPNTVC SETQPSGTRK AAKPFSALPM PTAIRSKLPA APVKRGSLFE PPSRFFGRFF VSDGRFFVSD LFCSSASGRV RAA // ID Q9JZ05_NEIMB Unreviewed; 285 AA. AC Q9JZ05; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41723.1}; GN OrderedLocusNames=NMB1349 {ECO:0000313|EMBL:AAF41723.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41723.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41723.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41723.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41723.1; -; Genomic_DNA. DR PIR; H81092; H81092. DR RefSeq; NP_274367.1; NC_003112.2. DR RefSeq; WP_002222347.1; NC_003112.2. DR STRING; 122586.NMB1349; -. DR PaxDb; Q9JZ05; -. DR EnsemblBacteria; AAF41723; AAF41723; NMB1349. DR GeneID; 903771; -. DR KEGG; nme:NMB1349; -. DR PATRIC; 20358355; VBINeiMen85645_1689. DR eggNOG; COG3782; LUCA. DR HOGENOM; HOG000261834; -. DR KO; K09977; -. DR OMA; QGFHAFE; -. DR OrthoDB; EOG60652J; -. DR BioCyc; NMEN122586:GHGG-1387-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR015003; DUF1853. DR Pfam; PF08907; DUF1853; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 285 AA; 32053 MW; 6F5D101451EE8DE9 CRC64; MNYALDALWW KLTSQPVRDL ASLLTAPPLW QSGCELSVRE LLGEHGFRYL LALDADPTRL TDYLAQRAPF GHRLGIYAEE LLAFWFANAP HAELLAHNLT VSGSDGNTQG AADFVARLNG KPYHIELTCK YYGGDTDSPE GMRGFDPKDT LLGKAAKLTA QLGLPHTSDG IRTLRQHGLP LNVKPVSIVR GIGFFPHGFH AFEPPLNPYG WRGIYIQDWA EYGFKRQEVR YHLLDRMAYL APARVAETET LNATEIRRID QGLIAVLECR PDGFWHEIER IMKAV // ID Q4W556_NEIMB Unreviewed; 68 AA. AC Q4W556; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 37. DE SubName: Full=MafB-related protein {ECO:0000313|EMBL:AAY52168.1}; GN OrderedLocusNames=NMB2119 {ECO:0000313|EMBL:AAY52168.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52168.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52168.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52168.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52168.1; -; Genomic_DNA. DR STRING; 122586.NMB2119; -. DR PaxDb; Q4W556; -. DR EnsemblBacteria; AAY52168; AAY52168; NMB2119. DR PATRIC; 20360412; VBINeiMen85645_2702. DR OMA; QTIRDFD; -. DR OrthoDB; EOG6VXFFH; -. DR BioCyc; NMEN122586:GHGG-2184-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 68 AA; 7478 MW; 6AE6909D2050530C CRC64; MGDYNDALND FNSLNVRNVQ TRPNGTITGN LPDGRAVNAR NDSSGGEPTL EITISNNRKI KIRYGNTR // ID Q9JYI1_NEIMB Unreviewed; 97 AA. AC Q9JYI1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41928.1}; GN OrderedLocusNames=NMB1575 {ECO:0000313|EMBL:AAF41928.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41928.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41928.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41928.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41928.1; -; Genomic_DNA. DR PIR; G81066; G81066. DR RefSeq; NP_274581.1; NC_003112.2. DR RefSeq; WP_002212818.1; NC_003112.2. DR ProteinModelPortal; Q9JYI1; -. DR STRING; 122586.NMB1575; -. DR PaxDb; Q9JYI1; -. DR EnsemblBacteria; AAF41928; AAF41928; NMB1575. DR GeneID; 904182; -. DR KEGG; nme:NMB1575; -. DR PATRIC; 20359014; VBINeiMen85645_2026. DR eggNOG; ENOG41067V3; Bacteria. DR eggNOG; COG1359; LUCA. DR HOGENOM; HOG000145619; -. DR OMA; RMVFVEQ; -. DR OrthoDB; EOG6MSS9K; -. DR BioCyc; NMEN122586:GHGG-1616-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007138; ABM_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR Pfam; PF03992; ABM; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS51725; ABM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 92 ABM. {ECO:0000259|PROSITE:PS51725}. SQ SEQUENCE 97 AA; 10850 MW; D32D9FBB6CB3FD58 CRC64; MSNIKIVALV TVKPEYTETL AAQFKELVKA SRAEEGNISY DLHQEIGKPN RFVFVENWKS QAAIDEHNAS AHFQAFVQSV DGKTEALEIV LMNEVAD // ID Q9JY79_NEIMB Unreviewed; 166 AA. AC Q9JY79; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42049.1}; GN OrderedLocusNames=NMB1701 {ECO:0000313|EMBL:AAF42049.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42049.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42049.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42049.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42049.1; -; Genomic_DNA. DR PIR; G81052; G81052. DR RefSeq; NP_274705.1; NC_003112.2. DR RefSeq; WP_010980976.1; NC_003112.2. DR ProteinModelPortal; Q9JY79; -. DR STRING; 122586.NMB1701; -. DR PaxDb; Q9JY79; -. DR EnsemblBacteria; AAF42049; AAF42049; NMB1701. DR GeneID; 903402; -. DR KEGG; nme:NMB1701; -. DR PATRIC; 20359357; VBINeiMen85645_2185. DR eggNOG; ENOG4105S5U; Bacteria. DR eggNOG; COG4706; LUCA. DR HOGENOM; HOG000282082; -. DR OMA; SRLIIQI; -. DR OrthoDB; EOG6384M8; -. DR BioCyc; NMEN122586:GHGG-1756-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR016776; Hydroxyacyl-ACP_deHydtase_prd. DR PIRSF; PIRSF020565; 3Ho_Ac_ACP_DH_prd; 1. DR SUPFAM; SSF54637; SSF54637; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 166 AA; 17836 MW; 7FEEB9B5A2638E4A CRC64; MDTLPECPIT NTASLLPHSG RMVLIDRITR YGDDFVEAGA QVSPNHILLL DDKLPYTAFI ELMAQAVGAY AGIQARKNAR SVRLGFLLGT RKLEIFAQSV PIGTHLLATA HMSIQDAGGM GVFDCELRWT DAPETSSETL PSDGILARAS LNVYSPEHPA GTTDAV // ID Q9JZW2_NEIMB Unreviewed; 389 AA. AC Q9JZW2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AAF41288.1}; GN OrderedLocusNames=NMB0877 {ECO:0000313|EMBL:AAF41288.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41288.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41288.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41288.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the peptidase S11 family. CC {ECO:0000256|RuleBase:RU004016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41288.1; -; Genomic_DNA. DR PIR; H81146; H81146. DR RefSeq; NP_273918.1; NC_003112.2. DR RefSeq; WP_002225372.1; NC_003112.2. DR ProteinModelPortal; Q9JZW2; -. DR STRING; 122586.NMB0877; -. DR PaxDb; Q9JZW2; -. DR EnsemblBacteria; AAF41288; AAF41288; NMB0877. DR GeneID; 902996; -. DR KEGG; nme:NMB0877; -. DR PATRIC; 20357159; VBINeiMen85645_1093. DR eggNOG; ENOG4105DZ1; Bacteria. DR eggNOG; COG1686; LUCA. DR HOGENOM; HOG000086623; -. DR KO; K07258; -. DR OMA; GTIDFKL; -. DR OrthoDB; EOG6RJV2H; -. DR BioCyc; NMEN122586:GHGG-913-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro. DR Gene3D; 2.60.410.10; -; 1. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR015956; Peniciliin-bd_prot-assoc. DR InterPro; IPR018044; Peptidase_S11. DR InterPro; IPR012907; Peptidase_S11_C. DR InterPro; IPR001967; Peptidase_S11_N. DR Pfam; PF07943; PBP5_C; 1. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SMART; SM00936; PBP5_C; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR SUPFAM; SSF69189; SSF69189; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 389 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332280. FT DOMAIN 285 375 PBP5_C. {ECO:0000259|SMART:SM00936}. SQ SEQUENCE 389 AA; 42632 MW; B85F875C302481D2 CRC64; MTAHKILPVL LSIILGVSHA TAASPAPNRP TVHAAPTFQT PETLTAAHIV IDLQSKQILS AKNINTPVEP AALTQLMTAY LVFKNMKSGN IQSEENLKIP ESAWASEGSR MFVRPGDTVS TDKLLKGMIA LSANDAALTL AGRLGNGSIE NFVQQMNKEA RRLGMKNTVF KNPTGLSREG QVSTAKDLAL LSEALMRDFP EYYPLFSIKS FKFKNIEQNN RNILLYRDNN VNGLKAGHTE SGGYNLAVSY SGNGRHILVI TLGSESAETR ASDNSKLLNW ALQAFDTPKI YPKGKTVAQI QISGGSKKTV RAGFLKEAYI TLPHKEAKMA EQILETIQPI PAPVKKGQIL GKIKIRQNGY TIAEKEIVAL ENVKKRSRWQ RLWACLTGQ // ID Q9K1N4_NEIMB Unreviewed; 408 AA. AC Q9K1N4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Twitching motility protein {ECO:0000313|EMBL:AAF40520.1}; GN OrderedLocusNames=NMB0051 {ECO:0000313|EMBL:AAF40520.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40520.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40520.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40520.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40520.1; -; Genomic_DNA. DR PIR; A81243; A81243. DR RefSeq; NP_273116.1; NC_003112.2. DR RefSeq; WP_002218483.1; NC_003112.2. DR ProteinModelPortal; Q9K1N4; -. DR STRING; 122586.NMB0051; -. DR PaxDb; Q9K1N4; -. DR EnsemblBacteria; AAF40520; AAF40520; NMB0051. DR GeneID; 902153; -. DR KEGG; nme:NMB0051; -. DR PATRIC; 20355095; VBINeiMen85645_0085. DR eggNOG; COG5008; LUCA. DR HOGENOM; HOG000008425; -. DR KO; K02670; -. DR OMA; ATSPHEF; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NMEN122586:GHGG-52-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006321; PilT. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01420; pilT_fam; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 158 310 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 408 AA; 45674 MW; BC246581994958CA CRC64; MNTDNLHDIL DEMVQVYSQK KQSRSETPAE IGAHFHPLLD RLCETAEAQN ASDILISKGF PPSLKINSAL TPQPQKALTG EETAAIAAST MNAEQSEIFR RDGEINYSVQ SRSGTRYRAN AYHSQGSAGL VLRRINHVIP QMQELGLPEK LKDLAVAPRG LLIIVGPTGS GKSTTMATML EHRNKTLPSH IVTIEDPIEF IYKPRRCIFT QREIGVDTIN WQTAVQNAMR QSPDVVCIGE VRSRESMEYA MQLAQTGHLC IFTLHANTAP QSLERILNFY PKEQHNQILI DIALNLTGII CQRLALKQDK TGRTAVVDLL INTPAIQDFI LKGDLMNISK IMETAKTDGM QTMDQNLFEL YRHGIISYEE ALRQSVSANN LRLHIQLHKE GKTPELLYDR VNGLNLIS // ID Q7DDJ9_NEIMB Unreviewed; 942 AA. AC Q7DDJ9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=2-oxoglutarate dehydrogenase, E1 component {ECO:0000313|EMBL:AAF41361.1}; DE EC=1.2.4.2 {ECO:0000313|EMBL:AAF41361.1}; GN Name=sucA {ECO:0000313|EMBL:AAF41361.1}; GN OrderedLocusNames=NMB0955 {ECO:0000313|EMBL:AAF41361.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41361.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41361.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41361.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41361.1; -; Genomic_DNA. DR PIR; C81139; C81139. DR RefSeq; NP_273993.1; NC_003112.2. DR RefSeq; WP_002213758.1; NC_003112.2. DR ProteinModelPortal; Q7DDJ9; -. DR SMR; Q7DDJ9; 86-942. DR STRING; 122586.NMB0955; -. DR PaxDb; Q7DDJ9; -. DR EnsemblBacteria; AAF41361; AAF41361; NMB0955. DR GeneID; 903075; -. DR KEGG; nme:NMB0955; -. DR PATRIC; 20357391; VBINeiMen85645_1210. DR eggNOG; ENOG4105C7P; Bacteria. DR eggNOG; COG0567; LUCA. DR HOGENOM; HOG000259588; -. DR KO; K00164; -. DR OMA; DWLDGRW; -. DR OrthoDB; EOG6V1M1F; -. DR BioCyc; NMEN122586:GHGG-992-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR032106; 2-oxogl_dehyd_N. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR031717; KGD_C. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR PANTHER; PTHR23152; PTHR23152; 1. DR Pfam; PF16078; 2-oxogl_dehyd_N; 1. DR Pfam; PF00676; E1_dh; 1. DR Pfam; PF16870; OxoGdeHyase_C; 1. DR Pfam; PF02779; Transket_pyr; 1. DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41361.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 594 791 Transket_pyr. FT {ECO:0000259|SMART:SM00861}. SQ SEQUENCE 942 AA; 105082 MW; 03322FE321984D4F CRC64; MMDEKLNFSY LFGSNAPYIE ELYEAFLENP DAVDEKWKQY FTDLSKQPGT VAVDVAHTPI RESFVTLAKK KIASAVAGGA DEAMLKKQVS VLRLISAYRI QGVGAAQLDP LKRIPPRDIE ALDPKFHGLS DADMALQFNM GEGDFANRGK LPLSQIISNL KQTYCGHIAL EYIYIPNTEE RRWVRNYFES VLSTPHYNAD QKRRILKEMT AAETLERYLH TKYVGQKRFG VEGGESAIAG LNYLIQNAGK DGVEEVIIGM AHRGRLNVLV NILGKKPGDL FAEFEGRAEI KLPSGDVKYH MGFSSDIATP HGPMHVSLAF NPSHLEIVNP VVEGSARAKQ KRLGENGRDK VLPVLIHGDS AFIGLGVNQA TFNLSKTRGY TTGGTVHIVI NNQIGFTTSD IRDTRSTVHC TDIAKMVSAP VIHVNGDDPE RVCFAIQAAL DYRKKFHKDI VIDVVCYRKW GHNEGDDPTL TQPMMYKKVS QHPGARALYT EQLIAEGVVT QAEADGYIQA YRDALDKGEH VEQTTLSNFQ RTQIDWSKYQ GKDWREHIET GLPAADIERL TEKFTAVPEG FALHPTAKRV IEARKAMASG KQAIDWGMAE TLAYASLVTK GHGVRISGED SGRGTFSHRH AVLHDQKREK WDDGTYVPLR HMGEGMGEFL VIDSILNEEA VMAFEYGFAC SAPDKLTIWE AQFGDFANGA QVTIDQFLSS GETKWGRLCG LTTILPHGYD GQGPEHSSAR VERWLQLCSE NNMQVIMPSE ASQMFHLLQR QVLGSYRKPL VIFMSKRLLR FKGAMSPLEN FTEGSTFRPV IGDTAERASN DSVKRVVLCA GQVYYDLEAG RAERKLEDDV AIVRVEQLYP FPYDEVKAEL AKYPNAKSVV WAQEEPKNQG AFYQIRHRIE DVISEEQKLS YAGRPSSASP AVGYSSKHIA QLKQLVEDAL AL // ID Q9K173_NEIMB Unreviewed; 148 AA. AC Q9K173; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=ComEA-related protein {ECO:0000313|EMBL:AAF40750.1}; GN OrderedLocusNames=NMB0299 {ECO:0000313|EMBL:AAF40750.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40750.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40750.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40750.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40750.1; -; Genomic_DNA. DR PIR; C81214; C81214. DR RefSeq; NP_273353.1; NC_003112.2. DR RefSeq; WP_010980774.1; NC_003112.2. DR ProteinModelPortal; Q9K173; -. DR STRING; 122586.NMB0299; -. DR PaxDb; Q9K173; -. DR EnsemblBacteria; AAF40750; AAF40750; NMB0299. DR GeneID; 902415; -. DR KEGG; nme:NMB0299; -. DR PATRIC; 20355710; VBINeiMen85645_0375. DR eggNOG; ENOG41083P1; Bacteria. DR eggNOG; COG1555; LUCA. DR HOGENOM; HOG000257817; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; NMEN122586:GHGG-319-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004787; Competence_ComE. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR01259; comE; 1. DR TIGRFAMs; TIGR00426; TIGR00426; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 74 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 78 97 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 108 127 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 148 AA; 15886 MW; 85A2EA3A8A30335A CRC64; MSVMAGRHPY GVRSGLRRNG LKLWDIHFRM TRFIVARCGL LFATLKGKTM KKMFVLFCML FSCAFSLAAV NINAASQQEL EALPGIGPAK AKAIAEYRAQ NGAFKSVDDL TKVKGIGPAV LAKLKDQASV GAPAPKAPAK PVLPADKK // ID Q9JYS6_NEIMB Unreviewed; 470 AA. AC Q9JYS6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 101. DE SubName: Full=DNA polymerase III, epsilon subunit {ECO:0000313|EMBL:AAF41810.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAF41810.1}; GN Name=dnaQ-1 {ECO:0000313|EMBL:AAF41810.1}; GN OrderedLocusNames=NMB1451 {ECO:0000313|EMBL:AAF41810.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41810.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41810.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41810.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41810.1; -; Genomic_DNA. DR PIR; D81081; D81081. DR RefSeq; NP_274462.1; NC_003112.2. DR RefSeq; WP_009347376.1; NC_003112.2. DR ProteinModelPortal; Q9JYS6; -. DR STRING; 122586.NMB1451; -. DR PaxDb; Q9JYS6; -. DR EnsemblBacteria; AAF41810; AAF41810; NMB1451. DR GeneID; 903871; -. DR KEGG; nme:NMB1451; -. DR PATRIC; 20358639; VBINeiMen85645_1831. DR eggNOG; ENOG4108JDX; Bacteria. DR eggNOG; COG0847; LUCA. DR HOGENOM; HOG000219014; -. DR KO; K02342; -. DR OMA; ILDWGKM; -. DR OrthoDB; EOG6PKFH3; -. DR BioCyc; NMEN122586:GHGG-1489-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAF41810.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41810.1}. FT DOMAIN 29 193 Exonuclease. {ECO:0000259|SMART:SM00479}. SQ SEQUENCE 470 AA; 52260 MW; 33A9280180069B07 CRC64; MLFEFKENKM IVASRWPLLE KVFLRFGMPV AVVDLESTGG NLYEDRVTEV ALVKFEQGRV VRHEWLVNPQ KPIPQFVAGL TGISDGMVAD APVFAEIAGE LFSVLKGCVL VAHNSRFDYT FLKHEFHRAG IGFSSPALCS VQLSRCLYPQ FYKHSLDSII ERLGIVVEDR HRAMADVSAL CDYLEYSLSE HGVEAWIRQC FRLMNPKPLP AALPERLREQ LYGLPDGMGV LACFDGGGKV NYIGTFERVY SEISALLDSG KAPFDWCNTE EVRFFPALGS LHAYKIKAEL VGRYHSDCYV SAKNLLKTFT TVRFEKGSDG MLNAKTAALK NGVTDNPPTG LFANKKAARR ALSSWAETYG LCPAAAGILP DGYAEDEPCP VYVSGRCDKA CGRSDEQVLA FAHKLPVLDW GKMHEVEITE TDPLTGEKVV LHGMGGALEM DDGLWYFDKD LPDAFKAKFK TDRKNIKEIG // ID Q9JZ08_NEIMB Unreviewed; 516 AA. AC Q9JZ08; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41720.1}; GN OrderedLocusNames=NMB1345 {ECO:0000313|EMBL:AAF41720.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41720.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41720.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41720.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41720.1; -; Genomic_DNA. DR PIR; E81092; E81092. DR RefSeq; NP_274364.1; NC_003112.2. DR RefSeq; WP_002244153.1; NC_003112.2. DR STRING; 122586.NMB1345; -. DR PaxDb; Q9JZ08; -. DR EnsemblBacteria; AAF41720; AAF41720; NMB1345. DR GeneID; 903767; -. DR KEGG; nme:NMB1345; -. DR PATRIC; 20358341; VBINeiMen85645_1682. DR eggNOG; ENOG4106AMM; Bacteria. DR eggNOG; COG5339; LUCA. DR HOGENOM; HOG000218994; -. DR OMA; PAFDYEE; -. DR OrthoDB; EOG6P8TJH; -. DR BioCyc; NMEN122586:GHGG-1383-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010352; DUF945. DR Pfam; PF06097; DUF945; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 516 AA; 57143 MW; D5904F3F9B6CA7C1 CRC64; MKKPLISVAA ALLGVALGTP YYLGVKAEES LTQQQKILQE TGFLTVESHQ YERGWFTSME TTVIRLKPEL LNNARKYLPD NLKTVLEQPV TLVNHITHGP FAGGFGTQAY IETEFKYAPE TEKVLERFFG KQVPASLANT VYFNGSGKME VSVPAFDYEE LSGIRLHWEG LTGETVYQKG FKSYRNGYDA PLFKIKLADK GDAAFEKVHF DSETSDGINP LALGSSNLTL EKFSLEWKEG VDYNVKLNEL VNLVTDLQIG AFINPNGSIA PSKIEVGKLA FSTKTGESGA FINSEGQFRF DTLVYGDEKY GPLDIHIAAE HLDASALTVL KRKFAQISAK KMTEEQIRND LIAAVKGEAS GLFTNNPVLD IKTFRFTLPS GKIDVGGKIM FKDMKKEDLN QLGLMLKKTE ADIRMSIPQK MLEDLAVSQA GNIFSVNAED EAEGRASLDD INETLRLMVD STVQSMAREK YLTLNGDQID TAISLKNNQL KLNGKTLQNE PEPDFDEGGM VSEPQQ // ID Q7DDC2_NEIMB Unreviewed; 212 AA. AC Q7DDC2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxyphosphogluconate aldolase {ECO:0000313|EMBL:AAF41758.1}; DE EC=4.1.2.- {ECO:0000313|EMBL:AAF41758.1}; DE EC=4.1.3.16 {ECO:0000313|EMBL:AAF41758.1}; GN Name=eda {ECO:0000313|EMBL:AAF41758.1}; GN OrderedLocusNames=NMB1394 {ECO:0000313|EMBL:AAF41758.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41758.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41758.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41758.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41758.1; -; Genomic_DNA. DR PIR; B81088; B81088. DR RefSeq; NP_274408.1; NC_003112.2. DR RefSeq; WP_002225133.1; NC_003112.2. DR ProteinModelPortal; Q7DDC2; -. DR STRING; 122586.NMB1394; -. DR PaxDb; Q7DDC2; -. DR EnsemblBacteria; AAF41758; AAF41758; NMB1394. DR GeneID; 903816; -. DR KEGG; nme:NMB1394; -. DR PATRIC; 20358475; VBINeiMen85645_1749. DR eggNOG; ENOG4108UHU; Bacteria. DR eggNOG; COG0800; LUCA. DR HOGENOM; HOG000233114; -. DR KO; K01625; -. DR OMA; KFFPAEY; -. DR OrthoDB; EOG67DPKT; -. DR BioCyc; NMEN122586:GHGG-1432-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR000887; Aldlse_KDPG_KHG. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR031337; KDPG/KHG_AS_1. DR InterPro; IPR031338; KDPG/KHG_AS_2. DR Pfam; PF01081; Aldolase; 1. DR TIGRFAMs; TIGR01182; eda; 1. DR PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1. DR PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF41758.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 212 AA; 21921 MW; 697EE92F9AC874FF CRC64; MSKLTPREIL TAGAVVPVMA IDDLSTAIDL SHALVEGGIP TLEITLRTPV GLDAIRLIAK EVPNAIVGAG TVTNPEQLKA VEDAGAVFAI SPGLHESLAK AGHNSGIPLI PGVATPGEIQ LALEHGIDTL KLFPAEVVGG KAMLKALYGP YADVRFCPTG GISLATAPEY LALPNVLCVG GSWLTPKEAV KNKDWDTITR LAKEAAALKP KA // ID Q9K117_NEIMB Unreviewed; 473 AA. AC Q9K117; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167}; DE EC=1.3.99.22 {ECO:0000256|PIRNR:PIRNR000167}; GN Name=hemN {ECO:0000313|EMBL:AAF40819.1}; GN OrderedLocusNames=NMB0379 {ECO:0000313|EMBL:AAF40819.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40819.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40819.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40819.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L- CC methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 CC 5'-deoxyadenosine. {ECO:0000256|PIRNR:PIRNR000167}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRNR:PIRNR000167, CC ECO:0000256|PIRSR:PIRSR000167-2}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III CC (AdoMet route): step 1/1. {ECO:0000256|PIRNR:PIRNR000167}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000167}. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III CC oxidase family. {ECO:0000256|PIRNR:PIRNR000167}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40819.1; -; Genomic_DNA. DR PIR; H81204; H81204. DR RefSeq; NP_273428.1; NC_003112.2. DR RefSeq; WP_002216474.1; NC_003112.2. DR ProteinModelPortal; Q9K117; -. DR STRING; 122586.NMB0379; -. DR PaxDb; Q9K117; -. DR EnsemblBacteria; AAF40819; AAF40819; NMB0379. DR GeneID; 902494; -. DR KEGG; nme:NMB0379; -. DR PATRIC; 20355923; VBINeiMen85645_0479. DR eggNOG; ENOG4105D4P; Bacteria. DR eggNOG; COG0635; LUCA. DR HOGENOM; HOG000257214; -. DR KO; K02495; -. DR OMA; CEIDPRH; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; NMEN122586:GHGG-401-MONOMER; -. DR UniPathway; UPA00251; UER00323. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR004558; Coprogen_oxidase_HemN. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR010723; HemN_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF000167; HemN; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00538; hemN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167- KW 2}; Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000167}; KW Iron {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2}; KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR000167, KW ECO:0000256|PIRSR:PIRSR000167-2}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000167, KW ECO:0000256|PIRSR:PIRSR000167-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000167}; KW Porphyrin biosynthesis {ECO:0000256|PIRNR:PIRNR000167}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167, KW ECO:0000256|PIRSR:PIRSR000167-1}. FT DOMAIN 67 288 Elp3. {ECO:0000259|SMART:SM00729}. FT REGION 129 130 S-adenosyl-L-methionine 2 binding. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT METAL 77 77 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR000167-2}. FT METAL 81 81 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR000167-2}. FT METAL 84 84 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR000167-2}. FT BINDING 71 71 S-adenosyl-L-methionine 1. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT BINDING 83 83 S-adenosyl-L-methionine 2; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000167- FT 1}. FT BINDING 128 128 S-adenosyl-L-methionine 1; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT BINDING 161 161 S-adenosyl-L-methionine 1. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT BINDING 188 188 S-adenosyl-L-methionine 2. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT BINDING 200 200 S-adenosyl-L-methionine 2. FT {ECO:0000256|PIRSR:PIRSR000167-1}. FT BINDING 225 225 S-adenosyl-L-methionine 2. FT {ECO:0000256|PIRSR:PIRSR000167-1}. SQ SEQUENCE 473 AA; 54254 MW; 1E1A110A4D882681 CRC64; MKIIQIQNNH NVNDDRPEFD RALIASLPAS GPRYTSYPTA DRFHDGFREG EYIKALHLRG MGALNKPLSL YIHIPFCNTI CYYCGCNKII TKDKSRADAY IEYLEKEMEL LAPHLNGRHQ LAQLHFGGGT PTFLSDEQIE RVFRMIRKHF ELIPTGEYSI EIDPRKVSRD TVLMLGRLGF NRMSIGIQDF DPKVQAAVNR IQSYEETKEV IDAAREAGFK SVSVDLIYGL PHQTSESIKT TIDTVLSLDP DRLALYHYAH LPHVFKPQRR IDTAAVPDSE EKLDMLQYCV QTLTERGYVF IGMDHFAKPD DELSIALKEG FLQRNFQGYS TYADCDLVAI GVSSIGKIGS TYSQNERDID AYYAAIDEGR LPIMRGYQLN QDDILRRNII QDLMCRFALD YRIYESMFGI PFDRYFKDEL ADLEKLAGLG LVRLNSHGLT VTPKGRFLIR NIAMVFDYHL RHKETKAKYS QTV // ID Q9JYK9_NEIMB Unreviewed; 157 AA. AC Q9JYK9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41890.1}; GN OrderedLocusNames=NMB1535 {ECO:0000313|EMBL:AAF41890.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41890.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41890.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41890.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41890.1; -; Genomic_DNA. DR PIR; C81072; C81072. DR STRING; 122586.NMB1535; -. DR PaxDb; Q9JYK9; -. DR EnsemblBacteria; AAF41890; AAF41890; NMB1535. DR BioCyc; NMEN122586:GHGG-1576-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 157 AA; 18931 MW; 3572A72FD36368BF CRC64; MFTQIPVYIL CAMPSNQVCQ CLRQFGMPFF QLCRRRTETL QRSLTQMQGI GFRRFFRFRD QPDRNRAYRS IKPCQLRQYR RCNHFQARCR HIVCRQKDKP AVFDTCRLKM RVQVGRQQFF HGGIQPPPLS RLFQKSGKQR VPPAQLFQIH KTYTQKD // ID Q9JZ52_NEIMB Unreviewed; 384 AA. AC Q9JZ52; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Ribonucleoside-diphosphate reductase, beta subunit {ECO:0000313|EMBL:AAF41664.1}; DE EC=1.17.4.1 {ECO:0000313|EMBL:AAF41664.1}; GN Name=nrdB {ECO:0000313|EMBL:AAF41664.1}; GN OrderedLocusNames=NMB1288 {ECO:0000313|EMBL:AAF41664.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41664.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41664.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41664.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41664.1; -; Genomic_DNA. DR PIR; G81100; G81100. DR RefSeq; NP_274308.2; NC_003112.2. DR ProteinModelPortal; Q9JZ52; -. DR SMR; Q9JZ52; 9-350. DR STRING; 122586.NMB1288; -. DR PaxDb; Q9JZ52; -. DR EnsemblBacteria; AAF41664; AAF41664; NMB1288. DR GeneID; 903710; -. DR KEGG; nme:NMB1288; -. DR PATRIC; 20358203; VBINeiMen85645_1613. DR eggNOG; ENOG4105E05; Bacteria. DR eggNOG; COG0208; LUCA. DR HOGENOM; HOG000278087; -. DR KO; K00526; -. DR OMA; LEPMFLG; -. DR OrthoDB; EOG6J48J7; -. DR BioCyc; NMEN122586:GHGG-1326-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR000358; RNR_small. DR InterPro; IPR030475; RNR_small_AS. DR PANTHER; PTHR23409; PTHR23409; 2. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41664.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 384 AA; 44046 MW; F848C1375384DE5B CRC64; MSCEHLTMSY STFPKTKNDA LNEPMFFGQP VNVARYDQQK YEVFEKLIEK QLSFFWRPEE IDVSRDRIDY ANLPEHEKHI FISNLKYQTL LDSIQGRSPN VALLPLVSIP ELETWIETWS FSETIHSRSY THIIRNIVND PSVVFDDIVE NEYITARAED IACYYDDLIE YTQYYNLLGE GVHNVGGKPV TVSLRGLKKK LYLCLMCVNV LEAIRFYVSF ACSFAFAERE LMEGNAKIIK LIARDEALHL TGTQHMLNLM RSGVDDSEMA EIAAELQDEC FQLFKKAAEQ EKEWAAYLFK DGSMIGLNKE ILSQYVEYIT NLRMQAVGLP AGFEGANQNP IPWINAWLSS DNVQVAPQEV EISSYLIGQI DSEVNTDDLG DFEL // ID Q9JXW5_NEIMB Unreviewed; 128 AA. AC Q9JXW5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42192.1}; GN OrderedLocusNames=NMB1858 {ECO:0000313|EMBL:AAF42192.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42192.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42192.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42192.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42192.1; -; Genomic_DNA. DR PIR; G81035; G81035. DR RefSeq; NP_274854.1; NC_003112.2. DR RefSeq; WP_002244305.1; NC_003112.2. DR PaxDb; Q9JXW5; -. DR EnsemblBacteria; AAF42192; AAF42192; NMB1858. DR GeneID; 903240; -. DR KEGG; nme:NMB1858; -. DR HOGENOM; HOG000027869; -. DR OMA; HYRFRRE; -. DR OrthoDB; EOG6KDM08; -. DR BioCyc; NMEN122586:GHGG-1914-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 128 AA; 15323 MW; B8DAAB888887F79B CRC64; MTYSGLNLNQ DKATKPQTVQ IVRQGEATLY WFLLIHYRFR RERRETQSLL MTRNTLKFIP FWSYKHITYA IFLYSRLPEN SGQEYLTQRK AEKATKNNLH LSRLVSPTLG VQTIQSFRLP LFVYKINF // ID Q9JZS6_NEIMB Unreviewed; 163 AA. AC Q9JZS6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41323.1}; GN OrderedLocusNames=NMB0915 {ECO:0000313|EMBL:AAF41323.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41323.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41323.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41323.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41323.1; -; Genomic_DNA. DR PIR; E81142; E81142. DR RefSeq; NP_273955.1; NC_003112.2. DR RefSeq; WP_002217437.1; NC_003112.2. DR STRING; 122586.NMB0915; -. DR PaxDb; Q9JZS6; -. DR EnsemblBacteria; AAF41323; AAF41323; NMB0915. DR GeneID; 903036; -. DR KEGG; nme:NMB0915; -. DR PATRIC; 20357267; VBINeiMen85645_1147. DR eggNOG; ENOG4106GS7; Bacteria. DR eggNOG; ENOG4111JCX; LUCA. DR HOGENOM; HOG000220736; -. DR OMA; YDIAEPL; -. DR OrthoDB; EOG6C5RPM; -. DR BioCyc; NMEN122586:GHGG-953-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031876; DUF4760. DR Pfam; PF15956; DUF4760; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 163 AA; 18812 MW; 7C6DE45A02B17475 CRC64; MFWQLTVVSV TAVIALGTIF INKKTSKQKA TLDVILNDYQ DAQFVEADNH ISPYIRGTAV DDNNARIDLY EIYQNKGGQW EKERGHLLTV INRHEFYACA INSGVLDEDL FKRLHCTNFI KLWNAVSPLV MKIREEERKD TIFRELEILV ALWKANPLKA SDL // ID Q9JZC9_NEIMB Unreviewed; 443 AA. AC Q9JZC9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Putative phage virion protein {ECO:0000313|EMBL:AAF41500.1}; GN OrderedLocusNames=NMB1109 {ECO:0000313|EMBL:AAF41500.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41500.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41500.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41500.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41500.1; -; Genomic_DNA. DR PIR; B81122; B81122. DR RefSeq; NP_274140.1; NC_003112.2. DR RefSeq; WP_002225234.1; NC_003112.2. DR STRING; 122586.NMB1109; -. DR PaxDb; Q9JZC9; -. DR EnsemblBacteria; AAF41500; AAF41500; NMB1109. DR GeneID; 903531; -. DR KEGG; nme:NMB1109; -. DR PATRIC; 20357784; VBINeiMen85645_1408. DR eggNOG; ENOG4105EKM; Bacteria. DR eggNOG; COG4228; LUCA. DR HOGENOM; HOG000042963; -. DR OMA; QIAHAFY; -. DR OrthoDB; EOG6W19M8; -. DR BioCyc; NMEN122586:GHGG-1145-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009826; DNA_circ_N. DR Pfam; PF07157; DNA_circ_N; 1. DR ProDom; PD332323; DNA_circ_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 93 DNA_circ_N. {ECO:0000259|Pfam:PF07157}. SQ SEQUENCE 443 AA; 47767 MW; 844ECA85C1A452CA CRC64; MSGWHTLLQD ASYKGVGFDI EVVDESNGKA LAEHARPFVQ GIDLEDMGMT GRQVQINAVF WGKGYAGRLK KLLDALEQPG GGVLVHPVWG RMHNMIAASW SYRHEADYVD YAGIDITFRE AAEAQEIFVF ENAFLVELEA LIANIDTYRE AAIGFVDAVL AVDAGVSALW GSALGIWSAA SGTFGAVRRL FDLDKIAFPD RGGYSAAAFK NGSAKLFADI SVMVDTGIRR EAGLADNAMH HAGWSPRQRF DGAAAVADRA AAIPDNLLTG RFSDGLQNRL NRLTAKQVQP VAQAVRLLST SSLLSVATAL IEAHGEEMTA PDLIEVNRAM RRRMQAEIAA LRAVQTAAAE SGGLTANAVY TEAYQTAESL RAAAGRLNAL VAAVINQKPP LIVRQAPIDG TIHQIAHEFY GDIARAAELV RLNPHIHHPA FIKRGTLVNS YAK // ID Q9JY73_NEIMB Unreviewed; 445 AA. AC Q9JY73; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Transporter {ECO:0000256|RuleBase:RU003732}; GN OrderedLocusNames=NMB1707 {ECO:0000313|EMBL:AAF42055.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42055.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42055.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42055.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) family. {ECO:0000256|RuleBase:RU003732}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42055.1; -; Genomic_DNA. DR PIR; F81050; F81050. DR RefSeq; NP_274711.1; NC_003112.2. DR RefSeq; WP_002224972.1; NC_003112.2. DR ProteinModelPortal; Q9JY73; -. DR STRING; 122586.NMB1707; -. DR PaxDb; Q9JY73; -. DR EnsemblBacteria; AAF42055; AAF42055; NMB1707. DR GeneID; 903394; -. DR KEGG; nme:NMB1707; -. DR PATRIC; 20359371; VBINeiMen85645_2191. DR eggNOG; ENOG4105C8J; Bacteria. DR eggNOG; COG0733; LUCA. DR HOGENOM; HOG000033129; -. DR KO; K03308; -. DR OMA; WIGYLGM; -. DR OrthoDB; EOG6PGK51; -. DR BioCyc; NMEN122586:GHGG-1763-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro. DR InterPro; IPR000175; Na/ntran_symport. DR PANTHER; PTHR11616; PTHR11616; 1. DR Pfam; PF00209; SNF; 2. DR PRINTS; PR00176; NANEUSMPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Symport {ECO:0000256|RuleBase:RU003732}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003732}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 106 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 239 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 321 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341 362 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 374 398 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 419 439 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 445 AA; 48376 MW; C24270848C92B853 CRC64; MSNHTSWSSK IGFVLAAAGS AIGLGAIWKF PYTAGTNGGA VFFLLFLIFT ILVALPVQLA EFYIGRTGGK NAVDSFRVLR PGTQWLWVGR MGVAACFILL SFYSVVGGWV LNYVVHSFTG AVHTGADFEA LFGATISNPA GSLSYQALFM LITVWVVKGG ISDGIEKANR YLMPGLFILF IALAIRSLTL PGAMEGVSFL LKPNWSYFKA DTMITALGQA FFALSIGVSA MITYASYLGK DQDMFRSGHT IMWMNLLVSL LAGLVIFPAV FAFGFEPSQG PGLIFIVLPA VFMKMPFGTV LFAVFMLLVV FATLTSAFSM LETVIASTIR QDERKRKKHT WLIGTAIFII GIPSALSFGV WGEFKVFGKT IFDLWDYVIS AVIMPIGALS VSIFTAWIQD KQSVLKDAGA GSTVPRAVLL LWLNTLRYLA PIAIIIVFIN SLDIL // ID Q9JXK9_NEIMB Unreviewed; 208 AA. AC Q9JXK9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42319.1}; GN OrderedLocusNames=NMB1992 {ECO:0000313|EMBL:AAF42319.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42319.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42319.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42319.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42319.1; -; Genomic_DNA. DR PIR; G81018; G81018. DR RefSeq; NP_274984.1; NC_003112.2. DR RefSeq; WP_002258733.1; NC_003112.2. DR ProteinModelPortal; Q9JXK9; -. DR STRING; 122586.NMB1992; -. DR PaxDb; Q9JXK9; -. DR EnsemblBacteria; AAF42319; AAF42319; NMB1992. DR GeneID; 904137; -. DR KEGG; nme:NMB1992; -. DR PATRIC; 20360081; VBINeiMen85645_2545. DR eggNOG; ENOG4108SME; Bacteria. DR eggNOG; ENOG4111GTD; LUCA. DR HOGENOM; HOG000146210; -. DR OMA; FRELWQA; -. DR OrthoDB; EOG6C5RS9; -. DR BioCyc; NMEN122586:GHGG-2049-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR003814; FwdEsu_dom. DR Pfam; PF02663; FmdE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 46 197 FmdE. {ECO:0000259|Pfam:PF02663}. SQ SEQUENCE 208 AA; 22294 MW; 0F50BAE1810C6B9F CRC64; MTQEHFPSFF NQAPTITVQD ALAEFLGAAE NGILTYRYAD AVRLCGHSCP TVAGAYLMVI KGLKALYGEE LPERGGIEAF MQGARDEGTV GVTASVVQLL TGAAPETGFG GIGMQGRFAR RHLLSFGVGE INGTLTLRRK DNGKTVAVGL NAALQPFAPE MRDIMPKAVS GSASAEELER FGQLWQARVK AFLTESADDP QFVIVREV // ID Q9JYJ4_NEIMB Unreviewed; 127 AA. AC Q9JYJ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:AAF41912.1}; DE EC=2.7.1.107 {ECO:0000313|EMBL:AAF41912.1}; GN Name=dgkA {ECO:0000313|EMBL:AAF41912.1}; GN OrderedLocusNames=NMB1558 {ECO:0000313|EMBL:AAF41912.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41912.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41912.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41912.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41912.1; -; Genomic_DNA. DR PIR; C81069; C81069. DR RefSeq; NP_274565.1; NC_003112.2. DR RefSeq; WP_002216810.1; NC_003112.2. DR STRING; 122586.NMB1558; -. DR PaxDb; Q9JYJ4; -. DR EnsemblBacteria; AAF41912; AAF41912; NMB1558. DR GeneID; 904121; -. DR KEGG; nme:NMB1558; -. DR PATRIC; 20358970; VBINeiMen85645_2004. DR eggNOG; ENOG41080IJ; Bacteria. DR eggNOG; COG0818; LUCA. DR HOGENOM; HOG000014819; -. DR KO; K00901; -. DR OMA; IGHEIHP; -. DR OrthoDB; EOG60W7XM; -. DR BioCyc; NMEN122586:GHGG-1599-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. DR InterPro; IPR000829; Diacylglycerol_kinase_prok. DR Pfam; PF01219; DAGK_prokar; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000313|EMBL:AAF41912.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41912.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 126 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 127 AA; 13758 MW; F8C9C6624B5C4D32 CRC64; MEPSSYAAEK KGKGGIRRVI NAFGYSIDGI AAAYRYEAAF RQVLWLNVLL VCAAFFWVSE TAVRLPLIIA SFVSVIVELF NTAVEAAVDH TSTEKHELAK LAKDAGSAAQ LFAMLMLAAV WLSALFG // ID Q9JXX0_NEIMB Unreviewed; 90 AA. AC Q9JXX0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42187.1}; GN OrderedLocusNames=NMB1853 {ECO:0000313|EMBL:AAF42187.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42187.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42187.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42187.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42187.1; -; Genomic_DNA. DR PIR; B81035; B81035. DR RefSeq; NP_274849.1; NC_003112.2. DR RefSeq; WP_010981000.1; NC_003112.2. DR STRING; 122586.NMB1853; -. DR PaxDb; Q9JXX0; -. DR EnsemblBacteria; AAF42187; AAF42187; NMB1853. DR GeneID; 903245; -. DR KEGG; nme:NMB1853; -. DR BioCyc; NMEN122586:GHGG-1909-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 90 AA; 10093 MW; 9230DF73F295946C CRC64; MPEISTAGIF QAAFIARQVE QTPRTFFQTT FELIGRECAA RHARGGLGLQ GKWRTRAYVP HIPYIRATAC YDTGVSIYKL GFSKPNILDN // ID Q9JY39_NEIMB Unreviewed; 454 AA. AC Q9JY39; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42100.1}; GN OrderedLocusNames=NMB1759 {ECO:0000313|EMBL:AAF42100.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42100.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42100.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42100.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42100.1; -; Genomic_DNA. DR PIR; F81046; F81046. DR RefSeq; NP_274759.1; NC_003112.2. DR RefSeq; WP_002222955.1; NC_003112.2. DR STRING; 122586.NMB1759; -. DR PaxDb; Q9JY39; -. DR EnsemblBacteria; AAF42100; AAF42100; NMB1759. DR GeneID; 903339; -. DR KEGG; nme:NMB1759; -. DR PATRIC; 20359485; VBINeiMen85645_2248. DR eggNOG; ENOG4107R3N; Bacteria. DR eggNOG; COG3177; LUCA. DR HOGENOM; HOG000126103; -. DR OMA; YWLFEYM; -. DR OrthoDB; EOG60PHCH; -. DR BioCyc; NMEN122586:GHGG-1814-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR003812; Fido. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02661; Fic; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 189 342 Fido. {ECO:0000259|PROSITE:PS51459}. FT COILED 347 385 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 454 AA; 52284 MW; 2D3F1FE58B5D3517 CRC64; MQHLTERMTQ IAKLLNSSAN NPDIDIPDFL TEIKDYSEFS VTDENGTYLH WDKFRRIHTE DTRMKWRAVK ESRKKIQKPI DFPFEHQFWF CIPDSLQARL HLIDKSCGSS IGTSSLGGFG RSEQNRFLLK SLIMEEAITS AQLEGAATTR KVAKDMLKSQ RKPKTKDEIM IVNNYHLMKK AVELKNTPLS VEMILDLHRI ATSNAIENKA EPGQFRQDDE IFIADINGNS LYQPPPHGQV HTLMEEVCAF ANNTYDGVEN PFIHPVVQAI ILHFLIGYIH PFGDGNGRTA RALFYWFMLK NGYWLFEYIS ISRLLKNAPA QYAKSYLYAE TDDLDLTYFI YYQCDIIKRA VADLEHYISD KQKHQQEFKA AIAQYTEKIG KLNQRQIGIL QKAVEESGKI FTAQEIANQY GISLNTARSD LSKLGEYRFL VPFKSGNALE YVAPQDLLER LEKK // ID Q9K1A6_NEIMB Unreviewed; 259 AA. AC Q9K1A6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=Geranyltranstransferase {ECO:0000313|EMBL:AAF40715.1}; DE EC=2.5.1.10 {ECO:0000313|EMBL:AAF40715.1}; GN Name=ispA {ECO:0000313|EMBL:AAF40715.1}; GN OrderedLocusNames=NMB0261 {ECO:0000313|EMBL:AAF40715.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40715.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40715.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40715.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000256|RuleBase:RU004466}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40715.1; -; Genomic_DNA. DR PIR; F81217; F81217. DR RefSeq; NP_273317.1; NC_003112.2. DR RefSeq; WP_010980766.1; NC_003112.2. DR ProteinModelPortal; Q9K1A6; -. DR STRING; 122586.NMB0261; -. DR PaxDb; Q9K1A6; -. DR EnsemblBacteria; AAF40715; AAF40715; NMB0261. DR GeneID; 902372; -. DR KEGG; nme:NMB0261; -. DR PATRIC; 20355600; VBINeiMen85645_0324. DR eggNOG; ENOG4105CTB; Bacteria. DR eggNOG; COG0142; LUCA. DR HOGENOM; HOG000009101; -. DR KO; K00795; -. DR OMA; EPAKYSL; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; NMEN122586:GHGG-276-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU004466, KW ECO:0000313|EMBL:AAF40715.1}. SQ SEQUENCE 259 AA; 27505 MW; E73CCD28B38F656A CRC64; MRYAALDGGK RLRPMLVLAA SELGEAVHEA VEQAMAAIEM IHVYSLVHDD MPAMDNDSLR RGKPTCHIKY GEATALLTGD ALQTQAFDVL SRPTELPAAR QLAMLSVLAK AGGSRGMAGG QAIDLANVGK QMVQADLEQM HSLKTGALIR AAVLLGATAC PDLSDAELSV LDAYAAKLGL AFQVIDDVLD CEADTATLGK TAGKDADNDK PTYVKLMGLE AARSYAHKLV AEAVALLEPF GDKALRLRQL AEFAVARKY // ID Q4W563_NEIMB Unreviewed; 199 AA. AC Q4W563; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 42. DE SubName: Full=PilN protein {ECO:0000313|EMBL:AAY52169.1}; GN Name=pilN {ECO:0000313|EMBL:AAY52169.1}; GN OrderedLocusNames=NMB1809 {ECO:0000313|EMBL:AAY52169.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52169.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52169.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52169.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52169.1; -; Genomic_DNA. DR RefSeq; NP_274806.1; NC_003112.2. DR RefSeq; WP_002214520.1; NC_003112.2. DR STRING; 122586.NMB1809; -. DR PaxDb; Q4W563; -. DR EnsemblBacteria; AAY52169; AAY52169; NMB1809. DR GeneID; 903123; -. DR KEGG; nme:NMB1809; -. DR PATRIC; 20359587; VBINeiMen85645_2299. DR eggNOG; ENOG4105N6D; Bacteria. DR eggNOG; COG3166; LUCA. DR HOGENOM; HOG000218781; -. DR KO; K02663; -. DR OMA; LFNFTIR; -. DR OrthoDB; EOG6W45SQ; -. DR BioCyc; NMEN122586:GHGG-1864-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007813; PilN. DR Pfam; PF05137; PilN; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 46 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 74 111 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 199 AA; 22257 MW; 03EFECBE7FEF03B5 CRC64; MNNLIKINLL PYREEMNKRK QQQFKTLMYG AVLTGVAAVA ATYLFIDNMI NNQSERNTLL ETSIAHLDTE LSEIQKLKQE KDAFLIKKNK IEELQLKRLQ AAKILDSLNE AVPGSTYLTS LDAVTADSYR LSGRTSSDNR VAAMMRAMPN TGIFKQPELL SIKKNNSHQE FTLQATLQPI VKAAESKENP ASGNAQEAN // ID Q7DDR8_NEIMB Unreviewed; 132 AA. AC Q7DDR8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40742.1}; GN OrderedLocusNames=NMB0291 {ECO:0000313|EMBL:AAF40742.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40742.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40742.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40742.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40742.1; -; Genomic_DNA. DR PIR; B81215; B81215. DR RefSeq; NP_273345.1; NC_003112.2. DR RefSeq; WP_002216361.1; NC_003112.2. DR STRING; 122586.NMB0291; -. DR PaxDb; Q7DDR8; -. DR EnsemblBacteria; AAF40742; AAF40742; NMB0291. DR GeneID; 902402; -. DR KEGG; nme:NMB0291; -. DR PATRIC; 20355682; VBINeiMen85645_0365. DR eggNOG; ENOG4105MGM; Bacteria. DR eggNOG; COG2259; LUCA. DR HOGENOM; HOG000198397; -. DR KO; K15977; -. DR OMA; GFPASQM; -. DR OrthoDB; EOG69SKFR; -. DR BioCyc; NMEN122586:GHGG-306-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032808; DoxX. DR Pfam; PF07681; DoxX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 123 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 132 AA; 13901 MW; 71089A3E31DE3C29 CRC64; MSDCCNRIQP VLLSVLRIVT AYLFLLHGTS KIFAFPIEMG SGSPGGLLLL AGILEIVGGI LLVLGLFARP AAFVLSGQMA VAYFMAHASG NALFPIANGG ESAVLFCFVF LYIAAAGGGA WSLDRLFFKR KA // ID Q9JZ50_NEIMB Unreviewed; 759 AA. AC Q9JZ50; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410}; DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410}; GN Name=nrdA {ECO:0000313|EMBL:AAF41667.1}; GN OrderedLocusNames=NMB1291 {ECO:0000313|EMBL:AAF41667.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41667.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41667.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41667.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}. CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + CC thioredoxin. {ECO:0000256|RuleBase:RU003410}. CC -!- PATHWAY: Genetic information processing; DNA replication. CC {ECO:0000256|RuleBase:RU003410}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase CC large chain family. {ECO:0000256|RuleBase:RU003410}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41667.1; -; Genomic_DNA. DR PIR; B81101; B81101. DR RefSeq; NP_274311.1; NC_003112.2. DR RefSeq; WP_002222380.1; NC_003112.2. DR ProteinModelPortal; Q9JZ50; -. DR SMR; Q9JZ50; 7-739. DR STRING; 122586.NMB1291; -. DR PaxDb; Q9JZ50; -. DR EnsemblBacteria; AAF41667; AAF41667; NMB1291. DR GeneID; 903713; -. DR KEGG; nme:NMB1291; -. DR PATRIC; 20358209; VBINeiMen85645_1616. DR eggNOG; ENOG4107QYD; Bacteria. DR eggNOG; COG0209; LUCA. DR HOGENOM; HOG000278076; -. DR KO; K00525; -. DR OMA; YELLWQM; -. DR OrthoDB; EOG6J48HC; -. DR BioCyc; NMEN122586:GHGG-1329-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00511196}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA replication {ECO:0000256|RuleBase:RU003410}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00511196}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003410, KW ECO:0000313|EMBL:AAF41667.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 97 ATP-cone. {ECO:0000259|PROSITE:PS51161}. SQ SEQUENCE 759 AA; 85022 MW; 8200DB333F49ACCF CRC64; MNTPTDLKVT KRDGRLEAID LDKIHRVVTW AADGLENVSV SQVELKSHIQ FYNGIRTDDI HETIIKAAAD LISEDTPDYQ YLAARLAIFH LRKIAYGEYE PPHLYDHVKK LTDAGKYDRH ILEDYSREEF DELNAYIDHE RDMSFSYAAV KQLEGKYLVQ NRVTRQIYET PQFLYVLVAM CLFSKYPKEA RLGYVKRFYD AVSTFKVSLP TPIMSGVRTP TRQFSSCVLI ECDDSLDSIN ATTSAIVKYV SQRAGIGINA GRIRGLDSEI RGGEARHTGC IPFFKMFQAA VKSCSQGGVR GGAATLFYPL WHIEAESLLV LKNNRGVEDN RIRQLDYGVQ INRLLYTRLI KGGNITLFSP NEVPGLYEAF FADQDEFERL YTKYEQDPDI RKRIIPAADL FSTLMQERAG TGRIYIQNVD HCNTHSPFDP RVAPVHQSNL CMEIALPTKP LDNINDPNGE IALCTLSAFN LGALNSLDEL EGLADLTVRA LDALLDYQGY PVEAARTSTM GRRSLGIGVI NYAYYLAKNG VRYSDGSALG LTHRTFEAIQ YYLLKASANL AKEYGACTLF NQTVYSQGKL PIDTYKKDLD AVCGEPLHYD WESLRAEIVK YGLRNSTLTA LMPSETSSQI ANATNGIEPP RGLVTVKASK DGILKQVVPE FETLKNAYET LWQLPGNEGY LKLVGVMQKF VDQSISANTA YDPGKFEGGK VSMKQMLKDL LTAYKYGVKT LYYHNTRDGA DDTQTDIQDD GCAGGACKI // ID Q9K1F2_NEIMB Unreviewed; 57 AA. AC Q9K1F2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40659.1}; GN OrderedLocusNames=NMB0202 {ECO:0000313|EMBL:AAF40659.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40659.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40659.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40659.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40659.1; -; Genomic_DNA. DR PIR; D81226; D81226. DR STRING; 122586.NMB0202; -. DR PaxDb; Q9K1F2; -. DR EnsemblBacteria; AAF40659; AAF40659; NMB0202. DR HOGENOM; HOG000027899; -. DR OMA; FQIRTTH; -. DR OrthoDB; EOG6T1X1T; -. DR BioCyc; NMEN122586:GHGG-213-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 57 AA; 6579 MW; 09D98A81C220A5D6 CRC64; MLSRQLYRIS FSVETPPLGH LSFGAVESDF IWEGRNPFRI RATHRATLYV SSCVLKH // ID Q7DDJ8_NEIMB Unreviewed; 95 AA. AC Q7DDJ8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41364.1}; GN OrderedLocusNames=NMB0958 {ECO:0000313|EMBL:AAF41364.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41364.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41364.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41364.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41364.1; -; Genomic_DNA. DR PIR; E81137; E81137. DR RefSeq; NP_273996.1; NC_003112.2. DR RefSeq; WP_002225316.1; NC_003112.2. DR STRING; 122586.NMB0958; -. DR PaxDb; Q7DDJ8; -. DR EnsemblBacteria; AAF41364; AAF41364; NMB0958. DR GeneID; 903078; -. DR KEGG; nme:NMB0958; -. DR PATRIC; 20357397; VBINeiMen85645_1213. DR HOGENOM; HOG000218901; -. DR OrthoDB; EOG6C0198; -. DR BioCyc; NMEN122586:GHGG-995-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 95 AA; 10885 MW; 7A2B44F48BB61BF3 CRC64; MNKEIVGIFF IPAGIISMCM AALWQMYVMM TETYTLNRFK DKELVWRVAL LFISFSLAVY LLCPNSRKKG IVFFILGGGG AAMYLLARMW LPFSK // ID Q9JYG1_NEIMB Unreviewed; 85 AA. AC Q9JYG1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41953.1}; GN OrderedLocusNames=NMB1600 {ECO:0000313|EMBL:AAF41953.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41953.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41953.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41953.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41953.1; -; Genomic_DNA. DR PIR; C81064; C81064. DR RefSeq; NP_274606.1; NC_003112.2. DR RefSeq; WP_010980963.1; NC_003112.2. DR STRING; 122586.NMB1600; -. DR PaxDb; Q9JYG1; -. DR EnsemblBacteria; AAF41953; AAF41953; NMB1600. DR GeneID; 904282; -. DR KEGG; nme:NMB1600; -. DR BioCyc; NMEN122586:GHGG-1648-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 85 AA; 9533 MW; DAD78DA4355063B4 CRC64; MSGINARPTN SIFSNLCQIF SSLQGCLKTQ TPFSDGLFSL KSPYRSIRKH RRIIMEVTIS AIINGEFADQ YGKRGSQFNE NGMLI // ID Q9JXW7_NEIMB Unreviewed; 299 AA. AC Q9JXW7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Transcriptional regulator, LysR family {ECO:0000313|EMBL:AAF42190.1}; GN OrderedLocusNames=NMB1856 {ECO:0000313|EMBL:AAF42190.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42190.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42190.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42190.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3HHF, ECO:0000213|PDB:3HHG} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 89-299. RX PubMed=19474343; DOI=10.1093/nar/gkp445; RA Sainsbury S., Lane L.A., Ren J., Gilbert R.J., Saunders N.J., RA Robinson C.V., Stuart D.I., Owens R.J.; RT "The structure of CrgA from Neisseria meningitidis reveals a new RT octameric assembly state for LysR transcriptional regulators."; RL Nucleic Acids Res. 37:4545-4558(2009). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42190.1; -; Genomic_DNA. DR PIR; E81035; E81035. DR RefSeq; NP_274852.1; NC_003112.2. DR RefSeq; WP_002223018.1; NC_003112.2. DR PDB; 3HHF; X-ray; 2.30 A; A/B=89-299. DR PDB; 3HHG; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-299. DR PDBsum; 3HHF; -. DR PDBsum; 3HHG; -. DR ProteinModelPortal; Q9JXW7; -. DR STRING; 122586.NMB1856; -. DR PaxDb; Q9JXW7; -. DR DNASU; 903242; -. DR EnsemblBacteria; AAF42190; AAF42190; NMB1856. DR GeneID; 903242; -. DR KEGG; nme:NMB1856; -. DR PATRIC; 20359737; VBINeiMen85645_2374. DR eggNOG; ENOG4105HEI; Bacteria. DR eggNOG; ENOG410XRV0; LUCA. DR HOGENOM; HOG000233519; -. DR OMA; CESPLRI; -. DR OrthoDB; EOG6Q8J00; -. DR BioCyc; NMEN122586:GHGG-1912-MONOMER; -. DR EvolutionaryTrace; Q9JXW7; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3HHF, ECO:0000213|PDB:3HHG}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 1 60 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. SQ SEQUENCE 299 AA; 33033 MW; 3CC589E8636EAA90 CRC64; MKTNSEELTV FVQVVESGSF SRAAEQLAMA NSAVSRIVKR LEEKLGVNLL NRTTRQLSLT EEGAQYFRRA QRILQEMAAA ETEMLAVHEI PQGVLSVDSA MPMVLHLLAP LAAKFNERYP HIRLSLVSSE GYINLIERKV DIALRAGELD DSGLRARHLF DSRFRVIASP EYLAKHGTPQ STEELAGHQC LGFTEPGSLN TWAVLDAQGN PYKISPHFTA SSGEILRSLC LSGCGIVCLS DFLVDNDIAE GKLIPLLAEQ TSDKTHPFNA VYYSDKAVNL RLRVFLDFLV EELGNNLCG // ID Q9JXE7_NEIMB Unreviewed; 114 AA. AC Q9JXE7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42399.1}; GN OrderedLocusNames=NMB2081 {ECO:0000313|EMBL:AAF42399.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42399.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42399.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42399.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42399.1; -; Genomic_DNA. DR PIR; G81009; G81009. DR RefSeq; NP_275070.1; NC_003112.2. DR RefSeq; WP_002225716.1; NC_003112.2. DR STRING; 122586.NMB2081; -. DR PaxDb; Q9JXE7; -. DR EnsemblBacteria; AAF42399; AAF42399; NMB2081. DR GeneID; 903974; -. DR KEGG; nme:NMB2081; -. DR PATRIC; 20360330; VBINeiMen85645_2662. DR HOGENOM; HOG000218713; -. DR OMA; GWKGWRL; -. DR OrthoDB; EOG6D8BCD; -. DR BioCyc; NMEN122586:GHGG-2147-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 109 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 114 AA; 12684 MW; A53D3BB0F512D517 CRC64; MLPNKVLGKY DWNVDGKTGI GAAWVVAAFI LPMLVWAIFM LSRMQGWLAP TKANPIWALV WLLICLPCLL IASKCLGWKG WRRVVNIFAC LTVCAILSVP ASLLIAFTLR DLLK // ID Q9JYN9_NEIMB Unreviewed; 693 AA. AC Q9JYN9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Carbon starvation protein A {ECO:0000313|EMBL:AAF41849.1}; GN Name=cstA {ECO:0000313|EMBL:AAF41849.1}; GN OrderedLocusNames=NMB1493 {ECO:0000313|EMBL:AAF41849.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41849.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41849.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41849.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41849.1; -; Genomic_DNA. DR PIR; C81078; C81078. DR RefSeq; NP_274501.1; NC_003112.2. DR RefSeq; WP_002225081.1; NC_003112.2. DR STRING; 122586.NMB1493; -. DR PaxDb; Q9JYN9; -. DR EnsemblBacteria; AAF41849; AAF41849; NMB1493. DR GeneID; 903915; -. DR KEGG; nme:NMB1493; -. DR PATRIC; 20358752; VBINeiMen85645_1885. DR eggNOG; ENOG4105D22; Bacteria. DR eggNOG; COG1966; LUCA. DR HOGENOM; HOG000220271; -. DR KO; K06200; -. DR OMA; WGFSISA; -. DR OrthoDB; EOG6H1PW0; -. DR BioCyc; NMEN122586:GHGG-1533-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009267; P:cellular response to starvation; IEA:InterPro. DR InterPro; IPR025299; CstA_C. DR InterPro; IPR003706; CstA_N. DR Pfam; PF02554; CstA; 1. DR Pfam; PF13722; CstA_5TM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 189 209 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 384 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 465 489 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 510 529 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 541 566 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 573 593 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 640 660 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 32 407 CstA. {ECO:0000259|Pfam:PF02554}. FT DOMAIN 463 591 CstA_5TM. {ECO:0000259|Pfam:PF13722}. SQ SEQUENCE 693 AA; 74518 MW; A315785E6E985DC0 CRC64; MKSLKTFLIW GIVVLVGLAS FTTLALSRGE QVSAVWMVTA AISVYCIAYR FYSLYIANRV MRLDPDRLTP AERHNDGLDY VPTHKGVLFG HHFAAIAGAG PLVGPVLAAQ MGYLPGTLWI IFGVVFAGAV QDMMVLFVSM RRDGKSLGDI VKQELGTVPG VIASIGILMI MVIIMAVLAL IVVKALVHSP WGTFTIAATM PIALFMGIYT RYIRPGKIGE ISIVGFILLM LAVIYGEDVA KSSIGHWFDL DGIQLTWAIM IYGFVASVLP VWLLLTPRDY LSTFLKIGTI AALALGIVIV NPALQMPAVT HFIDGSGPVF SGALFPFLFI TIACGAVSGF HALISSGTTP KMLENETHVR MIGYGGMLME SFVAIMALAA AASLDPGVYF AMNSPAALIG TDANTAAEVI TTKLQFPVDA ATLLHTAKEV GENTILSRAG GAPTLAVGMA HIMSRLIPGE AMMAFWYHFA LLFEALFILT AVDAGTRVAR FMIQDLGSIF YKPFGNTDSI PANLIATFFA VALWGYFLYT GVTDPLGGIN SLWPLFGIAN QMLAGVALIM CAVVLIKMKR DRYVWVVLVP AVGVLFVTCY AGLQKLFHSD PRISFLAHAG KYSDALAKNE ILAPAKDIGE MAQIIFNDKI NAGLTILFLS VVVIVAAYGL RTALKARKVG WPTAKEIPAV YRDGKQPEAQ SEA // ID Q9JY50_NEIMB Unreviewed; 96 AA. AC Q9JY50; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42089.1}; GN OrderedLocusNames=NMB1746 {ECO:0000313|EMBL:AAF42089.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42089.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42089.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42089.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42089.1; -; Genomic_DNA. DR PIR; A81048; A81048. DR STRING; 122586.NMB1746; -. DR PaxDb; Q9JY50; -. DR EnsemblBacteria; AAF42089; AAF42089; NMB1746. DR BioCyc; NMEN122586:GHGG-1801-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 96 AA; 11433 MW; 2CA980D1C56265CE CRC64; MNKNERDFFY ISNSDLDKLS ESYPDRPLSY VFYCYLKETG LLKNFSMDKC HNFFNRINFN ESCFEIKFKD DSFFIIGNGK IDVSDSNNFF SVSFEC // ID Q7DDD9_NEIMB Unreviewed; 106 AA. AC Q7DDD9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAF41586.1}; GN OrderedLocusNames=NMB1204 {ECO:0000313|EMBL:AAF41586.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41586.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41586.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41586.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3VK0} RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS). RX PubMed=22373915; DOI=10.1093/nar/gks177; RA Wang H.C., Ko T.P., Wu M.L., Ku S.C., Wu H.J., Wang A.H.; RT "Neisseria conserved protein DMP19 is a DNA mimic protein that RT prevents DNA binding to a hypothetical nitrogen-response transcription RT factor."; RL Nucleic Acids Res. 40:5718-5730(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41586.1; -; Genomic_DNA. DR PIR; C81110; C81110. DR RefSeq; NP_274229.1; NC_003112.2. DR RefSeq; WP_002213537.1; NC_003112.2. DR PDB; 3VK0; X-ray; 1.88 A; A/B/C=1-106. DR PDBsum; 3VK0; -. DR ProteinModelPortal; Q7DDD9; -. DR STRING; 122586.NMB1204; -. DR PaxDb; Q7DDD9; -. DR EnsemblBacteria; AAF41586; AAF41586; NMB1204. DR GeneID; 903626; -. DR KEGG; nme:NMB1204; -. DR PATRIC; 20357997; VBINeiMen85645_1511. DR eggNOG; ENOG41067QW; Bacteria. DR eggNOG; ENOG410XUC3; LUCA. DR HOGENOM; HOG000225390; -. DR OMA; ERLNLMT; -. DR OrthoDB; EOG615VS0; -. DR BioCyc; NMEN122586:GHGG-1241-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3VK0}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 26 80 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 106 AA; 11994 MW; 81D92D565BEE91B6 CRC64; MMGNKLTLPA ELPDEQDLRA VLAYNMRLFR VNKGWSQEEL ARQCGLDRTY VSAVERKRWN IALSNIEKMA AALGVAAYQL LLPPQERLKL MTNSADTRQM PSESGI // ID Q7DDA0_NEIMB Unreviewed; 163 AA. AC Q7DDA0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Acetolactate synthase III, small subunit {ECO:0000313|EMBL:AAF41929.1}; DE EC=2.2.1.6 {ECO:0000313|EMBL:AAF41929.1}; GN Name=ilvH {ECO:0000313|EMBL:AAF41929.1}; GN OrderedLocusNames=NMB1576 {ECO:0000313|EMBL:AAF41929.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41929.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41929.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41929.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41929.1; -; Genomic_DNA. DR PIR; H81066; H81066. DR RefSeq; NP_274582.1; NC_003112.2. DR RefSeq; WP_002212817.1; NC_003112.2. DR ProteinModelPortal; Q7DDA0; -. DR SMR; Q7DDA0; 1-163. DR STRING; 122586.NMB1576; -. DR PaxDb; Q7DDA0; -. DR EnsemblBacteria; AAF41929; AAF41929; NMB1576. DR GeneID; 904183; -. DR KEGG; nme:NMB1576; -. DR PATRIC; 20359016; VBINeiMen85645_2027. DR eggNOG; ENOG4108ZP8; Bacteria. DR eggNOG; COG0440; LUCA. DR HOGENOM; HOG000046747; -. DR KO; K01653; -. DR OMA; PYGIREI; -. DR OrthoDB; EOG6X3W8W; -. DR BioCyc; NMEN122586:GHGG-1617-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:InterPro. DR InterPro; IPR004789; Acetalactate_synth_ssu. DR InterPro; IPR019455; Acetolactate_synth_ssu_C. DR InterPro; IPR002912; ACT_dom. DR Pfam; PF01842; ACT; 1. DR Pfam; PF10369; ALS_ss_C; 1. DR TIGRFAMs; TIGR00119; acolac_sm; 1. DR PROSITE; PS51671; ACT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41929.1}. FT DOMAIN 4 78 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 163 AA; 18293 MW; 26BBE3997056F992 CRC64; MRHILSVLIE NESGAMSRVV GLFSARDYNI DSLAVAPTED KTLSRMTIVT HGDEQVIEQI TKQLNKLIEV IKVVDLNESR FVERELMLVK VRAAGKDRDE FLRLTEIYRG SIIDVTDRSY TIEITGSTDK LDSFLETVGR AQILETVRTG AAGIGRGERI LKI // ID Q9JYB8_NEIMB Unreviewed; 205 AA. AC Q9JYB8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=ComE operon protein 1-related protein {ECO:0000313|EMBL:AAF42006.1}; GN OrderedLocusNames=NMB1657 {ECO:0000313|EMBL:AAF42006.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42006.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42006.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42006.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42006.1; -; Genomic_DNA. DR PIR; H81057; H81057. DR RefSeq; NP_274662.1; NC_003112.2. DR RefSeq; WP_010980970.1; NC_003112.2. DR ProteinModelPortal; Q9JYB8; -. DR STRING; 122586.NMB1657; -. DR PaxDb; Q9JYB8; -. DR EnsemblBacteria; AAF42006; AAF42006; NMB1657. DR GeneID; 903459; -. DR KEGG; nme:NMB1657; -. DR eggNOG; ENOG41083P1; Bacteria. DR eggNOG; COG1555; LUCA. DR HOGENOM; HOG000257817; -. DR OMA; THSENPR; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; NMEN122586:GHGG-1706-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00426; TIGR00426; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 131 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 135 154 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 165 184 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 205 AA; 22294 MW; D70318495A25E630 CRC64; MVPRLPIPNR TVKRLSADDS VVLPCESRSL PNTHSENPRL FGGFCFARKK CLLCPEKMSV MAGRHPYGVR SGLRRNGLKL WDIHFRMTRF IVARCGLLFA TLKGKTMKKM FVLFCMLFSC AFSLAAVNIN AASQQELEAL PGIGPAKAKA IAEYRAQNGA FKSVDDLTKV KGIGPAVLAK LKDQASVGAP APKAPAKPVL PADKK // ID Q9K142_NEIMB Unreviewed; 336 AA. AC Q9K142; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041}; DE EC=1.3.1.91 {ECO:0000256|HAMAP-Rule:MF_02041}; DE AltName: Full=U20-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02041}; DE AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000256|HAMAP-Rule:MF_02041}; GN Name=dusA {ECO:0000256|HAMAP-Rule:MF_02041}; GN OrderedLocusNames=NMB0348 {ECO:0000313|EMBL:AAF40791.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40791.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40791.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40791.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. Specifically modifies CC U20 and U20a in tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20) in tRNA + NAD(P)(+) = CC uracil(20) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) = CC uracil(20a) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02041, CC ECO:0000256|PIRNR:PIRNR006621}; CC -!- SIMILARITY: Belongs to the Dus family. DusA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- SIMILARITY: Belongs to the dus family. CC {ECO:0000256|PIRNR:PIRNR006621}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40791.1; -; Genomic_DNA. DR PIR; B81210; B81210. DR RefSeq; NP_273397.1; NC_003112.2. DR RefSeq; WP_002224882.1; NC_003112.2. DR ProteinModelPortal; Q9K142; -. DR STRING; 122586.NMB0348; -. DR PaxDb; Q9K142; -. DR EnsemblBacteria; AAF40791; AAF40791; NMB0348. DR GeneID; 902463; -. DR KEGG; nme:NMB0348; -. DR PATRIC; 20355843; VBINeiMen85645_0440. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR HOGENOM; HOG000259834; -. DR KO; K05539; -. DR OMA; IPPLDYD; -. DR OrthoDB; EOG6C8MTR; -. DR BioCyc; NMEN122586:GHGG-369-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02041; DusA_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004653; DusA. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00742; yjbN; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02041}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 17 19 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 212 214 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 234 235 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT ACT_SITE 100 100 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_02041, FT ECO:0000256|PIRSR:PIRSR006621-1}. FT BINDING 70 70 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 139 139 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 172 172 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 97 97 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 184 184 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 187 187 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 302 302 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 305 305 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. SQ SEQUENCE 336 AA; 37995 MW; C2B0AFFFB5D1E077 CRC64; MNDNTHTLPP RHLSVAPMLD WTDRHYRYLA RQITRNTWLY SEMVNAGAIV YGDKDRFLMF NEGEQPVALQ LGGSDPSDLA KAAKAAEAYG YNEVNLNCGC PSPRVQKGSF GACLMNEVGL VADCLNAMQD AVKIPVTVKH RIGVDRQTEY QTVADFVGTL RDKTACKTFI VHARNAWLDG LSPKENRDVP PLKYDYVYRL KQEFPGLEII INGGITTNEA IAGHLQHVDG VMVGREAYHN PMVMREWDRL FYGDTRSPIE YADLVQRLYT YSQAQIQAGR GTILRHIVRH SLGLMHGLKG ARTWRRMLSD ATLLKDNDGS LILEAWKEVE RANMRE // ID Q7DDQ0_NEIMB Unreviewed; 365 AA. AC Q7DDQ0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40913.1}; GN OrderedLocusNames=NMB0476 {ECO:0000313|EMBL:AAF40913.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40913.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40913.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40913.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40913.1; -; Genomic_DNA. DR PIR; G81194; G81194. DR RefSeq; NP_273523.1; NC_003112.2. DR RefSeq; WP_002212572.1; NC_003112.2. DR ProteinModelPortal; Q7DDQ0; -. DR STRING; 122586.NMB0476; -. DR PaxDb; Q7DDQ0; -. DR EnsemblBacteria; AAF40913; AAF40913; NMB0476. DR GeneID; 902592; -. DR KEGG; nme:NMB0476; -. DR PATRIC; 20356204; VBINeiMen85645_0623. DR eggNOG; ENOG41060RD; Bacteria. DR eggNOG; ENOG41123GS; LUCA. DR HOGENOM; HOG000219085; -. DR OMA; FINACYA; -. DR OrthoDB; EOG6JTC6K; -. DR BioCyc; NMEN122586:GHGG-500-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011006; CheY-like_superfamily. DR SUPFAM; SSF52172; SSF52172; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 365 AA; 40836 MW; F7ECAA5088007D92 CRC64; MEVQLPKIKT VRVMLAGMTA QQESVFKMAF KMHNTTRYET VSPSDGSAVP DLVLADTDAE GGFELWKELA ERYKDIPVAV CSEKVPDSEV PYLPKPIRFE TLFPMLRKLL QGENVYGKSF IAPADRSAKN NGNVQRTVTI RQFNPNKGLL GALRFAEKNR QDIAILHGNK PVLIVFPSIQ RVLLTESVQK LEELCKDENL QVSCKTVPDN PQWREKAKVG IMSCMWQFSI WTAQGRLIYP ISPDTPFTLK SWPNLTRLAN VPGSIRLSAF LTKASVNLNV LYKVMPLNLN DILNYLAATY TTGFLSVDLK TVSQQAYSDM ADKINIGADS ASDSEMMKKA EKITTPSQSQ SRGLLQRLMK KLLGS // ID Q9JXQ6_NEIMB Unreviewed; 349 AA. AC Q9JXQ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 75. DE SubName: Full=Lacto-N-neotetraose biosynthesis glycosyl transferase LgtA {ECO:0000313|EMBL:AAF42258.1}; GN Name=lgtA {ECO:0000313|EMBL:AAF42258.1}; GN OrderedLocusNames=NMB1929 {ECO:0000313|EMBL:AAF42258.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42258.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42258.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42258.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42258.1; -; Genomic_DNA. DR PIR; D81027; D81027. DR RefSeq; NP_274923.1; NC_003112.2. DR RefSeq; WP_002257440.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ6; -. DR STRING; 122586.NMB1929; -. DR PaxDb; Q9JXQ6; -. DR EnsemblBacteria; AAF42258; AAF42258; NMB1929. DR GeneID; 904226; -. DR KEGG; nme:NMB1929; -. DR PATRIC; 20359905; VBINeiMen85645_2457. DR eggNOG; ENOG4107S6X; Bacteria. DR eggNOG; ENOG410ZVME; LUCA. DR HOGENOM; HOG000218750; -. DR OMA; KSGMGEY; -. DR OrthoDB; EOG6M0T47; -. DR BioCyc; NMEN122586:GHGG-1986-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42258.1}. FT DOMAIN 22 195 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 349 AA; 40618 MW; 4B9E245C34847DC3 CRC64; MPSEAFRRHR AYRENKLQPL VSVLICAYNV EKYFAQSLAA VVNQTWRNLD ILIVDDGSTD GTLAIAQRFQ EQDGRIRILA QPRNSGLIPS LNIGLDELAK SGGGGEYIAR TDADDIAAPD WIEKIVGEME KDRSIIAMGA WLEVLSEEKD GNRLARHHEH GKIWKKPTRH EDIADFFPFG NPIHNNTMIM RRSVIDGGLR YNTERDWAED YQFWYDVSKL GRLAYYPEAL VKYRLHANQV SSKYSIRQHE IAQGIQKTAR NDFLQSMGFK TRFDSLEYRQ IKAVAYELLE KHLPEEDFER ARRFLYQCFK RTDTLPAGAW LDFAADGRMR RLFTLRQYFG ILHRLLKNR // ID Q7DDT7_NEIMB Unreviewed; 164 AA. AC Q7DDT7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Putative bacteriocin resistance protein {ECO:0000313|EMBL:AAF40562.1}; GN OrderedLocusNames=NMB0103 {ECO:0000313|EMBL:AAF40562.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40562.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40562.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40562.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40562.1; -; Genomic_DNA. DR PIR; F81237; F81237. DR RefSeq; NP_273161.1; NC_003112.2. DR RefSeq; WP_009344947.1; NC_003112.2. DR ProteinModelPortal; Q7DDT7; -. DR STRING; 122586.NMB0103; -. DR PaxDb; Q7DDT7; -. DR EnsemblBacteria; AAF40562; AAF40562; NMB0103. DR GeneID; 902207; -. DR KEGG; nme:NMB0103; -. DR PATRIC; 20355215; VBINeiMen85645_0141. DR eggNOG; ENOG4108VMT; Bacteria. DR eggNOG; COG3271; LUCA. DR HOGENOM; HOG000218674; -. DR KO; K06992; -. DR OMA; FHISEIN; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NMEN122586:GHGG-109-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF03412; Peptidase_C39; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 122 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 164 AA; 18919 MW; D372A9949E5AAFE4 CRC64; MDFSCGAASI ATLLNNFYGR HYSEAEILDK MDKTQMRASF DDMQRIMPEL GFEAQGYALP FEQLVQLKIP VIVYLKYRKN NHFSVLNGIN GETVLLADPS LGHVSMSKSQ FLSAWKTRDG EMEGKILAIV PKNTDFVRNQ MFFNKNPVRQ TRFTVEQIQM RQKR // ID Q9K0I4_NEIMB Unreviewed; 434 AA. AC Q9K0I4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE RecName: Full=Ammonium transporter {ECO:0000256|RuleBase:RU362002}; GN OrderedLocusNames=NMB0615 {ECO:0000313|EMBL:AAF41042.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41042.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41042.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41042.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362002}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362002}. CC -!- SIMILARITY: Belongs to the ammonia transporter channel CC (TC 1.A.11.2) family. {ECO:0000256|RuleBase:RU362002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41042.1; -; Genomic_DNA. DR PIR; E81177; E81177. DR RefSeq; NP_273659.1; NC_003112.2. DR RefSeq; WP_002222836.1; NC_003112.2. DR ProteinModelPortal; Q9K0I4; -. DR STRING; 122586.NMB0615; -. DR PaxDb; Q9K0I4; -. DR EnsemblBacteria; AAF41042; AAF41042; NMB0615. DR GeneID; 902729; -. DR KEGG; nme:NMB0615; -. DR PATRIC; 20356517; VBINeiMen85645_0778. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR HOGENOM; HOG000017736; -. DR KO; K03320; -. DR OMA; IVGCLLT; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NMEN122586:GHGG-641-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.10.3430.10; -; 1. DR InterPro; IPR029020; Ammonium/urea_transptr. DR InterPro; IPR001905; Ammonium_transpt. DR InterPro; IPR018047; Ammonium_transpt_CS. DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom. DR PANTHER; PTHR11730; PTHR11730; 1. DR Pfam; PF00909; Ammonium_transp; 1. DR SUPFAM; SSF111352; SSF111352; 1. DR TIGRFAMs; TIGR00836; amt; 1. DR PROSITE; PS01219; AMMONIUM_TRANSP; 1. PE 3: Inferred from homology; KW Ammonia transport {ECO:0000256|RuleBase:RU362002}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU362002}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362002}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362002}; KW Transport {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 35 57 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 69 91 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 132 153 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 160 182 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 194 216 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 228 246 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 258 279 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 291 311 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 317 335 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 347 366 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 388 407 Helical. {ECO:0000256|RuleBase:RU362002}. FT DOMAIN 35 432 Ammonium_transp. FT {ECO:0000259|Pfam:PF00909}. SQ SEQUENCE 434 AA; 45352 MW; 56AEB88E683F2E04 CRC64; MKKHIWAASL LPASLSAEPL NWWKPYSAVN SGDTAWVMTA AALVLLMTLP GLALFYGGMV RKKNLLSTMM HSFSIATLVG ILWVAVGYSL AFTPGNAFIG GLGRVFLSGM QIDATAQMLT VSPNAPTVPE PVFMFFQMTF AIISTAIITG AFAERMKYSA MMLFSGIWFL LVYVPGAHWV WGGGFMSKGG VLDYAGGTVV HINAGIAGLV AALVLGRRIG YGREAMPPHN MAMTLIGAAM LWFGWFGFNA GSALAADAAA GMAMAVTQVS AVFGAAGWLA CEKIAGHKPS ALGLASGAVS GLVGITPAAG FTGPSGAAAI GILTAAACFV SVTVVKHKLR YDDSLDAFGI HGFGGLVGGI LTGIFFDNRI FGGDAAVWQQ LWIQVKDGVV MAAYSGLMSW AILKVVGKIC GGLRVGKDVE REGLDLNIHG ERVE // ID Q9JXU5_NEIMB Unreviewed; 321 AA. AC Q9JXU5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Putative ABC transporter, periplasmic solute-binding protein {ECO:0000313|EMBL:AAF42214.1}; GN OrderedLocusNames=NMB1880 {ECO:0000313|EMBL:AAF42214.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42214.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42214.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42214.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains Fe/B12 periplasmic-binding domain. CC {ECO:0000256|SAAS:SAAS00514624}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42214.1; -; Genomic_DNA. DR PIR; F81030; F81030. DR RefSeq; NP_274876.1; NC_003112.2. DR RefSeq; WP_002244310.1; NC_003112.2. DR ProteinModelPortal; Q9JXU5; -. DR STRING; 122586.NMB1880; -. DR PaxDb; Q9JXU5; -. DR EnsemblBacteria; AAF42214; AAF42214; NMB1880. DR GeneID; 904303; -. DR KEGG; nme:NMB1880; -. DR PATRIC; 20359793; VBINeiMen85645_2402. DR eggNOG; ENOG4105HWS; Bacteria. DR eggNOG; COG4607; LUCA. DR HOGENOM; HOG000099140; -. DR OMA; PRATSKY; -. DR OrthoDB; EOG61VZ9F; -. DR BioCyc; NMEN122586:GHGG-1936-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 321 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327689. FT DOMAIN 54 314 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. SQ SEQUENCE 321 AA; 34210 MW; B1A18B0D3C532CEB CRC64; MKPRFYWAAC AVLLTACSPE PAAEKTVSAA SASAATLTVP TARGDAVVPK NPERVAVYDW AALDTLTELG VNVGATTAPV RVDYLQPAFD KAATVGTLFE PDYEALHRYN PQLVITGGPG AEAYEQLAKN ATTIDLTVDN GNIRTSGEKQ METLARIFGK EARAAELKAQ IDALFAQTRE AAKGKGRGLV LSVTGNKVSA FGTQSRLASW IHGDIGLPPV DESLRNEGHG QPVSFEYIKE KNPDWIFIID RTAAIGQEGP AAVEVLDNAL VRGTNAWKRK QIIVMPAANY IVAGGARQLI QAAEQLKAAF KKAEPVAAGK K // ID Q9JZ11_NEIMB Unreviewed; 535 AA. AC Q9JZ11; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137}; DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137}; GN Name=aceF {ECO:0000313|EMBL:AAF41717.1}; GN OrderedLocusNames=NMB1342 {ECO:0000313|EMBL:AAF41717.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41717.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41717.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41717.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). CC {ECO:0000256|RuleBase:RU361137}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine CC = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. CC {ECO:0000256|RuleBase:RU361137}. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000256|RuleBase:RU361137}; CC Note=Binds 2 lipoyl cofactors covalently. CC {ECO:0000256|RuleBase:RU361137}; CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. {ECO:0000256|RuleBase:RU361137}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000256|RuleBase:RU361137}. CC -!- SIMILARITY: Contains 2 lipoyl-binding domains. CC {ECO:0000256|RuleBase:RU361137}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41717.1; -; Genomic_DNA. DR PIR; F81094; F81094. DR RefSeq; NP_274361.1; NC_003112.2. DR RefSeq; WP_002244152.1; NC_003112.2. DR ProteinModelPortal; Q9JZ11; -. DR SMR; Q9JZ11; 2-82, 106-186, 296-535. DR STRING; 122586.NMB1342; -. DR PaxDb; Q9JZ11; -. DR EnsemblBacteria; AAF41717; AAF41717; NMB1342. DR GeneID; 903764; -. DR KEGG; nme:NMB1342; -. DR PATRIC; 20358337; VBINeiMen85645_1680. DR eggNOG; ENOG4107QSN; Bacteria. DR eggNOG; COG0508; LUCA. DR HOGENOM; HOG000281562; -. DR KO; K00627; -. DR OMA; GKEFEPR; -. DR OrthoDB; EOG610413; -. DR BioCyc; NMEN122586:GHGG-1380-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. DR Gene3D; 4.10.320.10; -; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR004167; E3-bd. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 2. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 2. DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2. DR PROSITE; PS00189; LIPOYL; 2. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU361137, KW ECO:0000313|EMBL:AAF41717.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycolysis {ECO:0000256|RuleBase:RU361137}; KW Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550}; KW Pyruvate {ECO:0000313|EMBL:AAF41717.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU361137, KW ECO:0000313|EMBL:AAF41717.1}. FT DOMAIN 3 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. FT DOMAIN 107 181 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 535 AA; 55223 MW; F220E0F35F427C8D CRC64; MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA DAAGVVKEVK VKVGDKISEG GVILTVETGA AAAEAAPAAA EAQPAPAAAP AAAGGATVQV AVPDIGGHTD VDVIAVEIKV GDTVAEDDTL ITLETDKATM DVPCTAAGVV KAVFLKVGDK VSEGSAIIEV ETVGSAAAAP AQAAQAAAPA AAPPPTAAAA PAAAPAPSAP AAAKIDEAAF AKAHAGPSAR KLARELGVDL GQVKGTGLKG RIMGDDIKAF VKSVMQGGAA KPAAASASLG GGLDLLPWPK VDFSKFGNVE VKELSRIKKI SGQNLSRNWV VIPHVTVHEE ADMTELEEFR KQLNKEWERE GVKLSPLAFI IKASVSALKA FPEFNASLDG DNLVLKNYFN IGFAADTPNG LVVPVIKDVD QKGLKQISQE LTELSKKARE GKLKPQEMQG ACFTISSLGG IGGTGFTPIV NAPEVAILGV CKSQIKPVWN GKEFAPRLMC PLSLSFDHRV IDGAAGMRFT VFLAKLLKDF RRITL // ID Q9K1M0_NEIMB Unreviewed; 78 AA. AC Q9K1M0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40553.1}; GN OrderedLocusNames=NMB0091 {ECO:0000313|EMBL:AAF40553.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40553.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40553.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40553.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40553.1; -; Genomic_DNA. DR PIR; C81239; C81239. DR RefSeq; NP_273152.1; NC_003112.2. DR RefSeq; WP_002233390.1; NC_003112.2. DR STRING; 122586.NMB0091; -. DR PaxDb; Q9K1M0; -. DR EnsemblBacteria; AAF40553; AAF40553; NMB0091. DR GeneID; 902195; -. DR KEGG; nme:NMB0091; -. DR HOGENOM; HOG000220680; -. DR OrthoDB; EOG6B0B30; -. DR BioCyc; NMEN122586:GHGG-97-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 78 AA; 8310 MW; 62EB649BBEDC4F1C CRC64; MKELHTSELV EVSGGKFHIF AQGGGNLGKK DMVAVGKIGA SYSPNNSGVE FSVSKQFGYV QGLGVQFSKP TFGISKKW // ID Q9K159_NEIMB Unreviewed; 508 AA. AC Q9K159; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Fatty acid efflux system protein {ECO:0000313|EMBL:AAF40764.1}; GN Name=farB {ECO:0000313|EMBL:AAF40764.1}; GN OrderedLocusNames=NMB0319 {ECO:0000313|EMBL:AAF40764.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40764.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40764.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40764.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40764.1; -; Genomic_DNA. DR PIR; B81212; B81212. DR RefSeq; NP_273368.1; NC_003112.2. DR RefSeq; WP_002224867.1; NC_003112.2. DR ProteinModelPortal; Q9K159; -. DR STRING; 122586.NMB0319; -. DR PaxDb; Q9K159; -. DR EnsemblBacteria; AAF40764; AAF40764; NMB0319. DR GeneID; 902435; -. DR KEGG; nme:NMB0319; -. DR PATRIC; 20355769; VBINeiMen85645_0404. DR eggNOG; ENOG4105C0R; Bacteria. DR eggNOG; ENOG410XNN3; LUCA. DR HOGENOM; HOG000112190; -. DR KO; K03446; -. DR OMA; SSEQSTW; -. DR OrthoDB; EOG6ZH2DN; -. DR BioCyc; NMEN122586:GHGG-339-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004638; Drug-R_transpt_efflux_EmrB. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 3. DR TIGRFAMs; TIGR00711; efflux_EmrB; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|SAAS:SAAS00461639}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00461639, KW ECO:0000256|SAAS:SAAS00461653, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00461653, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00461653, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00461665}. FT TRANSMEM 50 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 304 322 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 334 351 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 363 381 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 478 496 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 14 501 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 508 AA; 55141 MW; D58F4BB7CDEA56C9 CRC64; MDYPPLKGAA LAWVTLSLGL AVFMEVLDTT IANVAVPVIA GNLGAATTQG TWVITSFSVA NAVSVPLTGF LAKRIGEVKL FTAAAVGFVI TSWLCGIAPN LQSLVVFRIL QGFIAGPLIP LSQSLLMASY PPAKRTLALA LWAMTVVVAP VLGPILGGWI SGNWHWGWIF FINIPIGIIS AWITWKHLKY RETETVKMPT DYVGLTLMVV GIGALQMMLD RGKELDWFAS GEIITLGVVA LVCLSYFIVW ELGEKYPIVD LSLFKDRNFT VGVIATSLGF MVYMGTLTLL PLVLQTNLGY TSTWAGLAAA PVGILPVFLS PLIGRFGNKI DMRLFVTASF LTFAFTFYWR TDFYADMDIG NVIWPQFWQG VGVAMFFLPL TTITLSHMKG GQIAAAGSLS NFLRVLMGGV GVSVVSTLWE RREALHHTRF AEHITPYSAT LHETAAHLSQ HGVSDIQTLG IINNTITQQG FIIGSNEIFM AGSLLFIIMI PVIWLAKPPF HNGGGGGH // ID Q9JY35_NEIMB Unreviewed; 152 AA. AC Q9JY35; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative toxin-activating protein {ECO:0000313|EMBL:AAF42104.1}; GN OrderedLocusNames=NMB1763 {ECO:0000313|EMBL:AAF42104.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42104.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42104.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42104.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42104.1; -; Genomic_DNA. DR PIR; A81045; A81045. DR RefSeq; NP_274763.1; NC_003112.2. DR RefSeq; WP_002224037.1; NC_003112.2. DR STRING; 122586.NMB1763; -. DR PaxDb; Q9JY35; -. DR EnsemblBacteria; AAF42104; AAF42104; NMB1763. DR GeneID; 903335; -. DR KEGG; nme:NMB1763; -. DR PATRIC; 20359491; VBINeiMen85645_2251. DR eggNOG; ENOG41090Q8; Bacteria. DR eggNOG; COG2994; LUCA. DR HOGENOM; HOG000249645; -. DR KO; K07389; -. DR OMA; GFACWAF; -. DR OrthoDB; EOG647TZC; -. DR BioCyc; NMEN122586:GHGG-1818-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:InterPro. DR GO; GO:0009404; P:toxin metabolic process; IEA:InterPro. DR InterPro; IPR003996; RTX_toxin-activating_protC_bac. DR Pfam; PF02794; HlyC; 1. DR PRINTS; PR01489; RTXTOXINC. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 152 AA; 17662 MW; 63B8F0580F8167A5 CRC64; MPITPPLNII SPKLYPNEQW NESEALGAIT WLWYQSPTHR QVPIVEMMTY ILPVLKNGQF ALFCKGTQPI GYISWAYFDE VAQAHYLESD RHLRDNSDWN CGDNIWLIQW FAPLGHSHQM RSAVRQLFPS TTVRALYHKG SDKGLRILTF KT // ID Q9K199_NEIMB Unreviewed; 154 AA. AC Q9K199; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885}; DE EC=2.1.1.207 {ECO:0000256|HAMAP-Rule:MF_01885}; DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000256|HAMAP-Rule:MF_01885}; GN Name=trmL {ECO:0000256|HAMAP-Rule:MF_01885}; GN OrderedLocusNames=NMB0268 {ECO:0000313|EMBL:AAF40722.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40722.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40722.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40722.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble CC position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and CC tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S- CC adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. CC {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 5- CC carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L- CC homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) CC in tRNA(Leu). {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(34) in tRNA CC = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA. CC {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC TrmL subfamily. {ECO:0000256|HAMAP-Rule:MF_01885}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40722.1; -; Genomic_DNA. DR PIR; E81218; E81218. DR RefSeq; NP_273324.1; NC_003112.2. DR RefSeq; WP_002218664.1; NC_003112.2. DR ProteinModelPortal; Q9K199; -. DR SMR; Q9K199; 1-154. DR STRING; 122586.NMB0268; -. DR PaxDb; Q9K199; -. DR EnsemblBacteria; AAF40722; AAF40722; NMB0268. DR GeneID; 902379; -. DR KEGG; nme:NMB0268; -. DR PATRIC; 20355620; VBINeiMen85645_0334. DR eggNOG; ENOG4108UIQ; Bacteria. DR eggNOG; COG0219; LUCA. DR HOGENOM; HOG000272756; -. DR KO; K03216; -. DR OMA; AGLDYWH; -. DR OrthoDB; EOG6RG038; -. DR BioCyc; NMEN122586:GHGG-283-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR016914; tRNA_cyt/urid_MeTfrase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:AAF40722.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|PIRSR:PIRSR029256-1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:AAF40722.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}. FT DOMAIN 2 142 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. FT BINDING 78 78 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. FT BINDING 100 100 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. FT BINDING 122 122 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. FT BINDING 130 130 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01885, FT ECO:0000256|PIRSR:PIRSR029256-1}. SQ SEQUENCE 154 AA; 16819 MW; 9188EBAE99B710EA CRC64; MFTIVLYQPE IPPNTGNIIR LCANTGADLH LVKPLGFPLD SAKMKRAGLD YHEFASLTVH ENFDDCLKAL AGRRIFALTT KGTARPDETA FQKGDVLLFG PETRGLPADI LDSLPAAQKI RLPMQPGSRS MNLSNTVAVI LFEAWRQHGY AGGV // ID Q9JXC7_NEIMB Unreviewed; 34 AA. AC Q9JXC7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=MafB-related protein {ECO:0000313|EMBL:AAF62341.1}; GN OrderedLocusNames=NMB2122 {ECO:0000313|EMBL:AAF62341.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62341.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62341.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62341.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62341.1; -; Genomic_DNA. DR RefSeq; NP_275108.1; NC_003112.2. DR RefSeq; WP_002215117.1; NC_003112.2. DR PaxDb; Q9JXC7; -. DR EnsemblBacteria; AAF62341; AAF62341; NMB2122. DR GeneID; 903449; -. DR KEGG; nme:NMB2122; -. DR PATRIC; 20360418; VBINeiMen85645_2705. DR HOGENOM; HOG000152748; -. DR BioCyc; NMEN122586:GHGG-2187-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 3805 MW; 772CE0C7BB833918 CRC64; MDDIRGIIQG AVNPLIYKVS KQKIIYNNKL ISGT // ID Q9JZN3_NEIMB Unreviewed; 157 AA. AC Q9JZN3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Putative modulator of drug activity B {ECO:0000313|EMBL:AAF41381.1}; GN OrderedLocusNames=NMB0977 {ECO:0000313|EMBL:AAF41381.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41381.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41381.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41381.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41381.1; -; Genomic_DNA. DR PIR; B81137; B81137. DR RefSeq; NP_274014.1; NC_003112.2. DR RefSeq; WP_010980879.1; NC_003112.2. DR ProteinModelPortal; Q9JZN3; -. DR SMR; Q9JZN3; 12-157. DR STRING; 122586.NMB0977; -. DR PaxDb; Q9JZN3; -. DR EnsemblBacteria; AAF41381; AAF41381; NMB0977. DR GeneID; 903097; -. DR KEGG; nme:NMB0977; -. DR PATRIC; 20357443; VBINeiMen85645_1236. DR eggNOG; ENOG4105NF4; Bacteria. DR eggNOG; COG2249; LUCA. DR HOGENOM; HOG000063966; -. DR OMA; VHDIFKG; -. DR OrthoDB; EOG6ZWJFM; -. DR BioCyc; NMEN122586:GHGG-1014-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 10 152 Flavodoxin_2. {ECO:0000259|Pfam:PF02525}. SQ SEQUENCE 157 AA; 18033 MW; 041578D24AA8198E CRC64; MTMQVFLTIP GYDVEAEIEK FVWMDAVIWQ MPGWWMHEPW TVKKYIDGVL TAGHGKLYQS DGRHSVNPTE GYGTGGLLQG KKHMLSLTWN APIEAFTREG DFFEGKGVDV LYMHFHKANE FLGMTRLPTF LCNDVVKNPQ VEKYLADYQA HLEKVFG // ID Q9K0N9_NEIMB Unreviewed; 129 AA. AC Q9K0N9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Type IV pilin protein {ECO:0000313|EMBL:AAF40976.1}; GN OrderedLocusNames=NMB0547 {ECO:0000313|EMBL:AAF40976.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40976.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40976.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40976.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40976.1; -; Genomic_DNA. DR PIR; A81187; A81187. DR RefSeq; NP_273592.1; NC_003112.2. DR RefSeq; WP_002226625.1; NC_003112.2. DR ProteinModelPortal; Q9K0N9; -. DR STRING; 122586.NMB0547; -. DR PaxDb; Q9K0N9; -. DR EnsemblBacteria; AAF40976; AAF40976; NMB0547. DR GeneID; 902662; -. DR KEGG; nme:NMB0547; -. DR PATRIC; 20356357; VBINeiMen85645_0697. DR eggNOG; ENOG4105VDS; Bacteria. DR eggNOG; COG4968; LUCA. DR HOGENOM; HOG000008197; -. DR KO; K02655; -. DR OMA; TNEGETC; -. DR OrthoDB; EOG6NWBPW; -. DR BioCyc; NMEN122586:GHGG-573-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031982; DUS_rpt_ComP. DR InterPro; IPR012902; N_methyl_site. DR Pfam; PF16732; ComP_DUS; 1. DR Pfam; PF13544; N_methyl_2; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 13 31 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 129 AA; 14562 MW; 262239D22038E809 CRC64; MKNVQKGFTL LELMIAVAIL GILTLITYPS YKTYIRRVRL SEVRTTLLHN AQTMERYYRQ KGTFKTYDKN KLKQNEYFDI TLSEVSPDHF TLQADPNPTT NDGETCVVTL NDGGTIAASG TNQSCPGFD // ID Q9K064_NEIMB Unreviewed; 306 AA. AC Q9K064; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Putative dTDP-L-rhamnose synthase {ECO:0000313|EMBL:AAF41169.1}; GN OrderedLocusNames=NMB0756 {ECO:0000313|EMBL:AAF41169.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41169.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41169.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41169.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41169.1; -; Genomic_DNA. DR PIR; C81164; C81164. DR RefSeq; NP_273798.1; NC_003112.2. DR RefSeq; WP_010980837.1; NC_003112.2. DR ProteinModelPortal; Q9K064; -. DR STRING; 122586.NMB0756; -. DR PaxDb; Q9K064; -. DR EnsemblBacteria; AAF41169; AAF41169; NMB0756. DR GeneID; 902871; -. DR KEGG; nme:NMB0756; -. DR PATRIC; 20356883; VBINeiMen85645_0960. DR eggNOG; ENOG4105DBZ; Bacteria. DR eggNOG; COG1091; LUCA. DR HOGENOM; HOG000227712; -. DR KO; K00067; -. DR OMA; IRTAWVY; -. DR OrthoDB; EOG6HTP2V; -. DR BioCyc; NMEN122586:GHGG-787-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005913; dTDP_dehydrorham_reduct. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029903; RmlD-like-bd. DR PANTHER; PTHR10491; PTHR10491; 1. DR Pfam; PF04321; RmlD_sub_bind; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01214; rmlD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 283 RmlD_sub_bind. FT {ECO:0000259|Pfam:PF04321}. SQ SEQUENCE 306 AA; 33580 MW; 140A02B7323091A1 CRC64; MRILLTGSKS QLARCLRDRL PEDWETIATD SASLDITDAD AVCNMVKSFQ PDAIVNTAAY TAVDKAEGDA AAAFAVNASA VYNLALAAHR AHARFIHIST DYVFDGKGKR PYQESDFTNP SNVYGQSKTA GELLALSANP DSLILRTSWL FSEYGDNFIR TMLNLARERS PLSAVHNQIG CPTYAGDLSA TIIRLLQHSN PVRGIYHYAG SKSVSWYEFA QHIFQAASQQ QTSFPVPELT AVSDKEYPTA APRPAYSILD CRKIENDFGI KPSDWQKALH RSFPSCSDAA RPSVSAVKHR LGGFLI // ID Q4W591_NEIMB Unreviewed; 124 AA. AC Q4W591; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52140.1}; GN OrderedLocusNames=NMB0020 {ECO:0000313|EMBL:AAY52140.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52140.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52140.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52140.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52140.1; -; Genomic_DNA. DR RefSeq; WP_010980744.1; NC_003112.2. DR RefSeq; YP_338285.1; NC_003112.2. DR ProteinModelPortal; Q4W591; -. DR SMR; Q4W591; 1-115. DR STRING; 122586.NMB0020; -. DR PaxDb; Q4W591; -. DR EnsemblBacteria; AAY52140; AAY52140; NMB0020. DR GeneID; 902123; -. DR KEGG; nme:NMB0020; -. DR PATRIC; 20354981; VBINeiMen85645_0027. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR OMA; IWPANNN; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-21-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 124 AA; 13284 MW; 7819940993930853 CRC64; MAEGQKSAVT EYYLNHGEWP GNNSSAGVAT SANIKGKYVE KVEVKNGVVT ATMLSSGVNK EIQGKKLSLW AKRQDGSVKW FYGQPVKRDN ASADAVKADT AANGKQIDTK HLPSTASTRK STPN // ID Q9JYV6_NEIMB Unreviewed; 257 AA. AC Q9JYV6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=FrpC operon protein {ECO:0000313|EMBL:AAF41775.1}; GN OrderedLocusNames=NMB1414 {ECO:0000313|EMBL:AAF41775.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41775.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41775.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41775.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41775.1; -; Genomic_DNA. DR PIR; D81086; D81086. DR RefSeq; NP_274426.1; NC_003112.2. DR RefSeq; WP_010980933.1; NC_003112.2. DR STRING; 122586.NMB1414; -. DR PaxDb; Q9JYV6; -. DR EnsemblBacteria; AAF41775; AAF41775; NMB1414. DR GeneID; 903836; -. DR KEGG; nme:NMB1414; -. DR PATRIC; 20358509; VBINeiMen85645_1766. DR HOGENOM; HOG000219111; -. DR BioCyc; NMEN122586:GHGG-1452-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010692; FrpC. DR Pfam; PF06901; FrpC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 257 AA; 29941 MW; 95BA456111AB62FE CRC64; MRPYATTIYQ LFILFIGSVF TMTSCEPVNE QTSFNNPEPM TGFEHTVTFD FQGTKMVIPY GYLARYTQDN ATKWLSDTPG QDAYSINLIE ISVYYKKTDQ GWVLEPYNQQ NKAHFIQFLR DGLDSVDDIV IRKDACSLST TMGERLLTYG VKKMPSAYPE YEAYEDKRHI PENPYFHEFY YIKKGENPAI ITHWNNRVNQ AEEDNYSTSV GSCINGFTVQ YYPFIREKQQ LTQQELVGYH QQVEQLVQSF VNNSSKK // ID Q7DD79_NEIMB Unreviewed; 207 AA. AC Q7DD79; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Cytochrome c4 {ECO:0000313|EMBL:AAF42142.1}; GN OrderedLocusNames=NMB1805 {ECO:0000313|EMBL:AAF42142.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42142.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42142.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42142.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- PTM: Binds 2 heme groups per subunit. CC {ECO:0000256|PIRSR:PIRSR000005-1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42142.1; -; Genomic_DNA. DR PIR; F81040; F81040. DR RefSeq; NP_274802.1; NC_003112.2. DR RefSeq; WP_002214509.1; NC_003112.2. DR ProteinModelPortal; Q7DD79; -. DR STRING; 122586.NMB1805; -. DR PaxDb; Q7DD79; -. DR EnsemblBacteria; AAF42142; AAF42142; NMB1805. DR GeneID; 903293; -. DR KEGG; nme:NMB1805; -. DR PATRIC; 20359579; VBINeiMen85645_2295. DR eggNOG; ENOG4106RE7; Bacteria. DR eggNOG; COG2863; LUCA. DR HOGENOM; HOG000221626; -. DR OMA; IAACAGC; -. DR OrthoDB; EOG6JDWB3; -. DR BioCyc; NMEN122586:GHGG-1860-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 2. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR008168; Cyt_C_IC. DR InterPro; IPR024167; Cytochrome_c4. DR Pfam; PF00034; Cytochrom_C; 2. DR PIRSF; PIRSF000005; Cytochrome_c4; 1. DR PRINTS; PR00605; CYTCHROMECIC. DR SUPFAM; SSF46626; SSF46626; 2. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Heme {ECO:0000256|PIRSR:PIRSR000005-1}; KW Iron {ECO:0000256|PIRSR:PIRSR000005-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000005-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 207 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287259. FT DOMAIN 22 207 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. FT BINDING 35 35 Heme 1 (covalent). FT {ECO:0000256|PIRSR:PIRSR000005-1}. FT BINDING 38 38 Heme 1 (covalent). FT {ECO:0000256|PIRSR:PIRSR000005-1}. FT BINDING 135 135 Heme 2 (covalent). FT {ECO:0000256|PIRSR:PIRSR000005-1}. FT BINDING 138 138 Heme 2 (covalent). FT {ECO:0000256|PIRSR:PIRSR000005-1}. SQ SEQUENCE 207 AA; 21989 MW; 29C843B52987AA0D CRC64; MKRLTLLAFV LAAGAVSASP KADVEKGKQV AATVCAACHA ADGNSGIAMY PRLAAQHTAY IYHQTIGIRD GKRTHGSAAV MKPVVMNLSD QDILNVSAFY AKQQPKSGEA NPKENPELGA KIYRGGLSDK KVPACMSCHG PSGAGMPGGG SEIQAYPRLG GQHQAYIVEQ MNAYKSGQRK NTIMEDIANR MSEEDLKAVA NFIQGLR // ID Q9K0S8_NEIMB Unreviewed; 559 AA. AC Q9K0S8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Hemolysin activator-related protein {ECO:0000313|EMBL:AAF62312.1}; GN OrderedLocusNames=NMB0496 {ECO:0000313|EMBL:AAF62312.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62312.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62312.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62312.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62312.1; -; Genomic_DNA. DR RefSeq; NP_273542.1; NC_003112.2. DR RefSeq; WP_002225614.1; NC_003112.2. DR ProteinModelPortal; Q9K0S8; -. DR STRING; 122586.NMB0496; -. DR PaxDb; Q9K0S8; -. DR EnsemblBacteria; AAF62312; AAF62312; NMB0496. DR GeneID; 902612; -. DR KEGG; nme:NMB0496; -. DR PATRIC; 20356242; VBINeiMen85645_0641. DR eggNOG; ENOG4105D5K; Bacteria. DR eggNOG; COG2831; LUCA. DR HOGENOM; HOG000218787; -. DR OMA; TSSAEFY; -. DR OrthoDB; EOG6TBHBP; -. DR BioCyc; NMEN122586:GHGG-521-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR InterPro; IPR005565; Hemolysn_activator_HlyB. DR InterPro; IPR013686; Polypept-transport_assoc_ShlB. DR InterPro; IPR027282; TPS. DR Pfam; PF08479; POTRA_2; 1. DR Pfam; PF03865; ShlB; 1. DR PIRSF; PIRSF029745; FhaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 64 129 POTRA_2. {ECO:0000259|Pfam:PF08479}. FT DOMAIN 156 498 ShlB. {ECO:0000259|Pfam:PF03865}. SQ SEQUENCE 559 AA; 63487 MW; E4D1BEB8D922E4B4 CRC64; MEIINDAELI RSMQRQQHID AELLTDANVR FEQPLEKNNY VLSEDETPCT RVNYISLDDK TVRKFSFLPS VLMKETAFKT GMCLGSNNLS RLQKAAQQIL IVRGYLTSQA IIQPQNMDSG ILKLRVSAGE IGDIRYEEKR DGKSAEGSIS AFNNKFPLYR NKILNLRDVE QGLENLRRLP SVKTDIQIIP SEEEGKSDLQ IKWQQNKPIR FSIGIDDAGG KTTGKYQGNV ALSFDNPLGL SDLFYVSYGR GLAHKTDLTD ATGTETESGS RSYSVHYSVP VKKWLFSFNH NGHRYHEATE GYSVNYDYNG KQYQSSLAAE RMLWRNRLHK TSVGMKLWTR QTYKYIDDAE IEVQRRRSAG WEAELRHRAY LNRWQLDGKL SYKRGTGMRQ SMPAPEENGG DILPGTSRMK IITASLDAAA PFILGKQQFF YATAIQAQWN KTPLVAQDKL SIGSRYTVRG FDGEQSLFGE RGFYWQNTLT WYFHPNHQFY LGADYGRVSG ESAQYVSGKQ LMGAVVGFRG GHKVGGMFAY DLFAGKPLHK PKGFQTTNTV YGFNLNYSF // ID Q9JXS3_NEIMB Unreviewed; 241 AA. AC Q9JXS3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42238.1}; GN OrderedLocusNames=NMB1908 {ECO:0000313|EMBL:AAF42238.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42238.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42238.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42238.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42238.1; -; Genomic_DNA. DR PIR; C81028; C81028. DR RefSeq; NP_274902.1; NC_003112.2. DR RefSeq; WP_002226727.1; NC_003112.2. DR ProteinModelPortal; Q9JXS3; -. DR STRING; 122586.NMB1908; -. DR PaxDb; Q9JXS3; -. DR EnsemblBacteria; AAF42238; AAF42238; NMB1908. DR GeneID; 904257; -. DR KEGG; nme:NMB1908; -. DR PATRIC; 20359859; VBINeiMen85645_2434. DR eggNOG; ENOG4107R8F; Bacteria. DR eggNOG; COG0313; LUCA. DR HOGENOM; HOG000258038; -. DR KO; K07056; -. DR OMA; ETPYRNR; -. DR OrthoDB; EOG61308G; -. DR BioCyc; NMEN122586:GHGG-1965-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR Gene3D; 3.30.950.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 216 TP_methylase. {ECO:0000259|Pfam:PF00590}. SQ SEQUENCE 241 AA; 26555 MW; 9BC422F28B9CC03B CRC64; MSEGMMSPVL YLIPTPLGTP DTPCLLPHEQ QAIVGLTDFV VEAEKTARAH LKHLGVTTPI RELNLQTLNE HTDLKTLPEL LKPLQEGRSM GIVSEAGCPA VADPGANLVA LAHKHGFEVR PLVGPSSLLL ALMASGANGQ SFAFKGYLPS EKNERIQAFR ALEQRSRQCG ETQIFIETPY RNDALLADAV ENLHPETRLC TATDLTLPTQ EIISQTIVQW RKRKEMPNLK KRPTIFVMYA G // ID Q9JZH0_NEIMB Unreviewed; 281 AA. AC Q9JZH0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE RecName: Full=Ribosomal RNA large subunit methyltransferase J {ECO:0000256|HAMAP-Rule:MF_00934}; DE EC=2.1.1.266 {ECO:0000256|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA (adenine(2030)-N6)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA m6A2030 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; GN Name=rlmJ {ECO:0000256|HAMAP-Rule:MF_00934}; GN OrderedLocusNames=NMB1061 {ECO:0000313|EMBL:AAF41457.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41457.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41457.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41457.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the adenine in position 2030 of CC 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(2030) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(6)-methyladenine(2030) in 23S CC rRNA. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00934}. CC -!- SIMILARITY: Belongs to the RlmJ family. {ECO:0000256|HAMAP- CC Rule:MF_00934}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41457.1; -; Genomic_DNA. DR PIR; G81126; G81126. DR RefSeq; NP_274094.1; NC_003112.2. DR RefSeq; WP_002225266.1; NC_003112.2. DR ProteinModelPortal; Q9JZH0; -. DR STRING; 122586.NMB1061; -. DR PaxDb; Q9JZH0; -. DR EnsemblBacteria; AAF41457; AAF41457; NMB1061. DR GeneID; 903478; -. DR KEGG; nme:NMB1061; -. DR PATRIC; 20357665; VBINeiMen85645_1349. DR eggNOG; ENOG4105D6S; Bacteria. DR eggNOG; COG2961; LUCA. DR HOGENOM; HOG000262479; -. DR KO; K07115; -. DR OMA; TYAIWYP; -. DR OrthoDB; EOG6Q8J0P; -. DR BioCyc; NMEN122586:GHGG-1098-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00934; 23SrRNA_methyltr_J; 1. DR InterPro; IPR007473; RlmJ. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04378; RsmJ; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00934}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00934}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00934}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00934}. FT REGION 144 145 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT ACT_SITE 165 165 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_00934}. FT BINDING 19 19 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 42 42 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00934}. FT BINDING 98 98 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 116 116 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT BINDING 165 165 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00934}. FT SITE 4 4 Interaction with substrate rRNA. FT {ECO:0000256|HAMAP-Rule:MF_00934}. SQ SEQUENCE 281 AA; 31977 MW; 551F110D91336623 CRC64; MLSYRHAFHA GNHADMLKHF TLFLVLQYFN RKDKPYWYID THGGAGVYNL EGSEAQKVGE YRQGIALLRQ AQNLPAELSD FAAHIQKILP SPKLYCGSPW LAQSLTRVGD KLRLFELHPT DFVHLQNNMG EAGLGKRGQV LREDGYKGLI SLLPPPPRRA TVLIDPPYEE KQDYRRVTET LKAALKRFES GCYLIWYPCL SREESRKLPE ELKKLLPDNY LHAELHVHAP KADGFGMHGS GMFVINPPYL LAEQLAANLP ALTRLLAQDE GSRYLLDSKI R // ID Q9JZI2_NEIMB Unreviewed; 241 AA. AC Q9JZI2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41438.1}; GN OrderedLocusNames=NMB1039 {ECO:0000313|EMBL:AAF41438.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41438.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41438.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41438.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41438.1; -; Genomic_DNA. DR PIR; B81129; B81129. DR RefSeq; NP_274073.1; NC_003112.2. DR RefSeq; WP_002213448.1; NC_003112.2. DR ProteinModelPortal; Q9JZI2; -. DR STRING; 122586.NMB1039; -. DR PaxDb; Q9JZI2; -. DR EnsemblBacteria; AAF41438; AAF41438; NMB1039. DR GeneID; 903176; -. DR KEGG; nme:NMB1039; -. DR PATRIC; 20357613; VBINeiMen85645_1323. DR eggNOG; ENOG4105WPN; Bacteria. DR eggNOG; COG1636; LUCA. DR HOGENOM; HOG000011197; -. DR KO; K09765; -. DR OMA; PNIHPYT; -. DR OrthoDB; EOG6S26FS; -. DR BioCyc; NMEN122586:GHGG-1076-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR003828; DUF208. DR Pfam; PF02677; DUF208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 241 AA; 27925 MW; 304DF22A6B96C2B2 CRC64; METQNKPTVT DIDRPILVPP GGHKKVLLHS CCAPCSGEVM EAMLASGIDY TIYFYNPNIH PHKEYMLRKE ENVRFAEKFG IPFIDKDDDY ENDRKEWFAK AKGMEFEPER GIRCTMCFDM RFEKAAQYAH EHGFPVFTSS LGISRWKNMA QINDCGHRAA APYDDVVYWD FNWRKGGGSA RMIEISKREN FYQQEYCGCA YSLRDSNAHR KSQGRIPIKL GVLYYGDEST QYEPAPIRVD K // ID Q9JZ48_NEIMB Unreviewed; 108 AA. AC Q9JZ48; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41669.1}; GN OrderedLocusNames=NMB1293 {ECO:0000313|EMBL:AAF41669.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41669.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41669.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41669.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41669.1; -; Genomic_DNA. DR PIR; H81098; H81098. DR RefSeq; NP_274313.1; NC_003112.2. DR RefSeq; WP_002233953.1; NC_003112.2. DR STRING; 122586.NMB1293; -. DR PaxDb; Q9JZ48; -. DR EnsemblBacteria; AAF41669; AAF41669; NMB1293. DR GeneID; 903715; -. DR KEGG; nme:NMB1293; -. DR PATRIC; 20358213; VBINeiMen85645_1618. DR HOGENOM; HOG000218989; -. DR OrthoDB; EOG6CP3ZJ; -. DR BioCyc; NMEN122586:GHGG-1331-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 108 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327852. SQ SEQUENCE 108 AA; 12385 MW; 4CF4A276E5C7F7FA CRC64; MSVKKMLAIL LSAILGLVST TAAAGTSEPA HRDTKHIRKA NKQMLHPECR KYLERRAAWY RSQGNVQELR ENKKARKAFR SLPYAEQKIQ CRAAYEAFDD FDGGSFRR // ID Q9K0A7_NEIMB Unreviewed; 159 AA. AC Q9K0A7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186}; DE Flags: Precursor; GN Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186}; GN OrderedLocusNames=NMB0707 {ECO:0000313|EMBL:AAF41124.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41124.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41124.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41124.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Together with LptD, is involved in the assembly of CC lipopolysaccharide (LPS) at the surface of the outer membrane. CC Required for the proper assembly of LptD. Binds LPS and may serve CC as the LPS recognition site at the outer membrane. CC {ECO:0000256|HAMAP-Rule:MF_01186}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. Interacts with LptD. {ECO:0000256|HAMAP- CC Rule:MF_01186}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP- CC Rule:MF_01186}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_01186}. CC -!- SIMILARITY: Belongs to the LptE lipoprotein family. CC {ECO:0000256|HAMAP-Rule:MF_01186}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41124.1; -; Genomic_DNA. DR PIR; D81168; D81168. DR RefSeq; NP_273749.1; NC_003112.2. DR RefSeq; WP_002217671.1; NC_003112.2. DR ProteinModelPortal; Q9K0A7; -. DR SMR; Q9K0A7; 30-159. DR STRING; 122586.NMB0707; -. DR PaxDb; Q9K0A7; -. DR EnsemblBacteria; AAF41124; AAF41124; NMB0707. DR GeneID; 902819; -. DR KEGG; nme:NMB0707; -. DR PATRIC; 20356761; VBINeiMen85645_0902. DR eggNOG; COG2980; LUCA. DR HOGENOM; HOG000218847; -. DR KO; K03643; -. DR OMA; ETLWAEM; -. DR OrthoDB; EOG63RGRX; -. DR BioCyc; NMEN122586:GHGG-735-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01186; LPS_assembly_LptE; 1. DR InterPro; IPR007485; LPS_assembly_LptE. DR Pfam; PF04390; LptE; 1. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01186}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_01186}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01186}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_01186}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|HAMAP-Rule:MF_01186}. FT SIGNAL 1 15 {ECO:0000256|HAMAP-Rule:MF_01186}. FT CHAIN 16 159 LPS-assembly lipoprotein LptE. FT {ECO:0000256|HAMAP-Rule:MF_01186}. FT /FTId=PRO_5005079082. FT LIPID 16 16 N-palmitoyl cysteine. {ECO:0000256|HAMAP- FT Rule:MF_01186}. FT LIPID 16 16 S-diacylglycerol cysteine. FT {ECO:0000256|HAMAP-Rule:MF_01186}. SQ SEQUENCE 159 AA; 17565 MW; 39DC40AFF706A0EE CRC64; MNKLFLTAAV LMLGACGFHL KGADGISPPL TYRSWHIEGG QALRFPLETA LYQASGRVDD AAGAQMTLRI DSVSQNKETY TVTRAAVINE YLLILTVEAQ VLKRGEPVGK PMTVSVRRVL AYADNEILGK QEEEAALWAE MRQDAAEQIV RRLTFLKAE // ID Q9JYB9_NEIMB Unreviewed; 197 AA. AC Q9JYB9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42005.1}; GN OrderedLocusNames=NMB1656 {ECO:0000313|EMBL:AAF42005.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42005.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42005.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42005.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42005.1; -; Genomic_DNA. DR PIR; G81057; G81057. DR RefSeq; NP_274661.1; NC_003112.2. DR RefSeq; WP_002218492.1; NC_003112.2. DR PaxDb; Q9JYB9; -. DR EnsemblBacteria; AAF42005; AAF42005; NMB1656. DR GeneID; 903460; -. DR KEGG; nme:NMB1656; -. DR PATRIC; 20359238; VBINeiMen85645_2131. DR eggNOG; ENOG4107957; Bacteria. DR eggNOG; ENOG410Z7YC; LUCA. DR HOGENOM; HOG000219062; -. DR OMA; NENSGHE; -. DR OrthoDB; EOG6W45R5; -. DR BioCyc; NMEN122586:GHGG-1705-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 197 AA; 21804 MW; B6C59F55EDAE5AC8 CRC64; MADGMGNLIG WEKTGLVVGK QWITAKDDKV SDVCNANGEM GVIGLYEPFS HGALTIPGHP NCRCEVVSVS GGELGEFAEK KELRKAAMQY ARDNFIGKSY VNKNSGHELK VTWQGVKHAA SKANQAELSI MTKLDDLLRY AKYEGSYSDR KGHPNIIAAH KYRAVAKVGN ESLNIGVIVR EFPDDHKHYD HFILKDE // ID Q9K0F0_NEIMB Unreviewed; 67 AA. AC Q9K0F0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41077.1}; GN OrderedLocusNames=NMB0657 {ECO:0000313|EMBL:AAF41077.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41077.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41077.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41077.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41077.1; -; Genomic_DNA. DR PIR; C81174; C81174. DR STRING; 122586.NMB0657; -. DR PaxDb; Q9K0F0; -. DR EnsemblBacteria; AAF41077; AAF41077; NMB0657. DR BioCyc; NMEN122586:GHGG-684-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7477 MW; 01BD2727D44D6F75 CRC64; MRTEFFKNPT LAPSTAAPWS KRQTAEKQTP SVVLPFADEY GSTPMPPKPS KPPSTLPPPK PQSWQKR // ID Q7DDU0_NEIMB Unreviewed; 349 AA. AC Q7DDU0; Q79AE8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Polysialic acid capsule biosynthesis protein SiaC {ECO:0000313|EMBL:AAF40535.1}; GN Name=siaC {ECO:0000313|EMBL:AAF40535.1}; GN OrderedLocusNames=NMB0068 {ECO:0000313|EMBL:AAF40535.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40535.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40535.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40535.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2WQP} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). RX PubMed=19719325; DOI=10.1021/bi9012758; RA Liu F., Lee H.J., Strynadka N.C., Tanner M.E.; RT "Inhibition of Neisseria meningitidis sialic acid synthase by a RT tetrahedral intermediate analogue."; RL Biochemistry 48:9194-9201(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40535.1; -; Genomic_DNA. DR RefSeq; NP_273132.1; NC_003112.2. DR RefSeq; WP_002215299.1; NC_003112.2. DR PDB; 2WQP; X-ray; 1.75 A; A=1-349. DR PDBsum; 2WQP; -. DR ProteinModelPortal; Q7DDU0; -. DR SMR; Q7DDU0; 2-349. DR STRING; 122586.NMB0068; -. DR PaxDb; Q7DDU0; -. DR EnsemblBacteria; AAF40535; AAF40535; NMB0068. DR GeneID; 902174; -. DR KEGG; nme:NMB0068; -. DR PATRIC; 20355137; VBINeiMen85645_0102. DR eggNOG; ENOG4105D2T; Bacteria. DR eggNOG; COG2089; LUCA. DR HOGENOM; HOG000284783; -. DR KO; K01654; -. DR OMA; CWDEEAV; -. DR OrthoDB; EOG6WX4KP; -. DR BioCyc; MetaCyc:MONOMER-14543; -. DR BioCyc; NMEN122586:GHGG-74-MONOMER; -. DR EvolutionaryTrace; Q7DDU0; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1210.10; -; 1. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013132; Neu5Ac_N. DR InterPro; IPR013974; SAF. DR Pfam; PF03102; NeuB; 1. DR Pfam; PF08666; SAF; 1. DR SMART; SM00858; SAF; 1. DR SUPFAM; SSF51269; SSF51269; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2WQP}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 292 349 AFP-like. {ECO:0000259|PROSITE:PS50844}. SQ SEQUENCE 349 AA; 38348 MW; 1C7C13EE5847E71A CRC64; MQNNNEFKIG NRSVGYNHEP LIICEIGINH EGSLKTAFEM VDAAYNAGAE VVKHQTHIVE DEMSDEAKQV IPGNADVSIY EIMERCALNE EDEIKLKEYV ESKGMIFIST PFSRAAALRL QRMDIPAYKI GSGECNNYPL IKLVASFGKP IILSTGMNSI ESIKKSVEII REAGVPYALL HCTNIYPTPY EDVRLGGMND LSEAFPDAII GLSDHTLDNY ACLGAVALGG SILERHFTDR MDRPGPDIVC SMNPDTFKEL KQGAHALKLA RGGKKDTIIA GEKPTKDFAF ASVVADKDIK KGELLSGDNL WVKRPGNGDF SVNEYETLFG KVAACNIRKG AQIKKTDIE // ID Q9K0I8_NEIMB Unreviewed; 321 AA. AC Q9K0I8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=Spermidine/putrescine ABC transporter, permease protein {ECO:0000313|EMBL:AAF41038.1}; GN Name=potB {ECO:0000313|EMBL:AAF41038.1}; GN OrderedLocusNames=NMB0611 {ECO:0000313|EMBL:AAF41038.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41038.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41038.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41038.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41038.1; -; Genomic_DNA. DR PIR; D81179; D81179. DR RefSeq; NP_273655.1; NC_003112.2. DR RefSeq; WP_002222839.1; NC_003112.2. DR ProteinModelPortal; Q9K0I8; -. DR STRING; 122586.NMB0611; -. DR PaxDb; Q9K0I8; -. DR EnsemblBacteria; AAF41038; AAF41038; NMB0611. DR GeneID; 902725; -. DR KEGG; nme:NMB0611; -. DR PATRIC; 20356511; VBINeiMen85645_0775. DR eggNOG; ENOG4105F38; Bacteria. DR eggNOG; COG1176; LUCA. DR HOGENOM; HOG000263582; -. DR KO; K11075; -. DR OMA; MLNTNFA; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; NMEN122586:GHGG-637-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 21 43 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 108 127 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 139 163 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 183 207 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 243 261 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 287 308 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 102 308 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 321 AA; 35787 MW; A2C7B7986C68C212 CRC64; MNLNKLKNKL FRRPGQRAVI AVPYIWLLVL FLIPFAIVLK ISFAEQEIAI PPFTPLTTID EDLGRLNIAV SYQNYADIFQ NFWSTLNPFG DGENSNIYLM TYWSSIKTAL TTTVICLLVG YPTAYAISRA NPSVRNGLLL AIMLPFWTSF LLRVYAWMGL LGHNGIVNNL LIKMGIISEP LDLFYNAFSL NLVMVYAYLP FMILPLYTQL VKLDNRLLEA ASDLGAGPVK SFLTITLPLS KTGIIAGSML VFVPAVGEFV IPELVGGSEN LMIGKVLWQA FFDQNNWPLA SAVAVVMVAL LVVPIALFQH YENRELEEGA K // ID Q7DDD1_NEIMB Unreviewed; 337 AA. AC Q7DDD1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN OrderedLocusNames=NMB1290 {ECO:0000313|EMBL:AAF41666.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41666.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41666.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41666.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC {ECO:0000256|RuleBase:RU000417}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000256|RuleBase:RU000416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41666.1; -; Genomic_DNA. DR PIR; A81101; A81101. DR RefSeq; NP_274310.1; NC_003112.2. DR RefSeq; WP_002222381.1; NC_003112.2. DR ProteinModelPortal; Q7DDD1; -. DR STRING; 122586.NMB1290; -. DR PaxDb; Q7DDD1; -. DR EnsemblBacteria; AAF41666; AAF41666; NMB1290. DR GeneID; 903712; -. DR KEGG; nme:NMB1290; -. DR PATRIC; 20358207; VBINeiMen85645_1615. DR eggNOG; ENOG4105DVF; Bacteria. DR eggNOG; COG0270; LUCA. DR HOGENOM; HOG000225506; -. DR KO; K00558; -. DR OMA; YLYRYAR; -. DR OrthoDB; EOG6PZXGV; -. DR BioCyc; NMEN122586:GHGG-1328-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00675; dcm; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41666.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41666.1}. FT DOMAIN 20 331 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 337 AA; 38291 MW; 2B94424FE9E76443 CRC64; MKNKIQNQLD NIVTLNNEKF TFIDLFAGIG GFRIAMENVG GRCVFSSEWD DKARQTYQVN FNDIPYGDIT LKETKAAIPS KFDVLTAGFP CQPFSIAGVS KKKSLGRETG FLDKAQGTLF FDVAEIIGKH RPKIFLLENV KNLVSHDKGN TFKVIKGTLE ELDYQIFYQV MNAKYYVPQN RERIFIVGFD RQYFNKEINF NFPSPPESQP KLKQILEDDV DNSFTLSDNL WLYLQNYAKK HKAKGNGFGF GLVDLDGISR TLSARYYKDG SEILIPQKGK NPRKLTPREC SRLMGFPKDF VIDAVSKTAA YKQFGNSIAV PLVQAIAKQI INELKNE // ID Q9JXP0_NEIMB Unreviewed; 180 AA. AC Q9JXP0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42280.1}; GN OrderedLocusNames=NMB1951 {ECO:0000313|EMBL:AAF42280.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42280.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42280.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42280.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42280.1; -; Genomic_DNA. DR PIR; H81023; H81023. DR RefSeq; NP_274945.1; NC_003112.2. DR RefSeq; WP_002225837.1; NC_003112.2. DR ProteinModelPortal; Q9JXP0; -. DR STRING; 122586.NMB1951; -. DR PaxDb; Q9JXP0; -. DR EnsemblBacteria; AAF42280; AAF42280; NMB1951. DR GeneID; 904199; -. DR KEGG; nme:NMB1951; -. DR PATRIC; 20359959; VBINeiMen85645_2484. DR eggNOG; ENOG4105KTH; Bacteria. DR eggNOG; COG1610; LUCA. DR HOGENOM; HOG000015154; -. DR KO; K09117; -. DR OMA; RDSIAQY; -. DR OrthoDB; EOG69SKHS; -. DR BioCyc; NMEN122586:GHGG-2008-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro. DR Gene3D; 1.10.10.410; -; 1. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR023168; GatB_Yqey_C. DR InterPro; IPR019004; Uncharacterised_YOR215C_mit. DR Pfam; PF09424; YqeY; 1. DR SUPFAM; SSF89095; SSF89095; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 38 178 YqeY. {ECO:0000259|Pfam:PF09424}. SQ SEQUENCE 180 AA; 19737 MW; 52D75DD8BEEA2153 CRC64; MRTHRKTCSA VCFAFQTASK PAVSIRHPSE DIMSLKIRLT EDMKTAMRAK DQVSLGTIRL INAAVKQFEV DERTEADDAK ITAILTKMVK QRKDSAKIYT EAGRQDLADK ENAEIEVLHR YLPQMLSAGE IRTEVEAAVA ETGAAGMADM GKVMGLLKTR LAGKADMGEV NKILKAVLTA // ID Q9K052_NEIMB Unreviewed; 325 AA. AC Q9K052; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Putative DNA polymerase III, delta prime subunit {ECO:0000313|EMBL:AAF41182.1}; GN OrderedLocusNames=NMB0769 {ECO:0000313|EMBL:AAF41182.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41182.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41182.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41182.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41182.1; -; Genomic_DNA. DR PIR; F81159; F81159. DR RefSeq; NP_273811.1; NC_003112.2. DR RefSeq; WP_002222732.1; NC_003112.2. DR ProteinModelPortal; Q9K052; -. DR STRING; 122586.NMB0769; -. DR PaxDb; Q9K052; -. DR EnsemblBacteria; AAF41182; AAF41182; NMB0769. DR GeneID; 902884; -. DR KEGG; nme:NMB0769; -. DR PATRIC; 20356911; VBINeiMen85645_0974. DR eggNOG; ENOG4108I64; Bacteria. DR eggNOG; COG0470; LUCA. DR HOGENOM; HOG000192592; -. DR KO; K02341; -. DR OMA; FAQGNHP; -. DR OrthoDB; EOG6W9X5M; -. DR BioCyc; NMEN122586:GHGG-800-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004622; DNA_pol_HolB. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00678; holB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 325 AA; 37001 MW; 1F4AB42DC58656D3 CRC64; MIYPWHNEQW RQIAEHWERR PNAWLFAGKK DTGKTTFARF AAKALLCETP APGCKPCGEC MSCHLFGQGS HPDFYEITPL SDEPENGRKL LQIKIDAVRE IIDNVYLTSV RGGLRVILIH PAESMNVQAA NSLLKVLEEP PPQVVFLLVS HAADKVLPTI KSRCRKMVLP APSHEEALAY LRERGVAEPE ERLAFHSGAP LFDEADGVRA LRIKLLDILA EPRLLKILDY AALFDKEKLP LAVFVGWMQK WLVDLGLCLQ HMKPVYYPAY EDRLLQTVSG FRPRNVFAAE DMLKQLAPYG FHTLNVKMQI EHLLINYLEL KKENG // ID Q9JXU6_NEIMB Unreviewed; 103 AA. AC Q9JXU6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42213.1}; GN OrderedLocusNames=NMB1879 {ECO:0000313|EMBL:AAF42213.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42213.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42213.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42213.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42213.1; -; Genomic_DNA. DR PIR; E81030; E81030. DR STRING; 122586.NMB1879; -. DR PaxDb; Q9JXU6; -. DR EnsemblBacteria; AAF42213; AAF42213; NMB1879. DR PATRIC; 20359791; VBINeiMen85645_2401. DR BioCyc; NMEN122586:GHGG-1935-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 103 AA; 11318 MW; 9C4D6692E9F9C8EB CRC64; MNTAAIYRQY QTYVRSDKSG WALDGCSDSA LIAQAKQPGL HLEMCINRFD SGITLSRMRG GGTGAFPTEI HNFSHNCALF VMVSGQNRLQ MGGREYRPSA GEI // ID Q9JZC7_NEIMB Unreviewed; 115 AA. AC Q9JZC7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41503.1}; GN OrderedLocusNames=NMB1112 {ECO:0000313|EMBL:AAF41503.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41503.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41503.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41503.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41503.1; -; Genomic_DNA. DR PIR; C81119; C81119. DR RefSeq; NP_274143.1; NC_003112.2. DR RefSeq; WP_002225232.1; NC_003112.2. DR STRING; 122586.NMB1112; -. DR PaxDb; Q9JZC7; -. DR EnsemblBacteria; AAF41503; AAF41503; NMB1112. DR GeneID; 903534; -. DR KEGG; nme:NMB1112; -. DR PATRIC; 20357790; VBINeiMen85645_1411. DR eggNOG; ENOG4105N1Q; Bacteria. DR eggNOG; COG4381; LUCA. DR HOGENOM; HOG000123658; -. DR OMA; GSYWADA; -. DR OrthoDB; EOG64R66W; -. DR BioCyc; NMEN122586:GHGG-1148-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010877; Phage_Mu_Gp46. DR Pfam; PF07409; GP46; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 115 AA; 13010 MW; 7268ABAAE89AE10C CRC64; MDKELNPSIG DYTGRTVDTL QNAVYIRLMT PLGSWWADKT LGSLLHLLQR EKDLQRVSLL AEQYADEALQ PIVKSGRADK ITVRAEQPHD GRLILHIRMD TAAGGFDYRH EVPVI // ID Q9K073_NEIMB Unreviewed; 164 AA. AC Q9K073; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine-pyrophosphokinase {ECO:0000313|EMBL:AAF41158.1}; DE EC=2.7.6.3 {ECO:0000313|EMBL:AAF41158.1}; GN Name=folK {ECO:0000313|EMBL:AAF41158.1}; GN OrderedLocusNames=NMB0745 {ECO:0000313|EMBL:AAF41158.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41158.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41158.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41158.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41158.1; -; Genomic_DNA. DR PIR; H81162; H81162. DR RefSeq; NP_273787.1; NC_003112.2. DR RefSeq; WP_002221222.1; NC_003112.2. DR ProteinModelPortal; Q9K073; -. DR STRING; 122586.NMB0745; -. DR PaxDb; Q9K073; -. DR EnsemblBacteria; AAF41158; AAF41158; NMB0745. DR GeneID; 902860; -. DR KEGG; nme:NMB0745; -. DR PATRIC; 20356861; VBINeiMen85645_0949. DR eggNOG; ENOG4105K8U; Bacteria. DR eggNOG; COG0801; LUCA. DR HOGENOM; HOG000217741; -. DR KO; K00950; -. DR OMA; DWFLNAA; -. DR OrthoDB; EOG6XHC8G; -. DR BioCyc; NMEN122586:GHGG-776-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.70.560; -; 1. DR InterPro; IPR000550; Hppk. DR Pfam; PF01288; HPPK; 1. DR SUPFAM; SSF55083; SSF55083; 1. DR TIGRFAMs; TIGR01498; folK; 1. DR PROSITE; PS00794; HPPK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000313|EMBL:AAF41158.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41158.1}. FT DOMAIN 91 102 HPPK. {ECO:0000259|PROSITE:PS00794}. SQ SEQUENCE 164 AA; 18182 MW; 87D55D0FF07A01AD CRC64; MNNRHFAVIA LGSNLENPAQ QVRAALDTLS SHPDIRLKQA SSLYMTAPVG YDNQPDFVNA VCTVSTTLDG IALLAELNRI EADFGRERSF RNAPRTLDLD IIDFDGISSD DTRLTLPHPR AHERSFVIRP LAEILPDFVL GKHGKVAELS KRLGNQGIRL LPDR // ID Q9JYF3_NEIMB Unreviewed; 389 AA. AC Q9JYF3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Trans-sulfuration enzyme family protein {ECO:0000313|EMBL:AAF41961.1}; GN OrderedLocusNames=NMB1609 {ECO:0000313|EMBL:AAF41961.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41961.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41961.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41961.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU362118}; CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. CC {ECO:0000256|RuleBase:RU362118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41961.1; -; Genomic_DNA. DR PIR; G81062; G81062. DR RefSeq; NP_274615.1; NC_003112.2. DR RefSeq; WP_002231905.1; NC_003112.2. DR ProteinModelPortal; Q9JYF3; -. DR STRING; 122586.NMB1609; -. DR PaxDb; Q9JYF3; -. DR EnsemblBacteria; AAF41961; AAF41961; NMB1609. DR GeneID; 904307; -. DR KEGG; nme:NMB1609; -. DR PATRIC; 20359106; VBINeiMen85645_2065. DR eggNOG; ENOG4105C28; Bacteria. DR eggNOG; COG0626; LUCA. DR HOGENOM; HOG000246417; -. DR KO; K10764; -. DR OMA; MTSQFAR; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; NMEN122586:GHGG-1657-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0071268; P:homocysteine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR006234; O-succ-hSer_sulfhydrylase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01325; O_suc_HS_sulf; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT MOD_RES 207 207 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 389 AA; 41911 MW; 8A331B1E3834F75E CRC64; MSKKLHPQTL AIRGGKEQTE YREHNQALFL TSSFMWDNAQ HAADLFSKKI KGFTYTRTAN PTTAAFEKRI AALEGAERAV ATSAGMSAIQ AAFFTFLQAG DHVISSRSLF GTTVGFINNI VAKFGIEVSH VSPTDINEWK AAVKANTKLL FLETPSNPLG EVADLEALAE LAHGIGALLV VDNSLLSPVG SQPLKHGADI SVSSATKAID GHGRVMGGVL AGSEELLAQV AMYCNSCGLA MSPFNAWQLL SGVETLSLRM EKQFDNALKI AQWLQAQPQV QAVYYTGLSD HPQAALIRKQ QNGGGIVIGF EVADQEAAWK VVDGVELFSR TANLGDVRST ITHPWTTTHG RMQPEEKLAA NIRPGLVRLS VGLEYVGDLI DDLKQALAR // ID Q9K116_NEIMB Unreviewed; 316 AA. AC Q9K116; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Cys regulon transcriptional activator {ECO:0000313|EMBL:AAF40821.1}; GN Name=cysB {ECO:0000313|EMBL:AAF40821.1}; GN OrderedLocusNames=NMB0381 {ECO:0000313|EMBL:AAF40821.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40821.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40821.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40821.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40821.1; -; Genomic_DNA. DR PIR; B81205; B81205. DR RefSeq; NP_273430.1; NC_003112.2. DR RefSeq; WP_002212453.1; NC_003112.2. DR ProteinModelPortal; Q9K116; -. DR STRING; 122586.NMB0381; -. DR PaxDb; Q9K116; -. DR EnsemblBacteria; AAF40821; AAF40821; NMB0381. DR GeneID; 902496; -. DR KEGG; nme:NMB0381; -. DR PATRIC; 20355927; VBINeiMen85645_0481. DR eggNOG; ENOG4105MBM; Bacteria. DR eggNOG; COG0583; LUCA. DR HOGENOM; HOG000260068; -. DR KO; K13634; -. DR OMA; QGHPLTK; -. DR OrthoDB; EOG6WQD4N; -. DR BioCyc; NMEN122586:GHGG-403-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 1 59 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. SQ SEQUENCE 316 AA; 35142 MW; 323298CCD38A70D8 CRC64; MKLQQLKYAL EVYQHNLNVS EAAEALFTSQ PGISKQIKLL EEEIGIQIFI RSGKRVVSVS QPGKVVLDIA ERILRDVQNI KNIGSEFTGQ DSGSLTVATT HTQARYALPL IVADFVKRYP KVNLTIKQGS PAAIARMVTS GEADLAIVTE RIDDHPELGK LPCYDWTHAV IVPNDHPLLE CRNPLRIEDL ARFPLITYEF AFNAGSSIAR AFSKARLEQP DVALAAADTD VLKTYVRLGL GVGLMAKMAY NPDTDGDLQL VDAAHLFEPS PTWIALRSDT YLRGYAYDFI QAFAPHLTRE KVDRILYTPI SEDFSI // ID Q9JYI7_NEIMB Unreviewed; 146 AA. AC Q9JYI7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Putative DNA polymerase holoenzyme chi subunit {ECO:0000313|EMBL:AAF41922.1}; GN OrderedLocusNames=NMB1568 {ECO:0000313|EMBL:AAF41922.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41922.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41922.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41922.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41922.1; -; Genomic_DNA. DR PIR; D81068; D81068. DR RefSeq; NP_274575.1; NC_003112.2. DR RefSeq; WP_002244237.1; NC_003112.2. DR ProteinModelPortal; Q9JYI7; -. DR STRING; 122586.NMB1568; -. DR PaxDb; Q9JYI7; -. DR EnsemblBacteria; AAF41922; AAF41922; NMB1568. DR GeneID; 904151; -. DR KEGG; nme:NMB1568; -. DR PATRIC; 20358998; VBINeiMen85645_2018. DR eggNOG; COG2927; LUCA. DR HOGENOM; HOG000263566; -. DR KO; K02339; -. DR OMA; YGAGQKV; -. DR OrthoDB; EOG68H887; -. DR BioCyc; NMEN122586:GHGG-1609-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.10110; -; 1. DR InterPro; IPR007459; DNA_pol3_chi. DR Pfam; PF04364; DNA_pol3_chi; 1. DR SUPFAM; SSF102400; SSF102400; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 146 AA; 16418 MW; 26BC2C0C9329C4D4 CRC64; MPKATFYTHV AQVPIFTCRL IARAIRDGGR ILVWSDSFGQ LQELDKMLWQ YEAESFIPHE IWETEEAMPS EPSVLLACGG NLPRIPEGMT VLNLSDGFWN TAPVLPARVL EIVGNSLEEL ADARERFTAY RRSGFAIEHH GMEGKA // ID Q9JZE1_NEIMB Unreviewed; 431 AA. AC Q9JZE1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41488.1}; GN OrderedLocusNames=NMB1096 {ECO:0000313|EMBL:AAF41488.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41488.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41488.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41488.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41488.1; -; Genomic_DNA. DR PIR; B81124; B81124. DR RefSeq; NP_274128.1; NC_003112.2. DR RefSeq; WP_002225244.1; NC_003112.2. DR STRING; 122586.NMB1096; -. DR PaxDb; Q9JZE1; -. DR EnsemblBacteria; AAF41488; AAF41488; NMB1096. DR GeneID; 903517; -. DR KEGG; nme:NMB1096; -. DR PATRIC; 20357753; VBINeiMen85645_1393. DR eggNOG; ENOG4108QUU; Bacteria. DR eggNOG; COG2369; LUCA. DR HOGENOM; HOG000218945; -. DR OMA; MQELAGM; -. DR OrthoDB; EOG6SNDXQ; -. DR BioCyc; NMEN122586:GHGG-1132-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006528; Phage_head_morphogenesis. DR InterPro; IPR020388; Put_Mu_head. DR Pfam; PF04233; Phage_Mu_F; 1. DR ProDom; PD097920; Uncharacterised_HI1570; 1. DR TIGRFAMs; TIGR01641; phageSPP1_gp7; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 56 188 Phage_Mu_F. {ECO:0000259|Pfam:PF04233}. SQ SEQUENCE 431 AA; 49323 MW; BAD3DA1E9E78177E CRC64; MPAPDLGFAL SLPPKKAIEW LESKKVTAES YRNLTASEIA KVYTIARMTD LDMLNDIKTS MVESAKSGQS FDDWRKGILN LLSNKGWLHP NGHNGKDIID PATGEVFGSP RRLETIYRTN MQTAYNAGQY QGYMANIDAR PYWMYDAVGD SRTRPAHSAI DGLVYRYDDP FWATFYPPNG YNCRCSVIAL SERDVERQGR IVGQSTADNL VETHKIYNKK GDTYLTLAYK APDGSLYTTD RGFDYNAGRM NYRPDLDKYD RALAHQFAKA EMGGADFKTS FKQLEKEFYE VKQRLDIDGK PDKEQKIKIR NALSRQLKFA AGVLSKETQE LAGMTRATVW LSDDTLVKQV DSREGQNFDD SYYAFLPDML QNPEHVIRDN RELIFTARYK GSALWAVLKY IKEVDEIYLQ SYRISNDKEI AKFMAKKKVL K // ID Q9K1D4_NEIMB Unreviewed; 230 AA. AC Q9K1D4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40682.1}; GN OrderedLocusNames=NMB0226 {ECO:0000313|EMBL:AAF40682.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40682.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40682.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40682.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40682.1; -; Genomic_DNA. DR PIR; D81223; D81223. DR RefSeq; NP_273283.1; NC_003112.2. DR RefSeq; WP_002215591.1; NC_003112.2. DR STRING; 122586.NMB0226; -. DR PaxDb; Q9K1D4; -. DR EnsemblBacteria; AAF40682; AAF40682; NMB0226. DR GeneID; 902338; -. DR KEGG; nme:NMB0226; -. DR PATRIC; 20355528; VBINeiMen85645_0288. DR eggNOG; ENOG4107UCH; Bacteria. DR eggNOG; COG1451; LUCA. DR HOGENOM; HOG000218649; -. DR KO; K07043; -. DR OMA; AKMPVHP; -. DR OrthoDB; EOG6FRCWC; -. DR BioCyc; NMEN122586:GHGG-241-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002725; DUF45. DR Pfam; PF01863; DUF45; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 230 AA; 26584 MW; EC88A5302E255B4D CRC64; MKRFTYTLSD GLCIEIELKR SAKKNLILRP VNMQTVSINV PPFFQDHALA NWLAANETIL RNTLAKTPVH PVSHPNLPEW IWYRGIKTKL DTHSQSHIRI TSSEILLPRK ETAAQIDHLR RLLNERAREY LLPRLEKHAA ETGLTPTATD LSNAKTFWGV CRPHTGIRLN WRLIGTPEYV ADYVCIHELC HLRHPDHSPR FWHLVNTLTP HTDNAKSWLK AHGRELFVLG // ID Q4W572_NEIMB Unreviewed; 240 AA. AC Q4W572; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=DnaJ protein, truncation {ECO:0000313|EMBL:AAY52149.1}; GN OrderedLocusNames=NMB1027 {ECO:0000313|EMBL:AAY52149.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52149.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52149.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52149.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52149.1; -; Genomic_DNA. DR RefSeq; NP_274061.1; NC_003112.2. DR RefSeq; WP_002217104.1; NC_003112.2. DR ProteinModelPortal; Q4W572; -. DR SMR; Q4W572; 2-67. DR STRING; 122586.NMB1027; -. DR PaxDb; Q4W572; -. DR EnsemblBacteria; AAY52149; AAY52149; NMB1027. DR GeneID; 903191; -. DR KEGG; nme:NMB1027; -. DR PATRIC; 20357589; VBINeiMen85645_1311. DR eggNOG; ENOG4105FTZ; Bacteria. DR eggNOG; COG2214; LUCA. DR eggNOG; COG3671; LUCA. DR HOGENOM; HOG000218979; -. DR OMA; SKRTQYD; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; NMEN122586:GHGG-1064-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 219 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 69 J. {ECO:0000259|PROSITE:PS50076}. SQ SEQUENCE 240 AA; 27910 MW; 54096B139B040D1B CRC64; MDKDLYAVLG VSPQAGADEI KRAYRKLAMK YHPDRNPGNP KAEEKFKEIQ RAYDTLSDLS KRMQYDASFR RHEERGRQEE AFRREQARRE QFYREQMRRE QAFRQAFERQ ASRSCHTYEP SGGGSGRNYV LAAYILFGLG AIMLFMPIVG VIFAYMPIVG VILAYMKRNS LDSIVYAAHT EYLIKTFWRT FWLYILGALT ALLGIGVLII IATNVWYFYR IIAGFIRFNG GRAVAPEKWI // ID Q7DDQ5_NEIMB Unreviewed; 508 AA. AC Q7DDQ5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Sodium/proline symporter {ECO:0000313|EMBL:AAF40841.1}; GN Name=putP {ECO:0000313|EMBL:AAF40841.1}; GN OrderedLocusNames=NMB0402 {ECO:0000313|EMBL:AAF40841.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40841.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40841.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40841.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) CC (TC 2.A.21) family. {ECO:0000256|RuleBase:RU362091}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40841.1; -; Genomic_DNA. DR PIR; G81202; G81202. DR RefSeq; NP_273451.1; NC_003112.2. DR RefSeq; WP_002224913.1; NC_003112.2. DR STRING; 122586.NMB0402; -. DR PaxDb; Q7DDQ5; -. DR EnsemblBacteria; AAF40841; AAF40841; NMB0402. DR GeneID; 902516; -. DR KEGG; nme:NMB0402; -. DR PATRIC; 20355987; VBINeiMen85645_0511. DR eggNOG; ENOG4105CK7; Bacteria. DR eggNOG; COG0591; LUCA. DR HOGENOM; HOG000282935; -. DR KO; K11928; -. DR OMA; VHKFDLS; -. DR OrthoDB; EOG6HB9QC; -. DR BioCyc; NMEN122586:GHGG-424-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005298; F:proline:sodium symporter activity; IEA:InterPro. DR GO; GO:0031402; F:sodium ion binding; IEA:InterPro. DR InterPro; IPR011851; Na/Pro_symporter. DR InterPro; IPR001734; Na/solute_symporter. DR InterPro; IPR018212; Na/solute_symporter_CS. DR PANTHER; PTHR11819; PTHR11819; 1. DR Pfam; PF00474; SSF; 1. DR TIGRFAMs; TIGR02121; Na_Pro_sym; 1. DR TIGRFAMs; TIGR00813; sss; 1. DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1. DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1. DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00431219}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00431219, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 149 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 251 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 373 392 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 404 423 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 430 448 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 468 486 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 508 AA; 54331 MW; 4BCD02894C8D8063 CRC64; MNPMYITFAI YLVAVLLIGL AAYFSTRNFD DYILGGRSLG PFVTAMSAGA SDMSGWLLMG LPGAIYLSGL NEAWIAIGLL VGAYFNWLLV AGRLRVHTEY ANNALTLPDY FFHRFGAGGH LMKVVSALII LFFFTIYCAS GIVAGATLFQ SLFEGMTYNQ AMWLGAGATI AYTFLGGFLA VSWTDTLQAS LMIFALILTP VMVYLGLGGA EQMSAAIQSV AAGTGKEYGS LFAGTTVIGI ISTAAWGLGY FGQPHILARF MAAESAKSLV SARRIGMTWM ALCLAGAVAV GYFGIAYFGA NPDKVSSMSG NHERIFIALS TLLFNPWIAG IILSAILAAV MSTLSCQLLV CSSAITEDFY KGFLRKNAQQ SELVWVGRLM VLAIAVISIL IASDPNSKVL GLVSYAWAGF GAAFGPIVIL SVLWKRITAY GALSGMVAGA LTVVVWAEWV KKPAQAAGES GLLTMYEIVP GFIVCLIVAV LVSLFNKEPS RETQERFEKA DADYRATR // ID Q9K114_NEIMB Unreviewed; 98 AA. AC Q9K114; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40824.1}; GN OrderedLocusNames=NMB0384 {ECO:0000313|EMBL:AAF40824.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40824.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40824.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40824.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40824.1; -; Genomic_DNA. DR PIR; E81205; E81205. DR STRING; 122586.NMB0384; -. DR PaxDb; Q9K114; -. DR EnsemblBacteria; AAF40824; AAF40824; NMB0384. DR BioCyc; NMEN122586:GHGG-406-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 98 AA; 10990 MW; FEB21E7BA5C844AF CRC64; MDGIVPDVCG TVCRIWFYHQ PFSVETPSVA AIEPNRWRKL PLCIRGGVQC GALICRLCVE TGWSVHTGTV WPKLKVKYAE TLNEPLYCLY GLCCLAMI // ID Q9K074_NEIMB Unreviewed; 159 AA. AC Q9K074; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41157.1}; GN OrderedLocusNames=NMB0744 {ECO:0000313|EMBL:AAF41157.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41157.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41157.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41157.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41157.1; -; Genomic_DNA. DR PIR; G81162; G81162. DR RefSeq; NP_273786.1; NC_003112.2. DR RefSeq; WP_002225446.1; NC_003112.2. DR STRING; 122586.NMB0744; -. DR PaxDb; Q9K074; -. DR EnsemblBacteria; AAF41157; AAF41157; NMB0744. DR GeneID; 902859; -. DR KEGG; nme:NMB0744; -. DR PATRIC; 20356859; VBINeiMen85645_0948. DR eggNOG; COG3467; LUCA. DR HOGENOM; HOG000218857; -. DR KO; K07005; -. DR OMA; MAVQPFL; -. DR OrthoDB; EOG6BS8R0; -. DR BioCyc; NMEN122586:GHGG-775-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR012349; Split_barrel_FMN-bd. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 159 AA; 18009 MW; 8D03E55E6BF95BCA CRC64; MPESIFKQIS LDILKLHRDS VYSLLATSGC NCQVHEAAYV NIDGKYYIAL SCEPEVGEVK TGILLIEDES RNLRLSWVGS ARELDCKDNA YKRALSALSR KLGRCKDRLH TAVQPFLLEL VPEKGRFSVG DEEVWISRND LVRALYPVGY SMRQAVFQI // ID Q9JZ21_NEIMB Unreviewed; 494 AA. AC Q9JZ21; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Carboxy-terminal peptidase {ECO:0000313|EMBL:AAF41707.1}; GN Name=prc {ECO:0000313|EMBL:AAF41707.1}; GN OrderedLocusNames=NMB1332 {ECO:0000313|EMBL:AAF41707.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41707.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41707.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41707.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the peptidase S41A family. CC {ECO:0000256|RuleBase:RU004404}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41707.1; -; Genomic_DNA. DR PIR; G81095; G81095. DR RefSeq; NP_274351.1; NC_003112.2. DR RefSeq; WP_002225159.1; NC_003112.2. DR ProteinModelPortal; Q9JZ21; -. DR STRING; 122586.NMB1332; -. DR PaxDb; Q9JZ21; -. DR EnsemblBacteria; AAF41707; AAF41707; NMB1332. DR GeneID; 903754; -. DR KEGG; nme:NMB1332; -. DR PATRIC; 20358319; VBINeiMen85645_1671. DR eggNOG; ENOG4105CN1; Bacteria. DR eggNOG; COG0793; LUCA. DR HOGENOM; HOG000038764; -. DR KO; K03797; -. DR OMA; DPHSSYY; -. DR OrthoDB; EOG6PS5W5; -. DR BioCyc; NMEN122586:GHGG-1370-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004447; Peptidase_S41A. DR InterPro; IPR005151; Tail-specific_protease. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF03572; Peptidase_S41; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00245; TSPc; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR TIGRFAMs; TIGR00225; prc; 1. DR PROSITE; PS50106; PDZ; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU004404}; KW Protease {ECO:0000256|RuleBase:RU004404}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Serine protease {ECO:0000256|RuleBase:RU004404}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 494 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327851. FT DOMAIN 93 161 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 494 AA; 53238 MW; CD96DD73AC0598AF CRC64; MSKPVFKKIA LYTLGAISGV AVSLAVQGFA AEKDRRDNEV LPVQSIRTMA EVYGQIKANY YQDKPDADLF EGAMKGMVAG LDPHSEYMDK KGYAEIKEST SGEFGGLGME IGQEDGFVKV VSPIEDTPAE RAGVKSGDFI VKIDNVSTRG MTVSEAVKKM RGKPGTKITL TLSRKNADKP IVVNLTRAII KVKSVRHHLI EPDYGYIRVS QFQERTVESV NTAAKELVKE NKGKPLKGLV LDLRDDPGGL LTGAVGVSAA FLPSEAVVVS TKGRDGKDRM VLKAIPEDYV YGMGGDSLAG IPAELKTIPM TVLVNSGSAS ASEIVAGALQ DHKRAVIVGT QSFGKGSVQT LIPLSNGSAV KLTTALYYTP NDRSIQAQGI VPDVEVKDKE RIFESREADL VGHIGNPLGG EDVNGETLAV PLEKDADKPA VKEKGKKKKD EDLSSRRIPN PAKDDQLRKA LDLVKSPEQW QKSLGLAAKK PVSNKDKKDK KDKK // ID Q9JXT3_NEIMB Unreviewed; 267 AA. AC Q9JXT3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Type II restriction enzyme DpnI {ECO:0000313|EMBL:AAF42227.1}; DE EC=3.1.21.4 {ECO:0000313|EMBL:AAF42227.1}; GN Name=dpnC {ECO:0000313|EMBL:AAF42227.1}; GN OrderedLocusNames=NMB1896 {ECO:0000313|EMBL:AAF42227.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42227.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42227.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42227.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42227.1; -; Genomic_DNA. DR PIR; F81029; F81029. DR RefSeq; NP_274891.1; NC_003112.2. DR RefSeq; WP_002225800.1; NC_003112.2. DR STRING; 122586.NMB1896; -. DR PaxDb; Q9JXT3; -. DR EnsemblBacteria; AAF42227; AAF42227; NMB1896. DR GeneID; 904280; -. DR KEGG; nme:NMB1896; -. DR PATRIC; 20359829; VBINeiMen85645_2419. DR eggNOG; ENOG4108HED; Bacteria. DR eggNOG; ENOG410YTMJ; LUCA. DR HOGENOM; HOG000067092; -. DR KO; K01155; -. DR OMA; HHIMCSI; -. DR OrthoDB; EOG67Q982; -. DR BioCyc; NMEN122586:GHGG-1953-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR InterPro; IPR010324; DRP. DR InterPro; IPR024064; FdhE-like. DR Pfam; PF06044; DpnI; 1. DR SUPFAM; SSF144020; SSF144020; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42227.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 267 AA; 31293 MW; D8B82C85A8CA8B09 CRC64; MNLFFDTELG KQQNKATHKI RVMSEAWLEK NGYCPCCGSK PMQRFANNKP VADLFCPNCH EQYELKSKNQ KTIGNSVPDG AYHTMLERIR SDTNPNFFFL AYKKADYSIR QLVLVPKHFI TPDMIIPRNK GIKNRPNHIM CSINLAPLPE SGKIFLIDNS RIIEPETVLK KWQSNLFLRN QNAERKGWLL AVMKCIDQLP EEFTLSQMYE FENKLSIQFP QNNHIRDKIR QQLQILRDQN TIEFIGRGLY KKSINCAQLP RYFDFKS // ID Q9JXN3_NEIMB Unreviewed; 275 AA. AC Q9JXN3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=VacJ-related protein {ECO:0000313|EMBL:AAF42290.1}; GN OrderedLocusNames=NMB1961 {ECO:0000313|EMBL:AAF42290.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42290.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42290.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42290.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42290.1; -; Genomic_DNA. DR PIR; B81022; B81022. DR RefSeq; NP_274955.1; NC_003112.2. DR RefSeq; WP_002214840.1; NC_003112.2. DR STRING; 122586.NMB1961; -. DR PaxDb; Q9JXN3; -. DR EnsemblBacteria; AAF42290; AAF42290; NMB1961. DR GeneID; 904189; -. DR KEGG; nme:NMB1961; -. DR PATRIC; 20359983; VBINeiMen85645_2496. DR eggNOG; ENOG410903C; Bacteria. DR eggNOG; COG2853; LUCA. DR HOGENOM; HOG000220800; -. DR KO; K04754; -. DR OMA; WRDYVPM; -. DR OrthoDB; EOG6677N2; -. DR BioCyc; NMEN122586:GHGG-2018-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR InterPro; IPR007428; VacJ. DR PANTHER; PTHR30035; PTHR30035; 1. DR Pfam; PF04333; MlaA; 1. DR PRINTS; PR01805; VACJLIPOPROT. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 275 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332228. SQ SEQUENCE 275 AA; 29513 MW; 75FD32FE6AA7443A CRC64; MKKTAYAFLL LIGFASAPAF AETRPADPYE GYNRAVFKFN DQADRYIFAP AARGYRKVAP KPVRAGVSNF FNNLCDVVSF GSNILRLDIK RASEDLVRVG INTTFGLGGL IDIAGAGGIP DNKNTLGDTF ASWGWKNSNY FVLPVLGPST VRDALGTGIT SVYSPKNIVF RTPVGRWGTT AVSAVSTREG LLDLTDSLDE AAIDKYSYTR DLYMKVRARQ TGATPAEGTE DNIDIDELVE SAETGAAETA VQEDSVSETQ AEAAGEAETQ PGTQP // ID Q9JY94_NEIMB Unreviewed; 332 AA. AC Q9JY94; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AAF42033.1}; DE EC=1.1.1.28 {ECO:0000313|EMBL:AAF42033.1}; GN Name=ldhA {ECO:0000313|EMBL:AAF42033.1}; GN OrderedLocusNames=NMB1685 {ECO:0000313|EMBL:AAF42033.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42033.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42033.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42033.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42033.1; -; Genomic_DNA. DR PIR; F81053; F81053. DR RefSeq; NP_274689.1; NC_003112.2. DR RefSeq; WP_002222131.1; NC_003112.2. DR ProteinModelPortal; Q9JY94; -. DR STRING; 122586.NMB1685; -. DR PaxDb; Q9JY94; -. DR EnsemblBacteria; AAF42033; AAF42033; NMB1685. DR GeneID; 903422; -. DR KEGG; nme:NMB1685; -. DR PATRIC; 20359321; VBINeiMen85645_2167. DR eggNOG; ENOG4105C5I; Bacteria. DR eggNOG; COG1052; LUCA. DR HOGENOM; HOG000136695; -. DR KO; K03778; -. DR OMA; VIVTAHQ; -. DR OrthoDB; EOG61VZ8G; -. DR BioCyc; NMEN122586:GHGG-1740-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003720, KW ECO:0000313|EMBL:AAF42033.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 328 2-Hacid_dh. {ECO:0000259|Pfam:PF00389}. FT DOMAIN 110 297 2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}. SQ SEQUENCE 332 AA; 36645 MW; EEB7648152C823E2 CRC64; MKIAIYGTKS YDREHFTRAN RHFGFELEFF DFMLDAKTAK MAEGAEAVCI FVNDDGSRPV LEKLAQIGVK TVALRCAGFN NVDLKAAEEL GLKVVRVPAY SPESVAEHTV GLMLTLNRRI HKAYQRTRDA NFSLEGLTGF NMYGKTAGVI GTGKIGIATM RILKGFGMNL LAYDPFCNPE AEKIGGKYVD LDELYARSDI ITLHCPATPE NHYMLNEAAF DKMKDGVMII NTSRGGLIDS AAAIEALKRR KIGALGMDVY ENERELFFED KSNDVITDDV FRRLSSCHNV LFTGHQAFLT EEALGNISEV TLSNIREVGQ TGDCGNAVRA DG // ID Q9K082_NEIMB Unreviewed; 149 AA. AC Q9K082; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=PTS system, nitrogen regulatory IIA protein {ECO:0000313|EMBL:AAF41149.1}; DE EC=2.7.1.69 {ECO:0000313|EMBL:AAF41149.1}; GN Name=ptsN {ECO:0000313|EMBL:AAF41149.1}; GN OrderedLocusNames=NMB0736 {ECO:0000313|EMBL:AAF41149.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41149.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41149.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41149.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2A0J} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS). RX PubMed=16092953; DOI=10.1186/1472-6807-5-13; RA Ren J., Sainsbury S., Berrow N.S., Alderton D., Nettleship J.E., RA Stammers D.K., Saunders N.J., Owens R.J.; RT "Crystal structure of nitrogen regulatory protein IIANtr from RT Neisseria meningitidis."; RL BMC Struct. Biol. 5:13-13(2005). CC -!- SIMILARITY: Contains PTS EIIA type-2 domain. CC {ECO:0000256|SAAS:SAAS00502352}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41149.1; -; Genomic_DNA. DR PIR; H81164; H81164. DR RefSeq; NP_273778.1; NC_003112.2. DR RefSeq; WP_002222750.1; NC_003112.2. DR PDB; 2A0J; X-ray; 2.50 A; A=1-149. DR PDBsum; 2A0J; -. DR ProteinModelPortal; Q9K082; -. DR SMR; Q9K082; 2-147. DR STRING; 122586.NMB0736; -. DR PaxDb; Q9K082; -. DR EnsemblBacteria; AAF41149; AAF41149; NMB0736. DR GeneID; 902849; -. DR KEGG; nme:NMB0736; -. DR PATRIC; 20356831; VBINeiMen85645_0936. DR eggNOG; ENOG4107RM2; Bacteria. DR eggNOG; COG1762; LUCA. DR HOGENOM; HOG000227559; -. DR KO; K02806; -. DR OMA; QSETTFE; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; NMEN122586:GHGG-765-MONOMER; -. DR EvolutionaryTrace; Q9K082; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR InterPro; IPR006320; PTS_Nitro_regul. DR Pfam; PF00359; PTS_EIIA_2; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR TIGRFAMs; TIGR01419; nitro_reg_IIA; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2A0J}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41149.1}. FT DOMAIN 6 149 PTS EIIA type-2. FT {ECO:0000259|PROSITE:PS51094}. SQ SEQUENCE 149 AA; 16092 MW; 1131ABCFD9285D66 CRC64; MSLIGEILPL SHIVLDMEVG SKKRLFEEAG LLLERESSLS HADVFECLFA REKLGSTGLG QGVAIPHGRH AGVKQATGAF IRTREPVGFD APDGKPVSLI FILLVPENAT GEHLEVLSKL AGKFSQKSIR ESLMTVSSAE EVRAILTEE // ID Q9JYP3_NEIMB Unreviewed; 164 AA. AC Q9JYP3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41845.1}; GN OrderedLocusNames=NMB1489 {ECO:0000313|EMBL:AAF41845.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41845.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41845.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41845.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41845.1; -; Genomic_DNA. DR PIR; G81077; G81077. DR RefSeq; NP_274497.1; NC_003112.2. DR RefSeq; WP_002216867.1; NC_003112.2. DR ProteinModelPortal; Q9JYP3; -. DR SMR; Q9JYP3; 1-164. DR STRING; 122586.NMB1489; -. DR PaxDb; Q9JYP3; -. DR EnsemblBacteria; AAF41845; AAF41845; NMB1489. DR GeneID; 903911; -. DR KEGG; nme:NMB1489; -. DR PATRIC; 20358746; VBINeiMen85645_1882. DR eggNOG; ENOG4105WEK; Bacteria. DR eggNOG; ENOG41123B4; LUCA. DR HOGENOM; HOG000220757; -. DR OMA; CIGHELL; -. DR OrthoDB; EOG6423DR; -. DR BioCyc; NMEN122586:GHGG-1529-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1590.10; -; 1. DR InterPro; IPR009888; CdiI-o11. DR InterPro; IPR023127; NMB0488-like_domain. DR Pfam; PF07262; DUF1436; 1. DR SUPFAM; SSF160207; SSF160207; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 164 AA; 18629 MW; 57C329C80670224A CRC64; MIFKQNQNYW AVFDANKETL IVQTCSGLGL TAIDHLYPPH ILPLDTDNET LGTTVLQALA NSRTFVYDSP EDQDFFDTEK IRQRYEDWVA KLCGNLGYKT RRALFKNMMS VDIWLHNGCL KISPSRHVKL EAWNAIDADD VILSLDNSPE EIGAGLKLAL SHCR // ID Q9JZM8_NEIMB Unreviewed; 380 AA. AC Q9JZM8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Chloride channel protein-related protein {ECO:0000313|EMBL:AAF41386.1}; GN OrderedLocusNames=NMB0982 {ECO:0000313|EMBL:AAF41386.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41386.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41386.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41386.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41386.1; -; Genomic_DNA. DR PIR; H81134; H81134. DR RefSeq; NP_274019.1; NC_003112.2. DR RefSeq; WP_010980880.1; NC_003112.2. DR ProteinModelPortal; Q9JZM8; -. DR STRING; 122586.NMB0982; -. DR PaxDb; Q9JZM8; -. DR EnsemblBacteria; AAF41386; AAF41386; NMB0982. DR GeneID; 903102; -. DR KEGG; nme:NMB0982; -. DR PATRIC; 20357455; VBINeiMen85645_1242. DR eggNOG; ENOG4106UAB; Bacteria. DR eggNOG; COG0038; LUCA. DR HOGENOM; HOG000184895; -. DR OMA; IQHVAYG; -. DR OrthoDB; EOG6F81SB; -. DR BioCyc; NMEN122586:GHGG-1019-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro. DR Gene3D; 1.10.3080.10; -; 1. DR InterPro; IPR014743; Cl-channel_core. DR InterPro; IPR001807; Cl-channel_volt-gated. DR Pfam; PF00654; Voltage_CLC; 1. DR PRINTS; PR00762; CLCHANNEL. DR SUPFAM; SSF81340; SSF81340; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|SAAS:SAAS00438323}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00438323, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 216 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 281 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 348 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 374 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 380 AA; 40077 MW; EC55EE67DD5E2E09 CRC64; MHFIQHTAYG YGADGVYTSF REGVAQASGM RRVAVLTLCG AVAGSGWWLL KRFGKPQIEI KAALKQPLQG LPFLTTVFHV LLQIITVGLG SPLGREVAPR EMTAAFAFAG GKRLGLDEGE MRLLIACASG AGLAAVYNVP LASTLFILEA MLGVWTQQAV AAALLTSVIA TAVARIGLGD VQQYHPANLT VNTSLLWFSA VIGPILGVAA VFFQRTAQKF PFIKRDNIKI IPLAVCMFAL IGVISVWFPE ILGNGKAGNQ LTFGGLTDWQ HSLGLTAVKW LVVLMALAVG AYGGLITPSM MLGSTIAFAA ATAWNSVFPE MSSESAAIVG AAVFLGVSLK MPLTAIAFIL ELTYAPVALL MPLCTGMAGA VWVAKKMGFK // ID Q7DD39_NEIMB Unreviewed; 133 AA. AC Q7DD39; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42430.1}; GN OrderedLocusNames=NMB2120 {ECO:0000313|EMBL:AAF42430.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42430.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42430.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42430.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42430.1; -; Genomic_DNA. DR PIR; A81005; A81005. DR RefSeq; NP_275106.1; NC_003112.2. DR RefSeq; WP_002215114.1; NC_003112.2. DR STRING; 122586.NMB2120; -. DR PaxDb; Q7DD39; -. DR EnsemblBacteria; AAF42430; AAF42430; NMB2120. DR GeneID; 903473; -. DR KEGG; nme:NMB2120; -. DR PATRIC; 20360414; VBINeiMen85645_2703. DR HOGENOM; HOG000218703; -. DR OMA; NERYAEW; -. DR OrthoDB; EOG683S9H; -. DR BioCyc; NMEN122586:GHGG-2185-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 133 AA; 15680 MW; ABC7C8C4C42FB65F CRC64; MKLKSLDFPT GYFYFDNAAI NSDKVEVIAV GYRNTDKTIK IFIEDVIHFR VVDESYFIDT FMDLISEDAD RALLHENGGQ SFFELLDECY AEWILKESYF PLNREFFKYY IFMFEQTFIE IIGSSATYSI IEG // ID Q9K0T9_NEIMB Unreviewed; 215 AA. AC Q9K0T9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40910.1}; GN OrderedLocusNames=NMB0473 {ECO:0000313|EMBL:AAF40910.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40910.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40910.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40910.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40910.1; -; Genomic_DNA. DR PIR; D81194; D81194. DR RefSeq; NP_273520.1; NC_003112.2. DR RefSeq; WP_010980799.1; NC_003112.2. DR STRING; 122586.NMB0473; -. DR ESTHER; neimb-q9k0t9; Duf_452. DR PaxDb; Q9K0T9; -. DR EnsemblBacteria; AAF40910; AAF40910; NMB0473. DR GeneID; 902589; -. DR KEGG; nme:NMB0473; -. DR PATRIC; 20356198; VBINeiMen85645_0620. DR eggNOG; ENOG4105HSA; Bacteria. DR eggNOG; COG2830; LUCA. DR HOGENOM; HOG000144228; -. DR KO; K09789; -. DR OMA; IVYFAGW; -. DR OrthoDB; EOG6S7XW4; -. DR BioCyc; NMEN122586:GHGG-497-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR007398; DUF452. DR Pfam; PF04301; DUF452; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 215 AA; 24900 MW; C034EE02F929401D CRC64; METKFYNHQG GHLILYFAGW GTPPDAVNHL ILPENHDLLI CYDYQDLNLD FDFSAYRHIR LVAWSMGVWA AERALQGIRL KSATAVNGTG LPCDDNFGIP CTVFKGTLEN LTENTRLKFE RRMCGDKASF EDYQQFPARP FGEIHQELIA LFAMIGQDRR TDLIRWTNAL VGSGDKIFMP ANQHRYWTPR CTVREIDVGH YLFSRFTHWS ALWNH // ID Q9JYJ5_NEIMB Unreviewed; 157 AA. AC Q9JYJ5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41911.1}; GN OrderedLocusNames=NMB1557 {ECO:0000313|EMBL:AAF41911.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41911.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41911.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41911.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41911.1; -; Genomic_DNA. DR PIR; B81069; B81069. DR RefSeq; NP_274564.1; NC_003112.2. DR RefSeq; WP_002222219.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ5; -. DR STRING; 122586.NMB1557; -. DR PaxDb; Q9JYJ5; -. DR EnsemblBacteria; AAF41911; AAF41911; NMB1557. DR GeneID; 904118; -. DR KEGG; nme:NMB1557; -. DR PATRIC; 20358968; VBINeiMen85645_2003. DR eggNOG; ENOG4105NG1; Bacteria. DR eggNOG; COG2847; LUCA. DR HOGENOM; HOG000217164; -. DR KO; K09796; -. DR OMA; KMGGAFM; -. DR OrthoDB; EOG699768; -. DR BioCyc; NMEN122586:GHGG-1598-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007410; DR1885-like_metal-bd. DR Pfam; PF04314; DUF461; 1. DR SUPFAM; SSF110087; SSF110087; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 157 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327711. FT DOMAIN 24 133 DUF461. {ECO:0000259|Pfam:PF04314}. SQ SEQUENCE 157 AA; 16977 MW; E05045AF107E0E2E CRC64; MKKLLAAVMM AGLAGAVSAA GVHVEDGWAR TTVEGMKIGG AFMKIHNDEA KQDFLLGGSS PVADRVEVHT HINDNGVMRM REVEGGVPLE AKSVTELKPG SYHVMFMGLK KQLKEGDKIP VTLKFKNAKA QTVQLEVKIA PMPAMNHGHH HGEAHQH // ID Q9JYJ1_NEIMB Unreviewed; 300 AA. AC Q9JYJ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41916.1}; GN OrderedLocusNames=NMB1562 {ECO:0000313|EMBL:AAF41916.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41916.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41916.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41916.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41916.1; -; Genomic_DNA. DR PIR; G81069; G81069. DR RefSeq; NP_274569.1; NC_003112.2. DR RefSeq; WP_002225035.1; NC_003112.2. DR STRING; 122586.NMB1562; -. DR PaxDb; Q9JYJ1; -. DR DNASU; 904132; -. DR EnsemblBacteria; AAF41916; AAF41916; NMB1562. DR GeneID; 904132; -. DR KEGG; nme:NMB1562; -. DR PATRIC; 20358980; VBINeiMen85645_2009. DR eggNOG; ENOG4105DWU; Bacteria. DR eggNOG; COG2431; LUCA. DR HOGENOM; HOG000275902; -. DR OMA; MLFIFAP; -. DR OrthoDB; EOG6N3CR6; -. DR BioCyc; NMEN122586:GHGG-1603-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005642; LysO. DR Pfam; PF03956; DUF340; 1. DR ProDom; PD022789; DUF340_prk_mem; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 185 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 226 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 299 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 300 AA; 31798 MW; DE27204CF19C46A2 CRC64; MDSLMTLLSV LIPMFAGFFI RVPKPYLPAL DKVLSVLVYA VLLLIGVSLS RVEDLGSRLD DMALTVLWLF VCTVGANLLA LAVLGKLFPW RIKGKGKGVS VGVSGSVGQL GCVLLGFAFG KLMRDIWMPS ESAGMYCLML LVFLIGVQLK SSGVSLRQVL VNRRGIRLSV WFMLSSLSGG LLFAASTDGV SWTKGLAMAS GFGWYSLSGL VMTEAYGAVW GSIMLLNDLA RELFALAFIP LLMKRFPDAA VGVGGATSMD FTLPVIQGAG GLEVVPVAVS FGVVVNIAAP FLMVVFSALG // ID Q9K0D5_NEIMB Unreviewed; 133 AA. AC Q9K0D5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41094.1}; GN OrderedLocusNames=NMB0676 {ECO:0000313|EMBL:AAF41094.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41094.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41094.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41094.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41094.1; -; Genomic_DNA. DR PIR; B81171; B81171. DR RefSeq; NP_273718.1; NC_003112.2. DR RefSeq; WP_002225502.1; NC_003112.2. DR STRING; 122586.NMB0676; -. DR PaxDb; Q9K0D5; -. DR EnsemblBacteria; AAF41094; AAF41094; NMB0676. DR GeneID; 902787; -. DR KEGG; nme:NMB0676; -. DR PATRIC; 20356655; VBINeiMen85645_0846. DR HOGENOM; HOG000218834; -. DR OrthoDB; EOG6VF34J; -. DR BioCyc; NMEN122586:GHGG-703-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 133 AA; 14989 MW; 7855097BD36AA5B0 CRC64; MQQHIEKWQH LSREEQKILA EVWGLVQNDD QEVHYEMLKL NAPDEASGEF WFRMAETLST LPPNRSLGLR MNGGRLATAV SILSVMIEDN PDIPQLWAQK ITALNYSGLN LNQYGVASPC RTICTVCGFV ALS // ID Q9JYA2_NEIMB Unreviewed; 279 AA. AC Q9JYA2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Cytochrome c5 {ECO:0000313|EMBL:AAF42025.1}; GN OrderedLocusNames=NMB1677 {ECO:0000313|EMBL:AAF42025.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42025.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42025.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42025.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42025.1; -; Genomic_DNA. DR PIR; G81054; G81054. DR RefSeq; NP_274681.1; NC_003112.2. DR RefSeq; WP_002216672.1; NC_003112.2. DR ProteinModelPortal; Q9JYA2; -. DR STRING; 122586.NMB1677; -. DR PaxDb; Q9JYA2; -. DR EnsemblBacteria; AAF42025; AAF42025; NMB1677. DR GeneID; 903433; -. DR KEGG; nme:NMB1677; -. DR PATRIC; 20359301; VBINeiMen85645_2158. DR eggNOG; ENOG4105MPD; Bacteria. DR eggNOG; COG3245; LUCA. DR OMA; VNDRIKP; -. DR OrthoDB; EOG6HMX9R; -. DR BioCyc; NMEN122586:GHGG-1731-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 2. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR002323; Cyt_CIE. DR Pfam; PF13442; Cytochrome_CBB3; 2. DR PRINTS; PR00607; CYTCHROMECIE. DR SUPFAM; SSF46626; SSF46626; 2. DR PROSITE; PS51007; CYTC; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 69 151 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. FT DOMAIN 195 275 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 279 AA; 28755 MW; 2947E501643EA22C CRC64; MKQLRDNKAQ GSALFTLVSG IVIVIAVLYF LIKLAGSGSF GDVDATTEAA TQTRIQPVGQ LTMGDGIPVG ERQGEQIFGK ICIQCHAADS NVPNAPKLEH NGDWAPRIAQ GFDTLFQHAL NGFNAMPAKG GAADLTDQEL KRAITYMANK SGGSFPNPDE AAPADNAASG TASAPADSAA PAEAKAEDKG AAAPAVGVDG KKVFEATCQV CHGGSIPGIP GIGKKDDWAP RIKKGKETLH KHALEGFNAM PAKGGNAGLS DDEVKAAVDY MANQSGAKF // ID Q7DDS4_NEIMB Unreviewed; 157 AA. AC Q7DDS4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40678.1}; GN OrderedLocusNames=NMB0222 {ECO:0000313|EMBL:AAF40678.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40678.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40678.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40678.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40678.1; -; Genomic_DNA. DR PIR; H81222; H81222. DR RefSeq; NP_273279.1; NC_003112.2. DR RefSeq; WP_002215584.1; NC_003112.2. DR STRING; 122586.NMB0222; -. DR PaxDb; Q7DDS4; -. DR EnsemblBacteria; AAF40678; AAF40678; NMB0222. DR GeneID; 902334; -. DR KEGG; nme:NMB0222; -. DR PATRIC; 20355518; VBINeiMen85645_0283. DR eggNOG; ENOG4105QF7; Bacteria. DR eggNOG; COG4304; LUCA. DR HOGENOM; HOG000218651; -. DR OMA; YENKYLG; -. DR OrthoDB; EOG6SBT2N; -. DR BioCyc; NMEN122586:GHGG-237-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR016630; UCP015278. DR Pfam; PF10004; DUF2247; 1. DR PIRSF; PIRSF015278; UCP015278; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 157 AA; 18473 MW; D197929CEA56582F CRC64; MNLDLTAQKV RLSWKDILWG YGNKYLGWAD VAAYARKMTL SDHDERVFKL SLINKSNILE LKPVLEDLAS EMRDYSPKNW LYVLLSDVFH RKEEFEDPLG EVEKIYADFD YPEEIESFVR YMPPKDGYIP SAHTYEENIA RLYSHWEHYL NNGGGQG // ID Q9JXL5_NEIMB Unreviewed; 143 AA. AC Q9JXL5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42313.1}; GN OrderedLocusNames=NMB1986 {ECO:0000313|EMBL:AAF42313.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42313.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42313.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42313.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42313.1; -; Genomic_DNA. DR PIR; E81019; E81019. DR RefSeq; NP_274978.1; NC_003112.2. DR RefSeq; WP_002225858.1; NC_003112.2. DR STRING; 122586.NMB1986; -. DR PaxDb; Q9JXL5; -. DR EnsemblBacteria; AAF42313; AAF42313; NMB1986. DR GeneID; 904146; -. DR KEGG; nme:NMB1986; -. DR PATRIC; 20360059; VBINeiMen85645_2534. DR eggNOG; ENOG4106E42; Bacteria. DR eggNOG; COG5346; LUCA. DR HOGENOM; HOG000218733; -. DR OMA; ANDYREI; -. DR OrthoDB; EOG60SCRQ; -. DR BioCyc; NMEN122586:GHGG-2043-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019284; Phage_Xfas53_Orf42. DR Pfam; PF10097; DUF2335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 135 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 143 AA; 15702 MW; B0098BB85D710154 CRC64; MTENAQDKAR QAVETVVKSP ELVEQILSDE YVQIMIARCF HSGPLPPPSD LAQYNDIISN GADRIMAMAE KEQAVRHETI RQDQTFNRRG QLYGFISAIL ILLFAVFLVW SGYPATAASL AGGTVFALAG AFVIGRSRDQ GKN // ID Q9JZQ6_NEIMB Unreviewed; 193 AA. AC Q9JZQ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41345.1}; GN OrderedLocusNames=NMB0939 {ECO:0000313|EMBL:AAF41345.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41345.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41345.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41345.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41345.1; -; Genomic_DNA. DR PIR; H81139; H81139. DR RefSeq; NP_273977.1; NC_003112.2. DR RefSeq; WP_002225324.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ6; -. DR STRING; 122586.NMB0939; -. DR PaxDb; Q9JZQ6; -. DR EnsemblBacteria; AAF41345; AAF41345; NMB0939. DR GeneID; 903059; -. DR KEGG; nme:NMB0939; -. DR PATRIC; 20357353; VBINeiMen85645_1191. DR eggNOG; ENOG410741R; Bacteria. DR eggNOG; COG0500; LUCA. DR HOGENOM; HOG000266064; -. DR OMA; LPYEWYN; -. DR OrthoDB; EOG6SBT26; -. DR BioCyc; NMEN122586:GHGG-976-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR010743; Methionine_synth_MetW. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF07021; MetW; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02081; metW; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 193 AA; 21844 MW; EF0E4DFE15DC9E70 CRC64; MNLRDDLQLI YDRIPEGSRV LDLGCGDGEL LAALVEHKKC SGYGIEIDTN SVIAAMSRGV NVIQADLEEG LTAFNDQSFD VIVLSQTIQA MQNTEKILRC LMRVAKQAIV SFPNFGYWRN RVQIALGGHM PVSERMPYHW YDTPNIHWCT LKDFDLLCAK NNIRILERAV MTGNRQVKHF PNLLGSLAFY RVG // ID Q9K0Q8_NEIMB Unreviewed; 172 AA. AC Q9K0Q8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40956.1}; GN OrderedLocusNames=NMB0526 {ECO:0000313|EMBL:AAF40956.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40956.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40956.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40956.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40956.1; -; Genomic_DNA. DR PIR; F81189; F81189. DR RefSeq; NP_273571.1; NC_003112.2. DR RefSeq; WP_002225596.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q8; -. DR STRING; 122586.NMB0526; -. DR PaxDb; Q9K0Q8; -. DR EnsemblBacteria; AAF40956; AAF40956; NMB0526. DR GeneID; 902641; -. DR KEGG; nme:NMB0526; -. DR PATRIC; 20356297; VBINeiMen85645_0668. DR eggNOG; ENOG4105NYV; Bacteria. DR eggNOG; ENOG4111Y66; LUCA. DR HOGENOM; HOG000063012; -. DR OMA; KPDWFGY; -. DR OrthoDB; EOG6T7N9G; -. DR BioCyc; NMEN122586:GHGG-551-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011440; DUF1543. DR Pfam; PF07566; DUF1543; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 66 DUF1543. {ECO:0000259|Pfam:PF07566}. FT DOMAIN 96 143 DUF1543. {ECO:0000259|Pfam:PF07566}. SQ SEQUENCE 172 AA; 19043 MW; C7D04C724DBC2DC7 CRC64; MPKLHMFYLG GNAGRSNIEV HDIQFAVCDN YREAVPALKA AWFGDADKIH IDGWQIVEWA DGYDIAVSET PKTKMPSEHA PRLYFANVGG YRAGQLAEAH AFGLFAAATP AEAKQKALQT LLTDSYVQQH KDNLKDVDNL LALDRIGNFH IRLTPNPHGK PAEIGFQGYL PI // ID Q9K0L5_NEIMB Unreviewed; 344 AA. AC Q9K0L5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Copper ABC transporter, periplasmic copper-binding protein {ECO:0000313|EMBL:AAF41006.1}; GN Name=nosD {ECO:0000313|EMBL:AAF41006.1}; GN OrderedLocusNames=NMB0578 {ECO:0000313|EMBL:AAF41006.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41006.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41006.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41006.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41006.1; -; Genomic_DNA. DR PIR; E81183; E81183. DR RefSeq; NP_273622.1; NC_003112.2. DR RefSeq; WP_002225557.1; NC_003112.2. DR ProteinModelPortal; Q9K0L5; -. DR STRING; 122586.NMB0578; -. DR PaxDb; Q9K0L5; -. DR EnsemblBacteria; AAF41006; AAF41006; NMB0578. DR GeneID; 902693; -. DR KEGG; nme:NMB0578; -. DR PATRIC; 20356437; VBINeiMen85645_0738. DR eggNOG; ENOG4105DH4; Bacteria. DR eggNOG; COG3420; LUCA. DR HOGENOM; HOG000286725; -. DR KO; K07218; -. DR OMA; NAFIGNR; -. DR OrthoDB; EOG64XXPS; -. DR BioCyc; NMEN122586:GHGG-604-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom. DR InterPro; IPR026464; NosD_copper_fam. DR InterPro; IPR007742; NosD_dom. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF05048; NosD; 1. DR SMART; SM00722; CASH; 1. DR SMART; SM00710; PbH1; 6. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR04247; NosD_copper_fam; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 94 264 CASH. {ECO:0000259|SMART:SM00722}. SQ SEQUENCE 344 AA; 38240 MW; 596B4BA7E60B72D0 CRC64; MSLPAMDAGI YLEETAPRAL IEHNNILDNS VGVYLHGSAD AMVRENKIVG DATLRVNERG NGVTVWNAPG AQVVGNDISK GRDGIFSNTS THNTYKNNRF SDLRFAVHYM YTNDSEISGN ISVGNNMGYV LMFSERLKVF DNIAVGSRDQ GIMLNYVNYS DIHDNIINKA GKCVFAYNAN YDKLFANHFE NCQIGIHFTA AIEGTSLHDN SFINNESQVK YVSTRFLDWS EGGHGNYWSD NSAFDLNGDG FGDSAYRPNG IIDQIIWRAP VSRLLMNSPA ISIVKWAQAQ FPAVLPGGVV DSKPLMKPYA PKIQTRYQAM KDELLKEVET RQSEWGRAEN GSLN // ID Q9JZB8_NEIMB Unreviewed; 63 AA. AC Q9JZB8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41552.1}; GN OrderedLocusNames=NMB1167 {ECO:0000313|EMBL:AAF41552.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41552.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41552.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41552.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41552.1; -; Genomic_DNA. DR PIR; E81113; E81113. DR STRING; 122586.NMB1167; -. DR PaxDb; Q9JZB8; -. DR EnsemblBacteria; AAF41552; AAF41552; NMB1167. DR BioCyc; NMEN122586:GHGG-1202-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 63 AA; 6792 MW; EFEC635950435A7D CRC64; MIQTVTASHK AISLTAFIYF CSCLNSQQFH FKARTPTGLR GYDADFQTMV ETPSGGAVGI GFA // ID Q9K0T0_NEIMB Unreviewed; 2703 AA. AC Q9K0T0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Hemagglutinin/hemolysin-related protein {ECO:0000313|EMBL:AAF40927.1}; GN OrderedLocusNames=NMB0493 {ECO:0000313|EMBL:AAF40927.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40927.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40927.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40927.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40927.1; -; Genomic_DNA. DR PIR; H81193; H81193. DR RefSeq; NP_273539.1; NC_003112.2. DR RefSeq; WP_002225616.1; NC_003112.2. DR ProteinModelPortal; Q9K0T0; -. DR STRING; 122586.NMB0493; -. DR PaxDb; Q9K0T0; -. DR EnsemblBacteria; AAF40927; AAF40927; NMB0493. DR GeneID; 902610; -. DR KEGG; nme:NMB0493; -. DR PATRIC; 20356236; VBINeiMen85645_0638. DR eggNOG; ENOG4105CKT; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000043051; -. DR KO; K15125; -. DR OMA; GGNTTHR; -. DR OrthoDB; EOG6K3ZW8; -. DR BioCyc; NMEN122586:GHGG-518-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR024973; ESPR. DR InterPro; IPR010069; Fil_hemagglutn_20-aa_x2_rpt. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR025157; Haemagluttinin_rpt. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF13018; ESPR; 1. DR Pfam; PF13332; Fil_haemagg_2; 2. DR Pfam; PF05860; Haemagg_act; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. DR TIGRFAMs; TIGR01731; fil_hemag_20aa; 7. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 99 219 Haemagg_act. {ECO:0000259|SMART:SM00912}. SQ SEQUENCE 2703 AA; 288264 MW; 214537D1F261F00A CRC64; MNRTLYKVVF NKHRNCMIAV AENAKREGKN TADTQAVGIL PNDIAGFAGF IHSISVISFS LSLLLGSALI LTSSSATAQG IVADKSAPAQ QQPTILQTGN GIPQVNIQTP TSAGVSVNQY AQFDVGNRGA ILNNSRSNTQ TQLGGWIQGN PWLARGEARV VVNQINSSHS SQLNGYIEVG GRRAEVVIAN PAGIAVNGGG FINASRATLT TAQPQYQAGD LSGFKIRQGN VVIAGHGLDA RDTDYTRILS YHSKIDAPVW GQDVRVVAGQ NDVAATGDAH SPILNNAAAN TSNNTANNGT HIPLFAIDTG KLGGMYANKI TLISTVEQAG IRNQGQWFAS AGNVAVNAEG KLVNTGMIAA TGENHAVSLH ARNVHNSGTV ASQDDANIHS QTLDNSGTVL SSGRLTVRNL GRLKNQNNGT IQAARLDMST GGLDNTGNIT QTGSQALDLV SAGKFDNSGK IGVSDVPQTG LNPNPSVIPQ IPSTATGSGS STVSVSKPGS NNPVSPTAPA KNYAVGRIQT TGAFDNAGSI NAGGQIDIAA QNGLGNSGSL NAAKLRVSGD SFNNTVKGKL QAHDLAVNTQ TAKNSGHLLT QTGKIDNREL HNAGEIAANN LTLIHSGRLS NDKKGNIRAA HLQLDTAGLH NAGNILADSG TVTTKNNLRN TGKVSVARLN TEGQTLDNTR GRIEAETVNI QSQQLTNQSG HITATEQLTI NSRNVDNQNG KLLSANQAQL AVSDGLYNQH GEIATNRQLS IHDKNQNTLA LNNADGTIQS AGNVSLQAKS LANNGTLTAG NKLDIALTDD FVVERDLTAG KQLNLSIKGR LKNTHTLQAG HTLKLNAGNI DNQVTGKIIG GEQTDITSEQ HVDNRGLINS DGLTHIGAGQ TLTNTGTGKI YGNHIALDAQ ILLNREETTE GSTKAGAIAA RKRLDIGAKE IHNQEGALLS SEGIFAVGNR LDEQHHAAGM ADTFVNGSAG LEVQGDALMS VRNMQNINNH FKTETYLAKA EKQVRDYTVL GQNTYYQAGK DGLFDNSQGQ KDQTTATFHL KNGSRIEANQ WHVRDYHIET YKERIIENRP AHITVGGDLT ASGQNWLNKD SRIVVGGRII TDDLNQKEIT NQSTTGKGRT DAVGTQWDSV TKKGWYSGRK RQRRTERNHT PYHDTQLFTH DFDTPVSVIQ QNAASPSFQP AASAIKLIDG VSTAAVNGQR IHTGNVVSLN NATVTLPNSS LYTTHPDNKG WLVETDPQFA DYRRWLGSDY MLQQLQLDTN HLHKRLGDGY YEQKLVNEQI HQLTGYRRLD GYRSDEEQFK ALMDNGLTAA KTFGLTPGIA LSAEQVARLT SDIVWMENQT VTLSDGSTQT VLVPKVYALA RKGDLNTSGG LISAEQVLLK LQNGNLTNSG TIAGRQAVLI QARNINSNGN IQADQIGLKA EKSINIDGGQ VQAGRLLTAQ AQNINLNGTT QTSGNERNGN TAIDRMAGIN VVGSHTEQVD NRTSDGILSL HASNDINLNA ATVSNQVKDG TTQITAGNNL NLGTIRTEHR EAYGTLDDEN HRHVRQSTEV GSSIRTQNGA LLRAGNDLKI RQGELEAEEG KTVLAAGRDV TISEGRQITE LDTSVSGKSK GILSSTKTHD RYRFSHDEAV GSNIGGGKMI VAAGQDINVR GSNLISDKGI VLKAGHDIDI STAHNRYTGN EYHESKKSGV MGTGGLGFTI GNRKTTDDTD RTNIVHTGSI IGSLNGDTVT VAGNRYRQTG STVSSPEGRN TVTAKSIDVE FANNRYATDY AHTQEQKGLT VALNVPVVQA AQNFIQAAQN VGKSKNKRVN AMAAANAAWQ SYQATQQMQQ FAPSSSAGQG QNNNQSPSIS VSITYGEQKS RNEQKRHYTE AAASQIIGKG QTTLAATGSG EQSNINITGS DVIGHAGTAL IADNHIRLQS AKQDGSEQSK NKSSGWNAGV AVKIGNGIRF GITAGGNIGK GKEQGGSTTH RHTHVGSTTG KTTIRSGGDT TLKGVQLIGK GIQADTRNLH IESVQDTETY QSKQQNGNVQ VTVGYGFSAS GSYRQSKVKA DHASVTGQSG IYAGEDGYQI KVRDNTDLKG GIITSSQSAE DKGKNLFQTA TLTASDIQNH SRYEGRSFGI GGSFDLNGGW DGTVTDKQGR PTDRISPAAG YGSDGDSKNS TTRSGVNTHN IHITDEAGQL ARTGRTAKET EARIYTGIDT ETADQHSGHL KNSFDKDAVA KEINLQREVT KEFGRNAAQA VAAVADKLGN TQSYERYQEA RTLLEAELQN TDSEAEKAAF RASLGQVNAY LAENQSRYDT WKEGGIGRSI LHGAAGGLTT GSLGGILAGG GTSLAAPYLD KAAENLGPAG KAAVNALGGA AIGYATGGSG GAVVGANVDW NNRQLHPKEM ALADKYAEAL KREVEKREGR KISSQEAAMR IRRQILRWVD KGSQDGYTDQ SVISLIGMKG EDKALGYTWD YRDYGARNPQ TYNDPKLFEE YRRQDKPEYR NLTWLHSGTK DTKIRQGERK NEEFALNVAE GLTSLVNPNP RIKVPILAGI RNLKNIKPTV TGSDPLLAGA GNIRIPANGN VAKGDRIPDT ALASKGIKHK NRKDQLEKNK KSGEDFEMEI YQKKVKQGFK PQRQITVKTK SGVKTRLDII SKEGGLDVCT ECKASITAPL TKNQKKAFPE IERTGATVVG KGKPGYPKGT KIEPTKVIIE RKR // ID Q9JYI0_NEIMB Unreviewed; 575 AA. AC Q9JYI0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 103. DE RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591}; DE EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591}; GN Name=ilvI {ECO:0000313|EMBL:AAF41930.1}; GN OrderedLocusNames=NMB1577 {ECO:0000313|EMBL:AAF41930.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41930.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41930.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41930.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC {ECO:0000256|RuleBase:RU003591}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU003591}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU003591}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|RuleBase:RU003591}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000256|RuleBase:RU003591}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC {ECO:0000256|RuleBase:RU003591}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|RuleBase:RU362132}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41930.1; -; Genomic_DNA. DR PIR; A81067; A81067. DR RefSeq; NP_274583.1; NC_003112.2. DR RefSeq; WP_002225031.1; NC_003112.2. DR ProteinModelPortal; Q9JYI0; -. DR STRING; 122586.NMB1577; -. DR PaxDb; Q9JYI0; -. DR EnsemblBacteria; AAF41930; AAF41930; NMB1577. DR GeneID; 904184; -. DR KEGG; nme:NMB1577; -. DR PATRIC; 20359018; VBINeiMen85645_2028. DR eggNOG; ENOG4105C7K; Bacteria. DR eggNOG; COG0028; LUCA. DR HOGENOM; HOG000258448; -. DR KO; K01652; -. DR OMA; MVWPMVP; -. DR OrthoDB; EOG6KT2NW; -. DR BioCyc; NMEN122586:GHGG-1618-MONOMER; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR012846; Acetolactate_synth_lsu. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00118; acolac_lg; 1. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|RuleBase:RU003591}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|RuleBase:RU003591}; KW Metal-binding {ECO:0000256|RuleBase:RU003591}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}; KW Transferase {ECO:0000256|RuleBase:RU003591, KW ECO:0000313|EMBL:AAF41930.1}. FT DOMAIN 4 167 TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}. FT DOMAIN 194 329 TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}. FT DOMAIN 393 541 TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}. SQ SEQUENCE 575 AA; 62812 MW; 4CCE5103BF2622A7 CRC64; MQLSGAQIIV QSLKAEGVEY VFGYPGGAVI EIYDALFQLN KFKHILTRHE QAAVHAADAY ARVSGKVGVA LVTSGPGVTN ALTGIATAYT DSIPMVVISG QVGNSLIGTD AFQEVDTVGI TRPCVKHNFL VTDINELAET IKKAFQIAAS GRPGPVVVDV PKDVTQAMAK FSYPQEDIFI RSYQPVVQGH IGQIKKAVQM LASAKRPVVY FGGGVVLGNA SEELTRFVRM TGAPCTGTLM GLGAYPSGDR QFLGMLGMHG TYEANLAMQN ADVVLAVGAR FDDRVVSVPS KFFEKAKKVI HIDVDPSSIA KRVKVDIPIV GDVKNVLSEM VALWQKQESV PSEDALGKWW KTIEEWRSRD CLWFDNGSEI IKPQYVIQKL AEITGNSAII TSDVGQHQMF AAQYYPFERP RQWLNSGGLG TMGVGLPYAI GAKLAAPDQD VFCITGDGSI QMNIQELSTC FQYRIPVNVI TLNNGYLGMV RQWQEIYYGG RESETYFDSL PDFVKLAEAY GHIGIRVDKK SDVEGALLEA LNQKDRLVFI DFLTDQKQNV MPMVGNGKGL DEMVLPPHMR ADGKA // ID Q9JXB1_NEIMB Unreviewed; 149 AA. AC Q9JXB1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42448.1}; GN OrderedLocusNames=NMB2140 {ECO:0000313|EMBL:AAF42448.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42448.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42448.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42448.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42448.1; -; Genomic_DNA. DR PIR; B81002; B81002. DR RefSeq; NP_275125.1; NC_003112.2. DR RefSeq; WP_002225738.1; NC_003112.2. DR STRING; 122586.NMB2140; -. DR PaxDb; Q9JXB1; -. DR EnsemblBacteria; AAF42448; AAF42448; NMB2140. DR GeneID; 903232; -. DR KEGG; nme:NMB2140; -. DR PATRIC; 20360472; VBINeiMen85645_2732. DR eggNOG; ENOG4109045; Bacteria. DR eggNOG; COG2259; LUCA. DR HOGENOM; HOG000198397; -. DR KO; K15977; -. DR OMA; LSMWAEL; -. DR OrthoDB; EOG61GGB6; -. DR BioCyc; NMEN122586:GHGG-2205-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032808; DoxX. DR Pfam; PF07681; DoxX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 100 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 136 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 149 AA; 16659 MW; 2BF9AC2200AA38BD CRC64; MKIGTTWQTA SAMLVLRLFA AYEFLESGLQ KWNGENWFSE INDQFPFPFN LLPDALNWNL AMYAELLLPV LLLLGLATRL SALGLMVVTA VAWAAVHAGS GYNVCDNGYK MALIYIVVLI PLLFQGAGGW SLDTLLKKRF CPRCRLKQD // ID Q9K021_NEIMB Unreviewed; 321 AA. AC Q9K021; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41218.1}; GN OrderedLocusNames=NMB0805 {ECO:0000313|EMBL:AAF41218.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41218.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41218.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41218.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41218.1; -; Genomic_DNA. DR PIR; D81155; D81155. DR RefSeq; NP_273847.1; NC_003112.2. DR RefSeq; WP_010980849.1; NC_003112.2. DR ProteinModelPortal; Q9K021; -. DR PaxDb; Q9K021; -. DR EnsemblBacteria; AAF41218; AAF41218; NMB0805. DR GeneID; 902920; -. DR KEGG; nme:NMB0805; -. DR PATRIC; 20356997; VBINeiMen85645_1017. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; EFAGHEE; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-836-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38004 MW; 83C817A17A1DD10E CRC64; MSHTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q4W592_NEIMB Unreviewed; 136 AA. AC Q4W592; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52139.1}; GN OrderedLocusNames=NMB0019 {ECO:0000313|EMBL:AAY52139.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52139.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52139.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52139.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52139.1; -; Genomic_DNA. DR RefSeq; WP_002243920.1; NC_003112.2. DR RefSeq; YP_338284.1; NC_003112.2. DR ProteinModelPortal; Q4W592; -. DR SMR; Q4W592; 1-119. DR STRING; 122586.NMB0019; -. DR PaxDb; Q4W592; -. DR EnsemblBacteria; AAY52139; AAY52139; NMB0019. DR GeneID; 902122; -. DR KEGG; nme:NMB0019; -. DR PATRIC; 20354979; VBINeiMen85645_0026. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR OMA; WTKRQDG; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-20-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 136 AA; 14498 MW; 407BE268285D5820 CRC64; MAEGQKSAVT EYYLNHGEWP GNNSSAGVAT SADIKGKYVK SVEVKNGVVT AQMASSNVNN EIKGKKLSLW AKRQAGSVKW FCGLPVTRAD NAKDDAVTAA ATGTDKIDTK HLPSTCRDDS SVVCIETPPT AFYKNT // ID Q9JY41_NEIMB Unreviewed; 76 AA. AC Q9JY41; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42098.1}; GN OrderedLocusNames=NMB1757 {ECO:0000313|EMBL:AAF42098.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42098.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42098.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42098.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42098.1; -; Genomic_DNA. DR PIR; D81046; D81046. DR STRING; 122586.NMB1757; -. DR PaxDb; Q9JY41; -. DR EnsemblBacteria; AAF42098; AAF42098; NMB1757. DR BioCyc; NMEN122586:GHGG-1812-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 76 AA; 9401 MW; 079FAEC6A4925BAC CRC64; MQGCDHYIFL FRSVYDFTVN CYSMCLAFQL PIFEYWRRHF HQCRNADQNS HKPYWFLWQQ HLSVCSSDHK SNMIGW // ID Q9K067_NEIMB Unreviewed; 77 AA. AC Q9K067; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41166.1}; GN OrderedLocusNames=NMB0753 {ECO:0000313|EMBL:AAF41166.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41166.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41166.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41166.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41166.1; -; Genomic_DNA. DR PIR; H81163; H81163. DR RefSeq; NP_273795.1; NC_003112.2. DR RefSeq; WP_002219546.1; NC_003112.2. DR ProteinModelPortal; Q9K067; -. DR STRING; 122586.NMB0753; -. DR PaxDb; Q9K067; -. DR EnsemblBacteria; AAF41166; AAF41166; NMB0753. DR GeneID; 902868; -. DR KEGG; nme:NMB0753; -. DR PATRIC; 20356879; VBINeiMen85645_0958. DR eggNOG; ENOG41065CF; Bacteria. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000250076; -. DR OMA; CHYHLDE; -. DR OrthoDB; EOG6RZB9Q; -. DR BioCyc; NMEN122586:GHGG-784-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR008554; Glutaredoxin-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF05768; DUF836; 1. DR SUPFAM; SSF52833; SSF52833; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 77 AA; 9300 MW; BF51CF4904DB967E CRC64; MKLTLMFREY CSLCHKMRDE LKPFQDEYGF GLEVVDVDEN PVLEEKYNEL VPVLLAGDEE ICHWFLDEDR LKQFLER // ID Q7DDI6_NEIMB Unreviewed; 304 AA. AC Q7DDI6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Putative transcriptional regulator {ECO:0000313|EMBL:AAF41447.1}; GN OrderedLocusNames=NMB1049 {ECO:0000313|EMBL:AAF41447.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41447.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41447.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41447.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41447.1; -; Genomic_DNA. DR PIR; A81128; A81128. DR RefSeq; NP_274083.1; NC_003112.2. DR RefSeq; WP_002213466.1; NC_003112.2. DR ProteinModelPortal; Q7DDI6; -. DR STRING; 122586.NMB1049; -. DR PaxDb; Q7DDI6; -. DR DNASU; 903186; -. DR EnsemblBacteria; AAF41447; AAF41447; NMB1049. DR GeneID; 903186; -. DR KEGG; nme:NMB1049; -. DR PATRIC; 20357635; VBINeiMen85645_1334. DR eggNOG; COG0583; LUCA. DR HOGENOM; HOG000218972; -. DR OMA; THFQYRV; -. DR OrthoDB; EOG67Q97S; -. DR BioCyc; NMEN122586:GHGG-1086-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 1 58 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. SQ SEQUENCE 304 AA; 33413 MW; 06ED214B4EDCFCD7 CRC64; MDAVQLKSFV AVAHEGNLTQ AAKRLFLSQP AVSAQIKALE EYVGTPLFRR TGKGMVLTRA GEILLPEAES LLQYKHKLEH FAKTLAGDYS EETSLGIIHP IDSAKLVALT DNIGQTAPKT RLHIQYGMSG EILSRIQHKT LHGGFILGNA AQRGIRSVFL QNLTYALICP QSQYPHLTRS LPQSLQECVW IEMSGVSGSR KHLHQFWRSN RLSPKKQILC DYPQTIIDLV AGGIGVAMVP GNKAEAAAKE GAGVAIIESC RHSMPLNFIY AEEYEDNPHV SLLLECIEKV WGVQAVQPPV VSDN // ID Q9JY71_NEIMB Unreviewed; 444 AA. AC Q9JY71; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185}; GN Name=gdhA {ECO:0000313|EMBL:AAF42057.1}; GN OrderedLocusNames=NMB1710 {ECO:0000313|EMBL:AAF42057.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42057.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42057.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42057.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000256|PIRNR:PIRNR000185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42057.1; -; Genomic_DNA. DR PIR; H81050; H81050. DR RefSeq; NP_274713.1; NC_003112.2. DR RefSeq; WP_002212610.1; NC_003112.2. DR ProteinModelPortal; Q9JY71; -. DR SMR; Q9JY71; 3-444. DR STRING; 122586.NMB1710; -. DR PaxDb; Q9JY71; -. DR EnsemblBacteria; AAF42057; AAF42057; NMB1710. DR GeneID; 903392; -. DR KEGG; nme:NMB1710; -. DR PATRIC; 20359379; VBINeiMen85645_2195. DR eggNOG; ENOG4105D82; Bacteria. DR eggNOG; COG0334; LUCA. DR HOGENOM; HOG000243799; -. DR KO; K00262; -. DR OMA; VPWVDDA; -. DR OrthoDB; EOG65XN4D; -. DR BioCyc; NMEN122586:GHGG-1765-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185, KW ECO:0000313|EMBL:AAF42057.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 201 443 ELFV_dehydrog. FT {ECO:0000259|SMART:SM00839}. SQ SEQUENCE 444 AA; 48490 MW; 8B2CFCCA89EF7DAF CRC64; MTDLNTLFAN LKQRNPNQEP FHQAVEEVFM SLDPFLAKNP KYTQQSLLER IVEPERVVMF RVTWQDDKGQ VQVNRGYRVQ MSSAIGPYKG GLRFHPTVDL GVLKFLAFEQ VFKNALTTLP MGGGKGGSDF DPKGKSDAEV MRFCQAFMTE LYRHIGADTD VPAGDIGVGG REIGYLFGQY KKIRNEFSSV LTGKGLEWGG SLIRPEATGY GCVYFAQAML QTRNDSFEGK RVLISGSGNV AQYAAEKAIQ LGAKVLTVSD SNGFVLFPDS GMTEAQLAAL IELKEVRRER VATYAKEQGL QYFEKQKPWG VAAEIALPCA TQNELDEEAA KTLLANGCYV VAEGANMPST LGAVEQFIKA GILYAPGKAS NAGGVATSGL EMSQNAIRLS WTREEVDQRL FGIMQSIHES CLKYGKVGDT VNYVNGANIA GFVKVADAML AQGF // ID Q9K190_NEIMB Unreviewed; 513 AA. AC Q9K190; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE RecName: Full=Putative lipid II flippase MurJ {ECO:0000256|PIRNR:PIRNR002869}; GN Name=mviN {ECO:0000313|EMBL:AAF40731.1}; GN OrderedLocusNames=NMB0277 {ECO:0000313|EMBL:AAF40731.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40731.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40731.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40731.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports CC lipid-linked peptidoglycan precursors from the inner to the outer CC leaflet of the cytoplasmic membrane. CC {ECO:0000256|PIRNR:PIRNR002869}. CC -!- SIMILARITY: Belongs to the MurJ/MviN family. CC {ECO:0000256|PIRNR:PIRNR002869}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40731.1; -; Genomic_DNA. DR PIR; B81217; B81217. DR RefSeq; NP_273333.1; NC_003112.2. DR RefSeq; WP_010980768.1; NC_003112.2. DR STRING; 122586.NMB0277; -. DR PaxDb; Q9K190; -. DR EnsemblBacteria; AAF40731; AAF40731; NMB0277. DR GeneID; 902388; -. DR KEGG; nme:NMB0277; -. DR PATRIC; 20355642; VBINeiMen85645_0345. DR eggNOG; ENOG4105CJR; Bacteria. DR eggNOG; COG0728; LUCA. DR HOGENOM; HOG000263812; -. DR KO; K03980; -. DR OMA; IFAEGSF; -. DR OrthoDB; EOG6C0131; -. DR BioCyc; NMEN122586:GHGG-292-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR004268; MurJ. DR Pfam; PF03023; MVIN; 1. DR PIRSF; PIRSF002869; MviN; 1. DR PRINTS; PR01806; VIRFACTRMVIN. DR TIGRFAMs; TIGR01695; murJ_mviN; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|PIRNR:PIRNR002869}; KW Cell shape {ECO:0000256|PIRNR:PIRNR002869}; KW Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002869}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|PIRNR:PIRNR002869, ECO:0000256|SAM:Phobius}; KW Peptidoglycan synthesis {ECO:0000256|PIRNR:PIRNR002869}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|PIRNR:PIRNR002869}. FT TRANSMEM 91 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 189 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 255 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 293 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 340 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 352 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 403 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 409 430 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 442 463 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 483 503 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 513 AA; 55775 MW; F63DAB5C46C1913D CRC64; MMNMLGALAK VGSLTMVSRV LGFVRDTVIA RAFGAGMATD AFFVAFKLPN LLRRVFAEGA FAQAFVPILA EYKETRSKEA AEAFIRHVAG MLSFVLVIVT ALGILAAPWV IYVSAPGFAQ DADKFQLSID LLRITFPYIL LISLSSFVGS VLNSYHKFGI PAFTPTFLNV SFIVFALFFV PYFDPPVTAL AWAVFVGGIL QLGFQLPWLA KLGFLKLPKL SFKDAAVNRV MKQMAPAILG VSVAQVSLVI NTIFASYLQS GSVSWMYYAD RMMELPSGVL GAALGTILLP TLSKHSANQD TEQFSALLDW GLRLCMLLTL PAAVGLAVLS FPLVATLFMY REFTLFDAQM TQHALIAYSF GLIGLIMIKV LAPGFYARQN IKTPVKIAIF TLICTQLMNL AFIGPLKHVG LSLAIGLGAC INAGLLFYLL RRHGIYQPGK GWAAFLAKML LSLAVMCGGL WAAQAYLPFE WAHAGGMRKA GQLCILIAVG GGLYFASLAA LGFRPRHFKR VEN // ID Q9JZ68_NEIMB Unreviewed; 365 AA. AC Q9JZ68; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41646.1}; GN OrderedLocusNames=NMB1269 {ECO:0000313|EMBL:AAF41646.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41646.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41646.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41646.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41646.1; -; Genomic_DNA. DR PIR; G81102; G81102. DR RefSeq; NP_274290.1; NC_003112.2. DR RefSeq; WP_002222398.1; NC_003112.2. DR STRING; 122586.NMB1269; -. DR PaxDb; Q9JZ68; -. DR EnsemblBacteria; AAF41646; AAF41646; NMB1269. DR GeneID; 903691; -. DR KEGG; nme:NMB1269; -. DR PATRIC; 20358153; VBINeiMen85645_1588. DR HOGENOM; HOG000218981; -. DR OMA; EGSHTRQ; -. DR OrthoDB; EOG6KQ6C6; -. DR BioCyc; NMEN122586:GHGG-1307-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 365 AA; 40300 MW; FB9B5CD2A0ADD2C8 CRC64; MNQTFTLPDT RPYPQNPIKN HLLLNAYQLA HNSSQASRKL SSGQLQTEIR GMLEQNHYIN LSLALTMSPD AGTYAALLSS VNAVLDCEKE GEVQWFALPV VLVSGCKKER AIEMKLPTEA LFACLQNYPH LRALTQETQW LPYLVHSSDL SAVAPDEWWR AKQNTEAAAQ HLRRFAPRPL LLPEGQSVHV VYALGFGSGK VQTALGQNLL QAGLPLMQVW QENLASEGVT LFANPLSPDS PVRALSDGSH TRQRMAMDVF AANAIRAVRM QSPRVGVVAA AKAGGQILFG FNATDGAFEV VPQVFSWQLS FTDNIAVIQQ NFLDLMAECR VEHVYLLHNP LGEQESIPSY AEALKREGHN PFFSA // ID Q4W561_NEIMB Unreviewed; 43 AA. AC Q4W561; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 41. DE SubName: Full=Leucyl-tRNA synthetase, truncation {ECO:0000313|EMBL:AAY52161.1}; GN OrderedLocusNames=NMB1894 {ECO:0000313|EMBL:AAY52161.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52161.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52161.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52161.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52161.1; -; Genomic_DNA. DR RefSeq; NP_274889.1; NC_003112.2. DR RefSeq; WP_002225799.1; NC_003112.2. DR STRING; 122586.NMB1894; -. DR PaxDb; Q4W561; -. DR EnsemblBacteria; AAY52161; AAY52161; NMB1894. DR GeneID; 903121; -. DR KEGG; nme:NMB1894; -. DR PATRIC; 20359825; VBINeiMen85645_2417. DR HOGENOM; HOG000027864; -. DR OrthoDB; EOG6N94M3; -. DR BioCyc; NMEN122586:GHGG-1951-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AAY52161.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAY52161.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 43 AA; 4672 MW; 30DE1B128C187B51 CRC64; MRDFDKPAEE AAEYAAEGAV KFIEGKPAKK IIAVPGRLEN IVV // ID Q9JXM9_NEIMB Unreviewed; 305 AA. AC Q9JXM9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Transcriptional regulator, AraC family {ECO:0000313|EMBL:AAF42296.1}; GN OrderedLocusNames=NMB1967 {ECO:0000313|EMBL:AAF42296.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42296.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42296.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42296.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH araC/xylS-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00503533}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42296.1; -; Genomic_DNA. DR PIR; H81022; H81022. DR RefSeq; NP_274961.1; NC_003112.2. DR RefSeq; WP_002221643.1; NC_003112.2. DR ProteinModelPortal; Q9JXM9; -. DR STRING; 122586.NMB1967; -. DR PaxDb; Q9JXM9; -. DR EnsemblBacteria; AAF42296; AAF42296; NMB1967. DR GeneID; 904175; -. DR KEGG; nme:NMB1967; -. DR PATRIC; 20359997; VBINeiMen85645_2503. DR eggNOG; ENOG410723Q; Bacteria. DR eggNOG; COG2207; LUCA. DR HOGENOM; HOG000218744; -. DR OMA; AHISFGH; -. DR OrthoDB; EOG6T4RX1; -. DR BioCyc; NMEN122586:GHGG-2024-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR InterPro; IPR018062; HTH_AraC-typ_CS. DR Pfam; PF12833; HTH_18; 1. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}; KW Transcription regulation {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}. FT DOMAIN 204 303 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 305 AA; 34029 MW; 14FCBAFA7430A4E1 CRC64; MEKAEHLNSS RFVNLVKSGG GSYVEGSYRF DTLSNGISIH GGTVTARCDF CSSRLAEPYV SFVLLLEGSL DFGINRCRFQ IDADGGKIVL IAVGEEVLFS RYLYRGGKTV KMTIKGMEQW LLRPEYARFA PLLYREPVRI WDLPPNLRGL AASCLKAVPK GHLGETLRRE ADVLRLLSDL WDTVSDGIGP AAGQTAEADA MPSEDFSRTL NAAFADGAHQ VNRLTDALNI SERTLQRRMR DHFGITASEW LHHKQMQHAL YLLQNGGKSI GETAYLCGYR HVSSFTQAFR QYFGSTPAET KKENR // ID Q9JZS8_NEIMB Unreviewed; 115 AA. AC Q9JZS8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=PemK protein {ECO:0000313|EMBL:AAF41321.1}; GN Name=pemK {ECO:0000313|EMBL:AAF41321.1}; GN OrderedLocusNames=NMB0913 {ECO:0000313|EMBL:AAF41321.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41321.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41321.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41321.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41321.1; -; Genomic_DNA. DR PIR; C81142; C81142. DR RefSeq; NP_273953.1; NC_003112.2. DR RefSeq; WP_002217440.1; NC_003112.2. DR ProteinModelPortal; Q9JZS8; -. DR STRING; 122586.NMB0913; -. DR PaxDb; Q9JZS8; -. DR EnsemblBacteria; AAF41321; AAF41321; NMB0913. DR GeneID; 903034; -. DR KEGG; nme:NMB0913; -. DR PATRIC; 20357261; VBINeiMen85645_1144. DR eggNOG; ENOG4105MZG; Bacteria. DR eggNOG; COG2337; LUCA. DR HOGENOM; HOG000290185; -. DR KO; K18841; -. DR OMA; LACPITT; -. DR OrthoDB; EOG67X204; -. DR BioCyc; NMEN122586:GHGG-951-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 2.30.30.110; -; 1. DR InterPro; IPR003477; PemK-like. DR InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib. DR Pfam; PF02452; PemK_toxin; 1. DR SUPFAM; SSF50118; SSF50118; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 115 AA; 12354 MW; CD6DB621B601CDA0 CRC64; MYIPDKGDIF HLNFDPSSGK EIKGGRFALA LSPKAFNRAT GLVFACPISQ GNAAAARSSG MISTLLGAGT ETQGNVHCHQ LKSLDWQIRK ASFKETVPDY VLDDVLARIG AVLFD // ID Q9JYW4_NEIMB Unreviewed; 242 AA. AC Q9JYW4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41767.1}; GN OrderedLocusNames=NMB1404 {ECO:0000313|EMBL:AAF41767.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41767.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41767.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41767.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41767.1; -; Genomic_DNA. DR PIR; A81087; A81087. DR RefSeq; NP_274418.1; NC_003112.2. DR RefSeq; WP_002247592.1; NC_003112.2. DR STRING; 122586.NMB1404; -. DR PaxDb; Q9JYW4; -. DR EnsemblBacteria; AAF41767; AAF41767; NMB1404. DR GeneID; 903826; -. DR KEGG; nme:NMB1404; -. DR PATRIC; 20358493; VBINeiMen85645_1758. DR HOGENOM; HOG000219009; -. DR OMA; IVLHITL; -. DR OrthoDB; EOG6JTC93; -. DR BioCyc; NMEN122586:GHGG-1442-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 9 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 210 227 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 242 AA; 28657 MW; C5533B4F53FF381C CRC64; MRHMKNKNYL LVFIVLHIAL IVINIVFGYF VFLFDFFAFL FFANVFLAVN LLFLEKNIKN KLLFLLPISI IIWMVIHISM INIKFYKFEH QIKEQNISSI TGVIKPHDSY NYVYDSNGYA KLKDNHRYGR VIRETPYIDV VASDVKNKSI RLSLVCGIHS YAPCANFIKF AKKPVKIYFY NQPQGDFIDN VIFEINDGNK SLYLLDKYKT FFLIENSVCI VLIILYLKFN LLLYRTYFNE LE // ID Q9JZP2_NEIMB Unreviewed; 531 AA. AC Q9JZP2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=FunZ protein {ECO:0000313|EMBL:AAF41367.1}; GN Name=funZ {ECO:0000313|EMBL:AAF41367.1}; GN OrderedLocusNames=NMB0961 {ECO:0000313|EMBL:AAF41367.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41367.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41367.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41367.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41367.1; -; Genomic_DNA. DR PIR; H81137; H81137. DR RefSeq; NP_273999.1; NC_003112.2. DR RefSeq; WP_002222614.1; NC_003112.2. DR STRING; 122586.NMB0961; -. DR PaxDb; Q9JZP2; -. DR EnsemblBacteria; AAF41367; AAF41367; NMB0961. DR GeneID; 903081; -. DR KEGG; nme:NMB0961; -. DR PATRIC; 20357405; VBINeiMen85645_1217. DR eggNOG; ENOG4108YRG; Bacteria. DR eggNOG; ENOG410ZY5S; LUCA. DR HOGENOM; HOG000118673; -. DR OMA; CHENATI; -. DR OrthoDB; EOG6KHG3R; -. DR BioCyc; NMEN122586:GHGG-998-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 531 AA; 62717 MW; 7BEAC85F071C3A32 CRC64; MKPLKTLEFG FVDAANYRRR ENKDLFNRIF VKGEYLDELC EPNISFLIGE KGTGKTAYAV YLTNNFYKNI HATTKFVRET DYSKFIQLKK ARHLTVSDFT SIWKVILYLL ISNQIKCKEN GILSSIFNKF KALDEAINEY YYGAFDPEIV QAITLIENSK EAAEMIFGKF VKLGEEESQQ ITFTESKFQA NLGFIERKFK DALSQLKLKD NHILFIDGID IRPSQIPFDE YHECVKGLAN AIWMLNNDIF PSIKDSKGRM RVVLLIRPDI FDSLGLQNQN TKLQDNSVFL DWRTDYKSYR SSKIFGVFDH LLRTQQEKQD SLEKGNSWDY YFPWNAPNLH DEYKNLTSFI SFLRKSYYRP RDILQMLTLL QKNKKSKEDY VVAEDFDNTS FQREYSIYLL GEIKDHLLFY YSQSDYQNFL KFFEFLNGKD RFKYSDFLKA FERLKKHLQT TSVEIPKFMS TANEFLQFLF DLNVIAYLDN PEDETKPYIH WCFKDRNYAN ISPKIKTETE YLIFSGLSKA LDVGTPFKNK Q // ID Q9K0W8_NEIMB Unreviewed; 122 AA. AC Q9K0W8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40876.1}; GN OrderedLocusNames=NMB0438 {ECO:0000313|EMBL:AAF40876.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40876.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40876.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40876.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40876.1; -; Genomic_DNA. DR PIR; G81198; G81198. DR RefSeq; NP_273486.1; NC_003112.2. DR RefSeq; WP_002224933.1; NC_003112.2. DR STRING; 122586.NMB0438; -. DR PaxDb; Q9K0W8; -. DR EnsemblBacteria; AAF40876; AAF40876; NMB0438. DR GeneID; 902554; -. DR KEGG; nme:NMB0438; -. DR PATRIC; 20356082; VBINeiMen85645_0556. DR eggNOG; ENOG41062YR; Bacteria. DR eggNOG; ENOG41122VE; LUCA. DR HOGENOM; HOG000219096; -. DR OMA; EHVRFEE; -. DR OrthoDB; EOG69KTW5; -. DR BioCyc; NMEN122586:GHGG-462-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 122 AA; 14446 MW; F357F1D45B86A186 CRC64; MKPLKRHPAL IGLSRDHHHS LSLCVRLLRT PEERHRDELE PHFSELETHF REEETKFAPI WQNVAPELKQ RFEKDHARLR QMMASPEYGN AAWNTAFATT LRDHARFEER ELFPAAEPFL PA // ID Q9K122_NEIMB Unreviewed; 225 AA. AC Q9K122; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40814.1}; GN OrderedLocusNames=NMB0372 {ECO:0000313|EMBL:AAF40814.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40814.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40814.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40814.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40814.1; -; Genomic_DNA. DR PIR; B81207; B81207. DR RefSeq; NP_273421.1; NC_003112.2. DR RefSeq; WP_002224904.1; NC_003112.2. DR ProteinModelPortal; Q9K122; -. DR STRING; 122586.NMB0372; -. DR PaxDb; Q9K122; -. DR EnsemblBacteria; AAF40814; AAF40814; NMB0372. DR GeneID; 902487; -. DR KEGG; nme:NMB0372; -. DR PATRIC; 20355903; VBINeiMen85645_0469. DR eggNOG; ENOG4105YIQ; Bacteria. DR eggNOG; ENOG41126JQ; LUCA. DR HOGENOM; HOG000219103; -. DR OrthoDB; EOG60GRTJ; -. DR BioCyc; NMEN122586:GHGG-394-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR028190; Ntox21. DR Pfam; PF15526; Ntox21; 1. DR SUPFAM; SSF51294; SSF51294; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 158 225 Ntox21. {ECO:0000259|Pfam:PF15526}. SQ SEQUENCE 225 AA; 25208 MW; 40896A604EAF3313 CRC64; MVKTADGYKA IARIRTGDRV FAKDEASGKT GYKPVTARYG NPYQETVYIE ISDGIGNNQT LISNKIHPFY SQGKWIQAGR LKKGDTLLSE SGAKQTVQNI TLKQQPLKAY NLTVADWHTY FVKGNRAETE GVWVHNDCPP RKTPSTPIYG NDSEAYAAAK ELGYRKIKER TRNDAAIFKK GKSYISRDVD SHNGGAWKEA SSPEKLNRKE TRNGTFDKNL NRIGD // ID Q9JXJ2_NEIMB Unreviewed; 149 AA. AC Q9JXJ2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Type IV pilin-related protein {ECO:0000313|EMBL:AAF62338.1}; GN OrderedLocusNames=NMB2016 {ECO:0000313|EMBL:AAF62338.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62338.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62338.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62338.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62338.1; -; Genomic_DNA. DR RefSeq; NP_275008.1; NC_003112.2. DR RefSeq; WP_002214937.1; NC_003112.2. DR ProteinModelPortal; Q9JXJ2; -. DR STRING; 122586.NMB2016; -. DR PaxDb; Q9JXJ2; -. DR EnsemblBacteria; AAF62338; AAF62338; NMB2016. DR GeneID; 904106; -. DR KEGG; nme:NMB2016; -. DR PATRIC; 20360135; VBINeiMen85645_2572. DR eggNOG; COG4968; LUCA. DR HOGENOM; HOG000218724; -. DR OrthoDB; EOG6NWBPW; -. DR BioCyc; NMEN122586:GHGG-2073-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031982; DUS_rpt_ComP. DR InterPro; IPR012902; N_methyl_site. DR Pfam; PF16732; ComP_DUS; 1. DR Pfam; PF13544; N_methyl_2; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 149 AA; 16835 MW; 71733EB3ACABD601 CRC64; MTDNRGFTLV ELISVVLILS VLALIVYPSY RNYVEKAKIN AVRAALLENA HFMEKFYLQN GRFKQTSTKW PSLPIKEAEG FCIRLNGIAR GALDSKFMLK AVAIDKDKNP FIIKMNENLV TFICKKSASS CSDGLDYFKG NDKDCKLLK // ID Q9JZK6_NEIMB Unreviewed; 187 AA. AC Q9JZK6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41411.1}; GN OrderedLocusNames=NMB1010 {ECO:0000313|EMBL:AAF41411.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41411.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41411.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41411.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41411.1; -; Genomic_DNA. DR PIR; C81131; C81131. DR RefSeq; NP_274045.1; NC_003112.2. DR RefSeq; WP_002225288.1; NC_003112.2. DR STRING; 122586.NMB1010; -. DR PaxDb; Q9JZK6; -. DR EnsemblBacteria; AAF41411; AAF41411; NMB1010. DR GeneID; 903148; -. DR KEGG; nme:NMB1010; -. DR PATRIC; 20357549; VBINeiMen85645_1291. DR BioCyc; NMEN122586:GHGG-1047-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 187 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329354. SQ SEQUENCE 187 AA; 20032 MW; 983444F6CFC931FC CRC64; MKILALLIAA TCALSACGSQ SEEQPASAQP QEQAQSELKT MPVSYTDYQS AANKGLNDQK TGLTLPEHVV PIDNAEGKNL LHDFSDGLTI LTVDTDKADK ITAVRVVWNT DAMPQKAEKL SKAAAALIAA TAPEDRTMLR DTGDQIEMAI DSHNAQKEPT REWARGGIAY KVTVTNLPSV VLTAKAE // ID Q7DDB9_NEIMB Unreviewed; 417 AA. AC Q7DDB9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41787.1}; GN OrderedLocusNames=NMB1426 {ECO:0000313|EMBL:AAF41787.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41787.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41787.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41787.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41787.1; -; Genomic_DNA. DR PIR; C81084; C81084. DR RefSeq; NP_274438.1; NC_003112.2. DR RefSeq; WP_002225119.1; NC_003112.2. DR STRING; 122586.NMB1426; -. DR PaxDb; Q7DDB9; -. DR EnsemblBacteria; AAF41787; AAF41787; NMB1426. DR GeneID; 903848; -. DR KEGG; nme:NMB1426; -. DR PATRIC; 20358549; VBINeiMen85645_1786. DR eggNOG; ENOG4105K3M; Bacteria. DR eggNOG; COG1914; LUCA. DR HOGENOM; HOG000287672; -. DR OMA; MCMFGTT; -. DR OrthoDB; EOG6MWNC9; -. DR BioCyc; NMEN122586:GHGG-1464-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001046; NRAMP_fam. DR Pfam; PF01566; Nramp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 288 309 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 348 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 373 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 416 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 417 AA; 45019 MW; CAE822107E0DB4F1 CRC64; MSEQHISTWK SKINALGPGI MMASAAVGGS HLIASTQAGA LYGWQIALII ILTNLFKYPF FRFSAHYTLD TGKSLIEGYA EKSRVYLWVF LILCILSATI NAGAVAIVTA AIVKMAIPSL MFDAGTVAAL IMASCLIILV SGRYRALDRV SKIIIVTLSI ATLAAAGIAM SRGMQMQSDF IEPTPWTLAG LGFLIALMGW MPAPIEISAI NSLWVTEKQR INPSEYRDGI FDFNVGYIAS AVLALVFLAL GAFVQYGNGE AVQMAGGKYI GQLINMYAVT IGGWSRPLVA FIAFACMYGT TITVVDGYAR AIAEPVRLLR GKDKTGNAEF FAWNIWVAGS GLAVIFWFDG VMANLLKFAM IAAFVSAPVF AWLNYRLVKG DEKHKLTSGM NALALAGLIY LTGFTVLFLL NLAGMFK // ID Q7DDN3_NEIMB Unreviewed; 528 AA. AC Q7DDN3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Putative L-lactate permease {ECO:0000313|EMBL:AAF40972.1}; GN OrderedLocusNames=NMB0543 {ECO:0000313|EMBL:AAF40972.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40972.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40972.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40972.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40972.1; -; Genomic_DNA. DR PIR; E81186; E81186. DR RefSeq; NP_273588.1; NC_003112.2. DR RefSeq; WP_002214399.1; NC_003112.2. DR STRING; 122586.NMB0543; -. DR PaxDb; Q7DDN3; -. DR EnsemblBacteria; AAF40972; AAF40972; NMB0543. DR GeneID; 902658; -. DR KEGG; nme:NMB0543; -. DR PATRIC; 20356345; VBINeiMen85645_0691. DR eggNOG; ENOG4105DAA; Bacteria. DR eggNOG; COG1620; LUCA. DR HOGENOM; HOG000278977; -. DR KO; K03303; -. DR OMA; WPARRAM; -. DR OrthoDB; EOG6Q8J3Z; -. DR BioCyc; NMEN122586:GHGG-569-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003804; Lactate_perm. DR PANTHER; PTHR30003; PTHR30003; 1. DR Pfam; PF02652; Lactate_perm; 1. DR TIGRFAMs; TIGR00795; lctP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 232 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 238 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 388 406 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 426 446 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 509 527 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 528 AA; 56823 MW; 31AA588DF84FA80D CRC64; MALFLSIFPI VLLIWLMVKK NSMPSYVALP ITAVLIYAIK LFYFDDAGML LNATAASGLV KTLTPITVIF GAIMFNRMME TTGCIDVIRK WLATISPNPV AQLMIIGWAF AFMIEGASGF GTPAAIAAPI LMSLGFNPLK VAIFTLVMNS VPVSFGAVGT PTWFGFAPLN LSAEDILAIG RQTGVMHFFA GFVIPVIGLG FIVPWSEIRK NLGFVAIAVF SCTIPYVALA MVNEEFPSLV AGAIGLMVSV FAANQGWGLS KDHAKDPNAE KVPFAQVAKA LAPLGMLIGM LVVTRIKQLG IKGILTSKEE WFSFQLPFDL SKITVSDSLT ITFGNIFGQD VSASYQTLYV PAWIPFVLTV WICILLYKTK FKDAWTIYSV TFNQTKKPLL ALMGALIMVQ LMLVGGDNSM VKIIGKEFAA MAGEHWVYFS PYLGAIGAFF SGSNTVSNLT FGPIQQQIAL DTGLSVTLIL ALQSVGGAMG NMVCLNNIIA VCTVLDVKNS EGAIIKKTVI PMAIYGVIAV VAAMIFFL // ID Q9JXT5_NEIMB Unreviewed; 103 AA. AC Q9JXT5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Helix-turn-helix family protein {ECO:0000313|EMBL:AAF42225.1}; GN OrderedLocusNames=NMB1891 {ECO:0000313|EMBL:AAF42225.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42225.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42225.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42225.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42225.1; -; Genomic_DNA. DR PIR; A81032; A81032. DR RefSeq; NP_274887.1; NC_003112.2. DR RefSeq; WP_002225796.1; NC_003112.2. DR ProteinModelPortal; Q9JXT5; -. DR STRING; 122586.NMB1891; -. DR PaxDb; Q9JXT5; -. DR EnsemblBacteria; AAF42225; AAF42225; NMB1891. DR GeneID; 904286; -. DR KEGG; nme:NMB1891; -. DR PATRIC; 20359819; VBINeiMen85645_2414. DR eggNOG; ENOG4105R5S; Bacteria. DR eggNOG; COG2944; LUCA. DR HOGENOM; HOG000265487; -. DR KO; K07726; -. DR OMA; ETMRNFD; -. DR OrthoDB; EOG6ZPSZQ; -. DR BioCyc; NMEN122586:GHGG-1948-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 48 102 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 103 AA; 11234 MW; F4ED8ECD0354BEB1 CRC64; MKYKNEALAA IHEMMEGAYN IGAIDKKTMR DFDKSCLTEI KPLSGGDIKA IREKEALSQA AFAIYLNVGK NHVSAWERGV KKPSGAALKL LTIVKNKGIE AIA // ID Q9JZ60_NEIMB Unreviewed; 668 AA. AC Q9JZ60; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Site-specific recombinase {ECO:0000313|EMBL:AAF41654.1}; GN Name=gcr {ECO:0000313|EMBL:AAF41654.1}; GN OrderedLocusNames=NMB1278 {ECO:0000313|EMBL:AAF41654.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41654.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41654.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41654.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41654.1; -; Genomic_DNA. DR PIR; F81101; F81101. DR RefSeq; NP_274298.1; NC_003112.2. DR RefSeq; WP_002244147.1; NC_003112.2. DR STRING; 122586.NMB1278; -. DR PaxDb; Q9JZ60; -. DR EnsemblBacteria; AAF41654; AAF41654; NMB1278. DR GeneID; 903700; -. DR KEGG; nme:NMB1278; -. DR PATRIC; 20358181; VBINeiMen85645_1602. DR eggNOG; ENOG4105DVU; Bacteria. DR eggNOG; COG4389; LUCA. DR HOGENOM; HOG000218986; -. DR OMA; RTGEHYI; -. DR OrthoDB; EOG6WDSC3; -. DR BioCyc; NMEN122586:GHGG-1316-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR011385; Site-sp_rcmbase. DR Pfam; PF10136; SpecificRecomb; 1. DR PIRSF; PIRSF015380; Site-sp_rcmb; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 391 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 436 459 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 479 505 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 544 564 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 597 624 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 668 AA; 74852 MW; 104988BB121C6483 CRC64; MADMKKITPQ NLRPLLSESL GHTDFVNVLN ALIKFLRRGG KKCAGERFDL IIDTFKQDRE LLSRFSRCFY IWLAQIHIYP ALIKLGIFSR HSFAREMGIR IYERFSPSYK DFANLGEVFL YLFHSENDDK WLQTLNIRQW LVLYELIRSH AEPSKLQTAG IRLADARLRA IEMLSVWTAS EAIEPDLIRI APRLLEADSS FVALQRETAK LVEHYRNGTT PYDTAHLEVM FDQCFSQIDY LRRKGTGAGS GSSVKVAHLL ERLRQTVDRL KLLTDIQTGA GNSNRLTIAL MNSLIYAAVE QYSTRHLRRS SIRMLARSIT ENKSHHGEHY ITRNRKEYFK MFYSAAGGGI IIALMALLKI RIGSLGLSPF LTSLSAGFNY GIGFMIIHML HCTVATKQPA MTAASFAEQV DLNEGGKAVD NKLAKLLIDV CRSQSVAVFG NVSIAILLAC AISFGYAHLY RLPILDAHTA AYQFKSIDII AYPTLWYAAI AGLWLFCSGI IAGFFDNRAD YLNLRQRLPF NPLLRKIMRP GPRRVLAAYI HKHYGSLVGN FIFGMLLGMT GYFGHLLGLP LDIRHVAFSS ANLGYAAVSG NVGLGTFVLG IFSVLAIGLV NLCVSFSLAL FVALRSRGTK IGSIRNLIKS FWNQIKSNPC ILFLPPAKEQ GHPPSDKP // ID Q9JZ74_NEIMB Unreviewed; 185 AA. AC Q9JZ74; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019}; DE Short=PPIase {ECO:0000256|RuleBase:RU363019}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019}; GN OrderedLocusNames=NMB1262 {ECO:0000313|EMBL:AAF41639.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41639.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41639.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41639.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. {ECO:0000256|RuleBase:RU363019}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363019}. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC {ECO:0000256|RuleBase:RU363019}. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC {ECO:0000256|RuleBase:RU363019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41639.1; -; Genomic_DNA. DR PIR; H81103; H81103. DR RefSeq; NP_274283.1; NC_003112.2. DR RefSeq; WP_002222405.1; NC_003112.2. DR ProteinModelPortal; Q9JZ74; -. DR STRING; 122586.NMB1262; -. DR PaxDb; Q9JZ74; -. DR EnsemblBacteria; AAF41639; AAF41639; NMB1262. DR GeneID; 903684; -. DR KEGG; nme:NMB1262; -. DR PATRIC; 20358139; VBINeiMen85645_1581. DR eggNOG; ENOG4108R5K; Bacteria. DR eggNOG; COG0652; LUCA. DR HOGENOM; HOG000065978; -. DR KO; K03767; -. DR OMA; NLDYPQP; -. DR OrthoDB; EOG6S26C3; -. DR BioCyc; NMEN122586:GHGG-1300-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PTHR11071; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; SSF50891; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU363019}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Rotamase {ECO:0000256|RuleBase:RU363019}; KW Signal {ECO:0000256|RuleBase:RU363019}. FT SIGNAL 1 22 {ECO:0000256|RuleBase:RU363019}. FT CHAIN 23 185 Peptidyl-prolyl cis-trans isomerase. FT {ECO:0000256|RuleBase:RU363019}. FT /FTId=PRO_5006529487. FT DOMAIN 29 183 PPIase cyclophilin-type. FT {ECO:0000259|PROSITE:PS50072}. SQ SEQUENCE 185 AA; 20040 MW; C5A588B51D6434AC CRC64; MKPKFKTVLT ALLLAVSLPS MAATHVLMET DMGNIRLVLD ESKAPKTVAN FVRYARKGFY DDTVFHRVID GFVIQGGGLT EDLAQKASDK AVANESGNGL KNTAGTIAMA RTTAPDSATS QFFINLADNA SLDYKNGQYG YTVFGRVESG MNTVSKIARV KTATRGFYQN VPVQPVKIRR VVVGQ // ID Q9JZN6_NEIMB Unreviewed; 29 AA. AC Q9JZN6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41373.1}; GN OrderedLocusNames=NMB0968 {ECO:0000313|EMBL:AAF41373.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41373.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41373.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41373.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41373.1; -; Genomic_DNA. DR PIR; B81136; B81136. DR RefSeq; NP_274006.1; NC_003112.2. DR RefSeq; WP_010980878.1; NC_003112.2. DR STRING; 122586.NMB0968; -. DR PaxDb; Q9JZN6; -. DR EnsemblBacteria; AAF41373; AAF41373; NMB0968. DR GeneID; 903088; -. DR KEGG; nme:NMB0968; -. DR PATRIC; 20357425; VBINeiMen85645_1227. DR HOGENOM; HOG000027914; -. DR BioCyc; NMEN122586:GHGG-1005-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 29 AA; 3575 MW; 8E5462A30E219EEE CRC64; MIMELLWQNI STSRRELTKL FLYKNLGLY // ID Q9K0M0_NEIMB Unreviewed; 201 AA. AC Q9K0M0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41000.1}; GN OrderedLocusNames=NMB0572 {ECO:0000313|EMBL:AAF41000.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41000.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41000.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41000.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41000.1; -; Genomic_DNA. DR PIR; G81182; G81182. DR RefSeq; NP_273616.1; NC_003112.2. DR RefSeq; WP_002222874.1; NC_003112.2. DR STRING; 122586.NMB0572; -. DR PaxDb; Q9K0M0; -. DR EnsemblBacteria; AAF41000; AAF41000; NMB0572. DR GeneID; 902687; -. DR KEGG; nme:NMB0572; -. DR PATRIC; 20356425; VBINeiMen85645_0732. DR eggNOG; ENOG4108XN7; Bacteria. DR eggNOG; COG3310; LUCA. DR HOGENOM; HOG000255677; -. DR KO; K09941; -. DR OMA; RSPYPML; -. DR OrthoDB; EOG6JHRKB; -. DR BioCyc; NMEN122586:GHGG-598-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009858; DUF1415. DR Pfam; PF07209; DUF1415; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 201 AA; 22264 MW; 8F663BF686E35440 CRC64; MTIMNINTSE NKDAVAEHTG QWLEKAVIGL NLCPFAKAPH VKNLVRIAIS EAKHLDGFLE DLDEELQRLG NTPATELETT LLVHPTLFPD FDVFNDMLDI ADAAVVENGL EGIVQIAPFH PDFQFEGTDS DDIGNYTNRS PYPTLHLIRE DSIAKAAQAF PDASAIFERN IALLEKMGHE GWAKLGITSC PYPHNKKNIS K // ID Q9K1B9_NEIMB Unreviewed; 157 AA. AC Q9K1B9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=NADH dehydrogenase I, E subunit {ECO:0000313|EMBL:AAF40699.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AAF40699.1}; GN Name=nuoE {ECO:0000313|EMBL:AAF40699.1}; GN OrderedLocusNames=NMB0245 {ECO:0000313|EMBL:AAF40699.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40699.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40699.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40699.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|PIRSR:PIRSR000216-1}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|PIRSR:PIRSR000216-1}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40699.1; -; Genomic_DNA. DR PIR; C81222; C81222. DR RefSeq; NP_273301.1; NC_003112.2. DR RefSeq; WP_002224830.1; NC_003112.2. DR ProteinModelPortal; Q9K1B9; -. DR STRING; 122586.NMB0245; -. DR PaxDb; Q9K1B9; -. DR EnsemblBacteria; AAF40699; AAF40699; NMB0245. DR GeneID; 902356; -. DR KEGG; nme:NMB0245; -. DR PATRIC; 20355566; VBINeiMen85645_0307. DR eggNOG; ENOG4105GKE; Bacteria. DR eggNOG; COG1905; LUCA. DR HOGENOM; HOG000257748; -. DR KO; K00334; -. DR OMA; IDPMEAF; -. DR OrthoDB; EOG689HX9; -. DR BioCyc; NMEN122586:GHGG-260-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01958; nuoE_fam; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000216-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|PIRSR:PIRSR000216-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000216-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000216-1}; KW Oxidoreductase {ECO:0000313|EMBL:AAF40699.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT METAL 82 82 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 87 87 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 123 123 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 127 127 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. SQ SEQUENCE 157 AA; 17147 MW; F4DF7F0411965DD8 CRC64; MLSAESLKQI DIELAKYPAD QRRSAIMGAL RIAQTEKGWL APETIAFVAD YIGITPAQAY EVATFYNMYD LEPVGKYKLT VCTNLPCALR GGMATGEYLK QKLGIGYGET TPDGKFTLVE GECMGACGDA PVMLVNNHSM CSFMTEEAIE KKLAELE // ID Q9K179_NEIMB Unreviewed; 303 AA. AC Q9K179; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Putative transcriptional regulator {ECO:0000313|EMBL:AAF40741.1}; GN OrderedLocusNames=NMB0290 {ECO:0000313|EMBL:AAF40741.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40741.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40741.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40741.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH lysR-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00523900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40741.1; -; Genomic_DNA. DR PIR; A81215; A81215. DR RefSeq; NP_273344.1; NC_003112.2. DR RefSeq; WP_002221945.1; NC_003112.2. DR ProteinModelPortal; Q9K179; -. DR STRING; 122586.NMB0290; -. DR PaxDb; Q9K179; -. DR EnsemblBacteria; AAF40741; AAF40741; NMB0290. DR GeneID; 902401; -. DR KEGG; nme:NMB0290; -. DR PATRIC; 20355680; VBINeiMen85645_0364. DR eggNOG; ENOG4108S8H; Bacteria. DR eggNOG; COG0583; LUCA. DR HOGENOM; HOG000233519; -. DR OMA; CANSETL; -. DR OrthoDB; EOG6Q8J00; -. DR BioCyc; NMEN122586:GHGG-305-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 1 59 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. SQ SEQUENCE 303 AA; 33710 MW; 8847104258FF3B83 CRC64; MDTLFSLKVF RQVVQSGGFT RAADALGIST AMASKHVSHL ENTVQAKLLH RNSRNLSLTE AGEEYYRQCS YALDTLDDAA QKAAGGTEKP QGLLRVTMPL WFAGSQICNW LAEYRERYPE VALELILDNR HVDLIAEGVD LALRVSQTLS PSLIARPLAE IEFALLASPD FLRRNGVPET PEEVAGLPAV LPTYTNQQKL DLTRKSDGKK YRLELTPVIR TDNTLMMREM IKAGACIGYQ PLWAAEHDLR CGTLVRLLPG YAVPTDRLNA VYADRAFLSA KVRSFIDFLN EKIASRKGCR NAV // ID Q9JYY9_NEIMB Unreviewed; 110 AA. AC Q9JYY9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 100. DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077}; GN OrderedLocusNames=NMB1366 {ECO:0000313|EMBL:AAF41740.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41740.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41740.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41740.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the thioredoxin family. CC {ECO:0000256|PIRNR:PIRNR000077}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC {ECO:0000256|RuleBase:RU004207}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41740.1; -; Genomic_DNA. DR PIR; C81090; C81090. DR RefSeq; NP_274384.1; NC_003112.2. DR RefSeq; WP_002213213.1; NC_003112.2. DR ProteinModelPortal; Q9JYY9; -. DR SMR; Q9JYY9; 3-110. DR STRING; 122586.NMB1366; -. DR PaxDb; Q9JYY9; -. DR EnsemblBacteria; AAF41740; AAF41740; NMB1366. DR GeneID; 903788; -. DR KEGG; nme:NMB1366; -. DR PATRIC; 20358397; VBINeiMen85645_1710. DR eggNOG; ENOG4105K63; Bacteria. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000292977; -. DR KO; K03671; -. DR OMA; MSEHIHY; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NMEN122586:GHGG-1404-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10438; PTHR10438; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PIRSF; PIRSF000077; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 110 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 34 37 Redox-active. FT {ECO:0000256|PIRSR:PIRSR000077-4}. SQ SEQUENCE 110 AA; 11831 MW; 5E16DFF18F495FD3 CRC64; MSSELIVHTS DAAFEKDVLN ADIPVLLDFW APWCGPCKMI APILDDIAAE FEGRLKVVKI NIDDNEATPS RFGVRGIPTL MVFKNGEVVA TKVGALAKGQ LTAFVEASIA // ID Q9JXJ0_NEIMB Unreviewed; 220 AA. AC Q9JXJ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42341.1}; GN OrderedLocusNames=NMB2018 {ECO:0000313|EMBL:AAF42341.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42341.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42341.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42341.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42341.1; -; Genomic_DNA. DR PIR; E81014; E81014. DR RefSeq; NP_275010.1; NC_003112.2. DR RefSeq; WP_002226778.1; NC_003112.2. DR ProteinModelPortal; Q9JXJ0; -. DR STRING; 122586.NMB2018; -. DR PaxDb; Q9JXJ0; -. DR EnsemblBacteria; AAF42341; AAF42341; NMB2018. DR GeneID; 904093; -. DR KEGG; nme:NMB2018; -. DR PATRIC; 20360149; VBINeiMen85645_2574. DR eggNOG; ENOG4108W1A; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06177; -. DR OMA; HSINCEP; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NMEN122586:GHGG-2080-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006508; PsdUridine_synth_RluA-like. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR01621; RluA-like; 1. DR PROSITE; PS01129; PSI_RLU; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 12 155 PseudoU_synth_2. FT {ECO:0000259|Pfam:PF00849}. SQ SEQUENCE 220 AA; 25005 MW; C6BFA7D1BA84C2CC CRC64; MDMLEILFRH QDFVAINKPG GISVHQDSGE TGLARTLAIQ LGVERVWLLH RLDKQTSGIL LFALNKESAS ALSGQFAGKS IKKTYLALSD RKPSKKQGWI KGGMEKSRCG MWKLTRNTEN IAVTRFHSIS IAEKLRLFIL EPHTGKTHQL RVAMKSLGSP ILGDSLYGGT ESETMFLYAW KIQFDYQNRQ IEIVAPLKNE WQTENIHRAL EEFCMENKID // ID Q9JZI0_NEIMB Unreviewed; 823 AA. AC Q9JZI0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 120. DE SubName: Full=Cation transport ATPase, E1-E2 family {ECO:0000313|EMBL:AAF41440.1}; GN OrderedLocusNames=NMB1042 {ECO:0000313|EMBL:AAF41440.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41440.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41440.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41440.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IB subfamily. CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Contains 1 HMA domain. CC {ECO:0000256|RuleBase:RU362081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41440.1; -; Genomic_DNA. DR PIR; D81129; D81129. DR RefSeq; NP_274076.1; NC_003112.2. DR RefSeq; WP_002219226.1; NC_003112.2. DR ProteinModelPortal; Q9JZI0; -. DR STRING; 122586.NMB1042; -. DR TCDB; 3.A.3.27.1; the p-type atpase (p-atpase) superfamily. DR PaxDb; Q9JZI0; -. DR EnsemblBacteria; AAF41440; AAF41440; NMB1042. DR GeneID; 903178; -. DR KEGG; nme:NMB1042; -. DR PATRIC; 20357621; VBINeiMen85645_1327. DR eggNOG; ENOG4105C59; Bacteria. DR eggNOG; COG2217; LUCA. DR HOGENOM; HOG000250398; -. DR KO; K01533; -. DR OMA; QMNMDHD; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NMEN122586:GHGG-1079-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR Gene3D; 2.70.150.10; -; 1. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR021993; ATPase-cat-bd. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006121; HMA_dom. DR InterPro; IPR027256; P-typ_ATPase_IB. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF12156; ATPase-cat_bd; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU362081}; KW Membrane {ECO:0000256|RuleBase:RU362081}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362081}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 175 198 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 210 231 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 243 265 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 271 290 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 428 450 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 456 475 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 766 785 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 791 809 Helical. {ECO:0000256|RuleBase:RU362081}. FT DOMAIN 92 158 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 823 AA; 89364 MW; 480D7D10F7C23C12 CRC64; MKKTCFHCGL DVPEHLHLTV RYENEDRETC CAGCQAVAQS IIDAGLGSYY KQRTADAQKT ELPPQEILDQ IRLYDLPEVQ SDFVETHGGT REAVLMLGGI TCAACVWLIE QQLLRTDGIV RIDLNYSTHR CRVVWDDGKI RLSDILLKIR QIGYTAAPYD AQKIEAANQK ERKQYIVRLA VAGLGMMQTM MFALPTYLYG GDIEPDFLQI LHWGGFLMVL PVVFYCAVPF YQGALRDLKN RRVGMDTPIT VAIIMTFIAG VYSLATNAGQ GMYFESIAML LFFLLGGRFM EHIARRKAGD AAERLVKLIP AFCHHMPDYP DTQETCEAAV VKLKAGDIVL VKPGETIPVD GTVLEGSSAV NESMLTGESL PVAKMPSEKV TAGTLNTQSP LIIRTDRTGG GTRLSHIVRL LDRALAQKPR TAELAEQYAS SFIFGELLLA VPVFIGWTLY ADAHTALWIT VALLVITCPC ALSLATPTAL AASTGTLARE GILIGGKQAI ETLAQTTDII FDKTGTLTQG KPAVRRISLL RGTDEAFVLA VAQALEQQSE HPLARAILNC RISDGSVPDI AIKQRLNRIG EGVGAQLTVN GETQVWALGR ASYVAEISGK EPQTEGGGSA VYLGSQSGFQ AVFYLTDPLK DSAAEAVRQL AGKNLTLHIL SGDRETAVAE TARALGVAHY RAQAMPEDKL EYVKALQKEG KKVLMIGDGI NDAPVLAQAD VSAAAAGGTD IARDGADIVL LNEDLRTVAH LLDQARRTRH IIRQNLIWAG AYNIIAVPLA VLGYVQPWIA ALGMSFSSLA VLGNALRLHK RGKMQSEKMP SEQ // ID Q9K007_NEIMB Unreviewed; 186 AA. AC Q9K007; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41234.1}; GN OrderedLocusNames=NMB0821 {ECO:0000313|EMBL:AAF41234.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41234.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41234.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41234.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41234.1; -; Genomic_DNA. DR PIR; D81154; D81154. DR PaxDb; Q9K007; -. DR EnsemblBacteria; AAF41234; AAF41234; NMB0821. DR PATRIC; 20357027; VBINeiMen85645_1032. DR HOGENOM; HOG000218869; -. DR OMA; MSTVQYG; -. DR OrthoDB; EOG6M0T66; -. DR BioCyc; NMEN122586:GHGG-852-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 99 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 186 AA; 20851 MW; 6CE7087513376B26 CRC64; MTANFAQTLV EIQDSLYRVV STVQYGDDNL KRLTADKRKQ YELNFKISEG STRVESDFKE TLVRFGRDML QDMPPKIRSA TLVALTTLLV GGALGYGYLE YLKQVASEGY QTERLYNAVD RLAESQERIT SAILKGARGA DFVQIGRRSY SREDISEANR RAERVPYGAE LVSDGNFTAV LSDIGD // ID Q7DDD4_NEIMB Unreviewed; 218 AA. AC Q7DDD4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Transcriptional regulator, LuxR family {ECO:0000313|EMBL:AAF41630.1}; GN OrderedLocusNames=NMB1250 {ECO:0000313|EMBL:AAF41630.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41630.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41630.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41630.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000707}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00504402}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41630.1; -; Genomic_DNA. DR PIR; C81104; C81104. DR RefSeq; NP_274273.1; NC_003112.2. DR RefSeq; WP_002225188.1; NC_003112.2. DR ProteinModelPortal; Q7DDD4; -. DR STRING; 122586.NMB1250; -. DR PaxDb; Q7DDD4; -. DR EnsemblBacteria; AAF41630; AAF41630; NMB1250. DR GeneID; 903672; -. DR KEGG; nme:NMB1250; -. DR PATRIC; 20358097; VBINeiMen85645_1561. DR eggNOG; ENOG4105WH1; Bacteria. DR eggNOG; COG2197; LUCA. DR HOGENOM; HOG000034813; -. DR KO; K07684; -. DR OMA; IRATFHG; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NMEN122586:GHGG-1287-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR000792; Tscrpt_reg_LuxR_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00196; GerE; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00038; HTHLUXR. DR SMART; SM00421; HTH_LUXR; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS00622; HTH_LUXR_1; 1. DR PROSITE; PS50043; HTH_LUXR_2; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000707, KW ECO:0000256|SAAS:SAAS00489599}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000707, KW ECO:0000256|SAAS:SAAS00526740}; KW Transcription regulation {ECO:0000256|RuleBase:RU000707, KW ECO:0000256|SAAS:SAAS00526740}. FT DOMAIN 4 120 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 146 211 HTH luxR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50043}. SQ SEQUENCE 218 AA; 23836 MW; C873991704758E25 CRC64; MTIKIILIDD HTLFRSGIKA LLSRQHGFEV IGEAADGLSG IKMISRLQPD VVLLDLDMPG MNGREALSQI ISINPQQAVI MLTVSEDSDD LTECMRIGAR GYLLKNINAD FLLESIRKAA EGDNVFSPEM TAKLVKSLIS PQPAQGTQAL SSLTPRELEI LGYLAAGHSN KIIARHLDLA ESTVKVHVQN LLRKLNLSSR VQAAVYAIRH NVPQPVPE // ID Q9JXY0_NEIMB Unreviewed; 231 AA. AC Q9JXY0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Mannose-1-phosphate guanyltransferase-related protein {ECO:0000313|EMBL:AAF42176.1}; GN OrderedLocusNames=NMB1841 {ECO:0000313|EMBL:AAF42176.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42176.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42176.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42176.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42176.1; -; Genomic_DNA. DR PIR; A81036; A81036. DR RefSeq; NP_274838.1; NC_003112.2. DR RefSeq; WP_002225669.1; NC_003112.2. DR ProteinModelPortal; Q9JXY0; -. DR STRING; 122586.NMB1841; -. DR PaxDb; Q9JXY0; -. DR EnsemblBacteria; AAF42176; AAF42176; NMB1841. DR GeneID; 903258; -. DR KEGG; nme:NMB1841; -. DR PATRIC; 20359689; VBINeiMen85645_2350. DR eggNOG; ENOG4108S0S; Bacteria. DR eggNOG; COG1208; LUCA. DR HOGENOM; HOG000283478; -. DR KO; K00992; -. DR OMA; AGVDDWV; -. DR OrthoDB; EOG6XHC75; -. DR BioCyc; NMEN122586:GHGG-1896-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42176.1}. FT DOMAIN 2 139 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 231 AA; 24537 MW; D02A35622345A189 CRC64; MKAMILAAGR GERMRPLTDT TPKPLLDVAG KPLIGWHLCR LKQAGFTEIV INHAWLGRQI EDALGDGSAY GVNIAYSPEP AGGLETAGGI AQALPLLGGQ PFLVVNGDVL TDIDFTAAFQ TASSLPEHIS AHLWLVENPP HNPDGDFSLL PDSSVRPEVN GGNGLTFSGV GIYRPEMFDG IEAGSVAKLA PVLRGEMRQN RVSGQKHTGL WLDVGTVCRL KEAQALAGAW K // ID Q9JY78_NEIMB Unreviewed; 242 AA. AC Q9JY78; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 97. DE SubName: Full=3-oxoacyl-(Acyl-carrier-protein) reductase {ECO:0000313|EMBL:AAF42050.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AAF42050.1}; GN Name=fabG-1 {ECO:0000313|EMBL:AAF42050.1}; GN OrderedLocusNames=NMB1702 {ECO:0000313|EMBL:AAF42050.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42050.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42050.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42050.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000256|RuleBase:RU000363}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42050.1; -; Genomic_DNA. DR PIR; H81052; H81052. DR RefSeq; NP_274706.1; NC_003112.2. DR RefSeq; WP_002222115.1; NC_003112.2. DR ProteinModelPortal; Q9JY78; -. DR STRING; 122586.NMB1702; -. DR PaxDb; Q9JY78; -. DR EnsemblBacteria; AAF42050; AAF42050; NMB1702. DR GeneID; 903401; -. DR KEGG; nme:NMB1702; -. DR PATRIC; 20359359; VBINeiMen85645_2186. DR eggNOG; ENOG4105C2D; Bacteria. DR eggNOG; COG1028; LUCA. DR KO; K00059; -. DR OMA; EQDVETH; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NMEN122586:GHGG-1757-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011285; FabG-rel. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01831; fabG_rel; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42050.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 242 AA; 26059 MW; 8C7BD07FBBBE4CC2 CRC64; MTETVLITGS NRGIGKAVAF GLAEDGFDIA VHCRSRRDEA EAVAEEIRAL GRNARVLQFD VSDREACREI LTADIEANGA YYGVVLNAGL TRDNTFPAFS DDDWDVVLRT NLDGFYNVLH PLVMPMIRRR KAGRIVCMAS VSGLTGNRGQ VNYSASKAGI IGAAKALAVE LAKRKITVNC VAPGLIDTDI IDENVPVEEI LKAVPAALMG LPEEVAHAVR FLMDEKAAYI TRQVIAVNGG LC // ID Q9K0N3_NEIMB Unreviewed; 90 AA. AC Q9K0N3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40983.1}; GN OrderedLocusNames=NMB0555 {ECO:0000313|EMBL:AAF40983.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40983.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40983.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40983.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40983.1; -; Genomic_DNA. DR PIR; A81186; A81186. DR RefSeq; NP_273599.1; NC_003112.2. DR RefSeq; WP_002225570.1; NC_003112.2. DR STRING; 122586.NMB0555; -. DR PaxDb; Q9K0N3; -. DR EnsemblBacteria; AAF40983; AAF40983; NMB0555. DR GeneID; 902670; -. DR KEGG; nme:NMB0555; -. DR PATRIC; 20356381; VBINeiMen85645_0710. DR HOGENOM; HOG000218804; -. DR OrthoDB; EOG6J1DH6; -. DR BioCyc; NMEN122586:GHGG-581-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 90 AA; 10285 MW; E7A038DD53A3A3FE CRC64; MKKTGKYLIY TAAFTAFCFA FQENRSEAKQ PDITLSASLC EQFNILNAKD MDAEQVSLSK ECDIIESSHD WEKEYGNLNE QEMLAGIVYE // ID Q9JZM0_NEIMB Unreviewed; 370 AA. AC Q9JZM0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=IS1106 transposase {ECO:0000313|EMBL:AAF41394.1}; GN OrderedLocusNames=NMB0991 {ECO:0000313|EMBL:AAF41394.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41394.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41394.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41394.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41394.1; -; Genomic_DNA. DR PIR; F81133; F81133. DR RefSeq; NP_274027.1; NC_003112.2. DR RefSeq; WP_002225296.1; NC_003112.2. DR PaxDb; Q9JZM0; -. DR EnsemblBacteria; AAF41394; AAF41394; NMB0991. DR GeneID; 903111; -. DR KEGG; nme:NMB0991; -. DR PATRIC; 20357481; VBINeiMen85645_1255. DR eggNOG; ENOG4105F2I; Bacteria. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000218682; -. DR KO; K07481; -. DR OMA; NNERDPD; -. DR OrthoDB; EOG67T5PN; -. DR BioCyc; NMEN122586:GHGG-1028-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR002559; Transposase_11. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF01609; DDE_Tnp_1; 1. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 51 122 DUF772. {ECO:0000259|Pfam:PF05598}. FT DOMAIN 139 302 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 370 AA; 42430 MW; 2EC3432FF8DAC7F8 CRC64; MSTFFRQTAQ AMIAKHINRF PLLKLDQVID WQPIEQYLNR QKTRYLRDHR GRPAYPLLSM FKAVLLGQWH SLSDPELEHS LITRIDFNLF CRFDELSIPD YSTLCRYRNW LAQDDTLSEL LELINCQLTE KGLKVEKASA AVIDATIIQT AGSEQRQAIE VDEEGQISGQ TTPSKDSDAR WIKKNGLYKL GYKQHTRTDA EGYIEKLHIT PANAHECKHL SPLLEGLPEG TTVYADKGYD SAENRQHLEE HQLLDGIMSK ACRNRPLSEV QTKRNRYLSK TRYSGLNLNQ DKATKPQTVQ IVRQGEATPY WFKFNPLYVV EQSFGTLHRK FRYARAAYFG LIKVSAQSHL KAMCLNLLKA ANRLSAPAAA // ID Q9JYK0_NEIMB Unreviewed; 548 AA. AC Q9JYK0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Putative tspB protein {ECO:0000313|EMBL:AAF41903.1}; GN OrderedLocusNames=NMB1548 {ECO:0000313|EMBL:AAF41903.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41903.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41903.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41903.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41903.1; -; Genomic_DNA. DR PIR; A81070; A81070. DR RefSeq; NP_274555.1; NC_003112.2. DR RefSeq; WP_010980956.1; NC_003112.2. DR PaxDb; Q9JYK0; -. DR EnsemblBacteria; AAF41903; AAF41903; NMB1548. DR GeneID; 904097; -. DR KEGG; nme:NMB1548; -. DR PATRIC; 20358930; VBINeiMen85645_1979. DR eggNOG; ENOG41067SK; Bacteria. DR eggNOG; ENOG410Y4J8; LUCA. DR HOGENOM; HOG000218809; -. DR OMA; YIKETGY; -. DR OrthoDB; EOG62NX16; -. DR BioCyc; NMEN122586:GHGG-1589-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008708; Neisseria_TspB. DR Pfam; PF05616; Neisseria_TspB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 548 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328322. SQ SEQUENCE 548 AA; 60710 MW; A1A6E0088151A8B3 CRC64; MKQNVMFIIL GRNFLKIILC FSFFVSKFAL ASVNAPGKFD RVEVYDDGRY LGIRGSDDKR RRIWKGVFDR ESGRYLTSEA QDLKVRHVST GASSTGKVSS VVSSSVSRAG VLAGVGKLAR LGAKLSTRAV PYVGTALLAH DVYETFKEDI QAQGYQYDPE TDKFVKGYEY SNCLWYEDKR RINRTYGCYG VDSSIMRLMS DDSRFPEVKE LMESQMYRLA RPFWNWHKEE LNKLSSLDWN NFVLNSCTFD WNGGDCVVNK GDDFRNGADF SLIRNSKYKE EMDAKKLEEI LSLKVDANPD KYIKATGYPG YSEKVEVAPG TKVNMGPVTD RNGNPVQVVA TFGRDSQGNT TVDVQVIPRP DLTPGSAEAP NAQPLPEVSP AENPANNPNP NENPGTSPNP EPDPDLNPDA NPDTDGQPGT RPDSPAVPGR TNGRDGKDGK DGKDGGLLCK FFPDILACDR LPESNPAEDL NLPSETVNVE FQKSGIFQDS AQCPAPVTFT VTVLDSSRQF AFSFENACTI AERLRYMLLA LAWAVAAFFC IRTVSREV // ID Q9K181_NEIMB Unreviewed; 716 AA. AC Q9K181; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Probable ATP-dependent helicase DinG {ECO:0000313|EMBL:AAF40739.1}; GN Name=dinG {ECO:0000313|EMBL:AAF40739.1}; GN OrderedLocusNames=NMB0287 {ECO:0000313|EMBL:AAF40739.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40739.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40739.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40739.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40739.1; -; Genomic_DNA. DR PIR; F81216; F81216. DR RefSeq; NP_273342.1; NC_003112.2. DR RefSeq; WP_002224852.1; NC_003112.2. DR ProteinModelPortal; Q9K181; -. DR STRING; 122586.NMB0287; -. DR PaxDb; Q9K181; -. DR EnsemblBacteria; AAF40739; AAF40739; NMB0287. DR GeneID; 902398; -. DR KEGG; nme:NMB0287; -. DR PATRIC; 20355674; VBINeiMen85645_0361. DR eggNOG; ENOG4105DVT; Bacteria. DR eggNOG; COG1199; LUCA. DR HOGENOM; HOG000242573; -. DR KO; K03722; -. DR OMA; MRALNSF; -. DR OrthoDB; EOG6742WF; -. DR BioCyc; NMEN122586:GHGG-302-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13307; Helicase_C_2; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAF40739.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000313|EMBL:AAF40739.1}; KW Hydrolase {ECO:0000313|EMBL:AAF40739.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAF40739.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 325 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51193}. FT DOMAIN 545 696 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 716 AA; 79280 MW; 2965610E4FC0606F CRC64; MLTDLEKNAI RDHYQNIGKN LPGFRPRASQ REMIAAVANA FSRTLAREEG GEPPKREGES IAVIEGPTGV GKSLAYLLAG GIMAQTRGKR LIVSSATVAL QEQLVDRDLP FLVEKSGLEL TFALAKGRGR YLCPYKLYRL TQSNAQQNLL GFEAPAVLWD SKPKPEELKL LRDIADEFSA RRFNGDRDTW PEKIDDAIWL KVTNDRHGCL KTACPNRPEC PFYLARDVLE TVDVVVANHD LLLADISMGG GVILPAPENS FYCIDEAHHL PKKALSRFAA EHSWNIAVWT LEKLPQLTGK IAALTDKAEL ANLADEAAAS LLDSLHEWQF HLAEEPSLSL GVSENDRRTN SEPTWLWEDG KIPEGLETTV SNTAIAARSL LKHVIGLNDA LSAARREKEQ DGALLDRLTS EFGLFIARIE QISAVWDLLS TVPLEGEEPL AKWITRRADD KNDYIFNASP ISSASHLANS LWRRAAGAVL TSATLQSLGN FNLMLRQTGL QWLPETTTLA LKSPFDFEKQ GELYIPPIYA SPKDPEAHTA AVIEWLPKLI SPTEAIGTLV LFSSRKQMQD VALRLPGDYL PLLLVQGELP KAVLLQKHHR AIEEGKASII FGLDSFAEGL DLPGTACVQV IIAKLPFAMP DNPIEKTQNR WIEQRGGNPF IEITVPEAGI KLIQAVGRLI RTEQDYGRVT ILDNRIKTQR YGQQLLAGLP PFKRIG // ID Q9JXB4_NEIMB Unreviewed; 70 AA. AC Q9JXB4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42445.1}; GN OrderedLocusNames=NMB2137 {ECO:0000313|EMBL:AAF42445.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42445.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42445.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42445.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42445.1; -; Genomic_DNA. DR PIR; G81001; G81001. DR STRING; 122586.NMB2137; -. DR PaxDb; Q9JXB4; -. DR EnsemblBacteria; AAF42445; AAF42445; NMB2137. DR PATRIC; 20360464; VBINeiMen85645_2728. DR eggNOG; ENOG4106HB9; Bacteria. DR eggNOG; ENOG410Y8F8; LUCA. DR HOGENOM; HOG000027910; -. DR OMA; YLATNCC; -. DR OrthoDB; EOG6KDKWX; -. DR BioCyc; NMEN122586:GHGG-2202-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 70 AA; 7554 MW; D14D00DCB4248A31 CRC64; MLKQPTRTLG GQRHCVLFGL APNGVWPAAY CYQMRGAPLP HLFTLTCAAK AAIGGFAFCS TFRRVTAPGR // ID Q9K0H9_NEIMB Unreviewed; 275 AA. AC Q9K0H9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41047.1}; GN OrderedLocusNames=NMB0621 {ECO:0000313|EMBL:AAF41047.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41047.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41047.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41047.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41047.1; -; Genomic_DNA. DR PIR; B81178; B81178. DR RefSeq; NP_273665.1; NC_003112.2. DR RefSeq; WP_002222832.1; NC_003112.2. DR STRING; 122586.NMB0621; -. DR PaxDb; Q9K0H9; -. DR EnsemblBacteria; AAF41047; AAF41047; NMB0621. DR GeneID; 902734; -. DR KEGG; nme:NMB0621; -. DR PATRIC; 20356531; VBINeiMen85645_0785. DR eggNOG; ENOG4105ED9; Bacteria. DR eggNOG; COG2833; LUCA. DR HOGENOM; HOG000261987; -. DR OMA; WRFAGMP; -. DR OrthoDB; EOG6GR36Q; -. DR BioCyc; NMEN122586:GHGG-647-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007402; DUF455. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR011197; UCP012318. DR Pfam; PF04305; DUF455; 1. DR PIRSF; PIRSF012318; UCP012318; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 275 AA; 31435 MW; ECE215AD2386086D CRC64; MKPDIYALLE RALLSGDPDE KGRLTDEAFA AVQNADGAET NAPPADFPRA GRPDKPVLVA PSQLTPRKMN TTEGYAAMLH AIAHIEFNAI NLALDAAYRF RTLPFQFVRD WVKVAKEEVY HFRLMRERLR AFGFDYGDFE AHNHLWDMAY KTAYDPLLRM ALVPRVLEAR GLDVTPGIRA KVAQRGDSET CGVLDIIYRD EVGHVAIGNR WYQHLCRERG LEPVALFRSL IARYDMFIFR GYVNIEAREK AGFSRFELDM LEDFEQGLKQ NKHAV // ID Q7DDU1_NEIMB Unreviewed; 347 AA. AC Q7DDU1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AAF40521.1}; GN Name=pilT-1 {ECO:0000313|EMBL:AAF40521.1}; GN OrderedLocusNames=NMB0052 {ECO:0000313|EMBL:AAF40521.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40521.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40521.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40521.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40521.1; -; Genomic_DNA. DR RefSeq; NP_273117.1; NC_003112.2. DR RefSeq; WP_002218487.1; NC_003112.2. DR ProteinModelPortal; Q7DDU1; -. DR STRING; 122586.NMB0052; -. DR PaxDb; Q7DDU1; -. DR EnsemblBacteria; AAF40521; AAF40521; NMB0052. DR GeneID; 902154; -. DR KEGG; nme:NMB0052; -. DR PATRIC; 20355097; VBINeiMen85645_0086. DR eggNOG; ENOG4105CZX; Bacteria. DR eggNOG; COG2805; LUCA. DR HOGENOM; HOG000008425; -. DR KO; K02669; -. DR OMA; PIEYVFP; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NMEN122586:GHGG-53-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006321; PilT. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01420; pilT_fam; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 193 207 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 347 AA; 38050 MW; 88314DB7EFDC7183 CRC64; MQITDLLAFG AKNKASDLHL SSGISPMIRV HGDMRRINLP EMSAEEVGNM VTSVMNDHQR KIYQQNLEVD FSFELPNVAR FRVNAFNIGR GPAAVFRTIP STVLSLEELK APSIFQKIAE SPRGMVLVTG PTGSGKSTTL AAMINYINET QPAHILTIED PIEFVHQSKK SLINQRELHQ HTLSFANALR SALREDPDVI LVGEMRDPET IGLALTAAET GHLVFGTLHT TGAAKTVDRI VDVFPAGEKE MVRSMLSESL TAVISQNLLK THDGNGRVAS HEILIANPAV RNLIRENKIT QINSVLQTGQ ASGMQTMDQS LQSLVRQGLI APEVARRRAQ NSESMSF // ID Q9JYP4_NEIMB Unreviewed; 477 AA. AC Q9JYP4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Succinate-semialdehyde dehydrogenase (NADP+) {ECO:0000313|EMBL:AAF41844.1}; DE EC=1.2.1.16 {ECO:0000313|EMBL:AAF41844.1}; GN Name=gabD {ECO:0000313|EMBL:AAF41844.1}; GN OrderedLocusNames=NMB1488 {ECO:0000313|EMBL:AAF41844.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41844.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41844.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41844.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41844.1; -; Genomic_DNA. DR PIR; F81077; F81077. DR RefSeq; NP_274496.1; NC_003112.2. DR RefSeq; WP_002225085.1; NC_003112.2. DR ProteinModelPortal; Q9JYP4; -. DR STRING; 122586.NMB1488; -. DR PaxDb; Q9JYP4; -. DR EnsemblBacteria; AAF41844; AAF41844; NMB1488. DR GeneID; 903910; -. DR KEGG; nme:NMB1488; -. DR PATRIC; 20358742; VBINeiMen85645_1880. DR eggNOG; ENOG4105C26; Bacteria. DR eggNOG; COG1012; LUCA. DR HOGENOM; HOG000271509; -. DR KO; K00135; -. DR OMA; PVAKMLY; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NMEN122586:GHGG-1528-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC. DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:InterPro. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR010102; Succ_semiAld_DH. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR01780; SSADH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003344, KW ECO:0000313|EMBL:AAF41844.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 22 470 Aldedh. {ECO:0000259|Pfam:PF00171}. SQ SEQUENCE 477 AA; 51170 MW; A96A006849F81A36 CRC64; MNEYSQLIKH PDISLPPVSD GIKVDNPATG ETLAFVRKTD SDKLKNLIQK AAAAQKLWAA KTALERADVL WRWYFQIKEN KEALARLMTM EQGKSLTEAR GEIDYAASFV RWFAEEARRI DGDVLTSVKA SQKLVVLKQP VGVTAAITPW NFPSAMIARK AAPALAVGCA MIVKPASLTP LSAYALASLA YEAGIPQDLL PVVSGSASEI GHEFATNPII RKISFTGSTE VGAKIFADSA ADIKKLSLEL GGNAPFIVFD DADLDKAVEG ALASKFRNSG QTCVCTNRVY AQSAIYDEFC RKLSEKAAAL KLGNGLEDGV NQGPLIEEKA VEKVEQHIAD ALAKGASCLT GGKRSALGGT FFEPTVLSGV TAQMAVAREE TFGPLCPVFR FETEAEVIEA ANNTEYGLAA YLFTADTARQ WRVGEALEYG MVGINTGLIS NEAAPFGGVK RSGLGREGSK YGADEYLELK YLCMDVG // ID Q9JZA9_NEIMB Unreviewed; 80 AA. AC Q9JZA9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41593.1}; GN OrderedLocusNames=NMB1211 {ECO:0000313|EMBL:AAF41593.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41593.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41593.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41593.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41593.1; -; Genomic_DNA. DR PIR; G81108; G81108. DR RefSeq; NP_274236.1; NC_003112.2. DR RefSeq; WP_002244136.1; NC_003112.2. DR STRING; 122586.NMB1211; -. DR PaxDb; Q9JZA9; -. DR EnsemblBacteria; AAF41593; AAF41593; NMB1211. DR GeneID; 903633; -. DR KEGG; nme:NMB1211; -. DR OrthoDB; EOG6SFPF4; -. DR BioCyc; NMEN122586:GHGG-1248-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 80 AA; 9162 MW; 7E0743E9D88A45B8 CRC64; MKYIVSISLA MGLAACSFGG FKPPPDDSVY WKYSRIEQEY PAMMSKNINL RIYSYEEYSK QIDDLFAKEK KTGKSAAMTQ // ID Q9K0M2_NEIMB Unreviewed; 473 AA. AC Q9K0M2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40998.1}; GN OrderedLocusNames=NMB0570 {ECO:0000313|EMBL:AAF40998.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40998.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40998.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40998.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40998.1; -; Genomic_DNA. DR PIR; E81182; E81182. DR RefSeq; NP_273614.1; NC_003112.2. DR RefSeq; WP_002222877.1; NC_003112.2. DR STRING; 122586.NMB0570; -. DR TCDB; 2.A.111.1.2; the na(+)/h(+) antiporter-e (nhae) family. DR PaxDb; Q9K0M2; -. DR EnsemblBacteria; AAF40998; AAF40998; NMB0570. DR GeneID; 902685; -. DR KEGG; nme:NMB0570; -. DR PATRIC; 20356419; VBINeiMen85645_0729. DR eggNOG; ENOG4105EDA; Bacteria. DR eggNOG; COG1055; LUCA. DR HOGENOM; HOG000257989; -. DR OMA; GNAPNLM; -. DR OrthoDB; EOG622PQ3; -. DR BioCyc; NMEN122586:GHGG-596-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031566; CitMHS_2. DR Pfam; PF16980; CitMHS_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 473 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327765. FT TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 220 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 305 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 355 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 367 391 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 403 424 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 445 470 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 473 AA; 51693 MW; 1710528183587B0D CRC64; MRHLPLFSLM LFPASVYAAD LDGANLNLLW GLPFALILLS IALGPLFFSH TWHHHYGKIT AFWTLLFLIP FSLVFGASAG IHTVAHALVE EYIPFILLLL ALYTISGGIL VWGDLNGTPK LNTALLAVGT ALASIMGTTG AAMLMIRPLL KANQNRTRRV HIVIFFIFLV ANIGGGLTPL GDPPLFLGFL KGVDFMWTVK HMFAPVLIST AVLLTAFYFI DNRFFKQESI AQDTPAQQEK PEKIAIFGKW NFLLLSGVVG AVLMSGLWKP EHPGFEILGS RYALQNLVRD VILIALTAVS MAITPKQVRA GNEFNFEPIA EVGKLFLGIF ITIFPVLSIL KAGEAGALGG VVSLVHDTAG HPINVMYFWM SGILSAFLDN APTYLVFFNM AGGDAQALMT GTLFHSLLAV SMGSVFMGAL TYIGNAPNFM VKAIAEQRGV PMPTFFGYMM WSVAFLTPVF IVHTLIFFVF KLL // ID Q9JY00_NEIMB Unreviewed; 280 AA. AC Q9JY00; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42150.1}; GN OrderedLocusNames=NMB1815 {ECO:0000313|EMBL:AAF42150.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42150.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42150.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42150.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42150.1; -; Genomic_DNA. DR PIR; H81038; H81038. DR RefSeq; NP_274812.1; NC_003112.2. DR RefSeq; WP_010980995.1; NC_003112.2. DR ProteinModelPortal; Q9JY00; -. DR SMR; Q9JY00; 2-254. DR STRING; 122586.NMB1815; -. DR PaxDb; Q9JY00; -. DR DNASU; 903285; -. DR EnsemblBacteria; AAF42150; AAF42150; NMB1815. DR GeneID; 903285; -. DR KEGG; nme:NMB1815; -. DR PATRIC; 20359615; VBINeiMen85645_2313. DR eggNOG; ENOG4105E7A; Bacteria. DR eggNOG; COG0121; LUCA. DR HOGENOM; HOG000256248; -. DR KO; K07008; -. DR OMA; YWVFAHN; -. DR OrthoDB; EOG62K1T4; -. DR BioCyc; NMEN122586:GHGG-1870-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR026869; Put_GATase_2. DR Pfam; PF13230; GATase_4; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 280 Glutamine amidotransferase type-2. FT {ECO:0000259|PROSITE:PS51278}. SQ SEQUENCE 280 AA; 31459 MW; 02542BE932CF4083 CRC64; MCQLLGMNCN TPTDIMFSFE GFRRRGGITD HHADGFGIGF FEGKGVRLFH DDKPSVNSPV ADLVRAYQIK SENVIAHIRK ASQGQTSLAN THPFMREMWG GYWLFAHNGH LIDFFPEQGE FFHPVGTTDS ERAFCHILNR LRTRFAARPD DDTLFDAIAG LTHEIRKFGL FNFMLSDGIA LFAHASTLLH YIVRQAPFGK ARLLDDDVMV DFAEVTTPSD RVAVIATLPL TRDESWSQLA VDELVMFREG NIVRHDRPEN PVYMSAEEGL EIARAAGVAV // ID Q9JYW6_NEIMB Unreviewed; 144 AA. AC Q9JYW6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41766.1}; GN OrderedLocusNames=NMB1402 {ECO:0000313|EMBL:AAF41766.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41766.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41766.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41766.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41766.1; -; Genomic_DNA. DR PIR; H81086; H81086. DR RefSeq; NP_274416.1; NC_003112.2. DR RefSeq; WP_002213118.1; NC_003112.2. DR STRING; 122586.NMB1402; -. DR PaxDb; Q9JYW6; -. DR EnsemblBacteria; AAF41766; AAF41766; NMB1402. DR GeneID; 903824; -. DR KEGG; nme:NMB1402; -. DR HOGENOM; HOG000219005; -. DR OrthoDB; EOG6358BS; -. DR BioCyc; NMEN122586:GHGG-1440-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 135 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 144 AA; 17054 MW; E9A6CE0756290351 CRC64; MDNKKEFINN LTNRYMWIYP LVLNILFLPF YQSYQSFFIA LGCLFALVRK MQSLDFKLQN HIVLLNIKSA WADKKVFLIR IVVSWLAVME IWMCFISESS TWVCGAFCLN SEILEKIFRG FGYSGSLYFL FILMIDLNKL RESI // ID Q9K026_NEIMB Unreviewed; 94 AA. AC Q9K026; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41213.1}; GN OrderedLocusNames=NMB0800 {ECO:0000313|EMBL:AAF41213.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41213.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41213.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41213.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41213.1; -; Genomic_DNA. DR PIR; G81157; G81157. DR RefSeq; NP_273842.1; NC_003112.2. DR RefSeq; WP_002244068.1; NC_003112.2. DR ProteinModelPortal; Q9K026; -. DR STRING; 122586.NMB0800; -. DR PaxDb; Q9K026; -. DR EnsemblBacteria; AAF41213; AAF41213; NMB0800. DR GeneID; 902915; -. DR KEGG; nme:NMB0800; -. DR PATRIC; 20356987; VBINeiMen85645_1012. DR eggNOG; ENOG4105HBR; Bacteria. DR eggNOG; COG1534; LUCA. DR HOGENOM; HOG000016279; -. DR KO; K07574; -. DR OMA; NKQLSNV; -. DR OrthoDB; EOG6SBT94; -. DR BioCyc; NMEN122586:GHGG-831-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.30.110.60; -; 1. DR InterPro; IPR001890; RNA-binding_CRM. DR InterPro; IPR017924; RNA-binding_YhbY. DR Pfam; PF01985; CRS1_YhbY; 1. DR ProDom; PD010559; RNA-binding_CRM; 1. DR SMART; SM01103; CRS1_YhbY; 1. DR SUPFAM; SSF75471; SSF75471; 1. DR TIGRFAMs; TIGR00253; RNA_bind_YhbY; 1. DR PROSITE; PS51295; CRM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 94 CRM. {ECO:0000259|PROSITE:PS51295}. SQ SEQUENCE 94 AA; 10505 MW; 8CEA0E1D1A9F26AE CRC64; MTDTKLNTKE ILELKARAHH LHPVVMVGQQ GLTDAVIKET DAALTAHELI KVRVFGDDRA ERIEICTALC EAVDAQLVQH IGKLLVLWRK NIEA // ID Q9K0W2_NEIMB Unreviewed; 410 AA. AC Q9K0W2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Putative bicyclomycin resistance protein {ECO:0000313|EMBL:AAF40882.1}; GN OrderedLocusNames=NMB0445 {ECO:0000313|EMBL:AAF40882.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40882.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40882.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40882.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40882.1; -; Genomic_DNA. DR PIR; G81196; G81196. DR RefSeq; NP_273492.1; NC_003112.2. DR RefSeq; WP_002222055.1; NC_003112.2. DR ProteinModelPortal; Q9K0W2; -. DR STRING; 122586.NMB0445; -. DR PaxDb; Q9K0W2; -. DR EnsemblBacteria; AAF40882; AAF40882; NMB0445. DR GeneID; 902561; -. DR KEGG; nme:NMB0445; -. DR PATRIC; 20356102; VBINeiMen85645_0567. DR eggNOG; ENOG4105C2C; Bacteria. DR eggNOG; ENOG410XNNX; LUCA. DR HOGENOM; HOG000143170; -. DR KO; K07552; -. DR OMA; ATDRANT; -. DR OrthoDB; EOG6RJV6T; -. DR BioCyc; NMEN122586:GHGG-469-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004812; Efflux_drug-R_Bcr/CmlA. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00710; efflux_Bcr_CflA; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 285 306 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 312 329 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 350 370 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 376 396 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 14 410 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 410 AA; 44266 MW; 4F760E986E45953F CRC64; MPSAHYPEMS EKLMAVLMAM LVTLMPFSID AYLPAIPEMA QSLNADVHRI EQSLSLFMFG TAFGQVVGGS VSDIKGRKPV ALTGLIVYCL AVAAIVFVSS AEQLLNLRVV QAFGAGMTVV IVGAMVRDYY SGRKAAQMFA LIGIILMVVP LVAPMVGALL QGLGGWQAIF VFLAAYSLVL LGLVQYFLPK PAVGGKIGRD VFGLVAGRFK RVLKTRAAMG YLFFQAFSFG SMFAFLTESS FVYQQLYRVT PHQYAWAFAL NIITMMFFNR VTAWRLKTGV HPQSILLWGI VVQFAANLSQ LAAVLFFGLP PFWLLVACVM FSVGTQGLVG ANTQACFMSY FKEEGGSANA VLGVFQSLIG AGVGMAATFL HDGSATVMAA TMTASTSCGI ALLWLCSHRA WKENGQSEYL // ID Q9JXH1_NEIMB Unreviewed; 266 AA. AC Q9JXH1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Ubiquinol--cytochrome c reductase, cytochrome c1 {ECO:0000313|EMBL:AAF42371.1}; DE EC=1.10.2.2 {ECO:0000313|EMBL:AAF42371.1}; GN Name=petC {ECO:0000313|EMBL:AAF42371.1}; GN OrderedLocusNames=NMB2051 {ECO:0000313|EMBL:AAF42371.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42371.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42371.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42371.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42371.1; -; Genomic_DNA. DR PIR; D81011; D81011. DR RefSeq; NP_275041.1; NC_003112.2. DR RefSeq; WP_010981022.1; NC_003112.2. DR ProteinModelPortal; Q9JXH1; -. DR STRING; 122586.NMB2051; -. DR PaxDb; Q9JXH1; -. DR DNASU; 904035; -. DR EnsemblBacteria; AAF42371; AAF42371; NMB2051. DR GeneID; 904035; -. DR KEGG; nme:NMB2051; -. DR PATRIC; 20360258; VBINeiMen85645_2629. DR eggNOG; ENOG4105EIX; Bacteria. DR eggNOG; COG2857; LUCA. DR HOGENOM; HOG000255217; -. DR KO; K00413; -. DR OMA; ACDQLTI; -. DR OrthoDB; EOG6C5RMW; -. DR BioCyc; NMEN122586:GHGG-2114-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR002326; Cyt_c1. DR PANTHER; PTHR10266; PTHR10266; 2. DR Pfam; PF02167; Cytochrom_C1; 1. DR PRINTS; PR00603; CYTOCHROMEC1. DR SUPFAM; SSF46626; SSF46626; 2. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42371.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327821. FT TRANSMEM 238 257 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 45 137 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 266 AA; 30276 MW; D67CAD6C85DF1F76 CRC64; MRAAKMKQTL KNWFAALLLA VPMSAAVASG GGHYEKVDID LRDQVSLQHG AQIFTNYCLS CHSASGMRFN RLKDIGLTDE EIKKNLMFTT DNVGDVMHSA MNPKDAAKWF GAAPPDLTLI ARSKGADYLY AYMRGFYKDP TRPSGWNNTV FDKVGMPHPL WEQQGVQAVE LDAKGQPVMV KDEHGEMKPK LYWESTGLHS RRLPNGKVIQ KEYDAYVRDL VNYLVYMGEP AQLQRKRIGY VVMIFLFAVM LPLAYFLNKE YWKDVH // ID Q9JXH6_NEIMB Unreviewed; 152 AA. AC Q9JXH6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=PTS system, IIAB component {ECO:0000313|EMBL:AAF42366.1}; GN OrderedLocusNames=NMB2046 {ECO:0000313|EMBL:AAF42366.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42366.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42366.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42366.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42366.1; -; Genomic_DNA. DR PIR; B81013; B81013. DR RefSeq; NP_275036.1; NC_003112.2. DR RefSeq; WP_010981021.1; NC_003112.2. DR ProteinModelPortal; Q9JXH6; -. DR STRING; 122586.NMB2046; -. DR PaxDb; Q9JXH6; -. DR EnsemblBacteria; AAF42366; AAF42366; NMB2046. DR GeneID; 904044; -. DR KEGG; nme:NMB2046; -. DR PATRIC; 20360246; VBINeiMen85645_2623. DR eggNOG; ENOG4105DAS; Bacteria. DR eggNOG; COG2893; LUCA. DR HOGENOM; HOG000095324; -. DR KO; K02821; -. DR OMA; RTHNMIG; -. DR OrthoDB; EOG6QRWFP; -. DR BioCyc; NMEN122586:GHGG-2109-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR Gene3D; 3.40.50.510; -; 1. DR InterPro; IPR004701; PTS_EIIA_man-typ. DR Pfam; PF03610; EIIA-man; 1. DR SUPFAM; SSF53062; SSF53062; 1. DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 133 PTS EIIA type-4. FT {ECO:0000259|PROSITE:PS51096}. SQ SEQUENCE 152 AA; 16531 MW; EF59F56C731760E5 CRC64; MRNRTHNMIG LLIITHETIG EAYRKLAHHF FPGGLPENVR ILGVQPTEDQ DDINNNAIAA LQEFPDNDGV LIMTDIFGAT PCNAARRLVR ENKSAILTGL NAPMMVKAVQ YSPAAEDLAA FTECVREAAV KGIFAITSAP EDLVCRRSGD AV // ID Q9JYI6_NEIMB Unreviewed; 371 AA. AC Q9JYI6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41923.1}; GN OrderedLocusNames=NMB1570 {ECO:0000313|EMBL:AAF41923.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41923.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41923.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41923.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41923.1; -; Genomic_DNA. DR PIR; E81068; E81068. DR RefSeq; NP_274576.1; NC_003112.2. DR RefSeq; WP_002212824.1; NC_003112.2. DR STRING; 122586.NMB1570; -. DR PaxDb; Q9JYI6; -. DR EnsemblBacteria; AAF41923; AAF41923; NMB1570. DR GeneID; 904153; -. DR KEGG; nme:NMB1570; -. DR PATRIC; 20359004; VBINeiMen85645_2021. DR eggNOG; ENOG4108M8S; Bacteria. DR eggNOG; COG0795; LUCA. DR HOGENOM; HOG000263579; -. DR KO; K07091; -. DR OMA; LAWWPIH; -. DR OrthoDB; EOG6TR0CJ; -. DR BioCyc; NMEN122586:GHGG-1611-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030922; LptF. DR InterPro; IPR005495; LptG/LptF_permease. DR Pfam; PF03739; YjgP_YjgQ; 1. DR TIGRFAMs; TIGR04407; LptF_YjgP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 267 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 297 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 347 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 371 AA; 41769 MW; ADC5085145FF2F6E CRC64; MIYQRNLIKE LSFTAVGIFV VLLAVLVSTQ AINLLGRAAD GRVAIDAVLA LVGFWVIGMT PLLLVLTAFI STLTVLTRYW RDSEMSVWLS CGLALKQWIR PVMQFAVPFA VLVAVMQLWV IPWAELRSRE YAEILKQKQE LSLVEAGEFN SLGKRNGRVY FVETFDTESG IMKNLFLREQ DKNGGDNIIF AKEGNFSLND NKRTLELRHG YRYSGTPGRA DYNQVSFQKL NLIISTTPKL IDPVSHRRTI PTAQLIGSSN PQHQAELMWR ISLTVSVLLL CLLAVPLSYF NPRSGHTYNI LIAIGLFLIY QNGLTLLFEA VEDGKIHFWL GLLPMHIIMF AVALILLRVR SMPSQPFWQA VGKSLTLKGG K // ID Q9K0T3_NEIMB Unreviewed; 300 AA. AC Q9K0T3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=PspA-related protein {ECO:0000313|EMBL:AAF62311.1}; GN OrderedLocusNames=NMB0490 {ECO:0000313|EMBL:AAF62311.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62311.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62311.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62311.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62311.1; -; Genomic_DNA. DR STRING; 122586.NMB0490; -. DR PaxDb; Q9K0T3; -. DR EnsemblBacteria; AAF62311; AAF62311; NMB0490. DR PATRIC; 20356234; VBINeiMen85645_0637. DR eggNOG; ENOG4107CGK; Bacteria. DR eggNOG; COG3210; LUCA. DR OrthoDB; EOG6K3ZW8; -. DR BioCyc; NMEN122586:GHGG-515-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 300 AA; 32555 MW; C05E6EBCA7872BF9 CRC64; MTVGYGFSAS GDYSQSKIRA DHASVTEQSG IYAGEDGYQI KVRDNTDLKG GIITSSQSAE DKGKNLFQTA TLTHSDIQNH SRYEGKSFGI GGSFDLNGGW DGTVTDKQGR PTDRISLAAG YGSDSDSQSS ITKSGINTRN IHITDEAGQL ARTGRTAKET EARIYTGIDT ETADQHSGRL KNSFDKDAVA KEINLQREVT KEFGRNATQA VAAVADKLGN TQSYERYQEA RTLLEAELQN TDSEAEKAAF RASLGQVNAY LAENQSRYDT WKEGGIGRSI LHGAGRQSAM RRAGMSVRRQ // ID Q9K149_NEIMB Unreviewed; 160 AA. AC Q9K149; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40781.1}; GN OrderedLocusNames=NMB0338 {ECO:0000313|EMBL:AAF40781.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40781.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40781.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40781.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40781.1; -; Genomic_DNA. DR PIR; E81211; E81211. DR RefSeq; NP_273387.2; NC_003112.2. DR STRING; 122586.NMB0338; -. DR PaxDb; Q9K149; -. DR EnsemblBacteria; AAF40781; AAF40781; NMB0338. DR GeneID; 902453; -. DR KEGG; nme:NMB0338; -. DR PATRIC; 20355821; VBINeiMen85645_0429. DR eggNOG; COG5416; LUCA. DR HOGENOM; HOG000257794; -. DR KO; K08992; -. DR OMA; FIYGANM; -. DR OrthoDB; EOG6G7R5G; -. DR BioCyc; NMEN122586:GHGG-359-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR InterPro; IPR010445; LapA_dom. DR Pfam; PF06305; DUF1049; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 121 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 79 136 DUF1049. {ECO:0000259|Pfam:PF06305}. SQ SEQUENCE 160 AA; 17664 MW; B800EB5C296AA8A7 CRC64; MERNGVFGKI VGNRILRMSS EHAAASYPKP CKSFKLAQSW FRVRSCLGGV FIYGANMKLI YTVIKIIILL LFLLLAVINT DAVTFSYLPG QKFDLPLIVV LFGAFVVGII FGMFALFGRL LSLRGENGRL RAEVKKNARL TGKELTAPPA QNAPESTKQP // ID Q7DD78_NEIMB Unreviewed; 215 AA. AC Q7DD78; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=PilO protein {ECO:0000313|EMBL:AAF42146.1}; GN Name=pilO {ECO:0000313|EMBL:AAF42146.1}; GN OrderedLocusNames=NMB1810 {ECO:0000313|EMBL:AAF42146.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42146.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42146.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42146.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42146.1; -; Genomic_DNA. DR PIR; B81041; B81041. DR RefSeq; NP_274807.1; NC_003112.2. DR RefSeq; WP_002217908.1; NC_003112.2. DR ProteinModelPortal; Q7DD78; -. DR STRING; 122586.NMB1810; -. DR PaxDb; Q7DD78; -. DR EnsemblBacteria; AAF42146; AAF42146; NMB1810. DR GeneID; 903289; -. DR KEGG; nme:NMB1810; -. DR PATRIC; 20359589; VBINeiMen85645_2300. DR eggNOG; ENOG4108XGI; Bacteria. DR eggNOG; COG3167; LUCA. DR HOGENOM; HOG000218780; -. DR KO; K02664; -. DR OMA; TARTFRY; -. DR OrthoDB; EOG6VQPV4; -. DR BioCyc; NMEN122586:GHGG-1865-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.60; -; 1. DR InterPro; IPR007445; PilO. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. DR Pfam; PF04350; PilO; 1. DR PIRSF; PIRSF016482; PilO; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 43 70 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 215 AA; 23315 MW; 7F7A604E3F49EA28 CRC64; MASKSSKTNL DLNNLHLLNL PARLFIALLA VAAVLGLGYA GLFKSQMESL EEYEAKETEL KNTYKQKSID AASLNNLRDE LASIRSAFDI MLKQLPTDAE IPNLVQELHQ AGSSNGLRLD SVMPQPPVDD GPIKRLPYSI SITGNYEQIS QFTRDVGSLS RIITLESLKI AQSPENGGNP DGKSSILNLS AIATTYQAKS VEELAAEAAQ NAEQK // ID Q9K0Q7_NEIMB Unreviewed; 140 AA. AC Q9K0Q7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Putative 6-pyruvoyl tetrahydrobiopterin synthase {ECO:0000313|EMBL:AAF40957.1}; GN OrderedLocusNames=NMB0527 {ECO:0000313|EMBL:AAF40957.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40957.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40957.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40957.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40957.1; -; Genomic_DNA. DR PIR; G81189; G81189. DR RefSeq; NP_273572.1; NC_003112.2. DR RefSeq; WP_002225595.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q7; -. DR STRING; 122586.NMB0527; -. DR PaxDb; Q9K0Q7; -. DR EnsemblBacteria; AAF40957; AAF40957; NMB0527. DR GeneID; 902642; -. DR KEGG; nme:NMB0527; -. DR PATRIC; 20356299; VBINeiMen85645_0669. DR eggNOG; ENOG4107XVI; Bacteria. DR eggNOG; COG0720; LUCA. DR HOGENOM; HOG000225068; -. DR KO; K01737; -. DR OMA; MVVWIFE; -. DR OrthoDB; EOG6FFSCJ; -. DR BioCyc; NMEN122586:GHGG-552-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR PANTHER; PTHR12589; PTHR12589; 1. DR Pfam; PF01242; PTPS; 1. DR TIGRFAMs; TIGR03367; queuosine_QueD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15709 MW; 157576F5179C9E0E CRC64; MKITKIFTFD SSHMLDGHDG KCQNLHGHTY KLEITVSDGI IKGGAKDGMV MDFTDLKAIV KQHITDPFDH AFIYHGGNSR ECQIAALLEG WNMKTLRLPC RTTAENMAVE MYGRLKNAGL NVCRVKLWET PTSCAEYEGE // ID Q9K169_NEIMB Unreviewed; 351 AA. AC Q9K169; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361}; DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361}; DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase {ECO:0000256|PIRNR:PIRNR001361}; DE AltName: Full=DAHP synthase {ECO:0000256|PIRNR:PIRNR001361}; DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361}; GN Name=aroG {ECO:0000313|EMBL:AAF40753.1}; GN OrderedLocusNames=NMB0307 {ECO:0000313|EMBL:AAF40753.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40753.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40753.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40753.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:4HSN, ECO:0000213|PDB:4HSO, ECO:0000213|PDB:4IXX} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=23754471; DOI=10.1002/pro.2293; RA Cross P.J., Pietersma A.L., Allison T.M., Wilson-Coutts S.M., RA Cochrane F.C., Parker E.J.; RT "Neisseria meningitidis expresses a single 3-deoxy-d-arabino- RT heptulosonate 7-phosphate synthase that is inhibited primarily by RT phenylalanine."; RL Protein Sci. 22:1087-1099(2013). RN [3] {ECO:0000213|PDB:4UMA, ECO:0000213|PDB:4UMB, ECO:0000213|PDB:4UMC} RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=25245459; DOI=10.1016/J.BIOORG.2014.08.003; RA Heyes L.C., Reichau S., Cross P.J., Jameson G.B., Parker E.J.; RT "Structural analysis of substrate-mimicking inhibitors in complex with RT Neisseria meningitidis 3-deoxy-d-arabino-heptulosonate 7-phosphate RT synthase - The importance of accommodating the active site water."; RL Bioorg. Chem. 57:242-250(2014). RN [4] {ECO:0000213|PDB:4UC5} RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS). RX PubMed=26794122; DOI=10.1021/JACS.5B13134; RA Lang E.J., Heyes L.C., Jameson G.B., Parker E.J.; RT "Calculated pKa Variations Expose Dynamic Allosteric Communication RT Networks."; RL J. Am. Chem. Soc. 138:2036-2045(2016). RN [5] {ECO:0000213|PDB:4UCG} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RX PubMed=26828675; DOI=10.1371/JOURNAL.PONE.0145187; RA Cross P.J., Heyes L.C., Zhang S., Nazmi A.R., Parker E.J.; RT "The Functional Unit of Neisseria meningitidis 3-Deoxy--Arabino- RT Heptulosonate 7-Phosphate Synthase Is Dimeric."; RL PLoS ONE 11:e0145187-e0145187(2016). CC -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) CC and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D- CC arabino-heptulosonate-7-phosphate (DAHP). CC {ECO:0000256|PIRNR:PIRNR001361}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + D-erythrose 4-phosphate CC + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + CC phosphate. {ECO:0000256|PIRNR:PIRNR001361}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 1/7. {ECO:0000256|PIRNR:PIRNR001361}. CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. CC {ECO:0000256|PIRNR:PIRNR001361}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40753.1; -; Genomic_DNA. DR PIR; F81214; F81214. DR RefSeq; NP_273357.1; NC_003112.2. DR RefSeq; WP_002221951.1; NC_003112.2. DR PDB; 4HSN; X-ray; 2.00 A; A/B/C/D=1-351. DR PDB; 4HSO; X-ray; 2.10 A; A/B/C/D=1-351. DR PDB; 4IXX; X-ray; 2.40 A; A/B/C/D=1-351. DR PDB; 4UC5; X-ray; 2.19 A; A/B/C/D=1-351. DR PDB; 4UCG; X-ray; 2.00 A; A/B/C/D=1-351. DR PDB; 4UMA; X-ray; 1.76 A; A/B/C/D=1-351. DR PDB; 4UMB; X-ray; 2.17 A; A/B/C/D=1-351. DR PDB; 4UMC; X-ray; 2.34 A; A/B/C/D=1-351. DR PDBsum; 4HSN; -. DR PDBsum; 4HSO; -. DR PDBsum; 4IXX; -. DR PDBsum; 4UC5; -. DR PDBsum; 4UCG; -. DR PDBsum; 4UMA; -. DR PDBsum; 4UMB; -. DR PDBsum; 4UMC; -. DR ProteinModelPortal; Q9K169; -. DR SMR; Q9K169; 9-346. DR STRING; 122586.NMB0307; -. DR PaxDb; Q9K169; -. DR EnsemblBacteria; AAF40753; AAF40753; NMB0307. DR GeneID; 902423; -. DR KEGG; nme:NMB0307; -. DR PATRIC; 20355725; VBINeiMen85645_0382. DR eggNOG; ENOG4105E99; Bacteria. DR eggNOG; COG0722; LUCA. DR HOGENOM; HOG000220501; -. DR KO; K01626; -. DR OMA; DGCIDWA; -. DR OrthoDB; EOG63JR9W; -. DR BioCyc; NMEN122586:GHGG-327-MONOMER; -. DR UniPathway; UPA00053; UER00084. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR InterPro; IPR006219; DHAP_synth_1. DR PANTHER; PTHR21225; PTHR21225; 1. DR Pfam; PF00793; DAHP_synth_1; 1. DR PIRSF; PIRSF001361; DAHP_synthase; 1. DR TIGRFAMs; TIGR00034; aroFGH; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4HSN, ECO:0000213|PDB:4HSO, KW ECO:0000213|PDB:4IXX, ECO:0000213|PDB:4UC5}; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361}; KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Manganese {ECO:0000213|PDB:4HSN, ECO:0000213|PDB:4HSO, KW ECO:0000213|PDB:4IXX, ECO:0000213|PDB:4UMA}; KW Metal-binding {ECO:0000213|PDB:4HSN, ECO:0000213|PDB:4HSO, KW ECO:0000213|PDB:4IXX, ECO:0000213|PDB:4UMA}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR001361, KW ECO:0000256|SAAS:SAAS00456513, ECO:0000313|EMBL:AAF40753.1}. FT DOMAIN 43 336 DAHP_synth_1. {ECO:0000259|Pfam:PF00793}. FT METAL 63 63 Manganese. {ECO:0000213|PDB:4HSN, FT ECO:0000213|PDB:4HSO, FT ECO:0000213|PDB:4IXX}. FT METAL 270 270 Manganese; via tele nitrogen. FT {ECO:0000213|PDB:4HSN, FT ECO:0000213|PDB:4HSO, FT ECO:0000213|PDB:4IXX}. FT METAL 304 304 Manganese. {ECO:0000213|PDB:4HSN, FT ECO:0000213|PDB:4HSO, FT ECO:0000213|PDB:4IXX}. FT METAL 324 324 Manganese. {ECO:0000213|PDB:4HSN, FT ECO:0000213|PDB:4HSO, FT ECO:0000213|PDB:4IXX}. SQ SEQUENCE 351 AA; 38656 MW; 30F29C231591EE4D CRC64; MTHHYPTDDI KIKEVKELLP PIAHLYELPI SKEASGLVHR TRQEISDLVH GRDKRLLVII GPCSIHDPKA ALEYAERLLK LRKQYENELL IVMRVYFEKP RTTVGWKGLI NDPHLDGTFD INFGLRQARS LLLSLNNMGM PASTEFLDMI TPQYYADLIS WGAIGARTTE SQVHRELASG LSCPVGFKNG TDGNLKIAID AIGAASHSHH FLSVTKAGHS AIVHTGGNPD CHVILRGGKE PNYDAEHVSE AAEQLRAAGV TDKLMIDCSH ANSRKDYTRQ MEVAQDIAAQ LEQDGGNIMG VMVESHLVEG RQDKPEVYGK SITDACIGWG ATEELLALLA GANKKRMARA S // ID Q9K014_NEIMB Unreviewed; 62 AA. AC Q9K014; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41226.1}; GN OrderedLocusNames=NMB0813 {ECO:0000313|EMBL:AAF41226.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41226.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41226.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41226.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41226.1; -; Genomic_DNA. DR PIR; D81156; D81156. DR STRING; 122586.NMB0813; -. DR PaxDb; Q9K014; -. DR EnsemblBacteria; AAF41226; AAF41226; NMB0813. DR HOGENOM; HOG000137694; -. DR OMA; RNNGAHY; -. DR OrthoDB; EOG6W9XJ8; -. DR BioCyc; NMEN122586:GHGG-844-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 62 AA; 7234 MW; FF6E60D61B527560 CRC64; MRNNGAHYIV KKCRAVRRRI QGIKVYSDCV YFMVKFGFND LTALSRRTGA VRILNRKEAP PF // ID Q9K144_NEIMB Unreviewed; 252 AA. AC Q9K144; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40789.1}; GN OrderedLocusNames=NMB0346 {ECO:0000313|EMBL:AAF40789.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40789.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40789.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40789.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40789.1; -; Genomic_DNA. DR PIR; H81209; H81209. DR RefSeq; NP_273395.1; NC_003112.2. DR RefSeq; WP_002221975.1; NC_003112.2. DR ProteinModelPortal; Q9K144; -. DR STRING; 122586.NMB0346; -. DR PaxDb; Q9K144; -. DR EnsemblBacteria; AAF40789; AAF40789; NMB0346. DR GeneID; 902461; -. DR KEGG; nme:NMB0346; -. DR PATRIC; 20355839; VBINeiMen85645_0438. DR eggNOG; COG0760; LUCA. DR HOGENOM; HOG000219114; -. DR OMA; PRRTGNT; -. DR OrthoDB; EOG654P29; -. DR BioCyc; NMEN122586:GHGG-367-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:InterPro. DR InterPro; IPR000297; PPIase_PpiC. DR Pfam; PF13145; Rotamase_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332310. FT DOMAIN 112 225 PpiC. {ECO:0000259|Pfam:PF13145}. SQ SEQUENCE 252 AA; 28684 MW; CF080C3A0A4ADCFE CRC64; MKQKKTAAAV IAAMLAGFAA AKAPEIDPAL VDTLVAQIMQ QADRHAEQSQ KPDGQAIRND AVRRLQTLEV LKNRALKEGL DKDKDVQNRF KIAEASFYAE EYVRFLERSE TVSEDELHKF YEQQIRMIKL QQVSFATEEE ARQAQQLLLK GLSFEGLMKR YPNDEQAFDG FIMAQQLPEP LASQFAAMNR GDVTRDPVKL GERYYLFKLS EVGKNPDAQP FELVRNQLEQ GLRQEKARLK IDALLEENGV KP // ID Q9JYB3_NEIMB Unreviewed; 262 AA. AC Q9JYB3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42012.1}; GN OrderedLocusNames=NMB1663 {ECO:0000313|EMBL:AAF42012.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42012.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42012.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42012.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42012.1; -; Genomic_DNA. DR PIR; A81056; A81056. DR RefSeq; NP_274668.1; NC_003112.2. DR RefSeq; WP_002222143.1; NC_003112.2. DR ProteinModelPortal; Q9JYB3; -. DR STRING; 122586.NMB1663; -. DR PaxDb; Q9JYB3; -. DR EnsemblBacteria; AAF42012; AAF42012; NMB1663. DR GeneID; 903447; -. DR KEGG; nme:NMB1663; -. DR PATRIC; 20359264; VBINeiMen85645_2140. DR eggNOG; ENOG4108R7Q; Bacteria. DR eggNOG; COG0561; LUCA. DR HOGENOM; HOG000184780; -. DR KO; K07024; -. DR OMA; INGQYNF; -. DR OrthoDB; EOG6DRPKW; -. DR BioCyc; NMEN122586:GHGG-1717-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 254 HAD-like_dom. {ECO:0000259|Pfam:PF08282}. SQ SEQUENCE 262 AA; 28261 MW; B62362722B5D222C CRC64; MNPKIVFFDI DDTLYRKYTD TLRPSVKTAV AALRGKGILT ALATGRSLAT IPEKVRDMMA EAGMDAVVTI NGQFALLHGK TVREVPMDAG LMGRVCAHLD GLGMDYAFVG GEGIAVSALS ECVCRALKHI ASDFFADKDY FSSKPVYQML VFAEENEMPL WSDIVEREGL KTVRWHEEAV DLLPAGASKT DGIRSVVEAL GWEMADVMAF GDGLNDVEML SEVGFGVAMG NGEQAAKEAA KYVCPSVDED GVLRGLQDLG VI // ID Q9K0W7_NEIMB Unreviewed; 384 AA. AC Q9K0W7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40877.1}; GN OrderedLocusNames=NMB0439 {ECO:0000313|EMBL:AAF40877.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40877.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40877.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40877.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40877.1; -; Genomic_DNA. DR PIR; H81198; H81198. DR RefSeq; NP_273487.1; NC_003112.2. DR RefSeq; WP_002222046.1; NC_003112.2. DR ProteinModelPortal; Q9K0W7; -. DR STRING; 122586.NMB0439; -. DR PaxDb; Q9K0W7; -. DR EnsemblBacteria; AAF40877; AAF40877; NMB0439. DR GeneID; 902555; -. DR KEGG; nme:NMB0439; -. DR PATRIC; 20356084; VBINeiMen85645_0557. DR eggNOG; ENOG4106JF3; Bacteria. DR eggNOG; COG3213; LUCA. DR HOGENOM; HOG000284064; -. DR KO; K07234; -. DR OMA; RWGWHAS; -. DR OrthoDB; EOG6VHZ9K; -. DR BioCyc; NMEN122586:GHGG-463-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010266; NnrS. DR Pfam; PF05940; NnrS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 238 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 279 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 305 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 345 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 357 375 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 384 AA; 41751 MW; 98BBB39D9D505D27 CRC64; MKFTKHPVWA MAFRPFYSLA ALYGALSVLL WGFGYTGTHE LSGFYWHAHE MIWGYAGLVV IAFLLTAVAT WTGQPPTRGG VLVGLTIFWL AARIAAFIPG WGASASGILG TLFFWYGAVC MALPVIRSQN QRNYVAVFAL FVLGGTHAAF HVQLHNGNLG GLLSGLQSGL VMVSGFIGLI GTRIISFFTS KRLNVPQIPS PKWVAQASLW LPMLTAMLMA HGVLAWLSAV FAFAAGVIFT VQVYRWWYKP VLKEPMLWIL FAGYLFTGLG LIAVGASYFK PAFLNLGVHL IGVGGIGVLT LGMMARTALG HTGNPIYPPP KAVPVAFWLM MAATAVRMVA VFSSGTAYTH SIRTSSVLFA LALLVYAWKY IPWLIRPRSD GRPG // ID Q7DDP7_NEIMB Unreviewed; 119 AA. AC Q7DDP7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40916.1}; GN OrderedLocusNames=NMB0479 {ECO:0000313|EMBL:AAF40916.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40916.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40916.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40916.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40916.1; -; Genomic_DNA. DR PIR; B81195; B81195. DR RefSeq; NP_273526.1; NC_003112.2. DR RefSeq; WP_002212575.1; NC_003112.2. DR ProteinModelPortal; Q7DDP7; -. DR STRING; 122586.NMB0479; -. DR PaxDb; Q7DDP7; -. DR EnsemblBacteria; AAF40916; AAF40916; NMB0479. DR GeneID; 902595; -. DR KEGG; nme:NMB0479; -. DR PATRIC; 20356210; VBINeiMen85645_0626. DR eggNOG; ENOG4108ZEK; Bacteria. DR eggNOG; COG2018; LUCA. DR HOGENOM; HOG000219083; -. DR KO; K07131; -. DR OMA; MIRIEMK; -. DR OrthoDB; EOG6S52PG; -. DR BioCyc; NMEN122586:GHGG-503-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 95 Robl_LC7. {ECO:0000259|SMART:SM00960}. SQ SEQUENCE 119 AA; 12494 MW; 3377CD7CD6BA0BE4 CRC64; MQQLLISILE DLNNTSTDII ASAVISTDGL PMATMLPSHL NSDRVGAISA TLLALGSRSV QELACGELEQ VMIKGKSGYI LLSQAGKDAV LVLVAKETGR LGLILLDAKR AARHIAEAI // ID Q9K1B7_NEIMB Unreviewed; 145 AA. AC Q9K1B7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40701.1}; GN OrderedLocusNames=NMB0247 {ECO:0000313|EMBL:AAF40701.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40701.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40701.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40701.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40701.1; -; Genomic_DNA. DR PIR; E81222; E81222. DR RefSeq; NP_273303.1; NC_003112.2. DR RefSeq; WP_002224832.1; NC_003112.2. DR STRING; 122586.NMB0247; -. DR PaxDb; Q9K1B7; -. DR EnsemblBacteria; AAF40701; AAF40701; NMB0247. DR GeneID; 902358; -. DR KEGG; nme:NMB0247; -. DR PATRIC; 20355570; VBINeiMen85645_0309. DR eggNOG; ENOG4106V9Y; Bacteria. DR eggNOG; ENOG410YQBS; LUCA. DR HOGENOM; HOG000218641; -. DR OMA; ERSENCA; -. DR OrthoDB; EOG6R2H0C; -. DR BioCyc; NMEN122586:GHGG-262-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 145 AA; 16606 MW; 105FEF88581CD138 CRC64; MVEAKIFILY GAANKGKSTT LNTLFNQICR KFSKFLVFFE RHGNGLDFVA VFDHEGQRIG FYSSGDNEYE VRGNLYKLYS HNCDFIFGTS RTRGGSCDAV GCYAELLHGD VNIINWCEKF EPTDEDNERA VKELFKSFKN IINEL // ID Q9JZI7_NEIMB Unreviewed; 423 AA. AC Q9JZI7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN OrderedLocusNames=NMB1033 {ECO:0000313|EMBL:AAF41432.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41432.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41432.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41432.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC {ECO:0000256|RuleBase:RU000417}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000256|RuleBase:RU000416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41432.1; -; Genomic_DNA. DR PIR; G81130; G81130. DR RefSeq; NP_274067.1; NC_003112.2. DR RefSeq; WP_002223735.1; NC_003112.2. DR ProteinModelPortal; Q9JZI7; -. DR STRING; 122586.NMB1033; -. DR PaxDb; Q9JZI7; -. DR EnsemblBacteria; AAF41432; AAF41432; NMB1033. DR GeneID; 903170; -. DR KEGG; nme:NMB1033; -. DR PATRIC; 20357601; VBINeiMen85645_1317. DR eggNOG; ENOG4107V6I; Bacteria. DR eggNOG; COG0270; LUCA. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; FITADNE; -. DR OrthoDB; EOG6PZXGV; -. DR BioCyc; NMEN122586:GHGG-1070-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR TIGRFAMs; TIGR00675; dcm; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41432.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41432.1}. FT DOMAIN 4 420 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 423 AA; 47737 MW; 64F0F43A6192686D CRC64; MQQIKFIDLF SGMSGIRKGF EQACRKQSVA CECVFTSEIK PAALEVLKQN YPDEVPYGDI TKIETGDIPD FDILLAGFPC QAFSFAGKRL GFEDTRGTLF FDVARILKAK KPKGFILENV EGLVTHDRKD PTQKIGRTLT VILETLETLG YYVSWKVLNA KDFGIPQNRK RIYLTGSLKS KPDLSFETTL SPKLKNILES GLPTESSPFI KKLLKKFPPS ELYGKSVKDK RGGKNNIHSW DIELKGTVTE EEKQLLNMLL KERRKKKWAS EIGIDWMDGM PLTKAQISTF YKHPNLQNIL DSLTDKGYLV LEHPKQKIGG RRIKDESLPK GYNIVSGKKS FEINKILDPN DVAPTLVAMD MEHLFVVDNG GLRTLTGKEG LRLFGYPDDY SFDIPKKDKY DLLGNTVAVP VIKAVSERLL HTL // ID Q9K1L5_NEIMB Unreviewed; 56 AA. AC Q9K1L5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40558.1}; GN OrderedLocusNames=NMB0096 {ECO:0000313|EMBL:AAF40558.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40558.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40558.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40558.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40558.1; -; Genomic_DNA. DR PIR; H81239; H81239. DR STRING; 122586.NMB0096; -. DR PaxDb; Q9K1L5; -. DR EnsemblBacteria; AAF40558; AAF40558; NMB0096. DR HOGENOM; HOG000220683; -. DR OrthoDB; EOG6358MV; -. DR BioCyc; NMEN122586:GHGG-102-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 55 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 56 AA; 6188 MW; F27A249309CBF74F CRC64; MNTETIYATV FCILAATISG LLVKFNVIKI ETSINSKFML LGISILIIGI FLSIFF // ID Q9JXD1_NEIMB Unreviewed; 118 AA. AC Q9JXD1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42421.1}; GN OrderedLocusNames=NMB2106 {ECO:0000313|EMBL:AAF42421.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42421.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42421.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42421.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42421.1; -; Genomic_DNA. DR PIR; A81007; A81007. DR RefSeq; NP_275093.1; NC_003112.2. DR RefSeq; WP_002225728.1; NC_003112.2. DR STRING; 122586.NMB2106; -. DR PaxDb; Q9JXD1; -. DR EnsemblBacteria; AAF42421; AAF42421; NMB2106. DR GeneID; 903929; -. DR KEGG; nme:NMB2106; -. DR PATRIC; 20360386; VBINeiMen85645_2689. DR HOGENOM; HOG000218701; -. DR OMA; VDWAYKN; -. DR OrthoDB; EOG63JRBD; -. DR BioCyc; NMEN122586:GHGG-2171-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR031891; DMP12. DR Pfam; PF16779; DMP12; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 118 AA; 13810 MW; 71E8D7A0E64421E2 CRC64; MNEHNLLIFC LKDNVSISEY TEMVDWAYEN IQSETVVEIT ENQIIEYQNR GLWGLVSEIT DNWLFGPSEG DWLIDKESIL AVKEKLQNSD FSTEPLVKNI IHVLEYAIKN EKTVIFHF // ID Q9JZG0_NEIMB Unreviewed; 220 AA. AC Q9JZG0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41466.1}; GN OrderedLocusNames=NMB1071 {ECO:0000313|EMBL:AAF41466.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41466.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41466.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41466.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41466.1; -; Genomic_DNA. DR PIR; H81125; H81125. DR RefSeq; NP_274104.1; NC_003112.2. DR RefSeq; WP_002233833.1; NC_003112.2. DR ProteinModelPortal; Q9JZG0; -. DR STRING; 122586.NMB1071; -. DR PaxDb; Q9JZG0; -. DR EnsemblBacteria; AAF41466; AAF41466; NMB1071. DR GeneID; 903490; -. DR KEGG; nme:NMB1071; -. DR PATRIC; 20357691; VBINeiMen85645_1362. DR eggNOG; ENOG4106RHG; Bacteria. DR eggNOG; COG3318; LUCA. DR HOGENOM; HOG000218931; -. DR KO; K07039; -. DR OMA; ANLMDDM; -. DR OrthoDB; EOG6N0HM6; -. DR BioCyc; NMEN122586:GHGG-1108-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.450.50; -; 1. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR004027; SEC_C_motif. DR InterPro; IPR011978; UPF0149. DR Pfam; PF02810; SEC-C; 1. DR Pfam; PF03695; UPF0149; 1. DR SUPFAM; SSF101327; SSF101327; 1. DR TIGRFAMs; TIGR02292; ygfB_yecA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 220 AA; 24955 MW; A453B9217CCC6D9A CRC64; MDSRKFTEAS KRRLSELLDA KSEQGNTMRC DEVQGFMTAL LSGPDKLTPL DWLPEVLGDE SQFTAAERSE IERLVLAMAM ETTAAMSDKK LPDLWLYENE DGGSDFYTWC NAYLYGLDIV PTDWFEAVDD EAFEELFYPI MALGGIYDEE ENGAIRLQFT EGELAELESE LPYALADIYR YWQAVINKPQ TVRREGEKTG RNDPCPCGSG RKYKACCGKN // ID Q9JY53_NEIMB Unreviewed; 475 AA. AC Q9JY53; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Putative secretion protein {ECO:0000313|EMBL:AAF42082.1}; GN OrderedLocusNames=NMB1738 {ECO:0000313|EMBL:AAF42082.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42082.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42082.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42082.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42082.1; -; Genomic_DNA. DR PIR; B81047; B81047. DR RefSeq; NP_274740.1; NC_003112.2. DR RefSeq; WP_002218333.1; NC_003112.2. DR ProteinModelPortal; Q9JY53; -. DR STRING; 122586.NMB1738; -. DR PaxDb; Q9JY53; -. DR EnsemblBacteria; AAF42082; AAF42082; NMB1738. DR GeneID; 903361; -. DR KEGG; nme:NMB1738; -. DR PATRIC; 20359441; VBINeiMen85645_2226. DR eggNOG; ENOG4105C42; Bacteria. DR eggNOG; ENOG410XNME; LUCA. DR HOGENOM; HOG000274493; -. DR KO; K11003; -. DR OMA; MFTKVDE; -. DR OrthoDB; EOG6PW254; -. DR BioCyc; NMEN122586:GHGG-1793-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR003997; Rtx_secretion_protD_GmN_bac. DR InterPro; IPR006144; Secretion_HlyD_CS. DR InterPro; IPR011053; Single_hybrid_motif. DR InterPro; IPR010129; T1SS_HlyD. DR PRINTS; PR01490; RTXTOXIND. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR01843; type_I_hlyD; 1. DR PROSITE; PS00543; HLYD_FAMILY; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 475 AA; 52651 MW; AC768A0E1460DAB7 CRC64; MFFSALKSFL SRYITVWRNV WAVRDQLKPP KRTAEEQAFL PAHLELTDTP VSAAPKWAAR FIMAFALLAL LWSWFGKIDI VAAASGKTVS GGRSKTIQPL ETAVVKAVHV RDGQHVKQGE TLAELEAVGT DSDVVQSEQA LQAAQLSKLR YEAVLAALES RTVPHIDMAQ ARSLGLSDAD VQSAQVLAQH QYQAWAAQDA QLQSALRGHQ AELQSAKAQE QKLVSVGAIE QQKTADYRRL RADNFISEHA FLEQQSKSVS NWNDLESTRG QMRQIQAAIA QAEQNRVLNT QNLKRDTLDA LRQANEQIDQ YRGQTDKAKQ RQQLMTIQSP ADGTVQELAT YTVGGVVQAA QKMMVIAPDD DKMDVEVLVL NKDIGFVEQG QDAVVKIESF PYTRYGYLTG KVKSVSHDAV SHEQLGLVYT AVVSLDKHTL NIDGKAVNLT AGMNVTAEIK TGKRRVLDYL LSPLQTKLDE SFRER // ID Q9JZL1_NEIMB Unreviewed; 74 AA. AC Q9JZL1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41406.1}; GN OrderedLocusNames=NMB1005 {ECO:0000313|EMBL:AAF41406.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41406.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41406.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41406.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41406.1; -; Genomic_DNA. DR PIR; C81133; C81133. DR RefSeq; NP_274040.1; NC_003112.2. DR RefSeq; WP_002225289.1; NC_003112.2. DR STRING; 122586.NMB1005; -. DR PaxDb; Q9JZL1; -. DR EnsemblBacteria; AAF41406; AAF41406; NMB1005. DR GeneID; 903141; -. DR KEGG; nme:NMB1005; -. DR PATRIC; 20357543; VBINeiMen85645_1288. DR eggNOG; ENOG4106FB7; Bacteria. DR eggNOG; ENOG410Y0MJ; LUCA. DR HOGENOM; HOG000071268; -. DR OMA; RSEWARY; -. DR OrthoDB; EOG6J1DHZ; -. DR BioCyc; NMEN122586:GHGG-1042-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR026365; BcepMu_gp16. DR TIGRFAMs; TIGR04111; BcepMu_gp16; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 74 AA; 8493 MW; 420336E561E1418B CRC64; MEKPLNFKPI SYPQTRESAA GWFKRNGVCK AHWAKYFNLE RTTVEHLLRG KLKGNFGKSH EAAVLLGMKE KSDD // ID Q9JYA7_NEIMB Unreviewed; 209 AA. AC Q9JYA7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Iron-starvation protein PigA {ECO:0000313|EMBL:AAF42018.1}; GN OrderedLocusNames=NMB1669 {ECO:0000313|EMBL:AAF42018.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42018.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42018.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42018.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42018.1; -; Genomic_DNA. DR PIR; G81056; G81056. DR RefSeq; NP_274674.1; NC_003112.2. DR RefSeq; WP_002218916.1; NC_003112.2. DR ProteinModelPortal; Q9JYA7; -. DR SMR; Q9JYA7; 8-206. DR STRING; 122586.NMB1669; -. DR PaxDb; Q9JYA7; -. DR EnsemblBacteria; AAF42018; AAF42018; NMB1669. DR GeneID; 903441; -. DR KEGG; nme:NMB1669; -. DR PATRIC; 20359278; VBINeiMen85645_2147. DR eggNOG; ENOG4105PY8; Bacteria. DR eggNOG; COG3230; LUCA. DR HOGENOM; HOG000219069; -. DR KO; K07215; -. DR OMA; NQITHEP; -. DR OrthoDB; EOG6R2GZQ; -. DR BioCyc; NMEN122586:GHGG-1723-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:InterPro. DR GO; GO:0006788; P:heme oxidation; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR InterPro; IPR016053; Haem_Oase-like. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR Pfam; PF01126; Heme_oxygenase; 1. DR SUPFAM; SSF48613; SSF48613; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 209 AA; 23433 MW; ACFDD8CA7A75C455 CRC64; MSETENQALT FAKRLKADTT AVHDSVDNLV MSVQPFVSKE NYIKFLKLQS VFHKAVDHIY KDAELNKAIP ELEYMARYDA VTQDLADLGD KPYEYGKPLP HETGNKAIGW LYCAEGSNLG AAFLFKHAQK LDYNGEHGAR HLAPHPDGRG KHWRAFVEHL NALNLTPEAE AEAIQGAREA FAFYKVVLRE TFGLAADAEA PEGMMPHRH // ID Q7DDC6_NEIMB Unreviewed; 248 AA. AC Q7DDC6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferse {ECO:0000313|EMBL:AAF41693.1}; DE EC=2.7.8.8 {ECO:0000313|EMBL:AAF41693.1}; GN Name=pssA {ECO:0000313|EMBL:AAF41693.1}; GN OrderedLocusNames=NMB1318 {ECO:0000313|EMBL:AAF41693.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41693.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41693.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41693.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I family. {ECO:0000256|RuleBase:RU003750}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41693.1; -; Genomic_DNA. DR PIR; E81096; E81096. DR RefSeq; NP_274337.1; NC_003112.2. DR RefSeq; WP_002213318.1; NC_003112.2. DR STRING; 122586.NMB1318; -. DR PaxDb; Q7DDC6; -. DR EnsemblBacteria; AAF41693; AAF41693; NMB1318. DR GeneID; 903740; -. DR KEGG; nme:NMB1318; -. DR PATRIC; 20358283; VBINeiMen85645_1653. DR eggNOG; ENOG4106PT6; Bacteria. DR eggNOG; COG1183; LUCA. DR HOGENOM; HOG000229370; -. DR KO; K17103; -. DR OMA; SGPIQYL; -. DR OrthoDB; EOG65XN45; -. DR BioCyc; NMEN122586:GHGG-1356-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase. DR InterPro; IPR000462; CDP-OH_P_trans. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR TIGRFAMs; TIGR00473; pssA; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003750, KW ECO:0000313|EMBL:AAF41693.1}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 215 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 241 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 248 AA; 27911 MW; 6239F50D1245F276 CRC64; METPTNTPQR SLRQNSIYLL PNSFTIAALF SAFYAITQSM HGRYETAAIA VFISMLLDGM DGRVARLTNS QSAFGEQLDS LADMVSFGVA PALIAYKWQL WQFGKIGYSV AFIYCACAAL RLALFNTLIG KVDKRWFIGV PSPTAAALIV GLIWVNHSVE KFPAVHWWAL GITLFAGLSM IVQIPFWSFK EINIRRQVPF VGMLLAVLLL LLVTWEPSLV LFLFFLGYSL SGYIMAARRF WKKYRKAD // ID Q9JXJ4_NEIMB Unreviewed; 82 AA. AC Q9JXJ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42338.1}; GN OrderedLocusNames=NMB2014 {ECO:0000313|EMBL:AAF42338.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42338.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42338.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42338.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42338.1; -; Genomic_DNA. DR PIR; C81016; C81016. DR STRING; 122586.NMB2014; -. DR PaxDb; Q9JXJ4; -. DR EnsemblBacteria; AAF42338; AAF42338; NMB2014. DR BioCyc; NMEN122586:GHGG-2071-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 82 AA; 9411 MW; 1DC4FD5AD2985DEB CRC64; MRSLLVRAMF GERMVGRFVL QSGKRSSENR VQTTFWFSWE GLWFKKTACV CTAHTLHTDS KFCVICRSGV PKDKDTVGQA TY // ID Q9K131_NEIMB Unreviewed; 26 AA. AC Q9K131; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40805.1}; GN OrderedLocusNames=NMB0362 {ECO:0000313|EMBL:AAF40805.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40805.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40805.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40805.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40805.1; -; Genomic_DNA. DR PIR; A81209; A81209. DR RefSeq; NP_273411.1; NC_003112.2. DR RefSeq; WP_010980783.1; NC_003112.2. DR STRING; 122586.NMB0362; -. DR PaxDb; Q9K131; -. DR EnsemblBacteria; AAF40805; AAF40805; NMB0362. DR GeneID; 902478; -. DR KEGG; nme:NMB0362; -. DR BioCyc; NMEN122586:GHGG-384-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 26 AA; 3101 MW; 3A4A3E475E836979 CRC64; MKVKAYISIF YTPTEKNTMN CLLDLY // ID Q9K188_NEIMB Unreviewed; 334 AA. AC Q9K188; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40733.1}; GN OrderedLocusNames=NMB0279 {ECO:0000313|EMBL:AAF40733.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40733.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40733.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40733.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40733.1; -; Genomic_DNA. DR PIR; D81217; D81217. DR RefSeq; NP_273335.1; NC_003112.2. DR RefSeq; WP_002224845.1; NC_003112.2. DR ProteinModelPortal; Q9K188; -. DR STRING; 122586.NMB0279; -. DR PaxDb; Q9K188; -. DR EnsemblBacteria; AAF40733; AAF40733; NMB0279. DR GeneID; 902390; -. DR KEGG; nme:NMB0279; -. DR PATRIC; 20355648; VBINeiMen85645_0348. DR eggNOG; ENOG4105EHM; Bacteria. DR eggNOG; COG3178; LUCA. DR HOGENOM; HOG000264348; -. DR KO; K07102; -. DR OMA; YGPVTYD; -. DR OrthoDB; EOG6VMTGR; -. DR BioCyc; NMEN122586:GHGG-294-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR011009; Kinase-like_dom. DR Pfam; PF01636; APH; 1. DR SUPFAM; SSF56112; SSF56112; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 22 249 APH. {ECO:0000259|Pfam:PF01636}. SQ SEQUENCE 334 AA; 39099 MW; 4AAB563963B0239B CRC64; MQRQIKLKNW LQTVYPERDF DLTFAAADAD FRRYFRATFS DGSSVVCMDA PPDKMSVAPY LKVQKLFDMV NVPQVLHADT DLGFVVLNDL GNTTFLTAML QEQGETAHKA LLLEAIGELV ELQKASREGV LPEYDRETML REINLFPEWF VAKELGRELT FKQRQLWQQT VDTLLPPLLA QPKVYVHRDF IVRNLMLTRG RPGVLDFQDA LYGPISYDLV SLLRDAFIEW EEEFVLDLVI RYWEKARAAG LPVPEAFDEF YRWFEWMGVQ RHLKVAGIFA RLYYRDGKDK YRPEIPRFLN YLRRVSRRYA ELAPLYALLV ELVGDEELET GFTF // ID Q9JZZ7_NEIMB Unreviewed; 921 AA. AC Q9JZZ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Putative type I restriction enzyme EcoR124II R protein {ECO:0000313|EMBL:AAF41246.1}; GN OrderedLocusNames=NMB0835 {ECO:0000313|EMBL:AAF41246.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41246.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41246.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41246.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41246.1; -; Genomic_DNA. DR PIR; C81153; C81153. DR RefSeq; NP_273876.1; NC_003112.2. DR RefSeq; WP_010980856.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ7; -. DR STRING; 122586.NMB0835; -. DR PaxDb; Q9JZZ7; -. DR EnsemblBacteria; AAF41246; AAF41246; NMB0835. DR GeneID; 902949; -. DR KEGG; nme:NMB0835; -. DR PATRIC; 20357057; VBINeiMen85645_1047. DR eggNOG; ENOG4105DZR; Bacteria. DR eggNOG; COG0610; LUCA. DR HOGENOM; HOG000003518; -. DR KO; K01153; -. DR OMA; NFKQKTH; -. DR OrthoDB; EOG6JTCB4; -. DR BioCyc; NMEN122586:GHGG-866-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:InterPro. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR. DR InterPro; IPR022625; TypeI_RM_Rsu_C. DR Pfam; PF12008; EcoR124_C; 1. DR Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00348; hsdR; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 183 328 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. SQ SEQUENCE 921 AA; 105754 MW; 569B8AD8E39AB6E7 CRC64; MRIRRRLKNI YLLDKKNLAR NHVQVINQFE QTGTHANRYD VTVLVNGLPL VQIELKKRGV AVREAFNQVH RYSKESFNSE NSLFKFLQIF VISNGTDTRY FANTTKRDKN SFDFTMNWAR SDNHPIKDLK DFTATFLQKS VLLGVLLHYS VFDANDTLLI MRPYQIAAAE RILWKINSSA QAKNWSKPES GGYVWHTTGS GKTLTSFKAA RLATESAFID KVFFVVDRKD LDYQTMKEYQ RFSPDSVNGS ESTAGLKRNL EKDDNKIIVT TIQKLNNLMK GEDNLPVYHQ RVVFIFDECH RSQFGEAQKN LKKKFKKFCQ FGFTGTPIFP ENALGAETTA GVFGRELHSY VITDAIRDEK VLKFKVDYND VRPQFKAVEA EQDEKKLSAA ENHKALLHPE RIREITQYIL NQFRQKTHRL NAGGKGFNAM FAVSSVDAAK CYYEAFKTQQ AGSLHPLKVA TIFSFAANEE QNAVGEIVDE TFEPEAMDSS AKEFLQAAIN DYNACFKTNF GTDSKAFQNY YRDLAKRVKN QEIDLLIVVG MFLTGFDAPT LNTLFVDKNL RYHGLMQAFS RTNRIYDATK TFGNIVCFRD LEQATIDAIT LFGDKNTKNV VLEKSYEEYM NGYTDSQTGE ARRGYLDVAK ELRERFPDPD KIETEKDKKD FAKLFGEYLR AENVLQNYDE FAALRELQSV DAADEDAMKA FQEKYYLSDE DVQEMRQVPM PSERAVQDYR SAYNDIRDWL RRQKAGEQKE QSKIDWDDVV FEVDLLKSQE INLDYILQLV FEHHKKIKGK AELVEEIRRI IRASIGHRAK EGLIVDFIND TDLDKVPDVP AILETFYTYA QEVMRHEAAG LIAAEGLNET AAKRYLISSL KRGYASENGT ELTETLPKMS PLNPQYLTKK QSVFQKIAAF VEKFAGIGTD I // ID Q9JYR8_NEIMB Unreviewed; 307 AA. AC Q9JYR8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41818.1}; GN OrderedLocusNames=NMB1459 {ECO:0000313|EMBL:AAF41818.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41818.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41818.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41818.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41818.1; -; Genomic_DNA. DR PIR; D81082; D81082. DR RefSeq; NP_274470.1; NC_003112.2. DR RefSeq; WP_002225105.1; NC_003112.2. DR STRING; 122586.NMB1459; -. DR PaxDb; Q9JYR8; -. DR EnsemblBacteria; AAF41818; AAF41818; NMB1459. DR GeneID; 903881; -. DR KEGG; nme:NMB1459; -. DR PATRIC; 20358661; VBINeiMen85645_1840. DR eggNOG; ENOG4105QYV; Bacteria. DR eggNOG; COG0697; LUCA. DR HOGENOM; HOG000000467; -. DR OMA; GHRLWGR; -. DR OrthoDB; EOG6GTZFQ; -. DR BioCyc; NMEN122586:GHGG-1499-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 143 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 155 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 270 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 304 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 8 142 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 158 265 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 307 AA; 32927 MW; BD0EFA4EB48FBD8C CRC64; MENQRPLLGF ALALLAAMTW GTLPIAVRQV LKFVDAPTLV WVRFTVAAAV LFVLLALGGR LPKRRDFSWC SFRLLLLGVA GISANFVLIA QGLHYISPTT TQVLWQISPF TMIVVGVLVF KDRMTAAQKI GLVLLLAGLL MFFNDKFGEL SGLGAYAKGV LLCAAGSMAW VCYAVAQKLL SAQFGPQQIL LLIYAASAAV FLPFAEPAHI GSLDGTLAWV CFAYCCLNTL IGYGSFGEAL KHWEASKVSA VTTLLPVFTV IFSLLGHYVM PDTFAAPDMN GLGYAGALIV VGGAVTAAVG DRLFKRR // ID Q7DDN0_NEIMB Unreviewed; 272 AA. AC Q7DDN0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Serine acetyltransferase {ECO:0000313|EMBL:AAF40988.1}; DE EC=2.3.1.30 {ECO:0000313|EMBL:AAF40988.1}; GN Name=cysE {ECO:0000313|EMBL:AAF40988.1}; GN OrderedLocusNames=NMB0560 {ECO:0000313|EMBL:AAF40988.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40988.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40988.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40988.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40988.1; -; Genomic_DNA. DR PIR; C81184; C81184. DR RefSeq; NP_273604.1; NC_003112.2. DR RefSeq; WP_002214372.1; NC_003112.2. DR ProteinModelPortal; Q7DDN0; -. DR SMR; Q7DDN0; 12-264. DR STRING; 122586.NMB0560; -. DR PaxDb; Q7DDN0; -. DR EnsemblBacteria; AAF40988; AAF40988; NMB0560. DR GeneID; 902675; -. DR KEGG; nme:NMB0560; -. DR PATRIC; 20356395; VBINeiMen85645_0717. DR eggNOG; ENOG4105D7W; Bacteria. DR eggNOG; COG1045; LUCA. DR HOGENOM; HOG000049437; -. DR KO; K00640; -. DR OMA; FHALQSY; -. DR OrthoDB; EOG6HMXK6; -. DR BioCyc; NMEN122586:GHGG-586-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR010493; Ser_AcTrfase_N. DR InterPro; IPR005881; Ser_O-AcTrfase. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF06426; SATase_N; 1. DR SMART; SM00971; SATase_N; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01172; cysE; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAF40988.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40988.1}. FT DOMAIN 13 117 SATase_N. {ECO:0000259|SMART:SM00971}. SQ SEQUENCE 272 AA; 29400 MW; 4CB74D8A916386EB CRC64; MKKDHLNTTG FDLWHTIREE TAAAVSAEPM LASFLHQTVL RHESLGSVLA YHLSSKLGSP IMDVRALFEI YQQALGSDTQ IGKCVEADLK AIYERDPACD EYSLPLLYFK GFHAIQAHRI NHRLYLDGRK TLAYFLQNRM SEVFGVDIHP AARFGYGLML DHATGFVAGE TAVLGNNISI LHGVTLGGSG KEGGDRHPKI GDGVMIGANA SILGNIRIGS NAKIGAGSVV VSDVPPSITV VGVPAKPVAR SLKTPSADMD QNIQFTEIDF MI // ID Q9K1C4_NEIMB Unreviewed; 483 AA. AC Q9K1C4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40694.1}; GN OrderedLocusNames=NMB0240 {ECO:0000313|EMBL:AAF40694.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40694.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40694.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40694.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40694.1; -; Genomic_DNA. DR PIR; F81221; F81221. DR RefSeq; NP_273296.1; NC_003112.2. DR RefSeq; WP_002218639.1; NC_003112.2. DR ProteinModelPortal; Q9K1C4; -. DR STRING; 122586.NMB0240; -. DR PaxDb; Q9K1C4; -. DR EnsemblBacteria; AAF40694; AAF40694; NMB0240. DR GeneID; 902351; -. DR KEGG; nme:NMB0240; -. DR PATRIC; 20355556; VBINeiMen85645_0302. DR eggNOG; ENOG4107ZSS; Bacteria. DR eggNOG; COG0421; LUCA. DR HOGENOM; HOG000218642; -. DR OMA; WTRVIAS; -. DR OrthoDB; EOG6716J0; -. DR BioCyc; NMEN122586:GHGG-255-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 200 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 483 AA; 53511 MW; 53C914D86FB5D097 CRC64; MLSFLSGLLS LGIEVLWVRM FSFAAQSVPQ AFSFTLACFL TGIAVGAYFG KRICRSRFVD IPFIGQCFLW AGIADFLILG AAWLLTGFSG FVHHAGIFIT LSAVVRGLIF PLVHHVGTDG NKSGRQVSNV YFANVAGSAL GPVLIGFVIL DFLSTQQIYL LICLISAAVP LFCTLFQKSL RLNAVSVAVS LMFGILMFLL PDSVFQNIAD RPDRLIENKH GIVAVYHRDG DKVVYGANVY DGAYNTDVFN SVNGIERAYL LPSLKSGIRR IFVVGLSTGS WARVLSAIPE MQSMIVAEIN PAYRSLIADE PQIAPLLQDK RVEIVLDDGR KWLRRHPDEK FDLILMNTTW YWRAYSTNLL SAEFLKQVQS HLTPDGIVMF NTTHSPHAFA TAVHSIPYAY RYGHMVVGSA TPVVFPNKEL LKQRLSRLIW PESGRHVFDS STVDAAAQKV VSRMLIQMTE PSAGAEVITD DNMIVEYKYG RGI // ID Q9JYQ2_NEIMB Unreviewed; 53 AA. AC Q9JYQ2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41836.1}; GN OrderedLocusNames=NMB1480 {ECO:0000313|EMBL:AAF41836.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41836.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41836.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41836.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41836.1; -; Genomic_DNA. DR PIR; E81079; E81079. DR STRING; 122586.NMB1480; -. DR PaxDb; Q9JYQ2; -. DR EnsemblBacteria; AAF41836; AAF41836; NMB1480. DR PATRIC; 20358726; VBINeiMen85645_1872. DR HOGENOM; HOG000027847; -. DR OMA; HHASPIE; -. DR OrthoDB; EOG6TJ84P; -. DR BioCyc; NMEN122586:GHGG-1520-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 52 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 53 AA; 6172 MW; CC1CCB424FADE754 CRC64; MSEQSEKNHN PLLEDERKNP VYRMGQAVAG FMLVVWAGVL ALVFFLVFRF WLS // ID Q9K0N6_NEIMB Unreviewed; 729 AA. AC Q9K0N6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983}; DE AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983}; GN Name=priA {ECO:0000256|HAMAP-Rule:MF_00983, GN ECO:0000313|EMBL:AAF40980.1}; GN OrderedLocusNames=NMB0551 {ECO:0000313|EMBL:AAF40980.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40980.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40980.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40980.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the restart of stalled replication forks. CC Recognizes and binds the arrested nascent DNA chain at stalled CC replication forks. It can open the DNA duplex, via its helicase CC activity, and promote assembly of the primosome and loading of the CC major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP- CC Rule:MF_00983}. CC -!- SUBUNIT: Component of the primosome. {ECO:0000256|HAMAP- CC Rule:MF_00983}. CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_00983}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40980.1; -; Genomic_DNA. DR PIR; F81185; F81185. DR RefSeq; NP_273596.1; NC_003112.2. DR RefSeq; WP_002247531.1; NC_003112.2. DR ProteinModelPortal; Q9K0N6; -. DR STRING; 122586.NMB0551; -. DR PaxDb; Q9K0N6; -. DR DNASU; 902666; -. DR EnsemblBacteria; AAF40980; AAF40980; NMB0551. DR GeneID; 902666; -. DR KEGG; nme:NMB0551; -. DR PATRIC; 20356365; VBINeiMen85645_0701. DR eggNOG; ENOG4105C25; Bacteria. DR eggNOG; COG1198; LUCA. DR HOGENOM; HOG000037413; -. DR KO; K04066; -. DR OMA; DMDTARI; -. DR OrthoDB; EOG6KT2K4; -. DR BioCyc; NMEN122586:GHGG-577-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00983; PriA; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005259; PriA. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00595; priA; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00983}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00983}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00983}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Primosome {ECO:0000256|HAMAP-Rule:MF_00983}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}. FT DOMAIN 209 376 Helicase ATP-binding. {ECO:0000256|HAMAP- FT Rule:MF_00983, FT ECO:0000259|PROSITE:PS51192}. FT DOMAIN 471 623 Helicase C-terminal. {ECO:0000256|HAMAP- FT Rule:MF_00983, FT ECO:0000259|PROSITE:PS51194}. FT NP_BIND 222 229 ATP. {ECO:0000256|HAMAP-Rule:MF_00983}. FT ZN_FING 436 448 C4-type. {ECO:0000256|HAMAP- FT Rule:MF_00983}. FT ZN_FING 463 479 C4-type. {ECO:0000256|HAMAP- FT Rule:MF_00983}. FT MOTIF 319 322 DEAH box. {ECO:0000256|HAMAP- FT Rule:MF_00983}. SQ SEQUENCE 729 AA; 81088 MW; C9A548285D46A6D3 CRC64; MIYHRIAVNV PLSDGLLTYS HSDPLPPGTR VLVPFRNKTV VGMVWETDIA PDMDMARILS VQTAFVEEKP LPESWRDLLA FTSRYYHYPT GQAVFAALPQ GLKETRAVEM PQPPLFYALN EAGRAQTPPP ARFNKKAALW DALLSGGMTM AALKQVNAQA AKLIEDWAEQ GWIETTEAAK PVLRSYHGQA SHSEFVLNAD QQQASDEIQT AFGSFQPFLL YGITGSGKTE VYFDAMAKVL AQGRQVLFLL PEINLTPQLL KRVENRFADV PTAVLHSQMA AGKRTQDYLR AMLGQAKLVI GTRLAVFTPM DDVGLIVVDE EHDGSFKQDN ELRYHARDLA VWRAKQGGCP IILGSATPSL ESWHKAQSGA YRLLQLTERA HTAAQLPQVD ILNVGRLKLD NGFSPQALQL LKQNFEAGGM SLVYLNRRGF APALFCGDCG YTFGCPNCSA KMVLHQRARQ LRCHHCDHRE PIPYKCPDCG NQDLTAVGHG TQRVEETLRT FLPKAAVVRV DRDSTAHKND WADLYRRIAD NKIDILVGTQ MLAKGHDFAR LNLVIVLNAD GSLYSADFRA PERLFAELMQ VSGRAGRADK PGKVLIQTQL PEHPVFAAVK AQDYAVFAEN ELNERQMFAM PPFGFQTAVR ADAPRVADAM EFLNAAKETL APLLPESVSQ FGAAPMLMVR LAERERAQIF LESPSRQDLH RAVSLWAQVL QQNRDGKIRW SVDVDPQEA // ID Q9K0L0_NEIMB Unreviewed; 271 AA. AC Q9K0L0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=FrpC operon protein {ECO:0000313|EMBL:AAF41012.1}; GN OrderedLocusNames=NMB0584 {ECO:0000313|EMBL:AAF41012.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41012.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41012.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41012.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41012.1; -; Genomic_DNA. DR PIR; B81182; B81182. DR RefSeq; NP_273628.1; NC_003112.2. DR RefSeq; WP_010980815.1; NC_003112.2. DR STRING; 122586.NMB0584; -. DR PaxDb; Q9K0L0; -. DR EnsemblBacteria; AAF41012; AAF41012; NMB0584. DR GeneID; 902699; -. DR KEGG; nme:NMB0584; -. DR PATRIC; 20356453; VBINeiMen85645_0746. DR HOGENOM; HOG000219111; -. DR OMA; DIGSCIN; -. DR OrthoDB; EOG6TBHDH; -. DR BioCyc; NMEN122586:GHGG-610-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010692; FrpC. DR Pfam; PF06901; FrpC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 271 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332295. SQ SEQUENCE 271 AA; 31454 MW; 8B20DE583D2DE22A CRC64; MRPYATTIYQ LFILFIGSVF TMTSCEPVNE KTDQKAVSAQ QAKEQTSFNN PEPMTGFEHT VTFDFQGTKM VIPYGYLARY TQDNATKWLS DTPGQDAYSI NLIEISVYYK KTDQGWVLEP YNQQNKAHFI QFLRDGLDSV DDIVIRKDAC SLSTTMGERL LTYGVKKMPS AYPEYEAYED KRHIPENPYF HEFYYIKKGE NPAIITHWNN RVNQAEEDNY STSVGSCING FTVQYYPFIR EKQQLTQQEL VGYHQQVEQL VQSFVNNSSK K // ID Q9K0R7_NEIMB Unreviewed; 133 AA. AC Q9K0R7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40945.1}; GN OrderedLocusNames=NMB0513 {ECO:0000313|EMBL:AAF40945.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40945.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40945.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40945.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2O5H} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND DISULFIDE BONDS. RA Kim Y., Li H., Gu M., Bargassa M., Joachimiak A.; RT "Uncharacterized Protein Conserved in Bacteria, COG3792 from Neisseria RT meningitidis."; RL Submitted (DEC-2006) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40945.1; -; Genomic_DNA. DR PIR; H81191; H81191. DR RefSeq; NP_273559.1; NC_003112.2. DR RefSeq; WP_002238290.1; NC_003112.2. DR PDB; 2O5H; X-ray; 1.90 A; A/B=1-133. DR PDBsum; 2O5H; -. DR ProteinModelPortal; Q9K0R7; -. DR SMR; Q9K0R7; 4-121. DR STRING; 122586.NMB0513; -. DR PaxDb; Q9K0R7; -. DR EnsemblBacteria; AAF40945; AAF40945; NMB0513. DR GeneID; 902629; -. DR KEGG; nme:NMB0513; -. DR PATRIC; 20356270; VBINeiMen85645_0655. DR eggNOG; COG3792; LUCA. DR HOGENOM; HOG000027882; -. DR OMA; PYPCEDE; -. DR OrthoDB; EOG6P075J; -. DR BioCyc; NMEN122586:GHGG-538-MONOMER; -. DR EvolutionaryTrace; Q9K0R7; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3510.10; -; 1. DR InterPro; IPR007670; DUF596. DR InterPro; IPR023138; NMB0513-like_domain. DR Pfam; PF04591; DUF596; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2O5H}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DISULFID 33 33 Interchain. {ECO:0000213|PDB:2O5H}. SQ SEQUENCE 133 AA; 15910 MW; 04BE7E3788AF85BE CRC64; MRKLNNHDVH KRYQDRLEED VEFTINYELP LSCLWSTIKD FSSDFEEKTE AFFILFKELL RRGHLKLQRD GQIIGHTPEE WEQIFREVWP EYEIEPNPLP GYAPFDIGMW LTVEAPAYAV WIDPEDGSEY WAG // ID Q9K1B3_NEIMB Unreviewed; 235 AA. AC Q9K1B3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40706.1}; GN OrderedLocusNames=NMB0252 {ECO:0000313|EMBL:AAF40706.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40706.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40706.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40706.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40706.1; -; Genomic_DNA. DR PIR; G81219; G81219. DR RefSeq; NP_273308.1; NC_003112.2. DR RefSeq; WP_002221911.1; NC_003112.2. DR STRING; 122586.NMB0252; -. DR PaxDb; Q9K1B3; -. DR EnsemblBacteria; AAF40706; AAF40706; NMB0252. DR GeneID; 902363; -. DR KEGG; nme:NMB0252; -. DR eggNOG; ENOG4105PVR; Bacteria. DR eggNOG; ENOG4111Y63; LUCA. DR HOGENOM; HOG000218640; -. DR OMA; RTERYID; -. DR OrthoDB; EOG6VF32F; -. DR BioCyc; NMEN122586:GHGG-267-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 235 AA; 27460 MW; FD386BF034F4DCF7 CRC64; MEGLINALKY LAEHEPIDNF EEIRTRNSPI ELPSGLSNFE QNIFLKENLS PKLQNDDSLK THYWIIREWG GIKSFKQSAE NSQLIRQFLS ELNSGKLSSG LLKISSLSKL ASFIDCERFA IYDSRAIFSL NWLLFKFTNA DLFFQPQGRN RELEIRNMNV LFHFSDIKPN YRKPDVSFHQ YCGLLQDLAK QVYGKQAKPY HIEMLLFKIA TTWICADMDQ LIKFDCLRNQ DFQTA // ID Q9K126_NEIMB Unreviewed; 152 AA. AC Q9K126; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40810.1}; GN OrderedLocusNames=NMB0368 {ECO:0000313|EMBL:AAF40810.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40810.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40810.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40810.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40810.1; -; Genomic_DNA. DR PIR; F81206; F81206. DR RefSeq; NP_273417.1; NC_003112.2. DR RefSeq; WP_002243987.1; NC_003112.2. DR STRING; 122586.NMB0368; -. DR PaxDb; Q9K126; -. DR EnsemblBacteria; AAF40810; AAF40810; NMB0368. DR GeneID; 902483; -. DR KEGG; nme:NMB0368; -. DR PATRIC; 20355893; VBINeiMen85645_0464. DR HOGENOM; HOG000219104; -. DR OMA; KEKSMVD; -. DR OrthoDB; EOG690MM7; -. DR BioCyc; NMEN122586:GHGG-390-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 152 AA; 17826 MW; 9B89230427C4DCAF CRC64; MVDAVVKTPE FLPFTSVGIF RFGADITQYK NILETFMYEP PDEFRTEYYE SPDSNLLISV KKKNKIISIF CYQELYFMGV NIIGLNFEDF KQLFHYPKSY GVDKYYLSNE SYPTYVYEFD EIGVQAWEAK GKIVTIIAGG KDNYSTEPYY DE // ID Q9JYV2_NEIMB Unreviewed; 289 AA. AC Q9JYV2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=HtrB/MsbB family protein {ECO:0000313|EMBL:AAF41779.1}; GN OrderedLocusNames=NMB1418 {ECO:0000313|EMBL:AAF41779.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41779.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41779.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41779.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41779.1; -; Genomic_DNA. DR PIR; D81085; D81085. DR RefSeq; NP_274430.1; NC_003112.2. DR RefSeq; WP_002244166.1; NC_003112.2. DR STRING; 122586.NMB1418; -. DR PaxDb; Q9JYV2; -. DR EnsemblBacteria; AAF41779; AAF41779; NMB1418. DR GeneID; 903840; -. DR KEGG; nme:NMB1418; -. DR PATRIC; 20358523; VBINeiMen85645_1773. DR eggNOG; ENOG4105D1S; Bacteria. DR eggNOG; COG1560; LUCA. DR HOGENOM; HOG000265960; -. DR KO; K02517; -. DR OMA; EMKFIFF; -. DR OrthoDB; EOG657J8B; -. DR BioCyc; NMEN122586:GHGG-1456-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR InterPro; IPR004960; LipA_acyltrans. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 289 AA; 33843 MW; 3BF100F050576512 CRC64; MKFIFFVLYV LQFLPFALLH KIADLTGLLA YLLVKPRRRI GEINLAKCFS EWSEEKRKTV LKQHFKHMAK LMLEYGLYWY APAGRLKSLV RYRNKHYLDD ALAAGEKVII LYPHFTAFEM AVYALNQDIP LISMYSHQKN KILDEQILKG RNRYHNVFLI GRTEGLRALV KQFRKSSAPF LYLPDQDFGR NDSVFVDFFG IQTATITGLS RIAALANAKV IPAIPVREAD NTVTLHFYPA WKSFPGEDAK ADAQRMNRFI EDRVREHPEQ YFWLHKRFKT RPEGSPDFY // ID Q9K0W3_NEIMB Unreviewed; 284 AA. AC Q9K0W3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40881.1}; GN OrderedLocusNames=NMB0444 {ECO:0000313|EMBL:AAF40881.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40881.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40881.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40881.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40881.1; -; Genomic_DNA. DR PIR; D81199; D81199. DR RefSeq; NP_273491.1; NC_003112.2. DR RefSeq; WP_002218821.1; NC_003112.2. DR STRING; 122586.NMB0444; -. DR PaxDb; Q9K0W3; -. DR EnsemblBacteria; AAF40881; AAF40881; NMB0444. DR GeneID; 902560; -. DR KEGG; nme:NMB0444; -. DR PATRIC; 20356100; VBINeiMen85645_0566. DR eggNOG; ENOG4107G69; Bacteria. DR eggNOG; COG0697; LUCA. DR HOGENOM; HOG000219095; -. DR OMA; TMFYQIL; -. DR OrthoDB; EOG6M0T4B; -. DR BioCyc; NMEN122586:GHGG-468-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 195 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 224 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 236 256 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 280 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 3 130 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 143 276 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 284 AA; 30248 MW; 5491E13D18932D49 CRC64; MFYQILALII WSSSFIAAKY VYGGIDPALM VGVRLLIAAL PALPACRRHV GKIPREEWKP LLIVSFVNYV LTLLLQFVGL KYTSAASASV IVGLEPLLMV FVGHFFFNDK ARAYHWICGA AAFAGVALLM AGGAEEGGEV GWFGCLLVLL AGAGFCAAMR PTQRLIARIG APAFTSVSIA AASLMCLPFS LALAQSYTVD WSVGMVLSLL YLGLGCGWYA YWLWNKGMSR VPANVSGLLI SLEPVVGVLL AVLILGEHLS PVSALGVFVV IAATLVAGRL SHQK // ID Q9JXZ6_NEIMB Unreviewed; 51 AA. AC Q9JXZ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42154.1}; GN OrderedLocusNames=NMB1819 {ECO:0000313|EMBL:AAF42154.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42154.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42154.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42154.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42154.1; -; Genomic_DNA. DR PIR; D81039; D81039. DR RefSeq; NP_274816.1; NC_003112.2. DR RefSeq; WP_009348015.1; NC_003112.2. DR STRING; 122586.NMB1819; -. DR PaxDb; Q9JXZ6; -. DR EnsemblBacteria; AAF42154; AAF42154; NMB1819. DR GeneID; 903281; -. DR KEGG; nme:NMB1819; -. DR PATRIC; 20359623; VBINeiMen85645_2317. DR HOGENOM; HOG000071366; -. DR OMA; SSIAKWR; -. DR OrthoDB; EOG6QCDKX; -. DR BioCyc; NMEN122586:GHGG-1874-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 51 AA; 5090 MW; 5B056A292117414A CRC64; MKIVLTTSMA GLGGTGTISS IAKWRAKTTP FSPTKSSAAS GATFPIGKSS T // ID Q9JYQ6_NEIMB Unreviewed; 268 AA. AC Q9JYQ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41832.1}; GN OrderedLocusNames=NMB1475 {ECO:0000313|EMBL:AAF41832.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41832.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41832.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41832.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41832.1; -; Genomic_DNA. DR PIR; A81079; A81079. DR RefSeq; NP_274484.1; NC_003112.2. DR RefSeq; WP_002225093.1; NC_003112.2. DR STRING; 122586.NMB1475; -. DR PaxDb; Q9JYQ6; -. DR EnsemblBacteria; AAF41832; AAF41832; NMB1475. DR GeneID; 903897; -. DR KEGG; nme:NMB1475; -. DR PATRIC; 20358715; VBINeiMen85645_1867. DR eggNOG; ENOG4105GGJ; Bacteria. DR eggNOG; COG5266; LUCA. DR HOGENOM; HOG000219017; -. DR OMA; CEQTQMF; -. DR OrthoDB; EOG622PN0; -. DR BioCyc; NMEN122586:GHGG-1515-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019613; DUF4198. DR Pfam; PF10670; DUF4198; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327848. SQ SEQUENCE 268 AA; 30197 MW; A6478A654C772E9B CRC64; MKKTLTLLAV SALFATSAHA HRVWVETAHT HGGEYLKADL GYGEFPELEP IAKDRLHIFS KPMQLVTEKG KENMIQRGTY NYQYRSNRPV KDGSYLVIAE YQPTFWSKNK AGWKQAGIKE MPDASYCEQT RMFGKNIVNV GHESADTAII TKPVGQNLEI VPLDNPANIH VGERFKVRVL FRGEPLPNAT VTATFDGFDT SDRSKTHKTE AQAFSDSTDD KGEVDIIPLR QGFWKANVEH KTDFPDQSVC QKQANYSTLT FQIGHSHH // ID Q9JZI8_NEIMB Unreviewed; 243 AA. AC Q9JZI8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Type II restriction enzyme NlaIV {ECO:0000313|EMBL:AAF41431.1}; DE EC=3.1.21.4 {ECO:0000313|EMBL:AAF41431.1}; GN Name=nlaIVR {ECO:0000313|EMBL:AAF41431.1}; GN OrderedLocusNames=NMB1032 {ECO:0000313|EMBL:AAF41431.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41431.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41431.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41431.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41431.1; -; Genomic_DNA. DR PIR; F81130; F81130. DR RefSeq; NP_274066.1; NC_003112.2. DR RefSeq; WP_002217109.1; NC_003112.2. DR STRING; 122586.NMB1032; -. DR PaxDb; Q9JZI8; -. DR EnsemblBacteria; AAF41431; AAF41431; NMB1032. DR GeneID; 903169; -. DR KEGG; nme:NMB1032; -. DR PATRIC; 20357599; VBINeiMen85645_1316. DR eggNOG; ENOG4105PZN; Bacteria. DR eggNOG; ENOG4111YAK; LUCA. DR HOGENOM; HOG000027816; -. DR KO; K01155; -. DR OMA; KIRLGVW; -. DR OrthoDB; EOG6T7N5S; -. DR BioCyc; NMEN122586:GHGG-1069-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR InterPro; IPR019064; Restrct_endonuc_II_NlaIV. DR Pfam; PF09564; RE_NgoBV; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41431.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 243 AA; 28811 MW; D779A44F060D373A CRC64; MVKLTAQQIF DKLLNEEKIL SVNGQIRFFL GDVDIIVKQK DVVGNIIQEW LGGWLRKREI EFDVSTNTQM PPDFFLNKKD RSRELLEVKA FNRNASPGFD IADFKMYSDE IIHKPYMLDV DYLIFGYDMD DNGNVTIKDL WLKKVWQITR SMDGWAINLQ VKKGVVHKIR PGVWYSINKK NMPMFECLED FVSAIEETVY QNPATRHNAS LWKKKFEEAY KKHYNRSISI PRWHEIAHKY KKK // ID Q9JZM1_NEIMB Unreviewed; 134 AA. AC Q9JZM1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41393.1}; GN OrderedLocusNames=NMB0990 {ECO:0000313|EMBL:AAF41393.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41393.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41393.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41393.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41393.1; -; Genomic_DNA. DR PIR; E81133; E81133. DR RefSeq; NP_274026.1; NC_003112.2. DR RefSeq; WP_002225297.1; NC_003112.2. DR STRING; 122586.NMB0990; -. DR PaxDb; Q9JZM1; -. DR EnsemblBacteria; AAF41393; AAF41393; NMB0990. DR GeneID; 903110; -. DR KEGG; nme:NMB0990; -. DR PATRIC; 20357479; VBINeiMen85645_1254. DR HOGENOM; HOG000218910; -. DR OMA; ANNRQPI; -. DR OrthoDB; EOG6QK4V0; -. DR BioCyc; NMEN122586:GHGG-1027-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 51 78 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 134 AA; 14889 MW; DE87408220FDCAF1 CRC64; MNLVKLLANN WQPIAIIALV GTGLAVSHHQ GYKSAFAKQQ AVIDKMERDK AQALLLSAQN YARELELARA EAKKYEVKAH AVGMALAKKQ AEVSRLKTER DLCKIPFPPD SRNPNTGFRL FSPQIPPNFT QIPP // ID Q9K1Q1_NEIMB Unreviewed; 317 AA. AC Q9K1Q1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:AAF40500.1}; DE EC=1.1.1.29 {ECO:0000313|EMBL:AAF40500.1}; GN Name=hprA {ECO:0000313|EMBL:AAF40500.1}; GN OrderedLocusNames=NMB0029 {ECO:0000313|EMBL:AAF40500.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40500.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40500.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40500.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40500.1; -; Genomic_DNA. DR PIR; H81245; H81245. DR RefSeq; NP_273095.1; NC_003112.2. DR RefSeq; WP_002225762.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q1; -. DR STRING; 122586.NMB0029; -. DR PaxDb; Q9K1Q1; -. DR EnsemblBacteria; AAF40500; AAF40500; NMB0029. DR GeneID; 902132; -. DR KEGG; nme:NMB0029; -. DR PATRIC; 20355007; VBINeiMen85645_0040. DR eggNOG; ENOG4105C5I; Bacteria. DR eggNOG; COG1052; LUCA. DR HOGENOM; HOG000136700; -. DR KO; K00018; -. DR OMA; DIIAHAP; -. DR OrthoDB; EOG6VXFC3; -. DR BioCyc; NMEN122586:GHGG-30-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003720, KW ECO:0000313|EMBL:AAF40500.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 26 317 2-Hacid_dh. {ECO:0000259|Pfam:PF00389}. FT DOMAIN 107 286 2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}. SQ SEQUENCE 317 AA; 33995 MW; 17A5448CAE63A0BC CRC64; MNHKKIVVLD ADTLPGRVFH FDFPHELAVY GTTGADETAE RVRDAHIVIT NKVMISADII AANPQLELIA VSATGVNNVD IGAAKAAGVA VCNVRAYGNE SVAEHAFMLM IALMRNLPAY QRDVAAGLWE KSPFFCHYGA PIRDLNGKTL AVFGRGNIGR TLAGYAQAFG MGVVFAEHKH ASAVREGYVS FEDAVRAADV LSLHCPLNAQ TENMIGENEL RQMKPGAVLI NCGRGGLVDE NALLAALKYG QIGGAGVDVL TNEPPKNGNP LLNARLPNLI VTPHTAWASR EALDRLFDIL LANIHAFVKG EAQNRVV // ID Q9JZ83_NEIMB Unreviewed; 287 AA. AC Q9JZ83; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41627.1}; GN OrderedLocusNames=NMB1246 {ECO:0000313|EMBL:AAF41627.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41627.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41627.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41627.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41627.1; -; Genomic_DNA. DR PIR; C81106; C81106. DR RefSeq; NP_274270.1; NC_003112.2. DR RefSeq; WP_010980911.1; NC_003112.2. DR ProteinModelPortal; Q9JZ83; -. DR STRING; 122586.NMB1246; -. DR PaxDb; Q9JZ83; -. DR EnsemblBacteria; AAF41627; AAF41627; NMB1246. DR GeneID; 903668; -. DR KEGG; nme:NMB1246; -. DR PATRIC; 20358089; VBINeiMen85645_1557. DR eggNOG; ENOG410627K; Bacteria. DR eggNOG; COG2607; LUCA. DR HOGENOM; HOG000255906; -. DR KO; K06923; -. DR OMA; YPFTQEH; -. DR OrthoDB; EOG6XQ3HX; -. DR BioCyc; NMEN122586:GHGG-1283-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008533; DUF815. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05673; DUF815; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 32 280 DUF815. {ECO:0000259|Pfam:PF05673}. SQ SEQUENCE 287 AA; 32360 MW; D75BA83C35BDB988 CRC64; MELNEFLDKA YAVLRRLDAV LPPEPGHTDW NALAFRWQSA GKKGFLEHLP DPHTFPLVRL AGVGRQTELL VRNTEQFIVG RPANNVLMSG ARGTGKSSLV KALLHEYADK GLRLIEVDKS DLIGLPYLLT LLKECPEKFI VFCDDLSFES GDETYKALKT ALDGGLSQRC ANVLVYATSN RRHLMPEYFD ENAGTTGMRG EIHQKEAVEE KISLSDRFGL WLSFYPFDQN DYLAAVQNWL EDFGVPYDET AQMAALQWAQ TRGSRSGRSA WQFACDWAGR LPKQRAL // ID Q9JY24_NEIMB Unreviewed; 34 AA. AC Q9JY24; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42118.1}; GN OrderedLocusNames=NMB1778 {ECO:0000313|EMBL:AAF42118.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42118.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42118.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42118.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42118.1; -; Genomic_DNA. DR PIR; F81044; F81044. DR RefSeq; NP_274778.1; NC_003112.2. DR RefSeq; WP_010980988.1; NC_003112.2. DR PaxDb; Q9JY24; -. DR EnsemblBacteria; AAF42118; AAF42118; NMB1778. DR GeneID; 903321; -. DR KEGG; nme:NMB1778; -. DR BioCyc; NMEN122586:GHGG-1833-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 4287 MW; D7D0E44F6D0F90E5 CRC64; MRNKKLRFLI FKSIYPQFLT LIKIKWVLIF KMKT // ID Q9JZV9_NEIMB Unreviewed; 286 AA. AC Q9JZV9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Sulfate ABC transporter, permease protein {ECO:0000313|EMBL:AAF41291.1}; GN Name=cysW {ECO:0000313|EMBL:AAF41291.1}; GN OrderedLocusNames=NMB0880 {ECO:0000313|EMBL:AAF41291.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41291.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41291.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41291.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41291.1; -; Genomic_DNA. DR PIR; C81147; C81147. DR RefSeq; NP_273921.1; NC_003112.2. DR RefSeq; WP_002225368.1; NC_003112.2. DR ProteinModelPortal; Q9JZV9; -. DR STRING; 122586.NMB0880; -. DR PaxDb; Q9JZV9; -. DR EnsemblBacteria; AAF41291; AAF41291; NMB0880. DR GeneID; 902999; -. DR KEGG; nme:NMB0880; -. DR PATRIC; 20357165; VBINeiMen85645_1096. DR eggNOG; ENOG4105ECW; Bacteria. DR eggNOG; COG4208; LUCA. DR HOGENOM; HOG000263697; -. DR KO; K02047; -. DR OMA; NEYQFSA; -. DR OrthoDB; EOG654P2T; -. DR BioCyc; NMEN122586:GHGG-916-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015419; F:sulfate transmembrane-transporting ATPase activity; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR011866; CysW_permease. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005667; Sulph_transpt2. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR00969; 3a0106s02; 1. DR TIGRFAMs; TIGR02140; permease_CysW; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00524216, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00524216, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00524216, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 246 266 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 64 271 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 286 AA; 31077 MW; 1C09A4F4A7519784 CRC64; MKPYSANPNL TEPRRLRVLL IAAALGFLLL MLVVPLVAVF YEALKGGWDL YLKSLNDPEA WSAIKLTLIT ALIVVPVNAV LGVAMAWLLT RFDFRGKQLL TTLLDLPFSV SPVVAGLMFV LLFGAHTALG GWLEAQGIQI IFAIPGIVLA TLFVTFPFVA REIIPLMQAQ GDSEEQAALI LGASGWQMFW RVTLPNIKWA LLYGIILTNA RAMGEFGAVS VVSGHIRGET NTVPLLVEIF YNEYNFTGAF ALSGVLALLA LATLAVQNII TKLQDKKLAA AERNAI // ID Q9JZ98_NEIMB Unreviewed; 640 AA. AC Q9JZ98; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 106. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41607.1}; GN OrderedLocusNames=NMB1226 {ECO:0000313|EMBL:AAF41607.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41607.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41607.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41607.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41607.1; -; Genomic_DNA. DR PIR; C81108; C81108. DR RefSeq; NP_274250.1; NC_003112.2. DR RefSeq; WP_002225202.1; NC_003112.2. DR ProteinModelPortal; Q9JZ98; -. DR STRING; 122586.NMB1226; -. DR PaxDb; Q9JZ98; -. DR EnsemblBacteria; AAF41607; AAF41607; NMB1226. DR GeneID; 903648; -. DR KEGG; nme:NMB1226; -. DR PATRIC; 20358043; VBINeiMen85645_1534. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR HOGENOM; HOG000271640; -. DR KO; K06158; -. DR OMA; FYLVHDK; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NMEN122586:GHGG-1263-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41607.1}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41607.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 246 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 313 527 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT COILED 591 618 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 640 AA; 71915 MW; 176E7990A93F4E1F CRC64; MIEIKNLTLQ RGLKVLLDKA NATVNPGQRV GLIGKNGTGK SSLFALIKGE ITQDGGDVSI PKNWRLASVS QETPDLDISA LDYVLQGDAE LQAFQTALRQ AEAQNDGMKQ AEYHAKLEEI DAYTAPARAA KLLNGLGFSQ EEHSRPVKSF SGGWRMRLNL AQALICRADL LLLDEPTNHL DLETVLWLEN HLASLPCTQI IISHDRDFLN AETTQTIELS QQKLTQYGGN YDFYQNERAQ RLAQQQAAYV KQQAQIKHLQ SFIDRFKAKA TKAVQAQSRM KALAKLERIA PAHLDSEFSF EFYHPDHLPN PLLKLEHADL GYEGKTVLHD ITLSLESGAR YGLLGVNGSG KSTFIKALAG TIDLLSGSIV RSEKLNIGYF AQHQLDTIRS DQNPVWHIQQ LSPEVREQEI RNFLGGFNFV GDMALQKTEP FSGGEKARLA LAMIIWQKPN LLLLDEPTNH LDLDMRHALT LALQSFQGAL IVVSHDRSLL EATTDSFLLI DKGRLKNFDG DLNDYRQWRL AQENAAVAPA ASAQSQSRKD TKRIEAQIRQ EKARRGKPIQ QKIDRAEKEM AQLSEIQTAC EAFLAQEEAY FEENKEKLQD TLSELAKVKT QLAQIEEVWL ACQEELEQIE TEIEKQFAER // ID Q9JZB1_NEIMB Unreviewed; 67 AA. AC Q9JZB1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41591.1}; GN OrderedLocusNames=NMB1209 {ECO:0000313|EMBL:AAF41591.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41591.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41591.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41591.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41591.1; -; Genomic_DNA. DR PIR; E81108; E81108. DR STRING; 122586.NMB1209; -. DR PaxDb; Q9JZB1; -. DR EnsemblBacteria; AAF41591; AAF41591; NMB1209. DR PATRIC; 20358005; VBINeiMen85645_1515. DR HOGENOM; HOG000095288; -. DR BioCyc; NMEN122586:GHGG-1246-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7010 MW; B0E3D43B53469D92 CRC64; MPSEGLSDGM PARTDAAWSG CRFEGVFNAK GNLSYDVFAA GALKKPGILG RSARLPGSIS AIYSKPY // ID Q7DDK3_NEIMB Unreviewed; 125 AA. AC Q7DDK3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Succinate dehydrogenase, cytochrome b556 subunit {ECO:0000313|EMBL:AAF41354.1}; GN Name=sdhC {ECO:0000313|EMBL:AAF41354.1}; GN OrderedLocusNames=NMB0948 {ECO:0000313|EMBL:AAF41354.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41354.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41354.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41354.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41354.1; -; Genomic_DNA. DR PIR; D81138; D81138. DR RefSeq; NP_273986.1; NC_003112.2. DR RefSeq; WP_002217390.1; NC_003112.2. DR ProteinModelPortal; Q7DDK3; -. DR STRING; 122586.NMB0948; -. DR PaxDb; Q7DDK3; -. DR EnsemblBacteria; AAF41354; AAF41354; NMB0948. DR GeneID; 903068; -. DR KEGG; nme:NMB0948; -. DR PATRIC; 20357379; VBINeiMen85645_1204. DR eggNOG; ENOG41080IC; Bacteria. DR eggNOG; COG2009; LUCA. DR HOGENOM; HOG000160252; -. DR KO; K00241; -. DR OMA; IVKFIVW; -. DR OrthoDB; EOG647V36; -. DR BioCyc; NMEN122586:GHGG-985-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS. DR InterPro; IPR014314; Succ_DH_cytb556. DR InterPro; IPR000701; Succ_DH_Fumarate_Rdtase_TM-su. DR Pfam; PF01127; Sdh_cyt; 1. DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1. DR PROSITE; PS01000; SDH_CYT_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 124 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 125 AA; 13776 MW; 09DC447F79D67400 CRC64; MSAKPRPVYL DLPNIRLPIP GIVSILHRIS GVGLFIMLPF LLYFLSGTLS QESAFETYRA IVSHPLVKLV LIGVLWAYLH HSLAGIRFLF LDAHKGLELN TARNTAKAVF ASALVLTVVL GALLW // ID Q9K1M3_NEIMB Unreviewed; 338 AA. AC Q9K1M3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40549.1}; GN OrderedLocusNames=NMB0086 {ECO:0000313|EMBL:AAF40549.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40549.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40549.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40549.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40549.1; -; Genomic_DNA. DR PIR; G81238; G81238. DR RefSeq; NP_273148.1; NC_003112.2. DR RefSeq; WP_002215314.1; NC_003112.2. DR STRING; 122586.NMB0086; -. DR PaxDb; Q9K1M3; -. DR EnsemblBacteria; AAF40549; AAF40549; NMB0086. DR GeneID; 902190; -. DR KEGG; nme:NMB0086; -. DR PATRIC; 20355177; VBINeiMen85645_0122. DR HOGENOM; HOG000218677; -. DR OMA; SFAHEDG; -. DR OrthoDB; EOG6HF5WM; -. DR BioCyc; NMEN122586:GHGG-92-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009739; DUF1311. DR Pfam; PF07007; DUF1311; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 338 AA; 36773 MW; F08EB593FE59995B CRC64; MYRKLIALPF ALLLAACGRE EPPKALECAN PAVLQGIRGN IQETLTQEAR SFAREDGRQF VDADKIIAAA YGLAFSLEHA SETQEGGRTF CIADLNITVP SETLADAKAN SPLLYGETAL SDIVRQKTGG NVEFKDGVLT AAVRFLPVKD GQTAFVDNTV GMAAQTLSAA LLPYGVKSIV MIDGKAVKKE DAVRILSGKA REEEPSKPTP EDILEHNAAG GDAGVPQAAE GAPEPEILHP DDGERADTVT VSRGEVEEAR VQNQRAESEI TKLWGGLDTD VQKELVGEQR KWAQEKISNC RQAAAQADRQ EYAEYLKLQC DTRMTRERIQ YLRGYSID // ID Q9K1J9_NEIMB Unreviewed; 231 AA. AC Q9K1J9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40578.1}; GN OrderedLocusNames=NMB0119 {ECO:0000313|EMBL:AAF40578.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40578.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40578.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40578.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40578.1; -; Genomic_DNA. DR PIR; A81237; A81237. DR RefSeq; NP_273177.1; NC_003112.2. DR RefSeq; WP_002216227.1; NC_003112.2. DR STRING; 122586.NMB0119; -. DR PaxDb; Q9K1J9; -. DR EnsemblBacteria; AAF40578; AAF40578; NMB0119. DR GeneID; 902223; -. DR KEGG; nme:NMB0119; -. DR PATRIC; 20355251; VBINeiMen85645_0159. DR eggNOG; ENOG4106PZM; Bacteria. DR eggNOG; ENOG410YDVN; LUCA. DR HOGENOM; HOG000218666; -. DR OMA; NTELECT; -. DR OrthoDB; EOG6ZH2FR; -. DR BioCyc; NMEN122586:GHGG-125-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 231 AA; 26807 MW; 07E790A5D714C040 CRC64; MMKDLNLSNS LFKGYNDKHG LMICGYEWGW SKADEAAYVA GEYKLPENKI DHTFANKSLY FGEQAKKWRY DNTIKNWFEM WGHPLDENGL GGAFEKSLVQ TNWAATQGNT IDNPDKFTQP EHIDNFLYHI EKLRPKVILF MGSRLADFLN NQNVLPRFEQ LVGKQTKPLE TVQKEFDGTR FNVKFQSFED CEVVCFPHPS ASRGLSYDYI ALFAPEMNRI LSDFKTTRGF K // ID Q9K0C1_NEIMB Unreviewed; 424 AA. AC Q9K0C1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Folylpolyglutamate synthase/dihydrofolate synthase {ECO:0000313|EMBL:AAF41110.1}; DE EC=6.3.2.17 {ECO:0000313|EMBL:AAF41110.1}; GN Name=folC {ECO:0000313|EMBL:AAF41110.1}; GN OrderedLocusNames=NMB0693 {ECO:0000313|EMBL:AAF41110.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41110.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41110.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41110.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC {ECO:0000256|PIRNR:PIRNR001563}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41110.1; -; Genomic_DNA. DR PIR; C81170; C81170. DR RefSeq; NP_273735.1; NC_003112.2. DR RefSeq; WP_002225490.1; NC_003112.2. DR ProteinModelPortal; Q9K0C1; -. DR STRING; 122586.NMB0693; -. DR PaxDb; Q9K0C1; -. DR EnsemblBacteria; AAF41110; AAF41110; NMB0693. DR GeneID; 902805; -. DR KEGG; nme:NMB0693; -. DR PATRIC; 20356715; VBINeiMen85645_0879. DR eggNOG; ENOG4105DPM; Bacteria. DR eggNOG; COG0285; LUCA. DR HOGENOM; HOG000019982; -. DR KO; K11754; -. DR OMA; FHALENI; -. DR OrthoDB; EOG6ZPSW2; -. DR BioCyc; NMEN122586:GHGG-721-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR InterPro; IPR001645; Folylpolyglutamate_synth. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR PANTHER; PTHR11136; PTHR11136; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01499; folC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:AAF41110.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 45 267 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. SQ SEQUENCE 424 AA; 46743 MW; 5E28B298D11E359D CRC64; MKTLQDWLSH LETAHSGGLI DMGLERTSEV KKRMKLEPQC PVVVVAGTNG KGSVCAYLTQ IYKQAGYKIG TLTSPHLLRY NERIAINAEP VSDDTIIASF ERIEAARGEI SLTYFEFNAL AAVDIFMREQ VDVMILEVGL GGRLDAVNAF DGDCAVVTSV DLDHQAFLGD TVEQVGFEKA GVFRSGKPAI CGQNPAPKSL LSHAEAIGAK LLMVQRDFEF HAMENIQWNY RFRPQHSDDP ARNRNALPFP ALRGTYQLSN AACALTVLEC LNDKLPVDIG AIKRGLLLVE NPGRFQVLPG RPLTVLDVGH NPHAARALRR SLINLAFAQK RTAVFSMLSD KDIDGVLETV KDQFDEWYIA PLDVPRGMTL ESLQNKLHEH SIENIQTFAA VREAYRAAAS KAGENDRIVV FGSFHTVADV MSVL // ID Q9K140_NEIMB Unreviewed; 150 AA. AC Q9K140; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40793.1}; GN OrderedLocusNames=NMB0350 {ECO:0000313|EMBL:AAF40793.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40793.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40793.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40793.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40793.1; -; Genomic_DNA. DR PIR; D81210; D81210. DR RefSeq; NP_273399.2; NC_003112.2. DR STRING; 122586.NMB0350; -. DR PaxDb; Q9K140; -. DR EnsemblBacteria; AAF40793; AAF40793; NMB0350. DR GeneID; 902465; -. DR KEGG; nme:NMB0350; -. DR PATRIC; 20355847; VBINeiMen85645_0442. DR eggNOG; ENOG41062RW; Bacteria. DR eggNOG; ENOG4112AEE; LUCA. DR HOGENOM; HOG000218645; -. DR OMA; KECSKET; -. DR OrthoDB; EOG6GTZM7; -. DR BioCyc; NMEN122586:GHGG-371-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR028964; Imm8. DR Pfam; PF15586; Imm8; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 150 AA; 17576 MW; 00F5F81BD0D78757 CRC64; MAKAIEIISP NEIYSDLIFK DPVPPHTIEY KMINLELKAI NLYDCAFEDF VPEIKDNFCV GIDLDIGTDD SDAADIFSVR ICSPKWILHN CFQNQRVKWG AGMMIMNEFN HSVIKSEIEK ILKECSKETW EKSLTYLLRF FSWEFEDYQC // ID Q9JYG3_NEIMB Unreviewed; 63 AA. AC Q9JYG3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41951.1}; GN OrderedLocusNames=NMB1598 {ECO:0000313|EMBL:AAF41951.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41951.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41951.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41951.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41951.1; -; Genomic_DNA. DR PIR; A81064; A81064. DR RefSeq; NP_274604.1; NC_003112.2. DR RefSeq; WP_002244243.1; NC_003112.2. DR STRING; 122586.NMB1598; -. DR PaxDb; Q9JYG3; -. DR EnsemblBacteria; AAF41951; AAF41951; NMB1598. DR GeneID; 904279; -. DR KEGG; nme:NMB1598; -. DR BioCyc; NMEN122586:GHGG-1646-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 63 AA; 7758 MW; 2C36B20E0D402666 CRC64; MHKKFESYFG KIIDKIIKED SYNNDDFLTD KKKALIYSVL IYENFNRGLV YRYFEKNYFV LVE // ID Q9JZP7_NEIMB Unreviewed; 27 AA. AC Q9JZP7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41359.1}; GN OrderedLocusNames=NMB0953 {ECO:0000313|EMBL:AAF41359.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41359.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41359.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41359.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41359.1; -; Genomic_DNA. DR PIR; A81139; A81139. DR RefSeq; NP_273991.1; NC_003112.2. DR RefSeq; WP_010980876.1; NC_003112.2. DR PaxDb; Q9JZP7; -. DR EnsemblBacteria; AAF41359; AAF41359; NMB0953. DR GeneID; 903073; -. DR KEGG; nme:NMB0953; -. DR BioCyc; NMEN122586:GHGG-990-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 27 AA; 3215 MW; 075633A40ECF9859 CRC64; MRHLKSACRQ ISKCKSRLKA KNVLRMQ // ID Q9K0R8_NEIMB Unreviewed; 140 AA. AC Q9K0R8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40944.1}; GN OrderedLocusNames=NMB0512 {ECO:0000313|EMBL:AAF40944.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40944.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40944.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40944.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40944.1; -; Genomic_DNA. DR PIR; G81191; G81191. DR RefSeq; NP_273558.1; NC_003112.2. DR RefSeq; WP_002222922.1; NC_003112.2. DR STRING; 122586.NMB0512; -. DR PaxDb; Q9K0R8; -. DR EnsemblBacteria; AAF40944; AAF40944; NMB0512. DR GeneID; 902628; -. DR KEGG; nme:NMB0512; -. DR HOGENOM; HOG000027881; -. DR OMA; YEFIFSE; -. DR OrthoDB; EOG69WFTJ; -. DR BioCyc; NMEN122586:GHGG-537-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 140 AA; 16742 MW; 5CFE82255718E86C CRC64; MKYMISFLKK TFELMSWVLV ILIIGTFYDY YQIRQYAELE KKSISNILLY AQKEKFRLES KDKYMRGGYT KYKFIFSEYS NTTFLNFIND LKKDNYLPLD GYGHGFLCRK GESISINIYP EINKFILVWG YPENLCADSN // ID Q9JYT6_NEIMB Unreviewed; 484 AA. AC Q9JYT6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41799.1}; GN OrderedLocusNames=NMB1438 {ECO:0000313|EMBL:AAF41799.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41799.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41799.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41799.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41799.1; -; Genomic_DNA. DR PIR; F81083; F81083. DR RefSeq; NP_274450.1; NC_003112.2. DR RefSeq; WP_002216936.1; NC_003112.2. DR ProteinModelPortal; Q9JYT6; -. DR STRING; 122586.NMB1438; -. DR PaxDb; Q9JYT6; -. DR EnsemblBacteria; AAF41799; AAF41799; NMB1438. DR GeneID; 903859; -. DR KEGG; nme:NMB1438; -. DR PATRIC; 20358589; VBINeiMen85645_1806. DR eggNOG; ENOG4107QR9; Bacteria. DR eggNOG; COG1139; LUCA. DR HOGENOM; HOG000262102; -. DR KO; K18929; -. DR OMA; HCPVYDK; -. DR OrthoDB; EOG6JTC5N; -. DR BioCyc; NMEN122586:GHGG-1476-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019516; P:lactate oxidation; IEA:InterPro. DR Gene3D; 3.40.50.10420; -; 2. DR InterPro; IPR004452; 4Fe-4S-bd. DR InterPro; IPR024569; 4Fe-4S-bd_C. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR024185; FTHF_cligase-like. DR InterPro; IPR003741; LUD_dom. DR Pfam; PF02589; DUF162; 1. DR Pfam; PF11870; DUF3390; 1. DR Pfam; PF13183; Fer4_8; 1. DR TIGRFAMs; TIGR00273; TIGR00273; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 308 330 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 358 388 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 484 AA; 53923 MW; 07D094E91B0F341F CRC64; MTTQTIKFHM KPETFKQNAA ISLQDKPLRK SLRTAMDMLM TKRKAVLTDE EELQSLRDLC EHVRQRSLSK LPALLEQLEE NLTKLGVKVH WAETPTEACQ IIHDIITAKN GKLMVKGKSM VSEEIELNHY LEAKGIKAVE SDLGEFIVQM AGEKPTHIVM PAIHKTKEQV SELFHQNLGT PLTDDVDQLT GFARKALRDI YSTADVGLSG VNFAVAETGT LCLVENEGNG RLSTTVPPVH IAITGIEKVV AKLSDIPPLY SLLPRSAIGQ NITTYFNMIT GPRRSEELDG PQEMHLVLLD NGRSQAYAED QMRRTLQCIR CGACMNHCPV YTRIGGAAYG TTYPGPIGEI ISPHLLGLDA TRDLPTACTM CGACVEVCPV RIPITEQMQR LRVEAQRSPT ETVPHPIRGQ GASHTFGEQM AWRTFNGIFS GSKTYRAFGW AATKFRNLTP RKQLGWTQNR VPMKPAKKTL HELMAEKMRQ KEQA // ID Q9JY07_NEIMB Unreviewed; 298 AA. AC Q9JY07; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=HtrB/MsbB family protein {ECO:0000313|EMBL:AAF42138.1}; GN OrderedLocusNames=NMB1801 {ECO:0000313|EMBL:AAF42138.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42138.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42138.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42138.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42138.1; -; Genomic_DNA. DR PIR; B81040; B81040. DR RefSeq; NP_274798.1; NC_003112.2. DR RefSeq; WP_002218369.1; NC_003112.2. DR STRING; 122586.NMB1801; -. DR PaxDb; Q9JY07; -. DR EnsemblBacteria; AAF42138; AAF42138; NMB1801. DR GeneID; 903297; -. DR KEGG; nme:NMB1801; -. DR PATRIC; 20359569; VBINeiMen85645_2290. DR eggNOG; ENOG4107WI0; Bacteria. DR eggNOG; COG1560; LUCA. DR HOGENOM; HOG000265961; -. DR KO; K02517; -. DR OMA; CCERLPD; -. DR OrthoDB; EOG6V4G92; -. DR BioCyc; NMEN122586:GHGG-1856-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR InterPro; IPR004960; LipA_acyltrans. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 298 AA; 33492 MW; 013437BC4DD6508F CRC64; MFRLQFRLFP PLRTAMHILL TALLKCLSLL PLSCLHTLGN RLGHLAFYLL KEDRARIVAN MRQAGLNPDP KTVKAVFAET AKGGLELAPA FFRKPEDIET MFKAVHGWEH VQQALDKHEG LLFITPHIGS YDLGGRYISQ QLPFPLTAMY KPPKIKAIDK IMQAGRVRGK GKTAPTSIQG VKQIIKALRS GEATIVLPDH VPSPQEGGEG VWVDFFGKPA YTMTLAAKLA HVKGVKTLFF CCERLPGGQG FDLHIRPVQG ELNGDKAHDA AVFNRNAEYW IRRFPTQYLF MYNRYKMP // ID Q9JZC3_NEIMB Unreviewed; 49 AA. AC Q9JZC3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41507.1}; GN OrderedLocusNames=NMB1117 {ECO:0000313|EMBL:AAF41507.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41507.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41507.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41507.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41507.1; -; Genomic_DNA. DR PIR; G81119; G81119. DR RefSeq; NP_274147.2; NC_003112.2. DR STRING; 122586.NMB1117; -. DR PaxDb; Q9JZC3; -. DR EnsemblBacteria; AAF41507; AAF41507; NMB1117. DR GeneID; 903539; -. DR KEGG; nme:NMB1117; -. DR PATRIC; 20357803; VBINeiMen85645_1417. DR eggNOG; COG3514; LUCA. DR OrthoDB; EOG651SZQ; -. DR BioCyc; NMEN122586:GHGG-1153-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025528; BrnA_antitoxin. DR Pfam; PF14384; BrnA_antitoxin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 49 AA; 5657 MW; 0568ADC04162E259 CRC64; MQKRNTGKTP KQLVTIRLSA DVVEKFRAGG KGWQTRINEV LRQYIAQLK // ID Q9JYU8_NEIMB Unreviewed; 375 AA. AC Q9JYU8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41784.1}; GN OrderedLocusNames=NMB1423 {ECO:0000313|EMBL:AAF41784.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41784.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41784.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41784.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41784.1; -; Genomic_DNA. DR PIR; A81086; A81086. DR RefSeq; NP_274435.1; NC_003112.2. DR RefSeq; WP_002225122.1; NC_003112.2. DR STRING; 122586.NMB1423; -. DR PaxDb; Q9JYU8; -. DR EnsemblBacteria; AAF41784; AAF41784; NMB1423. DR GeneID; 903845; -. DR KEGG; nme:NMB1423; -. DR PATRIC; 20358539; VBINeiMen85645_1781. DR eggNOG; ENOG4107R3N; Bacteria. DR eggNOG; COG3177; LUCA. DR HOGENOM; HOG000295052; -. DR OMA; PYCRIGN; -. DR OrthoDB; EOG6SR92R; -. DR BioCyc; NMEN122586:GHGG-1461-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR026287; AMPylator. DR InterPro; IPR025758; Fic/DOC_N. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR Pfam; PF13784; Fic_N; 1. DR PIRSF; PIRSF038925; AMP-prot_trans; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 111 261 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 375 AA; 42411 MW; 05154B2627DFC35B CRC64; MSNWKPNIPY NDLPPLPPKQ DIESKTILKR CIAARASLAR LKQAAELIPN QAMLINTLPV MEARASSEIE NIVTTTDKLF QSLQMDTERQ DPATKEALQY RTALFAGYES LTSRPLCTQT AIMVCNAIKH PYEMAIRKTG GTALKGGNSG NVVYTPPEGE ETIRGKLANW ERFIHESGDL DPLIIMAAAH YQFEAIHPFT DGNGRTGRIL NSLLLIEKGL LDLPILYLSR YIIENRADYY RLLLGVTERQ DWESWIIYIL DGVADTADWT VSKIDAIRRL FEQTRQHIRT HAQGIYTHEL VNLLFEQPYT RIANLEAAGI AKRQTASKYL KELSDIGVLQ EIVIGRDKLF IHPRLMELLR GEGNSFTSFQ SLVKA // ID Q9JYD5_NEIMB Unreviewed; 73 AA. AC Q9JYD5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41985.1}; GN OrderedLocusNames=NMB1635 {ECO:0000313|EMBL:AAF41985.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41985.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41985.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41985.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41985.1; -; Genomic_DNA. DR PIR; E81061; E81061. DR STRING; 122586.NMB1635; -. DR PaxDb; Q9JYD5; -. DR EnsemblBacteria; AAF41985; AAF41985; NMB1635. DR PATRIC; 20359174; VBINeiMen85645_2098. DR HOGENOM; HOG000152756; -. DR OrthoDB; EOG6K13WK; -. DR BioCyc; NMEN122586:GHGG-1684-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 73 AA; 8404 MW; 8F32435D6128BDBE CRC64; MSVANVIFSC SYWRIFKKSD YCVLCFYQFR HGEPHKLAEQ ENFSKLYQAF DYIDSVGSNF PVIITTDGCG LSS // ID Q9JZ10_NEIMB Unreviewed; 145 AA. AC Q9JZ10; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41718.1}; GN OrderedLocusNames=NMB1343 {ECO:0000313|EMBL:AAF41718.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41718.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41718.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41718.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2KXI} RP STRUCTURE BY NMR, AND DISULFIDE BONDS. RA Koehler C., Carlier L., Veggi D., Soriani M., Pizza M., Boelens R., RA Bonvin A.M.J.J.; RT "Solution NMR structure of the apoform of NarE (NMB1343)."; RL Submitted (MAY-2010) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41718.1; -; Genomic_DNA. DR PIR; G81094; G81094. DR RefSeq; NP_274362.1; NC_003112.2. DR RefSeq; WP_002219146.1; NC_003112.2. DR PDB; 2KXI; NMR; -; A=1-145. DR PDBsum; 2KXI; -. DR STRING; 122586.NMB1343; -. DR PaxDb; Q9JZ10; -. DR EnsemblBacteria; AAF41718; AAF41718; NMB1343. DR GeneID; 903765; -. DR KEGG; nme:NMB1343; -. DR eggNOG; ENOG41073V6; Bacteria. DR eggNOG; ENOG410Z5DW; LUCA. DR OMA; DLYDGCY; -. DR OrthoDB; EOG66MQSF; -. DR BioCyc; NMEN122586:GHGG-1381-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2KXI}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DISULFID 67 128 {ECO:0000213|PDB:2KXI}. SQ SEQUENCE 145 AA; 16339 MW; 900382FF572BAB3B CRC64; MGNFLYRGIS CQQDEQNNGQ LKPKGNKAEV AIRYDGKFKY DGKATHGPSV KNAVYAHQIE TGLYDGCYIS TTTDKEIAKK FATSSGIENG YIYVLNRDLF GQYSIFEYEV EHPENPNEKE VTIRAEDCGC IPEEVIIAKE LIEIN // ID Q9JXI4_NEIMB Unreviewed; 247 AA. AC Q9JXI4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AAF42355.1}; GN OrderedLocusNames=NMB2034 {ECO:0000313|EMBL:AAF42355.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42355.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42355.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42355.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42355.1; -; Genomic_DNA. DR PIR; G81013; G81013. DR RefSeq; NP_275025.1; NC_003112.2. DR RefSeq; WP_002225683.1; NC_003112.2. DR ProteinModelPortal; Q9JXI4; -. DR STRING; 122586.NMB2034; -. DR PaxDb; Q9JXI4; -. DR EnsemblBacteria; AAF42355; AAF42355; NMB2034. DR GeneID; 904064; -. DR KEGG; nme:NMB2034; -. DR PATRIC; 20360188; VBINeiMen85645_2593. DR eggNOG; ENOG4105E9Q; Bacteria. DR eggNOG; COG0204; LUCA. DR HOGENOM; HOG000026377; -. DR KO; K00655; -. DR OMA; FIQMILY; -. DR OrthoDB; EOG6XHC27; -. DR BioCyc; NMEN122586:GHGG-2096-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAF42355.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42355.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 70 184 PlsC. {ECO:0000259|SMART:SM00563}. SQ SEQUENCE 247 AA; 27922 MW; 6FD335E7EC7598E6 CRC64; MLIIRNLIYW LILCSTLIFL FPFMLLASPF RDGAHKMARV WVGILNWSLK HIVGLKYRII GAENIPDRPA VICAKHQSGW ETLALQDIFP PQVYVAKREL FKIPFFGWGL KLVKTIGIDR NNRREANEQL IKQGLVRKNE GYWITIFPEG TRLAPGKRGK YKLGGARMAK MFEMDIVPVA LNSGEFWPKN SFLKYPGEIT VVICPTIPHA SGSEAELMEK CEHLIETQQP LISGAGPFAA KMPSETA // ID Q9JYX2_NEIMB Unreviewed; 481 AA. AC Q9JYX2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000256|HAMAP-Rule:MF_00966, GN ECO:0000313|EMBL:AAF41756.1}; GN OrderedLocusNames=NMB1392 {ECO:0000313|EMBL:AAF41756.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41756.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41756.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41756.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00966}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41756.1; -; Genomic_DNA. DR PIR; G81089; G81089. DR RefSeq; NP_274406.1; NC_003112.2. DR RefSeq; WP_010980929.1; NC_003112.2. DR ProteinModelPortal; Q9JYX2; -. DR STRING; 122586.NMB1392; -. DR PaxDb; Q9JYX2; -. DR EnsemblBacteria; AAF41756; AAF41756; NMB1392. DR GeneID; 903814; -. DR KEGG; nme:NMB1392; -. DR PATRIC; 20358469; VBINeiMen85645_1746. DR eggNOG; ENOG4105D8W; Bacteria. DR eggNOG; COG0364; LUCA. DR HOGENOM; HOG000046191; -. DR KO; K00036; -. DR OMA; DNIYENT; -. DR OrthoDB; EOG61308Z; -. DR BioCyc; NMEN122586:GHGG-1430-MONOMER; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glucose metabolism {ECO:0000256|HAMAP-Rule:MF_00966}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00966}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966, KW ECO:0000313|EMBL:AAF41756.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 10 185 G6PD_N. {ECO:0000259|Pfam:PF00479}. FT DOMAIN 187 478 G6PD_C. {ECO:0000259|Pfam:PF02781}. FT NP_BIND 89 90 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT ACT_SITE 238 238 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 47 47 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 146 146 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 176 176 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 214 214 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 233 233 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 334 334 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. FT BINDING 339 339 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00966}. SQ SEQUENCE 481 AA; 54124 MW; 0153C52871861DBC CRC64; MSTQTNFDLV LFGATGDLAM RKLLPCLYQA HVAGLLHPEG RILGVSRSEL DTEGFLAKVE TSSKIHVKEN FSDEAWASFV ERFAYLKVDV TQPDDFAALG DLVKARKETD NVVIYLSTAP KFFAQACENL AAIGLNADNV RVVLEKPLGT DLASSQQINT DVARYFKEGQ IYRIDHYLGK ESLQNLLALR FANVMFEPLW NNKYIESVQL TIAEQLGVEE RGEFYDITGA LRDMVQNHLM QMLCMTAMEA PASLDADAVR DEKVKVIKSL KPLTVESVNE NVVRGQYTAA RGMNGYLEEI NVPQDSFTET YVAIKAEIEN ERWKGVPFYL RTGKRMAGKV AEIVLNFKDL NSHIFEGSRT APNRLVIELQ PYESVRLYTQ MKTPGAGNKV ETVPLATDLG KALEGRRAEA YERLLLDVIN GKLALFNRRD ELEAAWEYVM PILENWTNNT TPPHGYGAHS WGPEAARELL ARDGHKWHEE Q // ID Q9JZE6_NEIMB Unreviewed; 88 AA. AC Q9JZE6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41482.1}; GN OrderedLocusNames=NMB1090 {ECO:0000313|EMBL:AAF41482.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41482.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41482.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41482.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41482.1; -; Genomic_DNA. DR PIR; D81123; D81123. DR RefSeq; NP_274122.1; NC_003112.2. DR RefSeq; WP_002213717.1; NC_003112.2. DR STRING; 122586.NMB1090; -. DR PaxDb; Q9JZE6; -. DR EnsemblBacteria; AAF41482; AAF41482; NMB1090. DR GeneID; 903508; -. DR KEGG; nme:NMB1090; -. DR PATRIC; 20357743; VBINeiMen85645_1388. DR HOGENOM; HOG000218913; -. DR OMA; MMATLRD; -. DR OrthoDB; EOG6DVJVH; -. DR BioCyc; NMEN122586:GHGG-1126-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 22 49 {ECO:0000256|SAM:Coils}. FT COILED 60 87 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 88 AA; 10125 MW; 1258AB0920412F96 CRC64; MDFEFGFRTL WPIATAAFWF WVNGISGRLK EADKRIDDLK EELHAVKLSY HTKADAKADS TNIAAALERI ENKLEKVNEK LDRKADKS // ID Q9JXZ0_NEIMB Unreviewed; 708 AA. AC Q9JXZ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAF42164.1}; GN OrderedLocusNames=NMB1829 {ECO:0000313|EMBL:AAF42164.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42164.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42164.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42164.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU003357}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000256|RuleBase:RU003357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42164.1; -; Genomic_DNA. DR PIR; B81038; B81038. DR RefSeq; NP_274826.1; NC_003112.2. DR RefSeq; WP_009348031.1; NC_003112.2. DR ProteinModelPortal; Q9JXZ0; -. DR STRING; 122586.NMB1829; -. DR PaxDb; Q9JXZ0; -. DR EnsemblBacteria; AAF42164; AAF42164; NMB1829. DR GeneID; 903271; -. DR KEGG; nme:NMB1829; -. DR PATRIC; 20359647; VBINeiMen85645_2329. DR eggNOG; ENOG4105CNM; Bacteria. DR eggNOG; COG4773; LUCA. DR HOGENOM; HOG000220692; -. DR KO; K02014; -. DR OMA; NSHDVFA; -. DR OrthoDB; EOG60CWH4; -. DR BioCyc; NMEN122586:GHGG-1884-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015891; P:siderophore transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010105; TonB_sidphr_rcpt. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01783; TonB-siderophor; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Receptor {ECO:0000313|EMBL:AAF42164.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 708 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328306. FT DOMAIN 70 169 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 480 707 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 708 AA; 77068 MW; F3519B024FBBE4EE CRC64; MGQFMSVFRI NMTAATVLAA LSSSVFAAQT EGLETVHIKG QRSYNAIATE KNGDYSSFAA TVGTKIPASL REIPQSVSII TNQQVKDRNV DTFDQLARKT PGLRVLSNDD GRSSVYARGY EYSEYNIDGL PAQMQSINGT LPNLFAFDRV EVMRGPSGLF DSSGEMGGIV NLVRKRPTKA FQGHAAAGFG THKQYKAEAD VSGSLNSDGS VRGRVMAQTV GASPRPAEKN NRRETFYAAA DWDINPDTVL GAGYLYQQRR LAPYNGLPAD ANNKLPSLPQ HVFVGADWNK FKMHSHDVFA DLKHYFGNGG YGKVGMRYSD RKADSNYTFA GSKLNNTGQA DVAGLGTDIK QKAFAVDASY SRPFALGNTA NEFVIGADYN RLRSTNEQGR STLSKSVALD GFRALPYNGI LQNARAGNKG FNHSVTEENL DETGLYAKTV FRPLEGLSLI AGGRVGHHKI ESGDGKTLHK ASKTKFTSYA GAVYDIDGSN SLYASASQLY TPQTSIGTDG KLLKPREGNQ FEIGYKGSYM DDRLNTRVSF YRMKDKNAAA PLDSNNKKTR YAALGKRVME GVETEISGAM TPKWQIHAGY SYLHSQIKTA SNSRDEGIFL LMPKHSANLW TTYQVTSGLT IGGGVNAMSG ITSSAGIHAG GYATFDAMAA YRFTPKLKLQ INADNIFNRH YYARVGSEST FNIPGSERSL TANLRYSF // ID Q7DDM8_NEIMB Unreviewed; 71 AA. AC Q7DDM8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40990.1}; GN OrderedLocusNames=NMB0562 {ECO:0000313|EMBL:AAF40990.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40990.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40990.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40990.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40990.1; -; Genomic_DNA. DR PIR; E81184; E81184. DR RefSeq; NP_273606.1; NC_003112.2. DR RefSeq; WP_002219688.1; NC_003112.2. DR STRING; 122586.NMB0562; -. DR PaxDb; Q7DDM8; -. DR EnsemblBacteria; AAF40990; AAF40990; NMB0562. DR GeneID; 902677; -. DR KEGG; nme:NMB0562; -. DR PATRIC; 20356401; VBINeiMen85645_0720. DR eggNOG; ENOG4105WWM; Bacteria. DR eggNOG; COG2991; LUCA. DR HOGENOM; HOG000273689; -. DR KO; K05952; -. DR OMA; IEKECDC; -. DR OrthoDB; EOG693GV2; -. DR BioCyc; NMEN122586:GHGG-588-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007495; NqrM. DR Pfam; PF04400; DUF539; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 71 AA; 7717 MW; 09F2958C93A178F1 CRC64; MKTLLLTFGI FLTVIIGMAV GYIFSKRSIK GSCGGITALG MKKMCDCDTP CDTLQKKLDE EKQAGGIRVD R // ID Q9K0R2_NEIMB Unreviewed; 83 AA. AC Q9K0R2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40950.1}; GN OrderedLocusNames=NMB0518 {ECO:0000313|EMBL:AAF40950.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40950.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40950.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40950.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40950.1; -; Genomic_DNA. DR PIR; H81188; H81188. DR STRING; 122586.NMB0518; -. DR PaxDb; Q9K0R2; -. DR EnsemblBacteria; AAF40950; AAF40950; NMB0518. DR OrthoDB; EOG68SW8D; -. DR BioCyc; NMEN122586:GHGG-543-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 83 AA; 10094 MW; A701361433169F75 CRC64; MKIFWRIFMR QISLTDYFCK GLRFKHIAFR WFAYSLCHFQ CSKYTCSAKR KKTYRKTYFR SSCSGQSNST ICIKGGTRRK CYH // ID Q9JZ28_NEIMB Unreviewed; 316 AA. AC Q9JZ28; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881}; DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881}; GN Name=trxB {ECO:0000313|EMBL:AAF41699.1}; GN OrderedLocusNames=NMB1324 {ECO:0000313|EMBL:AAF41699.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41699.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41699.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41699.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. {ECO:0000256|RuleBase:RU003881}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003881}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881}; CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41699.1; -; Genomic_DNA. DR PIR; C81097; C81097. DR RefSeq; NP_274343.1; NC_003112.2. DR RefSeq; WP_002213296.1; NC_003112.2. DR ProteinModelPortal; Q9JZ28; -. DR SMR; Q9JZ28; 2-311. DR STRING; 122586.NMB1324; -. DR PaxDb; Q9JZ28; -. DR EnsemblBacteria; AAF41699; AAF41699; NMB1324. DR GeneID; 903746; -. DR KEGG; nme:NMB1324; -. DR PATRIC; 20358299; VBINeiMen85645_1661. DR eggNOG; ENOG4105C3M; Bacteria. DR eggNOG; COG0492; LUCA. DR HOGENOM; HOG000072912; -. DR KO; K00384; -. DR OMA; GQLEMNN; -. DR OrthoDB; EOG65XN2W; -. DR BioCyc; NMEN122586:GHGG-1362-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR InterPro; IPR005982; Thioredox_Rdtase. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR01292; TRX_reduct; 1. DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|RuleBase:RU003880}; KW Flavoprotein {ECO:0000256|RuleBase:RU003880}; KW NADP {ECO:0000256|RuleBase:RU003881}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003880, KW ECO:0000313|EMBL:AAF41699.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003880}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 300 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 316 AA; 33698 MW; 2986DA970C00F09C CRC64; MSQHRKLIIL GSGPAGYTAA VYAARANLNP VIITGIAQGG QLMTTTEVDN WPADADGVQG PELMARFLAH AERFGTEIIF DQINAVDLQK RPFTLKGDMG EYTCDALIVA TGASAKYLGL PSEEAFAGKG VSACATCDGF FYKNQDVAVV GGGNTAVEEA LYLANIAKTV TLIHRRSEFR AEKIMIDKLM KRVEEGKIIL KLESNLQEVL GDDRGVNGAL LKNNDGSEQQ IAVSGIFIAI GHKPNTDIFK GQLEMDEAGY LKTKGGTADN VGATNIEGVW AAGDVKDHTY RQAITSAASG CQAALDAERW LGSQNI // ID Q9K0E4_NEIMB Unreviewed; 391 AA. AC Q9K0E4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Oxygen-independent coprophorphyrinogen III oxidase family protein {ECO:0000313|EMBL:AAF41083.1}; GN OrderedLocusNames=NMB0665 {ECO:0000313|EMBL:AAF41083.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41083.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41083.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41083.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41083.1; -; Genomic_DNA. DR PIR; E81172; E81172. DR RefSeq; NP_273707.1; NC_003112.2. DR RefSeq; WP_002229174.1; NC_003112.2. DR ProteinModelPortal; Q9K0E4; -. DR STRING; 122586.NMB0665; -. DR PaxDb; Q9K0E4; -. DR EnsemblBacteria; AAF41083; AAF41083; NMB0665. DR GeneID; 902776; -. DR KEGG; nme:NMB0665; -. DR PATRIC; 20356629; VBINeiMen85645_0833. DR eggNOG; ENOG4105CSA; Bacteria. DR eggNOG; COG0635; LUCA. DR HOGENOM; HOG000015379; -. DR KO; K02495; -. DR OMA; PINHLSA; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; NMEN122586:GHGG-692-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR004559; Coprogen_oxidase_HemN-rel. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR010723; HemN_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 233 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 391 AA; 43360 MW; 6ED8D17299E35689 CRC64; MHTISFPNRT RLTALPPLSL YIHIPWCIKK CPYCDFNSHS LKNGLPEAAY IDALLTDLQL ELPNIWGRPV ETIFFGGGTP SLFQAESIDR LLSGVRSLLR LQPEAEITLE ANPGTFEIEK FQGFKDAGIT RLSIGVQSFN DDMLSRLGRV HNGKEALTAI DTALKLFDKV NIDLMYALPN QTVQTALDDV QTAIATGATH ISAYHLTMEP NTPFGHTPPK GLPQDEAALD IEDAVHGALE GAGFVHYETS AFAKPAMQCR HNLNYWQFGD YLGIGAGAHG KISYPDRIER TVRRRHPNDY LALMQSQPSE AVERKTVAAE DLPFEFMMNA LRLTDGVPAA MLQERTGVPS AKIMAQIETA RQKGLLETDP AVFRPTEKGR LFLNDLLQCF L // ID Q9JYL0_NEIMB Unreviewed; 46 AA. AC Q9JYL0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41889.1}; GN OrderedLocusNames=NMB1534 {ECO:0000313|EMBL:AAF41889.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41889.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41889.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41889.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41889.1; -; Genomic_DNA. DR PIR; B81072; B81072. DR RefSeq; NP_274541.1; NC_003112.2. DR RefSeq; WP_002212857.1; NC_003112.2. DR STRING; 122586.NMB1534; -. DR PaxDb; Q9JYL0; -. DR EnsemblBacteria; AAF41889; AAF41889; NMB1534. DR GeneID; 904062; -. DR KEGG; nme:NMB1534; -. DR OrthoDB; EOG6K142R; -. DR BioCyc; NMEN122586:GHGG-1575-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 46 AA; 5002 MW; 84C1A125507BE08F CRC64; MKFVAKCRSE TSVCATRRNL FQGFVNGGCT LISVKPNIIL SIGDLL // ID Q9K171_NEIMB Unreviewed; 52 AA. AC Q9K171; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40751.1}; GN OrderedLocusNames=NMB0305 {ECO:0000313|EMBL:AAF40751.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40751.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40751.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40751.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40751.1; -; Genomic_DNA. DR PIR; D81214; D81214. DR PaxDb; Q9K171; -. DR EnsemblBacteria; AAF40751; AAF40751; NMB0305. DR BioCyc; NMEN122586:GHGG-325-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 52 AA; 6308 MW; 0A796AE93FE72C0D CRC64; MLKTKRTHCL KKDLMGMRVF PTLFPFIYPH YRKKNMKKPC LHSHLQPCPP LR // ID Q9K0A9_NEIMB Unreviewed; 315 AA. AC Q9K0A9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Transporter {ECO:0000313|EMBL:AAF41122.1}; GN OrderedLocusNames=NMB0705 {ECO:0000313|EMBL:AAF41122.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41122.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41122.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41122.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3ZUX, ECO:0000213|PDB:3ZUY} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RX PubMed=21976025; DOI=10.1038/nature10450; RA Hu N.J., Iwata S., Cameron A.D., Drew D.; RT "Crystal structure of a bacterial homologue of the bile acid sodium RT symporter ASBT."; RL Nature 478:408-411(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41122.1; -; Genomic_DNA. DR PIR; B81168; B81168. DR RefSeq; NP_273747.1; NC_003112.2. DR RefSeq; WP_002244055.1; NC_003112.2. DR PDB; 3ZUX; X-ray; 2.20 A; A=1-86, A=88-315. DR PDB; 3ZUY; X-ray; 2.20 A; A=1-315. DR PDBsum; 3ZUX; -. DR PDBsum; 3ZUY; -. DR TCDB; 2.A.28.2.4; the bile acid:na(+) symporter (bass) family. DR PaxDb; Q9K0A9; -. DR EnsemblBacteria; AAF41122; AAF41122; NMB0705. DR GeneID; 902817; -. DR KEGG; nme:NMB0705; -. DR PATRIC; 20356753; VBINeiMen85645_0898. DR eggNOG; ENOG4105C09; Bacteria. DR eggNOG; COG0385; LUCA. DR HOGENOM; HOG000236200; -. DR KO; K03453; -. DR OMA; IMPGLAW; -. DR OrthoDB; EOG6SNDVN; -. DR BioCyc; NMEN122586:GHGG-733-MONOMER; -. DR EvolutionaryTrace; Q9K0A9; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002657; BilAc:Na_symport/Acr3. DR PANTHER; PTHR10361; PTHR10361; 1. DR Pfam; PF01758; SBF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3ZUX, ECO:0000213|PDB:3ZUY}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 94 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 284 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 315 AA; 32937 MW; 6AB4546AB1CDF486 CRC64; MNILSKISSF IGKTFSLWAA LFAAAAFFAP DTFKWAGPYI PWLLGIIMFG MGLTLKPSDF DILFKHPKVV IIGVIAQFAI MPATAWLLSK LLNLPAEIAV GVILVGCCPG GTASNVMTYL ARGNVALSVA VTSVSTLISP LLTPAIFLML AGEMLEIQAA GMLMSIVKMV LLPIVLGLIV HKVLGSKTEK LTDALPLVSV AAIVLIIGAV VGASKGKIME SGLLIFAVVV LHNGIGYLLG FFAAKWTGLP YDAQKTLTIE VGMQNSGLAA ALAAAHFAAA PVVAVPGALF SVWHNISGSL LATYWAAKAG KHKKP // ID Q9JY30_NEIMB Unreviewed; 2514 AA. AC Q9JY30; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Hemagglutinin/hemolysin-related protein {ECO:0000313|EMBL:AAF42109.1}; GN OrderedLocusNames=NMB1768 {ECO:0000313|EMBL:AAF42109.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42109.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42109.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42109.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42109.1; -; Genomic_DNA. DR PIR; F81045; F81045. DR RefSeq; NP_274768.1; NC_003112.2. DR RefSeq; WP_002247616.1; NC_003112.2. DR ProteinModelPortal; Q9JY30; -. DR STRING; 122586.NMB1768; -. DR PaxDb; Q9JY30; -. DR EnsemblBacteria; AAF42109; AAF42109; NMB1768. DR GeneID; 903330; -. DR KEGG; nme:NMB1768; -. DR PATRIC; 20359495; VBINeiMen85645_2253. DR eggNOG; ENOG4105CKT; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000043051; -. DR KO; K15125; -. DR OMA; YVERNIV; -. DR OrthoDB; EOG6K3ZW8; -. DR BioCyc; NMEN122586:GHGG-1823-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR024973; ESPR. DR InterPro; IPR010069; Fil_hemagglutn_20-aa_x2_rpt. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR025157; Haemagluttinin_rpt. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF13018; ESPR; 1. DR Pfam; PF13332; Fil_haemagg_2; 2. DR Pfam; PF05860; Haemagg_act; 1. DR Pfam; PF04829; PT-VENN; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. DR TIGRFAMs; TIGR01731; fil_hemag_20aa; 13. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 101 221 Haemagg_act. {ECO:0000259|SMART:SM00912}. FT COILED 2098 2132 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 2514 AA; 265617 MW; 95643A671B3BC268 CRC64; MNKTLYRVIF NRKRGAVVAV AETTKREGKS CADSDSGSAH VKSVPFGTTH APVCRSNIFS FSLLGFSLCL AVGTANIAFA DGIIADKAAP KTQQATILQT GNGIPQVNIQ TPTSAGVSVN QYAQFDVGNR GAILNNSRSN TQTQLGGWIQ GNPWLARGEA RVVVNQINSS HSSQMNGYIE VGGRRAEVVI ANPAGIAVNG GGFINASRAT LTTGQPQYQA GDLSGFKIRQ GNVVIAGHGL DARDTDFTRI LSYHSKIDAP VWGQDVRVVA GQNDVVATGN AHSPILNNAA ANTSNNTANN GTHIPLFAID TGKLGGMYAN KITLISTAEQ AGIRNQGQLF ASSGNVAIDA NGRLVNSGTM AAANAKDTDN TAEHKVNIRS QGVENSGTAV SQQGTQIHSQ SIQNTGTLLS SGEILIHNSG SLKNETSGTI EAARLAIDTD TLNNQGKLSQ TGSQKLHIDA QGKMDNRGRM GLQDTAPTAS NGSSNQTGNS YNASFHSSTT TPTTATGTGT ATVSISNITA PTFADGTIRT HGALDNSGSI IANGQTDVSA QQGLNNAGQI DIHQLNAKGS AFDNHNGTII SDAVHIQAGS LNNQNGNITT RQQLEIETDQ LDNAHGKLLS AEIADLAVSG SLNNQNGEIA TNQQLIIHDG QQSTAVIDNT NGTIQSGRDV AIQAKSLSNN GTLAADNKLD IALQDDFYVE RNIVAGNELS LSTRGSLKNS HTLQAGKRIR IKANNLDNAA QGNIQSGGTT DIGTQHNLTN RGLIDGQQTK IQAGQMNNIG TGRIYGDNIA IAATRLDNQD ENGTGAAIAA RENLNLGIGQ LNNRENSLIY SGNDMAVGGA LDTNGQATGK AQRIHNAGAT IEAAGKMRLG VEKLHNTNEH LKTQLVETGR EHIVDYEAFG RHELLREGTQ HELGWSVYND ESDHLRTPDG AAHENWHKYD YEKVTQKTQV TQTAPAKIIS GNDLTIDGKE VFNTDSQIIA GGNLIVQTEK DGLHNEQTFG EKKVFSENGK LHSYWREKHK GRDSTGHSEQ NYTLPEEITR NISLGSFAYE SHRKALSHHA PSQGTELPQS NGISLPYTSN SFTPLPSSSL YIINPVNKGY LVETDPRFAN YRQWLGSDYM LDSLKLDPNN LHKRLGDGYY EQRLINEQIA ELTGHRRLDG YQNDEEQFKA LMDNGATAAR SMNLSVGIAL SAEQVAQLTS DIVWLVQKEV KLPDGGTQTV LVPQVYVRVK NGDIDGKGAL LSGSNTQINV SGSLKNSGTI AGRNALIINT DTLDNIGGRI HAQKSAVTAT QDINNIGGML SAEQTLLLNA GNNINSQSTT ASSQNTQGSS TYLDRMAGIY ITGKEKGVLA AQAGKDINII AGQISNQSEQ GQTRLQAGRD INLDTVQTSK HQATHFDADN HVIRGSTNEV GSSIQTKGDV TLLSGNNLNA KAAEVSSANG TLAVSAKNDI NISAGINTTH VDDASKHTGR SGGGNKLVIT DKAQSHHETA QSSTFEGKQV VLQAGNDANI LGSNVISDNG TQIQAGNHVR IGTTQTQSQS ETYHQTQKSG LMSAGIGFTI GSKTNTQENQ SQSNEHTGST VGSLKGDTTI VAGKHYEQIG STVSSPEGNN TIYAQSIDIQ AAHNKLNSNT TQTYEQKGLT VAFSSPVTDL AQQAIAVAQS SKQVGQSKND RVNAMAAANA GWQAYQTGKS AQNLANGTTN AKQVSISITY GEQQNRQTTQ VQANQAQASQ IQAGGKTTLI ATGAAEQSNI NIAGSDVAGK AGTILIADND ITLQSAEQSN TERGQNKSAG WNAGAAVSFG QGGWSLGVTA GGNVGKGYGN GDSITHRHSH IGDKGSQTLI QSGGDTTIKG AQVRGKGVQV NAKNLSIQSV QDRETYQSKQ QNASAQVTVG YGFSAGGDYS QSKIRADHVS VTEQSGIYAG EDGYQIKVGN HTDLKGGIIT STQSAEDKGK NRFQTATLTH SDIKNHSQYK GESFGLGASA SISGKTLGQG AQNKPQNKHL TSVADKNSAS SSVGYGSDSD SQSSITKSGI NTRNIQITDE AAQIRLTGKT AAQTKADIDT NVTTDTAERH SGSLKNTFNK EAVQSELDLQ RTVSQDFSKN VQQANTEINQ HLDKLKADKE AAETAAAEAL ANGDMETAKR KAHEAQDAAA KADNWQQGKV ILNMLASGLA APTQSGAGIA AATASPAVSY AIGQHFKDLA GQNANGKLTA SQETAHVLAH AVLGAAVAAV GDNNALAGAL SAGGSEAAAP YISKWLYGKE KGSDLTAEEK ETVTAITNVL GTATGAAVGN SATDAAQGSL NAQSAVENND TVEQVKFALR HPRIAIAIGS VHKDPGSTLE PNISTIASTF QLNLFPNSEF GGEGGVGNAF RHVLWQATIT REFGKDIAVK VGNSHESGEK INYSIRRNLS LDKADEMIDQ LNNEIGREIA LNTNRLNTKE LVGLILETYK NNGFYQAERN SNGNYDVVRK RLSEKDYQNT SNILIHLDNT GAGFKIQQRR KQIRAQISAR QWRR // ID Q9JZ96_NEIMB Unreviewed; 144 AA. AC Q9JZ96; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41610.1}; GN OrderedLocusNames=NMB1229 {ECO:0000313|EMBL:AAF41610.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41610.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41610.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41610.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41610.1; -; Genomic_DNA. DR PIR; F81106; F81106. DR RefSeq; NP_274253.1; NC_003112.2. DR RefSeq; WP_002217157.1; NC_003112.2. DR STRING; 122586.NMB1229; -. DR PaxDb; Q9JZ96; -. DR EnsemblBacteria; AAF41610; AAF41610; NMB1229. DR GeneID; 903651; -. DR KEGG; nme:NMB1229; -. DR PATRIC; 20358049; VBINeiMen85645_1537. DR HOGENOM; HOG000218961; -. DR OrthoDB; EOG67X1VD; -. DR BioCyc; NMEN122586:GHGG-1266-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 144 AA; 16329 MW; DDA9CB514769DCA9 CRC64; MTEPKHEMLT KEQVAARKKA KAKIRTIRIW AWVILALLAL TALLSQCAMS KPQAKQKIVE SCVKNIPFAE KWQNDLRARG LDSNNTRLAV DYCKCMWEQP LDRLSEKQIR SFGKLGAQEQ LDLLGGANAF EARDKQCVAD LKSE // ID Q9JZP5_NEIMB Unreviewed; 477 AA. AC Q9JZP5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN Name=lpdA1 {ECO:0000313|EMBL:AAF41363.1}; GN OrderedLocusNames=NMB0957 {ECO:0000313|EMBL:AAF41363.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41363.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41363.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41363.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC {ECO:0000256|RuleBase:RU003692}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003692}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692}; CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000256|RuleBase:RU003692}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41363.1; -; Genomic_DNA. DR PIR; D81137; D81137. DR RefSeq; NP_273995.1; NC_003112.2. DR RefSeq; WP_002225317.1; NC_003112.2. DR ProteinModelPortal; Q9JZP5; -. DR SMR; Q9JZP5; 2-476. DR STRING; 122586.NMB0957; -. DR PaxDb; Q9JZP5; -. DR PRIDE; Q9JZP5; -. DR EnsemblBacteria; AAF41363; AAF41363; NMB0957. DR GeneID; 903077; -. DR KEGG; nme:NMB0957; -. DR PATRIC; 20357395; VBINeiMen85645_1212. DR eggNOG; ENOG4107QN2; Bacteria. DR eggNOG; COG1249; LUCA. DR HOGENOM; HOG000276708; -. DR KO; K00382; -. DR OMA; VYTQPEI; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; NMEN122586:GHGG-994-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01350; lipoamide_DH; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|RuleBase:RU003692}; KW Flavoprotein {ECO:0000256|RuleBase:RU003692}; KW Glycolysis {ECO:0000256|SAAS:SAAS00436429}; KW NAD {ECO:0000256|RuleBase:RU003692}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003692, KW ECO:0000313|EMBL:AAF41363.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 339 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. FT DOMAIN 358 466 Pyr_redox_dim. FT {ECO:0000259|Pfam:PF02852}. SQ SEQUENCE 477 AA; 50093 MW; 038C269471F12272 CRC64; MSQYDVVVIG AGPGGYVAAI RAAQLGFKTA CVDAGVNKAG NAPALGGTCL NVGCIPSKAL LQSSEHFHAA QHEFAEHGIT VGDVKFDAAK MIERKDAIVT KLTGGVKFLF QKNKVTSLFG TASFAGKNGD AYQIEVDNKG EKTVIEAKHV IVATGSVPRP LPQVAIDNVN VLDNEGALNL TEVPAKLGVI GSGVIGLEMG SVWNRVGAEV TILEAAPTFL AAADQQIAKE AFKYFTKEQG LSIELGVKIG DIKSEGKGVS VAYETAAGEA KTEVFDKLIV AIGRIPNTKG LNAEAVGLEK DERGFIKVDG ECRTNLPNVW AIGDVVRGPM LAHKASDEGV AVAERIAGQK PHIDFNNVPF VIYTDPEIAW VGKTEEQLKA EGVEYKKGTS GFGANGRALA MGKAKGTVKV LADAKTDRIL GVHMIGPVVS ELVTEGVTAL EFFASSEDIA RIIHAHPTLS EVVHEAALAA DKRALHG // ID Q7DDB3_NEIMB Unreviewed; 233 AA. AC Q7DDB3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Thermonuclease family protein {ECO:0000313|EMBL:AAF41866.1}; GN OrderedLocusNames=NMB1510 {ECO:0000313|EMBL:AAF41866.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41866.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41866.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41866.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41866.1; -; Genomic_DNA. DR PIR; B81076; B81076. DR RefSeq; NP_274518.1; NC_003112.2. DR RefSeq; WP_002219028.1; NC_003112.2. DR ProteinModelPortal; Q7DDB3; -. DR STRING; 122586.NMB1510; -. DR PaxDb; Q7DDB3; -. DR EnsemblBacteria; AAF41866; AAF41866; NMB1510. DR GeneID; 903976; -. DR KEGG; nme:NMB1510; -. DR PATRIC; 20358808; VBINeiMen85645_1914. DR eggNOG; ENOG4105KK6; Bacteria. DR eggNOG; COG1525; LUCA. DR HOGENOM; HOG000017398; -. DR OMA; MDSVGEW; -. DR OrthoDB; EOG632D5H; -. DR BioCyc; NMEN122586:GHGG-1550-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 2.40.50.90; -; 1. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR InterPro; IPR002071; Thermonucl_AS. DR Pfam; PF00565; SNase; 1. DR SMART; SM00318; SNc; 1. DR SUPFAM; SSF50199; SSF50199; 1. DR PROSITE; PS01123; TNASE_1; 1. DR PROSITE; PS50830; TNASE_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 72 200 TNase-like. FT {ECO:0000259|PROSITE:PS50830}. SQ SEQUENCE 233 AA; 25958 MW; 45B03D73385927A6 CRC64; MFRRHRHLKN MQIKKIMKWL PVALSLLGAL GYTGYGSEAV RTAVAVLDVL GAAGDAGSDA PARRRASAKS GHRYTGTVSK VYDGDTLHVI DGDGAKHKIR MAYIDAPEMK QAYGTRSRDN LRAAAEGRKV SVRVFDTDRY QREVAQVSVG KTDLNLMQVQ DGAAWHYKSY AKEQQDKADF ADYADAQIQA ERERKGLWKA KNPQAPWAYR RAGRSGGGNK DWMDAVGEWL GIW // ID Q9JY27_NEIMB Unreviewed; 601 AA. AC Q9JY27; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42115.1}; GN OrderedLocusNames=NMB1775 {ECO:0000313|EMBL:AAF42115.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42115.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42115.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42115.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42115.1; -; Genomic_DNA. DR PIR; C81044; C81044. DR RefSeq; NP_274775.1; NC_003112.2. DR RefSeq; WP_010980985.1; NC_003112.2. DR STRING; 122586.NMB1775; -. DR PaxDb; Q9JY27; -. DR EnsemblBacteria; AAF42115; AAF42115; NMB1775. DR GeneID; 903324; -. DR KEGG; nme:NMB1775; -. DR PATRIC; 20359507; VBINeiMen85645_2259. DR eggNOG; ENOG4105XIU; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000027878; -. DR OMA; TANKGKC; -. DR OrthoDB; EOG6RJV4N; -. DR BioCyc; NMEN122586:GHGG-1830-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 193 344 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 373 409 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 601 AA; 63023 MW; B085A73615935EE4 CRC64; MKTALPSRVV AESANLQSGW DAKLQGTQFE TTLGGAAIRA GVGDQARADA KIILEGIKSS VRTETVSSSK SALWQKQAGR GSNIETLQLP SFTGSVAPVL SAPGGYIVDI PKGNLKTEIE KLAKQPEYAY LKQLQVAKNV NWNQVQLAYD KWDYKQEGLT RAGAAIIALA VTVVTAGAGV GAALGLNGAA AAAADAAFAS LASQASVSLI NNKGDVGKTL KELGRSRTVK NLVVAAATAG VSNKLGASSL ATWSETPWVN NLNVNLANAG SAALINTAVN GGSLKDNLEA NILAALVNTA HGEAASKIKG LDQHYVAHKI AHAVAGCAAA AANKGKCQDG AIGAAVGEIV GEALVKNTDF SDMTPEQLDL EVKKITAYAK LAAGTVAGVT GGDVNTAAQT AQNAVENNAV KAVVTAAKVV YKVARKGLKN GKINVRDLKQ TLKDEGYNLA DNLTTLFDET LDWNDAKAVI DIVVGTELNR ANKGEAAQKV KEVLEKNRPY IPNKGAVPNM STYMKNNPFG KQLAQISEKT TLPTQQGQSV FLVKRNQGLL KTGDRFYLDG QHKNHLEVFD KNGNFKFVLN MDGSLNQMKT GAAKGRKLNL K // ID Q9JY34_NEIMB Unreviewed; 104 AA. AC Q9JY34; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42105.1}; GN OrderedLocusNames=NMB1764 {ECO:0000313|EMBL:AAF42105.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42105.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42105.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42105.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42105.1; -; Genomic_DNA. DR PIR; B81045; B81045. DR STRING; 122586.NMB1764; -. DR PaxDb; Q9JY34; -. DR EnsemblBacteria; AAF42105; AAF42105; NMB1764. DR HOGENOM; HOG000043052; -. DR OMA; DIGQHIS; -. DR OrthoDB; EOG6JMN3X; -. DR BioCyc; NMEN122586:GHGG-1819-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 104 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327834. SQ SEQUENCE 104 AA; 11849 MW; A43F2F76CA85A874 CRC64; MKKTLSNLVL ISFCSTMLTA CPFWGSCADW NCSKLNPRWE KAVDTCETEN LTFVLHELGN QLGYKSITEV SFSEIGQHIS YQCIHHGGGY NIRKDKQYGH LFVQ // ID Q9JXP8_NEIMB Unreviewed; 117 AA. AC Q9JXP8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42270.1}; GN OrderedLocusNames=NMB1941 {ECO:0000313|EMBL:AAF42270.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42270.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42270.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42270.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42270.1; -; Genomic_DNA. DR PIR; F81025; F81025. DR RefSeq; NP_274935.1; NC_003112.2. DR RefSeq; WP_002214803.1; NC_003112.2. DR STRING; 122586.NMB1941; -. DR PaxDb; Q9JXP8; -. DR EnsemblBacteria; AAF42270; AAF42270; NMB1941. DR GeneID; 904210; -. DR KEGG; nme:NMB1941; -. DR PATRIC; 20359929; VBINeiMen85645_2469. DR eggNOG; COG3312; LUCA. DR HOGENOM; HOG000218748; -. DR KO; K02116; -. DR OrthoDB; EOG6V1M7M; -. DR BioCyc; NMEN122586:GHGG-1998-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 110 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 117 AA; 12804 MW; 6ACD428B87C02357 CRC64; MKQIIILQSA VLSICAAVAF AVWGFAGFLS AVGGGLSYLL PTFVAVLLLK LFRGNPFLQS RMFVFGEILK VVLSLLSMLA VFAIWHQSLV FAPFLMGLLG VSHLVFLVLL RVKDYGR // ID Q9JYR1_NEIMB Unreviewed; 27 AA. AC Q9JYR1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41826.1}; GN OrderedLocusNames=NMB1469 {ECO:0000313|EMBL:AAF41826.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41826.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41826.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41826.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41826.1; -; Genomic_DNA. DR PIR; H81080; H81080. DR RefSeq; NP_274478.1; NC_003112.2. DR RefSeq; WP_010980942.1; NC_003112.2. DR STRING; 122586.NMB1469; -. DR PaxDb; Q9JYR1; -. DR EnsemblBacteria; AAF41826; AAF41826; NMB1469. DR GeneID; 903891; -. DR KEGG; nme:NMB1469; -. DR BioCyc; NMEN122586:GHGG-1509-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 27 AA; 3184 MW; 9881FB66DDF44631 CRC64; MGKISRLMEH GPIFKQNLNQ QLKKDKT // ID Q9JXS1_NEIMB Unreviewed; 167 AA. AC Q9JXS1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42240.1}; GN OrderedLocusNames=NMB1910 {ECO:0000313|EMBL:AAF42240.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42240.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42240.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42240.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42240.1; -; Genomic_DNA. DR PIR; E81028; E81028. DR RefSeq; NP_274904.1; NC_003112.2. DR RefSeq; WP_002221556.1; NC_003112.2. DR STRING; 122586.NMB1910; -. DR PaxDb; Q9JXS1; -. DR EnsemblBacteria; AAF42240; AAF42240; NMB1910. DR GeneID; 904254; -. DR KEGG; nme:NMB1910; -. DR PATRIC; 20359863; VBINeiMen85645_2436. DR eggNOG; ENOG4105ZKQ; Bacteria. DR eggNOG; COG1399; LUCA. DR HOGENOM; HOG000258049; -. DR KO; K07040; -. DR OMA; SANQDKP; -. DR OrthoDB; EOG61046G; -. DR BioCyc; NMEN122586:GHGG-1967-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR003772; DUF177. DR Pfam; PF02620; DUF177; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 167 AA; 18914 MW; 3BA4D71DE7AF8ED1 CRC64; MSDPNLIDLE IFAAEGQNLQ GSFLLEELDE RVSSHDYPAD RQTKISFTLT GGRDRLQRLF LDLNVKADMP LICQRCIKPM PFMLDESSRI VLFSNEESLD ESMLADEELE GILIEKELDV RTLVEDQILM SLPFSPRHED CGDNGTLEEV NRDKPNPFAV LAGLKSN // ID Q9K001_NEIMB Unreviewed; 514 AA. AC Q9K001; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Type I restriction enzyme EcoR124II M protein {ECO:0000313|EMBL:AAF41241.1}; DE EC=2.1.1.72 {ECO:0000313|EMBL:AAF41241.1}; GN Name=hsdM {ECO:0000313|EMBL:AAF41241.1}; GN OrderedLocusNames=NMB0829 {ECO:0000313|EMBL:AAF41241.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41241.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41241.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41241.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41241.1; -; Genomic_DNA. DR PIR; F81152; F81152. DR RefSeq; NP_273871.1; NC_003112.2. DR RefSeq; WP_002225404.1; NC_003112.2. DR ProteinModelPortal; Q9K001; -. DR STRING; 122586.NMB0829; -. DR PaxDb; Q9K001; -. DR DNASU; 902943; -. DR EnsemblBacteria; AAF41241; AAF41241; NMB0829. DR GeneID; 902943; -. DR KEGG; nme:NMB0829; -. DR PATRIC; 20357045; VBINeiMen85645_1041. DR eggNOG; ENOG4105CVR; Bacteria. DR eggNOG; COG0286; LUCA. DR HOGENOM; HOG000239472; -. DR KO; K03427; -. DR OMA; WASADIL; -. DR OrthoDB; EOG64JFNB; -. DR BioCyc; NMEN122586:GHGG-860-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR022749; D12N6_MeTrfase_N. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004546; Restrct_endonuc_typeI_HsdM. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF12161; HsdM_N; 1. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR TIGRFAMs; TIGR00497; hsdM; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF41241.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41241.1}. FT DOMAIN 11 158 HsdM_N. {ECO:0000259|Pfam:PF12161}. FT DOMAIN 173 480 N6_Mtase. {ECO:0000259|Pfam:PF02384}. FT COILED 484 514 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 514 AA; 57423 MW; 31013E580B4EC77B CRC64; MMTEMQQRAQ LHRQIWKIAD EVRGAVDGWD FKQYVLGTLF YRFISENFTD YMQAGDSSID YAAMPDSIIT PEIKDDAVKV KGYFIYPGQL FCNIAAEAHQ NEELNTKLKE IFTAIESSAS GYPSEQDIKG LFDDFDTTSS RLGSTVADKN KRLAAVLKGV AELDFGNFEN HHIDLFGDAY EYLISNYAAN AGKSGGEFFT PQSVSKLIAR LAVHGQEKVN KIYDPACGSG SLLLQAKKQF DEHIIEEGFF GQEINHTTYN LARMNMFLHN VNYNQFHIEL GDTLTNPKLK DSKPFDAIVS NPPYSINWIG SDDPTLINDD RFAPAGVLAP KSKADFAFIL HALNYLSGRG RAAIVSFPGI FYRGGAEQKI RQYLVEGNYV ETVIALAPNL FYGTGIAVNI LVLSKHKDNT DIQFIDASGF FKKETNNNVL IEEHIAEIVK LFADKADVPH IAQNAAQQTV KDNGYNLAVS SYVEAEDTRE IIDIKQLNAE IGETVAKIER LRREIDEVIA EIEA // ID Q9K0J9_NEIMB Unreviewed; 117 AA. AC Q9K0J9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41025.1}; GN OrderedLocusNames=NMB0597 {ECO:0000313|EMBL:AAF41025.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41025.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41025.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41025.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41025.1; -; Genomic_DNA. DR PIR; B81181; B81181. DR RefSeq; NP_273641.1; NC_003112.2. DR RefSeq; WP_002222851.1; NC_003112.2. DR STRING; 122586.NMB0597; -. DR PaxDb; Q9K0J9; -. DR EnsemblBacteria; AAF41025; AAF41025; NMB0597. DR GeneID; 902712; -. DR KEGG; nme:NMB0597; -. DR PATRIC; 20356479; VBINeiMen85645_0759. DR eggNOG; ENOG41067HH; Bacteria. DR eggNOG; COG3308; LUCA. DR HOGENOM; HOG000259406; -. DR OMA; EWFISPL; -. DR OrthoDB; EOG6HF642; -. DR BioCyc; NMEN122586:GHGG-623-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR018643; DUF2069_membrane. DR Pfam; PF09842; DUF2069; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 107 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 117 AA; 13237 MW; 146F8C04E9048B61 CRC64; MNRQTAYLLA SFSLIALIIL SLSWELWIAP LRPGGSWLAL KALPLCLPLS GILKKKIYTY QYSSMLVLIY FAEAVMRLFD AYPAEQICAA LSAVFSIIFF ISCLSFVKQY KETNNAR // ID Q4W558_NEIMB Unreviewed; 1139 AA. AC Q4W558; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=ATP-dependent RNA helicase HrpA, truncation {ECO:0000313|EMBL:AAY52152.1}; GN OrderedLocusNames=NMB2011 {ECO:0000313|EMBL:AAY52152.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52152.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52152.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52152.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52152.1; -; Genomic_DNA. DR RefSeq; NP_275003.1; NC_003112.2. DR RefSeq; WP_002223146.1; NC_003112.2. DR STRING; 122586.NMB2011; -. DR PaxDb; Q4W558; -. DR EnsemblBacteria; AAY52152; AAY52152; NMB2011. DR GeneID; 903114; -. DR KEGG; nme:NMB2011; -. DR PATRIC; 20360125; VBINeiMen85645_2567. DR eggNOG; COG1643; LUCA. DR HOGENOM; HOG000218727; -. DR OMA; NVTTWDI; -. DR OrthoDB; EOG6Q5NPH; -. DR BioCyc; NMEN122586:GHGG-2068-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR InterPro; IPR011709; DUF1605. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR024590; HrpA_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF11898; DUF3418; 2. DR Pfam; PF04408; HA2; 1. DR Pfam; PF07717; OB_NTP_bind; 1. DR SMART; SM00847; HA2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAY52152.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000313|EMBL:AAY52152.1}; KW Hydrolase {ECO:0000313|EMBL:AAY52152.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAY52152.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 24 114 HA2. {ECO:0000259|SMART:SM00847}. SQ SEQUENCE 1139 AA; 128795 MW; 6D5A605CA6E4E138 CRC64; MQNMKNQVRG SGMDARSNPA NVSDGLQNSS GHIGTNTRYR LTKLGEQIAR LPIDPKIARI LLAAKKHDCM AEILVIASAL SIQDPRERPL EARDASAKAH ERFTDKQSDF LAYLNIWDSF QRERDKGLSN KQLVQWCRQY FLSHLRMREW RELHHQLAQT AIEMGLTTKE AAFRRPPEVR QLTSSENAGD QDLSAKLKQK QLDKKQHRAQ IRAAKEAGYE QIHRALLTGL IANVGMKSPD GNDYTGARGS RFHLFPASAL FKAKPKWVMA AELVETTRLY ARDVAVIQPE WIEQEAPHLV RYHYFEPHWE QKRGEVVASE RVTLYGLTVL PRRPVSYGKV APEEAREIFI RSALVAQECD LKADFFVHNK KLIKEITELE HKSRKQDVLV DDEALFAFYN ERLPEMAWKD AQGSVWGSED SVRIIESDKA ERSSENERNE FRKNKRNGSR QNENHGNTVG WVENPTSAAT AKTVGFDNPT YAAQQTTPSP VGEGRGEGKT VAAQTNFSAT AANPLPNPLP QEREQSAAAS TISDDLRPAN LQQTAPSPVG EGWGEGKTVA TQTNFSATST NPLPQEREQS ASASTFSDDL RPANLQQPSP SPVGEGWGEG KTVATQTNFS ATSTLSDDSK PKKQPAPQKN RLKPLPLADI RTFQAWLKTA ERDNPRLLFL SRDDLMQHAA AHITEEQFPK FWQTADGKFK LSYRFEPHHP LDGVTMTVPL TVLNRLHAPS LEWLVPGMIR EKIQLQIKAL PKQIRRICVP VPEFITQFLS QNPDRNAPIL PQLAQAIAKT AGDIRIFEQI NQDEWAAFRL PEHCYFNLRI IDDGGQELAG GRKLHELQQQ LGQAAAVTFR DNTQEFERDN VTAWDIGTLP ESIKFARGKQ QLTGYLGLQK EKDGRIALRL FDTTEAAEQA HRQGVIELMK LQLKEQVKDL NKGIQGFTQA AMLLKHINAD TLRDDLTQAV CDRAFIGEDE LPRNEKAFKE QIKRARSRLP AVKEALSRYL QETAAVYAEL NSKLGKHPLT HLLRLRLQTL LAAGFATRTP WAQWPRLPIY LKAMTLRLEK YSSNPARDAA READIQELEQ MWQEKTDSLI KQGLPISDGL AAFKWMIEEL RVSLFAQELK TPYPVSVKRL LKEWEKIEK // ID Q9K183_NEIMB Unreviewed; 456 AA. AC Q9K183; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172}; DE Short=ASL {ECO:0000256|RuleBase:RU361172}; DE EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172}; DE AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172}; GN Name=purB {ECO:0000313|EMBL:AAF40737.1}; GN OrderedLocusNames=NMB0284 {ECO:0000313|EMBL:AAF40737.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40737.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40737.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40737.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- CC (5-phospho-D-ribosyl)imidazole-4-carboxamide. CC {ECO:0000256|RuleBase:RU361172}. CC -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. CC {ECO:0000256|RuleBase:RU361172}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC {ECO:0000256|RuleBase:RU361172}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000256|RuleBase:RU361172}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40737.1; -; Genomic_DNA. DR PIR; D81216; D81216. DR RefSeq; NP_273340.1; NC_003112.2. DR RefSeq; WP_002224850.1; NC_003112.2. DR ProteinModelPortal; Q9K183; -. DR SMR; Q9K183; 2-449. DR STRING; 122586.NMB0284; -. DR PaxDb; Q9K183; -. DR EnsemblBacteria; AAF40737; AAF40737; NMB0284. DR GeneID; 902395; -. DR KEGG; nme:NMB0284; -. DR PATRIC; 20355664; VBINeiMen85645_0356. DR eggNOG; ENOG4107QTF; Bacteria. DR eggNOG; COG0015; LUCA. DR HOGENOM; HOG000252916; -. DR KO; K01756; -. DR OMA; TFGKEMA; -. DR OrthoDB; EOG686NDB; -. DR BioCyc; NMEN122586:GHGG-299-MONOMER; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR InterPro; IPR013539; PurB_C. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF08328; ASL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00928; purB; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:AAF40737.1}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 13 312 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 331 446 ASL_C. {ECO:0000259|Pfam:PF08328}. SQ SEQUENCE 456 AA; 50435 MW; C9514419E0CE2A7E CRC64; MINPIASLSP LDGRYAQSVE ALRPIFSEYG LMKARVKVEL NWLKALAAEP KIAEVPPFSA ETLAEIDTVI ENFSLEDAAA VKAIEATTNH DVKAIEYWLK KRFAEVPEVA AVSEFIHFAC TSEDINNLSH ALMLQEAREA VLLPKLAEII EKLTAMAHDL AAVPMMSRTH GQPATPTTLG KETANVVYRL QRQFKNLQAQ EFLGKINGAV GNYNAHMVAY PDVDWETHCR NFVEISLGLT FNPYTIQIEP HDYMAEFFQT LSRINTILID FNRDVWGYIS LGYFKQKVKA GEVGSSTMPH KVNPIDFENS EGNLGMANAV LGFLSEKLPI SRWQRDLTDS TVLRNMGVGV GYAVLGFAAH LRGLNKLEPN PAALAADLDA TWELLAEPIQ TVMRRYGVAN PYEKLKDLTR GKGGITPEVL KGFIGLLEIP AEAKAKLLEL TPALYVGKAE ALAKRI // ID Q9JZB2_NEIMB Unreviewed; 67 AA. AC Q9JZB2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41590.1}; GN OrderedLocusNames=NMB1208 {ECO:0000313|EMBL:AAF41590.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41590.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41590.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41590.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41590.1; -; Genomic_DNA. DR PIR; G81110; G81110. DR STRING; 122586.NMB1208; -. DR PaxDb; Q9JZB2; -. DR EnsemblBacteria; AAF41590; AAF41590; NMB1208. DR OMA; RNRAYSP; -. DR OrthoDB; EOG65TS2V; -. DR BioCyc; NMEN122586:GHGG-1245-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7811 MW; 73688D41DF0A2E58 CRC64; MRALYAKAVG MTNFLFKIQT IIKRNRAYSP MPSKSVCCFL SVFLLLKLRI HLIHKEHLHL LTIAKNK // ID Q7DD55_NEIMB Unreviewed; 469 AA. AC Q7DD55; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Chloride channel protein-related protein {ECO:0000313|EMBL:AAF42333.1}; GN OrderedLocusNames=NMB2006 {ECO:0000313|EMBL:AAF42333.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42333.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42333.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42333.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42333.1; -; Genomic_DNA. DR PIR; D81017; D81017. DR RefSeq; NP_274998.1; NC_003112.2. DR RefSeq; WP_002225874.1; NC_003112.2. DR ProteinModelPortal; Q7DD55; -. DR STRING; 122586.NMB2006; -. DR PaxDb; Q7DD55; -. DR EnsemblBacteria; AAF42333; AAF42333; NMB2006. DR GeneID; 904114; -. DR KEGG; nme:NMB2006; -. DR PATRIC; 20360113; VBINeiMen85645_2561. DR eggNOG; ENOG4107S4D; Bacteria. DR eggNOG; COG0038; LUCA. DR HOGENOM; HOG000257545; -. DR OMA; EMTDNHA; -. DR OrthoDB; EOG6C0143; -. DR BioCyc; NMEN122586:GHGG-2063-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro. DR Gene3D; 1.10.3080.10; -; 1. DR InterPro; IPR014743; Cl-channel_core. DR InterPro; IPR001807; Cl-channel_volt-gated. DR Pfam; PF00654; Voltage_CLC; 1. DR PRINTS; PR00762; CLCHANNEL. DR SUPFAM; SSF81340; SSF81340; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|SAAS:SAAS00438323}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00438323, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 169 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 242 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 388 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 417 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 469 AA; 50048 MW; 02281B8F40EC9B6B CRC64; MTSTFPRRLA RKIRQTRRLS RKSIAFLFLL AGSALVALTA LFFAHLADFA LELNAKLVQQ YPWFAWVALP LGLPLIAWLT RKFAPFTAGS GIPQVIASLS LPYGAQKTRL IRLGQTLLKI PLTFLGMLFG ASIGREGPSV QVGAAVMGAW GAWCKKHGLA FKGMQENDLM AAGAAGGLAA AFNAPLAGVI FAIEELGRGI MLRWERQILL GVLASGFIQV AIQGNNPYFS GFNGGVLEHI FLWVALSGLV CGAAGGLFGR LLYRGAAAFA PRKIRGFIRN RPLLLAALMG LLLALLGTFY QGKTYGTGYH EAAQALHGIY EAPFGLAAAK WLATVFSYWA GVPGGIFTPS LTIGAVLGEH IAAIADISQG ANIIVLICMA AFLAGATQSP ITSAVVVMEM TGGQSLLFWM LIACIFASQV SRQFSPRPFY HASGMRFRQR VLQETAAQTG NAPARPQTAN SKTGMPSEN // ID Q9JYC1_NEIMB Unreviewed; 245 AA. AC Q9JYC1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42003.1}; GN OrderedLocusNames=NMB1654 {ECO:0000313|EMBL:AAF42003.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42003.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42003.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42003.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42003.1; -; Genomic_DNA. DR PIR; E81057; E81057. DR RefSeq; NP_274659.1; NC_003112.2. DR RefSeq; WP_002223538.1; NC_003112.2. DR ProteinModelPortal; Q9JYC1; -. DR STRING; 122586.NMB1654; -. DR PaxDb; Q9JYC1; -. DR EnsemblBacteria; AAF42003; AAF42003; NMB1654. DR GeneID; 903462; -. DR KEGG; nme:NMB1654; -. DR PATRIC; 20359232; VBINeiMen85645_2128. DR eggNOG; COG2849; LUCA. DR HOGENOM; HOG000219061; -. DR OMA; HGKEIKY; -. DR OrthoDB; EOG615VF2; -. DR BioCyc; NMEN122586:GHGG-1703-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011652; MORN_2. DR Pfam; PF07661; MORN_2; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 245 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329337. SQ SEQUENCE 245 AA; 27938 MW; 26E18D01357C3B7A CRC64; MKKLSRIVFS TVLLGFSAAL PAQTYSVYFN QNGKLTATMS SAAYIRQYSV VAGIAHAQDF YYPSMKKYSE PYIVASTQIK SFVPTLQNGM LILWHFNGQK KMAGGFSKGK PDGEWVNWYP NGKKSAVMPY KNGLSEGTGY RYYRNGGKES EIQFKQNKAN GVWKQWYADG SIKTEMVMVN DEPAKILTWD ESGRLLSELS IRHHQRNGVV LEWYEDGSKK SEAVYQDDKL VRKTQWDKDG YLIEP // ID Q9JY74_NEIMB Unreviewed; 56 AA. AC Q9JY74; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42054.1}; GN OrderedLocusNames=NMB1706 {ECO:0000313|EMBL:AAF42054.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42054.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42054.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42054.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42054.1; -; Genomic_DNA. DR PIR; D81053; D81053. DR RefSeq; NP_274710.1; NC_003112.2. DR RefSeq; WP_009346399.1; NC_003112.2. DR STRING; 122586.NMB1706; -. DR PaxDb; Q9JY74; -. DR EnsemblBacteria; AAF42054; AAF42054; NMB1706. DR GeneID; 903395; -. DR KEGG; nme:NMB1706; -. DR PATRIC; 20359369; VBINeiMen85645_2190. DR HOGENOM; HOG000219078; -. DR OrthoDB; EOG680X6Q; -. DR BioCyc; NMEN122586:GHGG-1762-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 56 AA; 6531 MW; 926EFC12E0F3BF62 CRC64; MQQTTKLYSF IGKKHPEFIL QNKKIPISPD ITQPIGKVLQ RLPRLVLPRQ VLCYNV // ID Q9JZ39_NEIMB Unreviewed; 78 AA. AC Q9JZ39; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41686.1}; GN OrderedLocusNames=NMB1311 {ECO:0000313|EMBL:AAF41686.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41686.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41686.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41686.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41686.1; -; Genomic_DNA. DR PIR; E81098; E81098. DR PaxDb; Q9JZ39; -. DR EnsemblBacteria; AAF41686; AAF41686; NMB1311. DR BioCyc; NMEN122586:GHGG-1349-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 63 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 78 AA; 9253 MW; 4369EEB3A08631B3 CRC64; MPSESQMGQQ FLQGRDTRIL LNLPVRLLRK DKGRKRYPAF LIYTCNSSPY LPIVFSYCAS IPYRFKKMPF PMGWVLYQ // ID Q9JZ35_NEIMB Unreviewed; 403 AA. AC Q9JZ35; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uracil permease {ECO:0000313|EMBL:AAF41690.1}; GN Name=uraA {ECO:0000313|EMBL:AAF41690.1}; GN OrderedLocusNames=NMB1315 {ECO:0000313|EMBL:AAF41690.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41690.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41690.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41690.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41690.1; -; Genomic_DNA. DR PIR; B81096; B81096. DR RefSeq; NP_274334.1; NC_003112.2. DR RefSeq; WP_002225164.1; NC_003112.2. DR STRING; 122586.NMB1315; -. DR PaxDb; Q9JZ35; -. DR EnsemblBacteria; AAF41690; AAF41690; NMB1315. DR GeneID; 903737; -. DR KEGG; nme:NMB1315; -. DR PATRIC; 20358277; VBINeiMen85645_1650. DR eggNOG; ENOG4105C2W; Bacteria. DR eggNOG; COG2233; LUCA. DR HOGENOM; HOG000038200; -. DR KO; K02824; -. DR OMA; DTTSIAH; -. DR OrthoDB; EOG6Z3KKZ; -. DR BioCyc; NMEN122586:GHGG-1353-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006042; Xan_ur_permease. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR TIGRFAMs; TIGR00801; ncs2; 1. DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 231 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 318 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 345 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 397 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 403 AA; 41842 MW; 274E44E788FCE25B CRC64; MNQLKLAVSG AQILFVAFGA MVLVPLLTGL NPALALLGAG LGTLLFQITT KRKVPIFLGS SFAFIAPIIY SVGEWGLPST MFGLFAAGFM YFVFAALIRW RGLAAVHKLL PPVVIGPVIM VIGLSVAVAA SSMAMGQADG KQVIDYTDSL ILSGFTFAVT AIVSVFGSRM MKLIPILIGV ASGYVLALLM GLVDTASIAH APWFAVPHFE TPQINWQAAL FMLPVAVAPA IEHIGGIMAI GNVTGKDYTK DPGLDKTLAG DGLGVCVAGL IGGPPVTTYG EVTGAVMITK NSNPVIMTWA AVFAVCMAFF GKFNAFLASI PMPVMGGIML LLFGTIASLG VKTLIDAKVD LMLPKNLVIV SSVLTTGIGG MTLKLGSFSF AGVGLCAVLA IMLNSLLPDP KES // ID Q7DDC7_NEIMB Unreviewed; 383 AA. AC Q7DDC7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41681.1}; GN OrderedLocusNames=NMB1306 {ECO:0000313|EMBL:AAF41681.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41681.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41681.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41681.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41681.1; -; Genomic_DNA. DR PIR; H81097; H81097. DR RefSeq; NP_274325.1; NC_003112.2. DR RefSeq; WP_002220874.1; NC_003112.2. DR ProteinModelPortal; Q7DDC7; -. DR STRING; 122586.NMB1306; -. DR PaxDb; Q7DDC7; -. DR EnsemblBacteria; AAF41681; AAF41681; NMB1306. DR GeneID; 903728; -. DR KEGG; nme:NMB1306; -. DR PATRIC; 20358255; VBINeiMen85645_1639. DR eggNOG; ENOG4105D6Z; Bacteria. DR eggNOG; COG1485; LUCA. DR HOGENOM; HOG000259599; -. DR KO; K06916; -. DR OMA; MRTHFHR; -. DR OrthoDB; EOG63NMFD; -. DR BioCyc; NMEN122586:GHGG-1344-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR005654; ATPase_AFG1-like. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12169; PTHR12169; 1. DR Pfam; PF03969; AFG1_ATPase; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 383 AA; 43684 MW; 0124B7AD9C29B31F CRC64; MSNRDQLFKA PPFENHSPLT WYQAASQLPN FIRDDAQAAA IEHLDRLWTE LMMFKRKRNR FLGRSLRSPQ VPKGLYFYGG VGRGKSFLMD AFFGCLPYRR KRRVHFHAFM AEIHQRLKTL KSESNPLKSV AAEIAKETRV LCFDEFHVSD IADAMILGRL LENLLNEGVV LVATSNYAPS ELYPQGQNRS SFLPTIALIE SSLTVLNVDG GEDYRLRTLR PAEIFFTPAN EENEAKLAKL FKEMTGITDL NPGISTIHGR EIPHKAESGR AIWFDFRALC FGPRSQSDYL YLAEHYEMVF ISGLEQLSPQ EKAEARRLTW LIDVLYDFRV KLCATGAVDV NHIYTEGDFA EEFTRTASRM VEMQSEVYLE QPHLTLSPKA SGG // ID Q7DDJ1_NEIMB Unreviewed; 56 AA. AC Q7DDJ1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Rubredoxin {ECO:0000256|PIRNR:PIRNR000071}; GN OrderedLocusNames=NMB0993 {ECO:0000313|EMBL:AAF41396.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41396.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41396.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41396.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000256|PIRNR:PIRNR000071, CC ECO:0000256|PIRSR:PIRSR000071-1}; CC Note=Binds 1 Fe(3+) ion per subunit. CC {ECO:0000256|PIRNR:PIRNR000071, ECO:0000256|PIRSR:PIRSR000071-1}; CC -!- SIMILARITY: Belongs to the rubredoxin family. CC {ECO:0000256|PIRNR:PIRNR000071}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41396.1; -; Genomic_DNA. DR PIR; H81133; H81133. DR RefSeq; NP_274029.1; NC_003112.2. DR RefSeq; WP_002217326.1; NC_003112.2. DR ProteinModelPortal; Q7DDJ1; -. DR SMR; Q7DDJ1; 1-53. DR STRING; 122586.NMB0993; -. DR PaxDb; Q7DDJ1; -. DR EnsemblBacteria; AAF41396; AAF41396; NMB0993. DR GeneID; 903115; -. DR KEGG; nme:NMB0993; -. DR PATRIC; 20357499; VBINeiMen85645_1266. DR eggNOG; ENOG4105VCQ; Bacteria. DR eggNOG; COG1773; LUCA. DR HOGENOM; HOG000223371; -. DR OMA; SKDMFEP; -. DR OrthoDB; EOG69SKK0; -. DR BioCyc; NMEN122586:GHGG-1030-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR024922; Rubredoxin. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR024935; Rubredoxin_dom. DR InterPro; IPR018527; Rubredoxin_Fe_BS. DR Pfam; PF00301; Rubredoxin; 1. DR PIRSF; PIRSF000071; Rubredoxin; 1. DR PRINTS; PR00163; RUBREDOXIN. DR PROSITE; PS00202; RUBREDOXIN; 1. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|SAAS:SAAS00496620}; KW Iron {ECO:0000256|PIRNR:PIRNR000071, ECO:0000256|PIRSR:PIRSR000071-1, KW ECO:0000256|SAAS:SAAS00496614}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|PIRSR:PIRSR000071-1, ECO:0000256|SAAS:SAAS00496609}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|SAAS:SAAS00496620}. FT DOMAIN 1 52 Rubredoxin-like. FT {ECO:0000259|PROSITE:PS50903}. FT METAL 6 6 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 9 9 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 39 39 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 42 42 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. SQ SEQUENCE 56 AA; 6369 MW; F2CE9EA86E7DB8C9 CRC64; MAQYMCGPCG WIYDEEHGDP EHGIAPGTKF EDIPDDWKCP ECGVGKEDFY LLDFVI // ID Q9JYD1_NEIMB Unreviewed; 446 AA. AC Q9JYD1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41993.1}; GN OrderedLocusNames=NMB1644 {ECO:0000313|EMBL:AAF41993.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41993.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41993.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41993.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41993.1; -; Genomic_DNA. DR PIR; C81058; C81058. DR RefSeq; NP_274649.1; NC_003112.2. DR RefSeq; WP_002224999.1; NC_003112.2. DR ProteinModelPortal; Q9JYD1; -. DR STRING; 122586.NMB1644; -. DR PaxDb; Q9JYD1; -. DR EnsemblBacteria; AAF41993; AAF41993; NMB1644. DR GeneID; 903472; -. DR KEGG; nme:NMB1644; -. DR PATRIC; 20359208; VBINeiMen85645_2116. DR eggNOG; ENOG4105INH; Bacteria. DR eggNOG; ENOG410XP0M; LUCA. DR HOGENOM; HOG000219059; -. DR OMA; RAHPQWS; -. DR OrthoDB; EOG6NWBPV; -. DR BioCyc; NMEN122586:GHGG-1693-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR021871; DUF3482. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF11981; DUF3482; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 151 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 50050 MW; 732BDDE2E3451366 CRC64; MNKQPLSLAV VGHTNTGKTS LLRTLLRDSG FGEVKNAPST TRHVEEAAIS DGADTLVFLY DTPGLEDAGG VLEWLENHTD NRSDGIERLQ QFLGSHGAHH DFNQEAKVLR QVLQSDMAMY VIDAREPVLD KYRDELTILS WCAKPVMPVF NFTGGQLPES WTTMLARRNL HVFAGFDTVA FDFEGELRLW ENLATMLPER STLDRLTAMR RREWQRLDGE ARREIADFLI DAAAFRQEVD ENEDTATVLQ TMQAEIRQLE RQMQQRLFAL YRFYHSEIDG GDWMPQAFRQ DPFDSELLKQ YGIRTGTGAA TGALIGLGLD IATLGGSLGL GTAIGGFLGG ILPNTRTISD KLAGRQTLHT DPETLTLLAA RALDLLHVLQ TRGHAAQSDI ELHSRKVPWD AARLPPELNK ARSHWKWSSL NTHRPETSRA ERREYAEKLG IRLAGK // ID Q9JY44_NEIMB Unreviewed; 33 AA. AC Q9JY44; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Cryptic plasmid protein A-related protein {ECO:0000313|EMBL:AAF42095.1}; GN OrderedLocusNames=NMB1754 {ECO:0000313|EMBL:AAF42095.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42095.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42095.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42095.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42095.1; -; Genomic_DNA. DR PIR; A81046; A81046. DR RefSeq; NP_274754.1; NC_003112.2. DR RefSeq; WP_010980981.1; NC_003112.2. DR PaxDb; Q9JY44; -. DR EnsemblBacteria; AAF42095; AAF42095; NMB1754. DR GeneID; 903344; -. DR KEGG; nme:NMB1754; -. DR BioCyc; NMEN122586:GHGG-1809-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 33 AA; 3753 MW; D4BC2ADA7CD09E23 CRC64; MFHTLPEALK RTEIAAARQK LTELRRMLVS KGG // ID Q9K078_NEIMB Unreviewed; 557 AA. AC Q9K078; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE RecName: Full=DNA repair protein RecN {ECO:0000256|PIRNR:PIRNR003128}; DE AltName: Full=Recombination protein N {ECO:0000256|PIRNR:PIRNR003128}; GN Name=recN {ECO:0000313|EMBL:AAF41153.1}; GN OrderedLocusNames=NMB0740 {ECO:0000313|EMBL:AAF41153.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41153.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41153.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41153.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: May be involved in recombinational repair of damaged CC DNA. {ECO:0000256|PIRNR:PIRNR003128}. CC -!- SIMILARITY: Belongs to the RecN family. CC {ECO:0000256|PIRNR:PIRNR003128}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41153.1; -; Genomic_DNA. DR PIR; D81165; D81165. DR RefSeq; NP_273782.1; NC_003112.2. DR RefSeq; WP_002247552.1; NC_003112.2. DR ProteinModelPortal; Q9K078; -. DR STRING; 122586.NMB0740; -. DR PaxDb; Q9K078; -. DR EnsemblBacteria; AAF41153; AAF41153; NMB0740. DR GeneID; 902853; -. DR KEGG; nme:NMB0740; -. DR PATRIC; 20356843; VBINeiMen85645_0942. DR eggNOG; ENOG4105C4F; Bacteria. DR eggNOG; COG0497; LUCA. DR HOGENOM; HOG000009327; -. DR KO; K03631; -. DR OMA; QVICVTH; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NMEN122586:GHGG-769-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR004604; DNA_recomb/repair_RecN. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR PANTHER; PTHR11059; PTHR11059; 1. DR Pfam; PF02463; SMC_N; 1. DR PIRSF; PIRSF003128; RecN; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00634; recN; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|PIRNR:PIRNR003128}; KW DNA repair {ECO:0000256|PIRNR:PIRNR003128}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 14 508 SMC_N. {ECO:0000259|Pfam:PF02463}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 61299 MW; 7840D6BF2E9286D2 CRC64; MLLTLSLRDF VIVENLNLDF QSGFTVLTGE TGAGKSITLD AIGLLLGDKA DYSQVRSGAK EAQLSALFDI SHLPVLKAEL YEQGLLNDGE EELSIRRIID AKGKSRSFIN NQAATLAQLK AVGSQLIDIH GQNAHHSLNQ EAAQRELLDA FAGSREQAET VRQLYQNWAN AKKALQEAQE HADAVIIERE RLEWQFNELN QLDIKQGEWE ALSQSHDSLA HSAELLQAAE EVGSKIDGDN GIQRHIYQCQ KLLANLQNIE PRFAESLNML ASIEAELGEI SANMRDVAGR SDINPNELAA QEQRMGELMG MARKYRIEPE ELPAKLAEIE ERLQSLQAAA DLDALEHNVA HNFAEYQEAA HILSAMRHQA AERLSGETTE HMQHLAMKGA RFDIVLLPSS PTAHGLEQVQ FQVAANKGNP PRLLNKVASG GELARISLAL QVVASQYTQV PTLIFDEVDT GIGGGVAEMV GKALRALGRK HQVLAVTHLP QVASCGENHW RVRKHSEGEQ TVSEISILDE IQRIEEVARM LGGEVITDTT RQHAAELLQL ASKNSLF // ID Q7DD40_NEIMB Unreviewed; 105 AA. AC Q7DD40; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42429.1}; GN OrderedLocusNames=NMB2118 {ECO:0000313|EMBL:AAF42429.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42429.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42429.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42429.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42429.1; -; Genomic_DNA. DR PIR; H81004; H81004. DR RefSeq; NP_275104.1; NC_003112.2. DR RefSeq; WP_002215112.1; NC_003112.2. DR PaxDb; Q7DD40; -. DR EnsemblBacteria; AAF42429; AAF42429; NMB2118. DR GeneID; 903488; -. DR KEGG; nme:NMB2118; -. DR PATRIC; 20360410; VBINeiMen85645_2701. DR OrthoDB; EOG67T5NK; -. DR BioCyc; NMEN122586:GHGG-2183-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 105 AA; 12256 MW; 0D0D3EF73BC92A6A CRC64; MKKNIFHNVS LYEIIFSDNG NTLTLSFTDT IEGNYFGYIK CSNILNFKLD TNNFVDYEDK EDSLFPLFIP EIELYKYQFY SEIIIDVGII IKISAETINF EPLGK // ID Q9K0K2_NEIMB Unreviewed; 808 AA. AC Q9K0K2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41021.1}; GN OrderedLocusNames=NMB0593 {ECO:0000313|EMBL:AAF41021.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41021.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41021.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41021.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41021.1; -; Genomic_DNA. DR PIR; F81180; F81180. DR RefSeq; NP_273637.1; NC_003112.2. DR RefSeq; WP_002244037.1; NC_003112.2. DR ProteinModelPortal; Q9K0K2; -. DR STRING; 122586.NMB0593; -. DR PaxDb; Q9K0K2; -. DR EnsemblBacteria; AAF41021; AAF41021; NMB0593. DR GeneID; 902708; -. DR KEGG; nme:NMB0593; -. DR PATRIC; 20356471; VBINeiMen85645_0755. DR eggNOG; COG0454; LUCA. DR eggNOG; COG1042; LUCA. DR HOGENOM; HOG000218822; -. DR OMA; HRGILAC; -. DR OrthoDB; EOG6FFS5B; -. DR BioCyc; NMEN122586:GHGG-619-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR Pfam; PF13302; Acetyltransf_3; 1. DR Pfam; PF13380; CoA_binding_2; 1. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 637 789 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 808 AA; 89115 MW; 6AE44801CC0F66A5 CRC64; MSAQTDPGYF FMPNHIILIG ASEQPYSLGE RVLSNLLSTP FQGKITPVNP RHHTIAGLPA YTSLNKIPGN ADLIIAVTLP DSYDTLFKTC RKKQLRHIIL IQDWDNLSAA ELHTAETAIR KHHGNGLNIT ACTTAGIQLP SLGLNISTQD GYAAGHTAIL TGNAAVSRQI DNILNKLRQG TSRHISLHPG ISPITSADWL NRFGHSLHTK TAVLHHNPEE DQRKLFSAIR QFTRHTPLIL HITCRTTETD RAVLHCLARH CNFLVSFNAD DLEAALRAQL SDLPPLSRLD ILSDTPAEWL HAHAPKNLTL HFPNLPHHIR NGHLTGTPTP SICHDIASRQ LAHPDTQAVL TILSPSGHED YKKTARALIR LSEQTAKPLL VSSPFSDGIT HFDTPTQAIR TLSYRNTAAA LKQAQLDIAP PQPCRLKTPQ PQNIKKALAA ANPSLLAEAL HLPPYRHTTH NAVQFQFDSH PLYGDILTAR CNGQTTAVLP PFTTLDSRHL ARFAELDGTQ TLDQFLHTLT VIPEYRQHIL GITLNLNGGQ YSSDFLLKTP ETHDTPKRKN TGKAAQTLEH AAAKMQSAAA YLKHKNPTAA EFLRHTSEAA AELLGSKTET GAAVPNVLAP YPAAYPKTLS LRNNTTVTIT PILPEDAEAK QQFVRSLGPE ARYTRFMTHT NELPAATLAR LCNPDYHCEA AWTAKDADSN IVAVVRHSRL NRNECEFGIT LAEHMRGSGL AQKMMELIIQ TAAQQGYRTM SADILKTNTP MIKLAEKSGF TLKESDTEKN LYRAYLNLAA DKTTEKTNKN LRTDHKIT // ID Q7DD98_NEIMB Unreviewed; 301 AA. AC Q7DD98; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Transcriptional regulator MtrA {ECO:0000313|EMBL:AAF41944.1}; GN Name=mtrA {ECO:0000313|EMBL:AAF41944.1}; GN OrderedLocusNames=NMB1591 {ECO:0000313|EMBL:AAF41944.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41944.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41944.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41944.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH araC/xylS-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00503533}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41944.1; -; Genomic_DNA. DR PIR; A81066; A81066. DR RefSeq; NP_274597.1; NC_003112.2. DR RefSeq; WP_002212798.1; NC_003112.2. DR ProteinModelPortal; Q7DD98; -. DR STRING; 122586.NMB1591; -. DR PaxDb; Q7DD98; -. DR EnsemblBacteria; AAF41944; AAF41944; NMB1591. DR GeneID; 904265; -. DR KEGG; nme:NMB1591; -. DR PATRIC; 20359064; VBINeiMen85645_2044. DR eggNOG; ENOG4105E7U; Bacteria. DR eggNOG; ENOG4111N2I; LUCA. DR HOGENOM; HOG000136816; -. DR KO; K18991; -. DR OMA; EATFHIV; -. DR OrthoDB; EOG690MBW; -. DR BioCyc; NMEN122586:GHGG-1639-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR032783; AraC_lig. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type. DR Pfam; PF12852; Cupin_6; 1. DR Pfam; PF12833; HTH_18; 1. DR PRINTS; PR00032; HTHARAC. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 2. DR SUPFAM; SSF51182; SSF51182; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}; KW Transcription regulation {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}. FT DOMAIN 196 297 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 301 AA; 33424 MW; 3FA14A589583C96C CRC64; MDILDKLVDF AQLTGSVDVQ CLLGGQWSVR HETLQREGLV HIVTSGSGYL CIDGETSPRP VSTGDIVFFP RGLGHVLSHD GKCGESLQPD MRQHGAFTVK QCGNGQDMSL FCARFRYDTH ADLMNGLPET VFLNIAHPSL QYVVSMLQLE SKKPLTGTVS MVNALSSVLL VLILRAYLEQ DKDVELSGVL KGWQDKRLGH LIQKVIDKPE DEWNVDKMVA AANMSRAQLM RRFKSRVGLS PHAFVNHIRL QKGALLLKKN PDSVLSVALS VGFQSETHFG KAFKRQYHVS PGQYRKEGGQ K // ID Q7DDK4_NEIMB Unreviewed; 245 AA. AC Q7DDK4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Peroxiredoxin 2 family protein/glutaredoxin {ECO:0000313|EMBL:AAF41352.1}; GN OrderedLocusNames=NMB0946 {ECO:0000313|EMBL:AAF41352.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41352.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41352.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41352.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41352.1; -; Genomic_DNA. DR PIR; G81140; G81140. DR RefSeq; NP_273984.1; NC_003112.2. DR RefSeq; WP_002213776.1; NC_003112.2. DR ProteinModelPortal; Q7DDK4; -. DR SMR; Q7DDK4; 8-243. DR STRING; 122586.NMB0946; -. DR PeroxiBase; 4780; NmPrxGrx. DR PaxDb; Q7DDK4; -. DR PRIDE; Q7DDK4; -. DR EnsemblBacteria; AAF41352; AAF41352; NMB0946. DR GeneID; 903066; -. DR KEGG; nme:NMB0946; -. DR PATRIC; 20357373; VBINeiMen85645_1201. DR eggNOG; ENOG4105EHV; Bacteria. DR eggNOG; COG0678; LUCA. DR eggNOG; COG0695; LUCA. DR OMA; DKMFIEP; -. DR OrthoDB; EOG6PKFB5; -. DR BioCyc; NMEN122586:GHGG-983-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 2. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR011906; Glutaredoxin_dom. DR InterPro; IPR014025; Glutaredoxin_subgr. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR Pfam; PF08534; Redoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02190; GlrX-dom; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 162 245 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. SQ SEQUENCE 245 AA; 26912 MW; D655F9F8382F33A9 CRC64; MALQDRTGQK VPSVVFRTRV GDTWKDVSTD DLFKGKKVVV FSLPGAFTPT CSSSHLPRYN ELFGAFKENG VDAIYCVSVN DTFVMNAWAA EEESDNIYMI PDGNGEFTEG MGMLVGKEDL GFGKRSWRYS MLVNDGVVEK MFIEPEEPGD PFKVSDADTM LQFVAPDWKA QESVAIFTKP GCQFCAKAKQ ALQDKGLSYE EIVLGKDATV TSVRAITGKM TAPQVFIGGK YIGGSEDLEA YLAKN // ID Q9K1C6_NEIMB Unreviewed; 67 AA. AC Q9K1C6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40691.1}; GN OrderedLocusNames=NMB0236 {ECO:0000313|EMBL:AAF40691.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40691.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40691.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40691.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40691.1; -; Genomic_DNA. DR PIR; C81221; C81221. DR STRING; 122586.NMB0236; -. DR PaxDb; Q9K1C6; -. DR EnsemblBacteria; AAF40691; AAF40691; NMB0236. DR PATRIC; 20355546; VBINeiMen85645_0297. DR BioCyc; NMEN122586:GHGG-251-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7743 MW; 382C345A6B7C1BF7 CRC64; MLKRNLGFDT FKLITIFFLG IRRLQSKHIR AIWDDKSGAI VIRDPNSKDG GTAFRPTLGK TYFDKQK // ID Q7DD77_NEIMB Unreviewed; 181 AA. AC Q7DD77; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=PilP protein {ECO:0000313|EMBL:AAF42147.1}; GN Name=pilP {ECO:0000313|EMBL:AAF42147.1}; GN OrderedLocusNames=NMB1811 {ECO:0000313|EMBL:AAF42147.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42147.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42147.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42147.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2IVW} RP STRUCTURE BY NMR OF 69-181. RX PubMed=17007878; DOI=10.1016/j.jmb.2006.08.078; RA Golovanov A.P., Balasingham S., Tzitzilonis C., Goult B.T., Lian L.Y., RA Homberset H., Tonjum T., Derrick J.P.; RT "The solution structure of a domain from the Neisseria meningitidis RT lipoprotein PilP reveals a new beta-sandwich fold."; RL J. Mol. Biol. 364:186-195(2006). RN [3] {ECO:0000213|PDB:4AV2} RP STRUCTURE BY ELECTRON MICROSCOPY (26.00 ANGSTROMS). RX PubMed=23028322; DOI=10.1371/journal.ppat.1002923; RA Berry J.L., Phelan M.M., Collins R.F., Adomavicius T., Tonjum T., RA Frye S.A., Bird L., Owens R., Ford R.C., Lian L.Y., Derrick J.P.; RT "Structure and assembly of a trans-periplasmic channel for type IV RT pili in Neisseria meningitidis."; RL PLoS Pathog. 8:e1002923-e1002923(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42147.1; -; Genomic_DNA. DR PIR; C81041; C81041. DR RefSeq; NP_274808.1; NC_003112.2. DR RefSeq; WP_002214522.1; NC_003112.2. DR PDB; 2IVW; NMR; -; A=69-181. DR PDB; 4AV2; EM; 26.00 A; M/N/O/P/Q/R/S/T/U/V/W/X=1-181. DR PDBsum; 2IVW; -. DR PDBsum; 4AV2; -. DR ProteinModelPortal; Q7DD77; -. DR SMR; Q7DD77; 69-181. DR IntAct; Q7DD77; 1. DR STRING; 122586.NMB1811; -. DR PaxDb; Q7DD77; -. DR EnsemblBacteria; AAF42147; AAF42147; NMB1811. DR GeneID; 903288; -. DR KEGG; nme:NMB1811; -. DR PATRIC; 20359591; VBINeiMen85645_2301. DR eggNOG; ENOG4105K8H; Bacteria. DR eggNOG; COG3168; LUCA. DR HOGENOM; HOG000281372; -. DR KO; K02665; -. DR OMA; CQANDES; -. DR OrthoDB; EOG6GBMC8; -. DR BioCyc; NMEN122586:GHGG-1866-MONOMER; -. DR EvolutionaryTrace; Q7DD77; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007446; Pilus_assembly_PilP. DR Pfam; PF04351; PilP; 1. DR PIRSF; PIRSF016481; Pilus_assembly_PilP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2IVW, ECO:0000213|PDB:4AV2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 181 AA; 20068 MW; F08ED4DBF0E4E27F CRC64; MKHYALLISF LALSACSQGS EDLNEWMAQT RREAKAEIIP FQAPTLPVAP VYSPPQLTGP NAFDFRRMET DKKGENAPDT KRIKETLEKF SLENMRYVGI LKSGQKVSGF IEAEGYVYTV GVGNYLGQNY GRIESITDDS IVLNELIEDS TGNWVSRKAE LLLNSSDKNT EQAAAPAAEQ N // ID Q9K0K7_NEIMB Unreviewed; 291 AA. AC Q9K0K7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAF41015.1}; GN OrderedLocusNames=NMB0587 {ECO:0000313|EMBL:AAF41015.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41015.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41015.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41015.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU003943}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003943}. CC -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. CC {ECO:0000256|RuleBase:RU003943}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41015.1; -; Genomic_DNA. DR PIR; H81179; H81179. DR RefSeq; NP_273631.1; NC_003112.2. DR RefSeq; WP_002222859.1; NC_003112.2. DR ProteinModelPortal; Q9K0K7; -. DR STRING; 122586.NMB0587; -. DR PaxDb; Q9K0K7; -. DR EnsemblBacteria; AAF41015; AAF41015; NMB0587. DR GeneID; 902702; -. DR KEGG; nme:NMB0587; -. DR PATRIC; 20356459; VBINeiMen85645_0749. DR eggNOG; ENOG4105CC5; Bacteria. DR eggNOG; COG1108; LUCA. DR HOGENOM; HOG000181428; -. DR KO; K02075; -. DR OMA; GVFVVWR; -. DR OrthoDB; EOG6GR389; -. DR BioCyc; NMEN122586:GHGG-613-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR InterPro; IPR001626; ABC_3. DR InterPro; IPR029022; ABC_BtuC-like. DR Pfam; PF00950; ABC-3; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003943}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 121 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 199 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 273 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 291 AA; 30755 MW; D3CF11FC63F794A6 CRC64; MNLYDLLLAP FAEFDFMRYA LASVFCLSLS AAPVGVFLVM RRMSLIGDAL SHAVLPGAAV GYMFAGLSLP AMGLGGVAAG MLMALLAGLV SRFTTLKEDA NFAAFYLSSL AIGVVLVSKN GSSVDLLHLL FGSVLAVDIP ALQLIAAVSS LTLITLAVIY RPLVLESIDP LFLKSVGGKG GLWHVLFLVL VVMNLVSGFQ ALGTLMSVGL MMLPAITARL WAKHMGALIL LSVLTALLCG LSGLLISYHI EIPSGPAIIL CCSVLYLFSV ILGKEGGILT KWLKNHRHHT T // ID Q9K0V6_NEIMB Unreviewed; 255 AA. AC Q9K0V6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40888.1}; GN OrderedLocusNames=NMB0451 {ECO:0000313|EMBL:AAF40888.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40888.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40888.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40888.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40888.1; -; Genomic_DNA. DR PIR; E81197; E81197. DR RefSeq; NP_273498.1; NC_003112.2. DR RefSeq; WP_002212540.1; NC_003112.2. DR STRING; 122586.NMB0451; -. DR PaxDb; Q9K0V6; -. DR EnsemblBacteria; AAF40888; AAF40888; NMB0451. DR GeneID; 902567; -. DR KEGG; nme:NMB0451; -. DR PATRIC; 20356116; VBINeiMen85645_0574. DR eggNOG; ENOG4107GJ0; Bacteria. DR eggNOG; COG0730; LUCA. DR HOGENOM; HOG000219093; -. DR KO; K07090; -. DR OMA; PETFRRW; -. DR OrthoDB; EOG6DG2S0; -. DR BioCyc; NMEN122586:GHGG-475-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002781; TM_pro_TauE-like. DR Pfam; PF01925; TauE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 245 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 255 AA; 28101 MW; 1D467BD7FC269D49 CRC64; MQEIMQSIVF VAAAILHGIT GMGFPMLGTT ALAFIMPLSK VVALVALPSL LMSLLVLCSN NKKGFWQEIV YYLKTYKLLA IGSVVGSILG VKLLLILPVS WLLLLMAIIT LYYSVNGILN VCAKAKNIQV VANNKNMVLF GFLAGIIGGS TNAMSPILLI FLLSETENKN RIVKSSNLCY LLAKIVQIYM LRDQYWLLNK SEYGLIFLLS VLSVIGLYVG IRLRTKISPN FFKMLIFIVL LVLALKIGHS GLIKL // ID Q9JZZ8_NEIMB Unreviewed; 321 AA. AC Q9JZZ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41245.1}; GN OrderedLocusNames=NMB0834 {ECO:0000313|EMBL:AAF41245.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41245.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41245.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41245.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41245.1; -; Genomic_DNA. DR PIR; B81153; B81153. DR RefSeq; NP_273875.1; NC_003112.2. DR RefSeq; WP_002216744.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ8; -. DR STRING; 122586.NMB0834; -. DR PaxDb; Q9JZZ8; -. DR EnsemblBacteria; AAF41245; AAF41245; NMB0834. DR GeneID; 902948; -. DR KEGG; nme:NMB0834; -. DR PATRIC; 20357055; VBINeiMen85645_1046. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; SIHERPP; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-865-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38034 MW; 4E79DDCA19C9134C CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDTLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JZC6_NEIMB Unreviewed; 186 AA. AC Q9JZC6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41504.1}; GN OrderedLocusNames=NMB1114 {ECO:0000313|EMBL:AAF41504.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41504.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41504.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41504.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41504.1; -; Genomic_DNA. DR PIR; D81119; D81119. DR RefSeq; NP_274144.1; NC_003112.2. DR RefSeq; WP_002222498.1; NC_003112.2. DR STRING; 122586.NMB1114; -. DR PaxDb; Q9JZC6; -. DR EnsemblBacteria; AAF41504; AAF41504; NMB1114. DR GeneID; 903536; -. DR KEGG; nme:NMB1114; -. DR PATRIC; 20357797; VBINeiMen85645_1414. DR eggNOG; ENOG4105G8H; Bacteria. DR eggNOG; COG3778; LUCA. DR HOGENOM; HOG000123636; -. DR OMA; DLKPAHT; -. DR OrthoDB; EOG66F05W; -. DR BioCyc; NMEN122586:GHGG-1150-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018755; Phage_Mu_Gp48. DR Pfam; PF10076; DUF2313; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 186 AA; 20472 MW; 4E4D86A473139B7C CRC64; MSYQDILRGL LPPVSYARNA PRVRAQAEID GAALDAVAES AQSVADAVDP RSAGQMLADW ERVLGLDGTG KNRQHRVLAV MAKLNETGGL SIPYFVRLAE AAGYQIQIDE PQPFRAGVNR AGDRLAPQEI MWVWHVNVRG GNNRITRFRA GISAAGDRLT DYSDAVIESL FNRLKPAHTA IRFTYR // ID Q7DD43_NEIMB Unreviewed; 123 AA. AC Q7DD43; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42424.1}; GN OrderedLocusNames=NMB2110 {ECO:0000313|EMBL:AAF42424.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42424.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42424.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42424.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42424.1; -; Genomic_DNA. DR PIR; C81004; C81004. DR RefSeq; NP_275097.1; NC_003112.2. DR RefSeq; WP_002218307.1; NC_003112.2. DR ProteinModelPortal; Q7DD43; -. DR STRING; 122586.NMB2110; -. DR PaxDb; Q7DD43; -. DR EnsemblBacteria; AAF42424; AAF42424; NMB2110. DR GeneID; 903922; -. DR KEGG; nme:NMB2110; -. DR PATRIC; 20360394; VBINeiMen85645_2693. DR eggNOG; ENOG4106XG7; Bacteria. DR eggNOG; ENOG410YXBT; LUCA. DR HOGENOM; HOG000218700; -. DR OrthoDB; EOG6C017S; -. DR BioCyc; NMEN122586:GHGG-2175-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1580.10; -; 1. DR InterPro; IPR018958; SMI1/KNR4-like_dom. DR Pfam; PF09346; SMI1_KNR4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 116 SMI1_KNR4. {ECO:0000259|Pfam:PF09346}. SQ SEQUENCE 123 AA; 14481 MW; D3CCAE02C46B2969 CRC64; MIKQNSFVPY PEAMLPKGFK YPQSYLKLAQ STHAINYDEQ YSFPWWFENA ESNISEVIDI YFEITGIPNL LPFARNQEWA ACFDISDKSG NPKIIVVNLD NTKYYETFEN FDTWLKEAEN DGW // ID Q9JZQ0_NEIMB Unreviewed; 467 AA. AC Q9JZQ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 100. DE SubName: Full=Putative 2-oxoglutarate dehydrogenase, E3 component, lipoamide dehydrogenase {ECO:0000313|EMBL:AAF41353.1}; GN OrderedLocusNames=NMB0947 {ECO:0000313|EMBL:AAF41353.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41353.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41353.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41353.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41353.1; -; Genomic_DNA. DR PIR; C81138; C81138. DR RefSeq; NP_273985.1; NC_003112.2. DR RefSeq; WP_010980874.1; NC_003112.2. DR ProteinModelPortal; Q9JZQ0; -. DR STRING; 122586.NMB0947; -. DR PaxDb; Q9JZQ0; -. DR EnsemblBacteria; AAF41353; AAF41353; NMB0947. DR GeneID; 903067; -. DR KEGG; nme:NMB0947; -. DR PATRIC; 20357375; VBINeiMen85645_1202. DR eggNOG; ENOG4105CCC; Bacteria. DR eggNOG; COG1249; LUCA. DR HOGENOM; HOG000276709; -. DR KO; K00382; -. DR OMA; IDDHTQI; -. DR OrthoDB; EOG6ZPSW0; -. DR BioCyc; NMEN122586:GHGG-984-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 3. DR SUPFAM; SSF55424; SSF55424; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 326 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. FT DOMAIN 349 457 Pyr_redox_dim. FT {ECO:0000259|Pfam:PF02852}. SQ SEQUENCE 467 AA; 50761 MW; 26237791AA516086 CRC64; MKKIQADVVV IGGGTAGMGA FRNARLHSDN VYLIENNVFG TTCARVGCMP SKLLIAAAEA RHHALHTDPF GVHLDKDSIV VNGEEVMQRV KSERDRFVGF VVADVEEWPA DKRIMGSAKF IDEHTVQIDE HTQITAKSFV IATGSRPVIL PQWQSLGNRL IINDDVFSWD TLPKRVAVFG PGVIGLELGQ ALHRLGVKVE IFGLGGIIGG ISDPVVSDEA NAVFGEELKL HLDAKTEVKL DADGNVEVHW EQDGEKGVFV AEYMLAAVGR RPNVDNIGLE NINIEKDARG VPVADPLTMQ TSIPHIFIAG DASNQLPLLH EAADQGKIAG DNAGRYPNIG GGLRRSTIGV VFTSPQIGFV GLKYAQVAAQ YQADEFVIGE VSFKNQGRSR VMLVNKGHMR LYAEKATGRF IGAEIVGPAA EHLAHLLAWA HQMKMTVPQM LDMPFYHPVI EEGLRTALRD ADAKLKA // ID Q9JYU4_NEIMB Unreviewed; 598 AA. AC Q9JYU4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:AAF41789.1}; GN OrderedLocusNames=NMB1428 {ECO:0000313|EMBL:AAF41789.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41789.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41789.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41789.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41789.1; -; Genomic_DNA. DR PIR; E81084; E81084. DR RefSeq; NP_274440.1; NC_003112.2. DR RefSeq; WP_002244167.1; NC_003112.2. DR ProteinModelPortal; Q9JYU4; -. DR STRING; 122586.NMB1428; -. DR PaxDb; Q9JYU4; -. DR EnsemblBacteria; AAF41789; AAF41789; NMB1428. DR GeneID; 903850; -. DR KEGG; nme:NMB1428; -. DR PATRIC; 20358553; VBINeiMen85645_1788. DR eggNOG; ENOG4107QW9; Bacteria. DR eggNOG; COG0006; LUCA. DR HOGENOM; HOG000255711; -. DR KO; K01262; -. DR OMA; YRPGKWG; -. DR OrthoDB; EOG6QZMPK; -. DR BioCyc; NMEN122586:GHGG-1466-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.350.10; -; 2. DR Gene3D; 3.90.230.10; -; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR028980; Creatinase/Aminopeptidase_P_N. DR InterPro; IPR000587; Creatinase_N. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR032416; Peptidase_M24_C. DR Pfam; PF01321; Creatinase_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF16188; Peptidase_M24_C; 1. DR SUPFAM; SSF53092; SSF53092; 2. DR SUPFAM; SSF55920; SSF55920; 1. PE 4: Predicted; KW Aminopeptidase {ECO:0000313|EMBL:AAF41789.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41789.1}; KW Protease {ECO:0000313|EMBL:AAF41789.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 130 Creatinase_N. {ECO:0000259|Pfam:PF01321}. FT DOMAIN 307 520 Peptidase_M24. FT {ECO:0000259|Pfam:PF00557}. FT DOMAIN 537 596 Peptidase_M24_C. FT {ECO:0000259|Pfam:PF16188}. SQ SEQUENCE 598 AA; 64852 MW; EDDEDC60895C272E CRC64; MNTVSNYLSA LREAMKAQGL DALVIPSADP HLSEYLPEHW QARRELSGFT GSVGTFVLTT DEAGVWVDSR YWEQAAKQLA GSGIVLQKSG QVPPYNEWLA ASLPENAAVG IPSDMVSLTG KRTLAQSLAA KNIRIEHPDN LLNQVWTNRP ALPAETVFIH DPDYVSETAA EKLARVRAVM AEKGADYHLV SSLDDIAWLT NLRGSDVPFN PVFVSFLLIG KDNAVLFTDR CRLNAEAAAA LQTAGIAVEP YAQVADKLAQ IGGVLLIEPN KTAVSTLVRL PESVRLIEGI NPSTLFKSCK SEADIARIRE AMEHDGAALC GFFAEFEDII GNGGSLTEID VDTMLYRHRS VRPGFISLSF DTIAGFNANG ALPHYSATPE SHSTISGNGL LLIDSGAQYK GGTTDITRVV PVGTPSAEQK SDNTLVLKAH IALAEAVFPE NIPSPLIDAI CRKPLWQAQC DYGHGTGHGV GYFLNVHEGP QRIAFAAPAT PETAMKKGMV TSIEPGLYRP GKWGIRIENL AANQAVAAPQ ETEFGSFLCF ETLTLCPIDT RLMDTALMTD GEIDWVNRYH AEVRRRLEPL TEGAAKAWLI KRTEPLAR // ID Q9JYN2_NEIMB Unreviewed; 175 AA. AC Q9JYN2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41858.1}; GN OrderedLocusNames=NMB1502 {ECO:0000313|EMBL:AAF41858.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41858.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41858.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41858.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41858.1; -; Genomic_DNA. DR PIR; B81075; B81075. DR RefSeq; NP_274510.1; NC_003112.2. DR RefSeq; WP_002238123.1; NC_003112.2. DR STRING; 122586.NMB1502; -. DR PaxDb; Q9JYN2; -. DR EnsemblBacteria; AAF41858; AAF41858; NMB1502. DR GeneID; 903936; -. DR KEGG; nme:NMB1502; -. DR HOGENOM; HOG000004538; -. DR OMA; IYILRIS; -. DR OrthoDB; EOG6Q8J9V; -. DR BioCyc; NMEN122586:GHGG-1542-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 57 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 175 AA; 20769 MW; E7696C5D6B47DF90 CRC64; MEFVNNLVIF SFLLLMLIPI FFVVYGIYHK IRYRKICILR TSFILLVVIL CSMYYIYCRY LDQQKVAYYC IDEQCISIVH LYKDYGINSP TYARIYAGKI LFRFQVRAKN YAELLMEDDI SISKKILGNK FIIYGSLPVI YGNVDNIEVK EATGYIDRSS TDYIVSRNLK FRHLY // ID Q9JZH7_NEIMB Unreviewed; 469 AA. AC Q9JZH7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:AAF41444.1}; DE EC=4.2.3.1 {ECO:0000313|EMBL:AAF41444.1}; GN Name=thrC {ECO:0000313|EMBL:AAF41444.1}; GN OrderedLocusNames=NMB1046 {ECO:0000313|EMBL:AAF41444.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41444.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41444.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41444.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41444.1; -; Genomic_DNA. DR PIR; F81127; F81127. DR RefSeq; NP_274080.1; NC_003112.2. DR RefSeq; WP_002244109.1; NC_003112.2. DR ProteinModelPortal; Q9JZH7; -. DR STRING; 122586.NMB1046; -. DR PaxDb; Q9JZH7; -. DR EnsemblBacteria; AAF41444; AAF41444; NMB1046. DR GeneID; 903183; -. DR KEGG; nme:NMB1046; -. DR PATRIC; 20357629; VBINeiMen85645_1331. DR eggNOG; ENOG4105D98; Bacteria. DR eggNOG; COG0498; LUCA. DR HOGENOM; HOG000230745; -. DR KO; K01733; -. DR OMA; PIFALNE; -. DR OrthoDB; EOG65BDJX; -. DR BioCyc; NMEN122586:GHGG-1083-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.1380.10; -; 1. DR InterPro; IPR029144; Thr_synth_N. DR InterPro; IPR004450; Thr_synthase-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR Pfam; PF14821; Thr_synth_N; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00260; thrC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF41444.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 79 Thr_synth_N. {ECO:0000259|Pfam:PF14821}. FT DOMAIN 102 335 PALP. {ECO:0000259|Pfam:PF00291}. SQ SEQUENCE 469 AA; 51619 MW; 8F62F8264342E1D2 CRC64; MKYISTRGET AHKPFSEVLL MGLAPDGGLM LPEHYPQIGR ETLDKWRGLA YPELAFEIMR LFVTDIPEDD LRDILNRTYT EAAFGTKEIT PVRTLSDGIK IQALSNGPTL AFKDMAMQFL GNAFEYVLNK EGKKLNILGA TSGDTGSAAE YALRGKKGVN VFMLSPDGKM SAFQRAQMYS LQDENIHNIA VKGMFDDCQD IVKAVQNDAA FKEKYHIGTV NSINWGRIVA QVVYYFAGYF NATSSNDETV SFCVPSGNFG NVCAGHIAKQ MGLPIRRLIV ATNENDVLDE FFKTGAYRPR NSAHTYVTSS PSMDISKASN FERFVFDLMD RDPAEINTLW AEVAAGKGFD LRFALDKVGG KYGFTSGKST HADRLATIKQ VYEQDQELID PHTADGVKVA REVREEGEMV VCLETALAAK FDATIREAVG DAAIPRPAAL EGLENLPQRV QTVPNSADAV KGIIEQTLA // ID Q9K1C5_NEIMB Unreviewed; 119 AA. AC Q9K1C5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40692.1}; GN OrderedLocusNames=NMB0237 {ECO:0000313|EMBL:AAF40692.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40692.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40692.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40692.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40692.1; -; Genomic_DNA. DR PIR; D81221; D81221. DR RefSeq; NP_273294.1; NC_003112.2. DR RefSeq; WP_002215099.1; NC_003112.2. DR STRING; 122586.NMB0237; -. DR PaxDb; Q9K1C5; -. DR EnsemblBacteria; AAF40692; AAF40692; NMB0237. DR GeneID; 902348; -. DR KEGG; nme:NMB0237; -. DR PATRIC; 20355548; VBINeiMen85645_0298. DR eggNOG; ENOG4106CPE; Bacteria. DR eggNOG; ENOG410Y1XS; LUCA. DR HOGENOM; HOG000218645; -. DR OrthoDB; EOG6GTZM7; -. DR BioCyc; NMEN122586:GHGG-252-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR028964; Imm8. DR Pfam; PF15586; Imm8; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 119 AA; 14200 MW; 6465624063C18745 CRC64; MIKLDLKSIN LYDIDFEKFT PEIPDNFHRW IDLDIGIEGE QGSSIFSLCI CSPKWISHHC NKEGFFWSNA LILEQFDHKI IKSEIDKILE YCSKETWDLT LSNLLRFFSW EFEDYNPNT // ID Q9K1J2_NEIMB Unreviewed; 47 AA. AC Q9K1J2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40588.1}; GN OrderedLocusNames=NMB0129 {ECO:0000313|EMBL:AAF40588.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40588.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40588.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40588.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40588.1; -; Genomic_DNA. DR PIR; F81235; F81235. DR RefSeq; NP_273187.1; NC_003112.2. DR RefSeq; WP_003690108.1; NC_003112.2. DR STRING; 122586.NMB0129; -. DR PaxDb; Q9K1J2; -. DR EnsemblBacteria; AAF40588; AAF40588; NMB0129. DR GeneID; 902237; -. DR KEGG; nme:NMB0129; -. DR BioCyc; NMEN122586:GHGG-139-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5553 MW; 25B5762F4F54C250 CRC64; MSKTVGIVRF NRNCPTQTVV LKHIARLLVR CLFRLPRWWD IVLVSCL // ID Q9JY49_NEIMB Unreviewed; 501 AA. AC Q9JY49; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Putative tspB protein {ECO:0000313|EMBL:AAF42090.1}; GN OrderedLocusNames=NMB1747 {ECO:0000313|EMBL:AAF42090.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42090.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42090.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42090.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42090.1; -; Genomic_DNA. DR PIR; B81048; B81048. DR RefSeq; NP_274748.1; NC_003112.2. DR RefSeq; WP_010980980.1; NC_003112.2. DR STRING; 122586.NMB1747; -. DR PaxDb; Q9JY49; -. DR EnsemblBacteria; AAF42090; AAF42090; NMB1747. DR GeneID; 903350; -. DR KEGG; nme:NMB1747; -. DR PATRIC; 20359461; VBINeiMen85645_2236. DR eggNOG; ENOG41067SK; Bacteria. DR eggNOG; ENOG410Y4J8; LUCA. DR HOGENOM; HOG000218809; -. DR OMA; YEYANCL; -. DR OrthoDB; EOG62NX16; -. DR BioCyc; NMEN122586:GHGG-1802-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR008708; Neisseria_TspB. DR Pfam; PF05616; Neisseria_TspB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 478 498 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 501 AA; 55807 MW; 676E578DA217E46D CRC64; MYALSEKYND NGFKAYKVLG EGGGIHTEYN YKFDKSLNLN VLESSTGARS LEKVPVKVTA SVSRAAVLSG VGKLARLGAK LSTRAVPYVG TALLAHDVYE TFKEDIQAQG YQYDPETDKF VKGYEYSNCL WYEDKRRINR TYGCYGVDSS IMRLMSDDSR FPEVKELMES QMYRLARPFW NWHKEELNKL SSLDWNNFVL NRCTFNWNGG DCLVNKGDDF RNGADFSLIR NSKYKEEMDA KKLEEILSLK VDANPDKYIK ATGYPGYSEK VEVAPGTKVN MGPVTDRNGN PVQVVATFGR DSQGNTTVDV QVIPRPDLTP GSAEAPNAQP LPEVSPAENP ANNPNPNENP GTSPNPEPDP DLNPDANPDT DGQPGTRPDS PAVPDRPNGR HRKERKEGED GGLLCDYFPE ILACQEMGKP SDGMFHDISI PQVIDDKTWS SHNFLPSNGV CPQPKTFHVF GRQYQASYEP LCVFAEKIRF AVLLAFIIMS AFVVFGSLKG K // ID Q9JZD6_NEIMB Unreviewed; 197 AA. AC Q9JZD6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41493.1}; GN OrderedLocusNames=NMB1102 {ECO:0000313|EMBL:AAF41493.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41493.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41493.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41493.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41493.1; -; Genomic_DNA. DR PIR; C81121; C81121. DR RefSeq; NP_274133.1; NC_003112.2. DR RefSeq; WP_002225239.1; NC_003112.2. DR STRING; 122586.NMB1102; -. DR PaxDb; Q9JZD6; -. DR EnsemblBacteria; AAF41493; AAF41493; NMB1102. DR GeneID; 903524; -. DR KEGG; nme:NMB1102; -. DR PATRIC; 20357768; VBINeiMen85645_1400. DR eggNOG; ENOG4105J8U; Bacteria. DR eggNOG; COG5003; LUCA. DR HOGENOM; HOG000219054; -. DR OMA; PTLEHIN; -. DR OrthoDB; EOG6C5RQC; -. DR BioCyc; NMEN122586:GHGG-1138-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014972; Phage_Mu_Gp37. DR Pfam; PF08873; DUF1834; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 197 AA; 21766 MW; EFA6892675DFFBC3 CRC64; MVRTVKSYNG EADDLAGQIH TLPAVWVTYG GSKVEPASTG GVCGRYQDTA EFVVMVAARN LRNEQAQRQG GIDSREIGSN DLIRAVRRLL DGQRLGFADS RGLVPKAVRA IANHVLVQNA AVSIYAVEYA IRFNTCGLEN DRYPERTDNP DDPNHIFTKY QGTLSEPWPD FEGLDGKIYD PQSADEIPVN LTLKDKQ // ID Q7DDI2_NEIMB Unreviewed; 72 AA. AC Q7DDI2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41455.1}; GN OrderedLocusNames=NMB1059 {ECO:0000313|EMBL:AAF41455.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41455.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41455.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41455.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41455.1; -; Genomic_DNA. DR PIR; E81126; E81126. DR RefSeq; NP_274092.1; NC_003112.2. DR RefSeq; WP_002213659.1; NC_003112.2. DR ProteinModelPortal; Q7DDI2; -. DR PaxDb; Q7DDI2; -. DR EnsemblBacteria; AAF41455; AAF41455; NMB1059. DR GeneID; 903476; -. DR KEGG; nme:NMB1059; -. DR PATRIC; 20357661; VBINeiMen85645_1347. DR eggNOG; COG2841; LUCA. DR HOGENOM; HOG000275055; -. DR KO; K09794; -. DR OMA; FERHNEL; -. DR OrthoDB; EOG63VC4F; -. DR BioCyc; NMEN122586:GHGG-1096-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007420; DUF465. DR Pfam; PF04325; DUF465; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 72 AA; 8250 MW; 3D0F137D23E8211C CRC64; MFPEYRDLIS KLKQENSRFA RLFDEHNELD DKITGLVNNP VTSGAETIDE LKKAKLKLKD ELYAILQKAA GK // ID Q9JXT9_NEIMB Unreviewed; 167 AA. AC Q9JXT9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42220.1}; GN OrderedLocusNames=NMB1886 {ECO:0000313|EMBL:AAF42220.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42220.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42220.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42220.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42220.1; -; Genomic_DNA. DR PIR; D81031; D81031. DR RefSeq; NP_274882.1; NC_003112.2. DR RefSeq; WP_002223047.1; NC_003112.2. DR ProteinModelPortal; Q9JXT9; -. DR STRING; 122586.NMB1886; -. DR PaxDb; Q9JXT9; -. DR EnsemblBacteria; AAF42220; AAF42220; NMB1886. DR GeneID; 904292; -. DR KEGG; nme:NMB1886; -. DR PATRIC; 20359807; VBINeiMen85645_2409. DR eggNOG; ENOG4108ZGC; Bacteria. DR eggNOG; COG1956; LUCA. DR HOGENOM; HOG000022909; -. DR KO; K07170; -. DR OMA; FQGQPAC; -. DR OrthoDB; EOG6QP15Z; -. DR BioCyc; NMEN122586:GHGG-1942-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.450.40; -; 1. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF_dom-like. DR Pfam; PF13185; GAF_2; 1. DR SMART; SM00065; GAF; 1. DR SUPFAM; SSF55781; SSF55781; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 31 165 GAF. {ECO:0000259|SMART:SM00065}. SQ SEQUENCE 167 AA; 18278 MW; 3C6E3573888C6275 CRC64; MHALHFSASD KAALYREVLP QIESVVADEA DWVANLANTA AVLKEAFGWF WVGFYLVDTR SDELVLAPFQ GPLACTRIPF GRGVCGQAWA KGETVVVKDV NAHPDHIACS SLSRSEIVVP LFSDGRCIGV LDADSEHLAQ FDETDALYLG ELAKILEKRF EASRQAV // ID Q9JXD2_NEIMB Unreviewed; 483 AA. AC Q9JXD2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=MafB protein {ECO:0000313|EMBL:AAF62340.1}; GN Name=mafB {ECO:0000313|EMBL:AAF62340.1}; GN OrderedLocusNames=NMB2105 {ECO:0000313|EMBL:AAF62340.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62340.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62340.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62340.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62340.1; -; Genomic_DNA. DR RefSeq; NP_275092.1; NC_003112.2. DR RefSeq; WP_002225727.1; NC_003112.2. DR PaxDb; Q9JXD2; -. DR EnsemblBacteria; AAF62340; AAF62340; NMB2105. DR GeneID; 903930; -. DR KEGG; nme:NMB2105; -. DR PATRIC; 20360384; VBINeiMen85645_2688. DR HOGENOM; HOG000218708; -. DR OMA; VRYDINI; -. DR OrthoDB; EOG680WXC; -. DR BioCyc; NMEN122586:GHGG-2170-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 483 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328293. SQ SEQUENCE 483 AA; 52789 MW; D6B5AEFA8AEBAA02 CRC64; MNLPIQKFMM LFAAAISLLQ IPISHANGLD ARLRDDMQAK HYEPGGKYHL FGNARGSVKK RVYAVQTFDA TAVSPVLPIT HERTGFEGVI GYETHFSGHG HEVHSPFDHH DSKSTSDFSG GVDGGFTVYQ LHRTGSEIHP EDGYDGPQGS DYPPPGGARD IYSYYVKGTS TKTKTNIVPQ APFSDRWLKE NAGAASGFFS RADEAGKLIW ESDPNKNWWA NRMDDVRGIV QGAVNPFLMG FQGVGIGAIT DSAVSPVTDT AAQQTLQGIN DLGKLSPEAQ LAAASLLQDS AFAVKDGINS AKQWADAHPN ITATAQTALS AAEAAGTVWR GKKVELNPTK WDWVKNTGYK KPAARHMQTL DGEMAGGNKP IKSLPNSAAE KRKQNFEKFN SNWSSASFDS VHKTLTPNAP GILSPDKVKT RYTSLDGKIT IIKDNENNYF RIHDNSRKQY LDSNGNAVKT GNLQGKQAKD YLQQQTHIRN LDK // ID Q9JYA8_NEIMB Unreviewed; 791 AA. AC Q9JYA8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Hemoglobin receptor {ECO:0000313|EMBL:AAF42017.1}; GN Name=hmbR {ECO:0000313|EMBL:AAF42017.1}; GN OrderedLocusNames=NMB1668 {ECO:0000313|EMBL:AAF42017.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42017.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42017.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42017.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU003357}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000256|RuleBase:RU003357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42017.1; -; Genomic_DNA. DR PIR; F81056; F81056. DR RefSeq; NP_274673.1; NC_003112.2. DR RefSeq; WP_002222141.1; NC_003112.2. DR ProteinModelPortal; Q9JYA8; -. DR STRING; 122586.NMB1668; -. DR PaxDb; Q9JYA8; -. DR EnsemblBacteria; AAF42017; AAF42017; NMB1668. DR GeneID; 903442; -. DR KEGG; nme:NMB1668; -. DR PATRIC; 20359276; VBINeiMen85645_2146. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR HOGENOM; HOG000152301; -. DR KO; K16087; -. DR OMA; DSSKHKY; -. DR OrthoDB; EOG6HB9KP; -. DR BioCyc; NMEN122586:GHGG-1722-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Receptor {ECO:0000313|EMBL:AAF42017.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 791 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327705. FT DOMAIN 46 158 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 490 790 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 791 AA; 89219 MW; F055F59A6A36ED3A CRC64; MKPLQMLPIA ALVGSIFGNP VLAADEAATE TTPVKAEIKA VRVKGQRNAP AAVERVNLNR IKQEMIRDNK DLVRYSTDVG LSDSGRHQKG FAVRGVEGNR VGVSIDGVNL PDSEENSLYA RYGNFNSSRL SIDPELVRNI EIVKGADSFN TGSGALGGGV NYQTLQGRDL LLDDRQFGVM MKNGYSTRNR EWTNTLGFGV SNDRVDAALL YSQRRGHETE SAGNRGYAVE GEGSGANIRG SARGIPDSSK HKYHSFLGKI AYQINDNHRI GASLNGQQGH NYTVEESYNL TASSWREADD VNRRRNANLF YEWMPDSNWL SSLKADFDYQ KTKVAAVNNK GSFPMDYSTW TRNYNQKDLD EIYNRSMDTR FKRFTLRLDS HPLQLGGGRH RLSFKTFVSR RDFENLNRDD YYFSGRVVRT TSSIQHPVKT TNYGFSLSDQ IQWNDVFSSR AGIRYDHTKM TPQELNAECH ACDKTPPAAN TYKGWSGFVG LAAQLNQAWR VGYDITSGYR VPNASEVYFT YNHGSGNWLP NPNLKAERST THTLSLQGRS EKGMLDANLY QSNYRNFLSE EQKLTTSGTP GCTEENAYYG ICSDPYKEKL DWQMKNIDKA RIRGIELTGR LNVDKVASFV PEGWKLFGSL GYAKSKLSGD NSLLSTQPLK VIAGIDYESP SEKWGVFSRL TYLGAKKVKD AQYTVYENKG WGTPLQKKVK DYPWLNKSAY VFDMYGFYKP AKNLTLRAGV YNLFNRKYTT WDSLRGLYSY STTNAVDRDG KGLDRYRAPG RNYAVSLEWK F // ID Q9K076_NEIMB Unreviewed; 119 AA. AC Q9K076; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41155.1}; GN OrderedLocusNames=NMB0742 {ECO:0000313|EMBL:AAF41155.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41155.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41155.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41155.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41155.1; -; Genomic_DNA. DR PIR; E81162; E81162. DR RefSeq; NP_273784.1; NC_003112.2. DR RefSeq; WP_002247553.1; NC_003112.2. DR STRING; 122586.NMB0742; -. DR PaxDb; Q9K076; -. DR EnsemblBacteria; AAF41155; AAF41155; NMB0742. DR GeneID; 902857; -. DR KEGG; nme:NMB0742; -. DR PATRIC; 20356855; VBINeiMen85645_0946. DR eggNOG; ENOG4105MNW; Bacteria. DR eggNOG; COG3536; LUCA. DR HOGENOM; HOG000261620; -. DR OMA; TAINLHK; -. DR OrthoDB; EOG6DNTDC; -. DR BioCyc; NMEN122586:GHGG-773-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010376; DUF971. DR Pfam; PF06155; DUF971; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 91 DUF971. {ECO:0000259|Pfam:PF06155}. SQ SEQUENCE 119 AA; 13346 MW; 91EB40C5D69EA0E5 CRC64; MNNIPVEIRL LKNRTVLVLT YGDEPKNLPA EFLRVYSPSA EVRGHGVGQD VLQTGKADVQ IADLQPVGQY ALKISFSDGH DSGLYDWAYL HRLAYGYDAM WQEYLDKLAA AGASRFEEK // ID Q4W588_NEIMB Unreviewed; 135 AA. AC Q4W588; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52143.1}; GN OrderedLocusNames=NMB0023 {ECO:0000313|EMBL:AAY52143.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52143.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52143.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52143.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52143.1; -; Genomic_DNA. DR RefSeq; WP_002221782.1; NC_003112.2. DR RefSeq; YP_338288.1; NC_003112.2. DR ProteinModelPortal; Q4W588; -. DR SMR; Q4W588; 1-117. DR STRING; 122586.NMB0023; -. DR PaxDb; Q4W588; -. DR EnsemblBacteria; AAY52143; AAY52143; NMB0023. DR GeneID; 902126; -. DR KEGG; nme:NMB0023; -. DR PATRIC; 20354993; VBINeiMen85645_0033. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR OMA; ANGRKTT; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-24-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 135 AA; 14356 MW; A126D34C9B24EB2D CRC64; MAEGQKSAVT EYYLNHGEWP GNNTSAGVAS SSTIKGKYVK EVTVANGVIT ATMLSSGVNK EIQGKKLSLW AKRQDGSVKW FCGQPVTRTD AKADTVAAAA KTADNINTKH LPSTCRDASS VVCIETPPTA FYKNT // ID Q9K008_NEIMB Unreviewed; 130 AA. AC Q9K008; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41233.1}; GN OrderedLocusNames=NMB0820 {ECO:0000313|EMBL:AAF41233.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41233.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41233.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41233.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41233.1; -; Genomic_DNA. DR PIR; C81154; C81154. DR RefSeq; NP_273862.1; NC_003112.2. DR RefSeq; WP_002213939.1; NC_003112.2. DR STRING; 122586.NMB0820; -. DR PaxDb; Q9K008; -. DR EnsemblBacteria; AAF41233; AAF41233; NMB0820. DR GeneID; 902935; -. DR KEGG; nme:NMB0820; -. DR PATRIC; 20357023; VBINeiMen85645_1030. DR HOGENOM; HOG000218660; -. DR OMA; CPTHEVV; -. DR OrthoDB; EOG65F8VK; -. DR BioCyc; NMEN122586:GHGG-851-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007929; DUF723. DR Pfam; PF05265; DUF723; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 130 AA; 14531 MW; 815F92A1A2CA1046 CRC64; MGKRMTFDTA KSRFQEKFPH LELLEFSGIY KPSSVRCPTH GVVQLLYYDT AIKSKYGCPE CGKLKMKENT PPQNQKPVSI LDTATGETLT FPSVQAAAKA LNTPYGSIRT KLDGRSNPDN LVCNRYKVLL // ID Q7DD42_NEIMB Unreviewed; 89 AA. AC Q7DD42; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42425.1}; GN OrderedLocusNames=NMB2112 {ECO:0000313|EMBL:AAF42425.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42425.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42425.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42425.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42425.1; -; Genomic_DNA. DR PIR; D81004; D81004. DR RefSeq; NP_275099.1; NC_003112.2. DR RefSeq; WP_002224189.1; NC_003112.2. DR PaxDb; Q7DD42; -. DR EnsemblBacteria; AAF42425; AAF42425; NMB2112. DR GeneID; 903919; -. DR KEGG; nme:NMB2112; -. DR PATRIC; 20360398; VBINeiMen85645_2695. DR HOGENOM; HOG000218705; -. DR OMA; VNRVYTY; -. DR OrthoDB; EOG606593; -. DR BioCyc; NMEN122586:GHGG-2177-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 89 AA; 10448 MW; E20797E0913BD40D CRC64; MMTESHGYLS NNLPVKIIND IIYATQLVED LVLGKIKIVD FLKSYNNFYC WLGFDELPQS EKIKFLSYLN ILSIHKEIQD ETVNRVYTD // ID Q9K1K4_NEIMB Unreviewed; 180 AA. AC Q9K1K4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40572.1}; GN OrderedLocusNames=NMB0113 {ECO:0000313|EMBL:AAF40572.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40572.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40572.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40572.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40572.1; -; Genomic_DNA. DR PIR; C81236; C81236. DR RefSeq; NP_273171.1; NC_003112.2. DR RefSeq; WP_010980754.1; NC_003112.2. DR STRING; 122586.NMB0113; -. DR PaxDb; Q9K1K4; -. DR EnsemblBacteria; AAF40572; AAF40572; NMB0113. DR GeneID; 902217; -. DR KEGG; nme:NMB0113; -. DR PATRIC; 20355239; VBINeiMen85645_0153. DR eggNOG; ENOG4108VD5; Bacteria. DR eggNOG; ENOG4111KFK; LUCA. DR HOGENOM; HOG000266169; -. DR OMA; WKRFTFT; -. DR OrthoDB; EOG65XN25; -. DR BioCyc; NMEN122586:GHGG-119-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025500; DUF4390. DR Pfam; PF14334; DUF4390; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 180 AA; 19759 MW; D9F456092699027E CRC64; MLPAFQNVAA EGIDVSRAEA RITDGGQLSI SSRFQTELPD QLQQALRRGV PLNFTLSWQL SAPIIASYRF KLGQLIGDDD NIDYKLSFHP LTNRYRVTVG AFSTDYDTLD AALRATGAVA NWKVLNKGAL SGAEAGETKA EIRLTLSTSK LPKPFQINAL TSQNWHLDSG WKPLNIIGNK // ID Q9JZF1_NEIMB Unreviewed; 390 AA. AC Q9JZF1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 80. DE SubName: Full=Putative bacteriophage DNA transposition protein B {ECO:0000313|EMBL:AAF41475.1}; GN OrderedLocusNames=NMB1083 {ECO:0000313|EMBL:AAF41475.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41475.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41475.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41475.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41475.1; -; Genomic_DNA. DR PIR; E81122; E81122. DR RefSeq; NP_274115.1; NC_003112.2. DR RefSeq; WP_002225250.1; NC_003112.2. DR ProteinModelPortal; Q9JZF1; -. DR STRING; 122586.NMB1083; -. DR PaxDb; Q9JZF1; -. DR EnsemblBacteria; AAF41475; AAF41475; NMB1083. DR GeneID; 903500; -. DR KEGG; nme:NMB1083; -. DR PATRIC; 20357721; VBINeiMen85645_1377. DR eggNOG; ENOG4108XHG; Bacteria. DR eggNOG; COG2842; LUCA. DR KO; K07132; -. DR OMA; MQDSKAK; -. DR OrthoDB; EOG64R633; -. DR BioCyc; NMEN122586:GHGG-1119-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR014875; Mor_transcription_activator. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13401; AAA_22; 1. DR Pfam; PF08765; Mor; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 70 HTH cro/C1-type DNA-binding. FT {ECO:0000259|SMART:SM00530}. SQ SEQUENCE 390 AA; 43090 MW; FEDCA790AA959D61 CRC64; MKQINQALQQ KLVEFKEKSG MNQTQLARGI GTSPASISMY LNGTYAEKGG NYETIEPKIE AFLEMQDSKA QREELVLGFV STKTTRRIAE VMRDAHEGGE TVVIYGQAGL GKTQAVKNYC EKNPAAILIE ANPSFTALVL MRKLATAAKV SAMGSLNDLF ESVSDRLRDS GRLIVVDEAE NLPLRALEIV RRLHDETGCG LVLSGMPRLV ANLRGKHGEL VQLYSRVSVA LNLGESLPDD ELFEIAKAAL PDAVKHLLPD SVQALITVIG FNETLELVRL MGGTTYPLRQ GYTKNSQSRV AYLEEIIGSE AAGRLVEAMA PCNLFIPRCE TALYELRNRK IRSQFDRQTA GGTPAYEAVN DLALAHRLSD RHVWRILKQA DKEAEQENLF // ID Q9JY02_NEIMB Unreviewed; 371 AA. AC Q9JY02; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=PilM protein {ECO:0000313|EMBL:AAF42145.1}; GN Name=pilM {ECO:0000313|EMBL:AAF42145.1}; GN OrderedLocusNames=NMB1808 {ECO:0000313|EMBL:AAF42145.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42145.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42145.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42145.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42145.1; -; Genomic_DNA. DR PIR; A81041; A81041. DR RefSeq; NP_274805.1; NC_003112.2. DR RefSeq; WP_002214517.1; NC_003112.2. DR ProteinModelPortal; Q9JY02; -. DR STRING; 122586.NMB1808; -. DR PaxDb; Q9JY02; -. DR EnsemblBacteria; AAF42145; AAF42145; NMB1808. DR GeneID; 903290; -. DR KEGG; nme:NMB1808; -. DR PATRIC; 20359585; VBINeiMen85645_2298. DR eggNOG; COG4972; LUCA. DR HOGENOM; HOG000218782; -. DR KO; K02662; -. DR OMA; ANQYIPF; -. DR OrthoDB; EOG66QM0S; -. DR BioCyc; NMEN122586:GHGG-1863-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005883; PilM. DR Pfam; PF11104; PilM_2; 1. DR PIRSF; PIRSF019169; PilM; 1. DR TIGRFAMs; TIGR01175; pilM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 371 AA; 41367 MW; 94CFF451B4FBD372 CRC64; MRLFKSLKNP KKTDAKLPKK SSGLNNRAAI GIDIDQHSIK MVQLSGRSLN QIQLEKYVIA KLPKNIIQGN KVQNYDQLVT YLQQAYAKLG TSCKNIIASV PQNLATIEQL TYTDKDAELD LQGFVESSIS EVSSISLEEA NYDYQVLSQS AAGEAVLAVA SRKDEIEPLI DAFNAAGMKL SALDVDIFGQ YNAYALWINH FAPELAAEKV AIFGVYAAQT YALVIQDGKI LYKQETSVSE EQLNQLIQRT YQVTEEKAEE IINSPQKPSD YQESVANYFN QQITQEIQRV LQFYYTTQTA DDMTDIKHIL LTGEAARQEG IAQTVASQTN ADVQCVHPAR YFADNLKTDK QQFELDAPTL TRAFGLAVRG L // ID Q9K112_NEIMB Unreviewed; 558 AA. AC Q9K112; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF40827.1}; GN OrderedLocusNames=NMB0387 {ECO:0000313|EMBL:AAF40827.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40827.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40827.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40827.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40827.1; -; Genomic_DNA. DR PIR; H81205; H81205. DR RefSeq; NP_273436.1; NC_003112.2. DR RefSeq; WP_002243991.1; NC_003112.2. DR ProteinModelPortal; Q9K112; -. DR STRING; 122586.NMB0387; -. DR PaxDb; Q9K112; -. DR EnsemblBacteria; AAF40827; AAF40827; NMB0387. DR GeneID; 902502; -. DR KEGG; nme:NMB0387; -. DR PATRIC; 20355937; VBINeiMen85645_0486. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR HOGENOM; HOG000271639; -. DR KO; K06020; -. DR OMA; KVIEFQD; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NMEN122586:GHGG-409-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR022374; ABC_ATP-bd_ChvD. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03719; ABC_ABC_ChvD; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40827.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40827.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 262 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 327 553 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 558 AA; 62072 MW; 755930C62A5AE9FC CRC64; MSQQYVYSML RVSKVVPPQK TIIKDISLSF FPGAKIGLLG LNGAGKSTVL RIMAGVDKEF EGEAVPMGGI KIGYLPQEPE LDPEKTVREE VESGLGEVAA AQKRLEEVYA EYANPDADFD ALAEEQGRLE AIIAAGSSTG GGAEHELEIA ADALRLPEWD AKIDNLSGGE KRRVALCKLL LSKPDMLLLD EPTNHLDAES VEWLEQFLVR FPGTVVAVTH DRYFLDNAAE WILELDRGHG IPWKGNYSSW LEQKEKRLEN EAKSEAARVK AMKQELEWVR QNAKGRQAKS KARLARFEEM SNYEYQKRNE TQEIFIPVAE RLGNEVIEFV NVSKSFGDKV LIDDLSFKVP AGAIVGIIGP NGAGKSTLFK MISGKEQPDS GEVKIGQTVK MSLIDQSREG LQNDKTVFDN IAEGRDILQV GQFEIPARQY LGRFNFKGSD QSKIAGQLSG GERGRLHLAK TLLSGGNVLL LDEPSNDLDV ETLRALEDAL LEFAGSVMVI SHDRWFLDRI ATHILACEGD SKWVFFDGNY QEYEADKKRR LGEEGAKPKR IKYKPVTR // ID Q9JZS7_NEIMB Unreviewed; 78 AA. AC Q9JZS7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=PemI protein {ECO:0000313|EMBL:AAF41322.1}; GN Name=pemI {ECO:0000313|EMBL:AAF41322.1}; GN OrderedLocusNames=NMB0914 {ECO:0000313|EMBL:AAF41322.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41322.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41322.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41322.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41322.1; -; Genomic_DNA. DR PIR; D81142; D81142. DR RefSeq; NP_273954.1; NC_003112.2. DR RefSeq; WP_002222638.1; NC_003112.2. DR ProteinModelPortal; Q9JZS7; -. DR STRING; 122586.NMB0914; -. DR PaxDb; Q9JZS7; -. DR EnsemblBacteria; AAF41322; AAF41322; NMB0914. DR GeneID; 903035; -. DR KEGG; nme:NMB0914; -. DR PATRIC; 20357263; VBINeiMen85645_1145. DR eggNOG; ENOG4107FKI; Bacteria. DR eggNOG; COG2336; LUCA. DR HOGENOM; HOG000289070; -. DR KO; K18842; -. DR OMA; CDTKAFF; -. DR OrthoDB; EOG6Z3KS9; -. DR BioCyc; NMEN122586:GHGG-952-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR InterPro; IPR007159; SpoVT-AbrB_dom. DR Pfam; PF04014; MazE_antitoxin; 1. DR SMART; SM00966; SpoVT_AbrB; 1. DR PROSITE; PS51740; SPOVT_ABRB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 47 SpoVT-AbrB. FT {ECO:0000259|PROSITE:PS51740}. SQ SEQUENCE 78 AA; 8798 MW; B6AD1ED460D817C6 CRC64; MLRVQKWGNS AAVRLPADML KQLDFKIGDA LVAEVHNGEL RVRAARRFRL ADLLAEMEET PPRVEGWEIL DDAGNEVV // ID Q9K0X0_NEIMB Unreviewed; 213 AA. AC Q9K0X0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40874.1}; GN OrderedLocusNames=NMB0436 {ECO:0000313|EMBL:AAF40874.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40874.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40874.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40874.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains YrdC-like domain. CC {ECO:0000256|SAAS:SAAS00501982}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40874.1; -; Genomic_DNA. DR PIR; E81198; E81198. DR RefSeq; NP_273484.1; NC_003112.2. DR RefSeq; WP_010980794.1; NC_003112.2. DR ProteinModelPortal; Q9K0X0; -. DR SMR; Q9K0X0; 8-211. DR STRING; 122586.NMB0436; -. DR PaxDb; Q9K0X0; -. DR EnsemblBacteria; AAF40874; AAF40874; NMB0436. DR GeneID; 902552; -. DR KEGG; nme:NMB0436; -. DR PATRIC; 20356076; VBINeiMen85645_0553. DR eggNOG; ENOG4107RTD; Bacteria. DR eggNOG; COG0009; LUCA. DR HOGENOM; HOG000076162; -. DR OMA; HPKKKTV; -. DR OrthoDB; EOG6C5RT4; -. DR BioCyc; NMEN122586:GHGG-460-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00057; TIGR00057; 1. DR PROSITE; PS51163; YRDC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 21 206 YrdC-like. {ECO:0000259|PROSITE:PS51163}. SQ SEQUENCE 213 AA; 23415 MW; C4B17295E9F7194D CRC64; MTIRKQTMAQ FFAIHPDNPQ ERLIKQAVEI VNKGGVVVYP TDSCYALGCK LGDKAAMERI LSIRKIDLKH HLTLMCADLS ELGTYAKVDN VQFRQLKAAT PGPYTFILQA TKDVPARTLH PKRKTIGLRI PDNAIAQALL GELGEPLLSC TLMLPEDGEP LTDPYEIRER LEHAVDLVID GGWCGTEPTT VVDMTDGTEL VRQGCGDTAV FGL // ID Q9K0G2_NEIMB Unreviewed; 608 AA. AC Q9K0G2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=MafB-related protein {ECO:0000313|EMBL:AAF62313.1}; GN OrderedLocusNames=NMB0643 {ECO:0000313|EMBL:AAF62313.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62313.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62313.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62313.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62313.1; -; Genomic_DNA. DR RefSeq; NP_273686.1; NC_003112.2. DR RefSeq; WP_002244044.1; NC_003112.2. DR STRING; 122586.NMB0643; -. DR PaxDb; Q9K0G2; -. DR EnsemblBacteria; AAF62313; AAF62313; NMB0643. DR GeneID; 902755; -. DR KEGG; nme:NMB0643; -. DR PATRIC; 20356587; VBINeiMen85645_0812. DR eggNOG; ENOG4106WPA; Bacteria. DR eggNOG; ENOG410ZMD6; LUCA. DR HOGENOM; HOG000220700; -. DR OMA; TQREWEN; -. DR OrthoDB; EOG64R617; -. DR BioCyc; NMEN122586:GHGG-670-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR003115; ParB/Sulfiredoxin_dom. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. DR SUPFAM; SSF110849; SSF110849; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 608 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328364. SQ SEQUENCE 608 AA; 66593 MW; AC6D4599E358BC55 CRC64; MGISRKISLI LSILAVCLPM HAHASDLAND SFIRQVLDRQ HFEPDGKYHL FGSRGELAER SGHIGLGKIQ SHQLGNLMIQ QAAIKGNIGY IVRFSDHGHE VHSPFDNHAS HSDSDEAGSP VDGFSLYRIH WDGYEHHPAD GYDGPQGGGY PAPKGARDIY SYDIKGVAQN IRLNLTDNRS TGQRLADRFH NAGSMLTQGV GDGFKRATRY SPELDRSGNA AEAFNGTADI VKNIIGAAGE IVGAGDAVQG ISEGSNIAVM HGLGLLSTEN KMARINDLAD MAQLKDYAAA AIRDWAVQNP NAAQGIEAVS NIFMAAIPIK GIGAVRGKYG LGGITAHPIK RSQMGAIALP KGKSAVSDNF ADAAYAKYPS PYHSRNIRSN LEQRYGKENI TSSTVPPSNG KNVKLADQRH PKTGVPFDGK GFPNFEKHVK YDTKLDIQEL SGGGIPKAKP VFDAKPRWEV DRKLNKLTTR EQVEKNVQEI RNGNINSNFS QHAQLEREIN KLKSADEINF ADGMGKFTDS MNDKAFSRLV KSVKENGFTN PVVEYVEING KAYIVRGNNR VFAAEYLGRI HELKFKKVDF PVPNTSWKNP TDVLNESGNV KRPRYRSK // ID Q9JZV3_NEIMB Unreviewed; 204 AA. AC Q9JZV3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative type IV pilus assembly protein PilV {ECO:0000313|EMBL:AAF41297.1}; GN OrderedLocusNames=NMB0887 {ECO:0000313|EMBL:AAF41297.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41297.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41297.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41297.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41297.1; -; Genomic_DNA. DR PIR; F81145; F81145. DR RefSeq; NP_273928.1; NC_003112.2. DR RefSeq; WP_010980865.1; NC_003112.2. DR STRING; 122586.NMB0887; -. DR PaxDb; Q9JZV3; -. DR EnsemblBacteria; AAF41297; AAF41297; NMB0887. DR GeneID; 903006; -. DR KEGG; nme:NMB0887; -. DR PATRIC; 20357181; VBINeiMen85645_1104. DR eggNOG; COG4967; LUCA. DR HOGENOM; HOG000218894; -. DR KO; K02671; -. DR OMA; IHYAVCK; -. DR OrthoDB; EOG680X1B; -. DR BioCyc; NMEN122586:GHGG-923-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR013362; Pilus_4_PilV. DR TIGRFAMs; TIGR02523; type_IV_pilV; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 204 AA; 22122 MW; 5BD194556F5F6DAC CRC64; MNMKNNDCFR LKDSQSGMAL IEVLVAMLVL TIGILALLSV QLRTVASVRE AETQTIVSQI TQNLMEGMLM NPTIDSDSNK KNYNLYMGNH TLSAVDGDFA IDAMKTKGQL AEAQLKRFSY ELKNALPDAA AIHYAVCKDS SGNAPTLSGN AFSSNCDNKA NGDTLIKVLW VNDSAGDSDI SRTNLEVSGD NIVYTYQARV GGRE // ID Q9JXR5_NEIMB Unreviewed; 135 AA. AC Q9JXR5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42247.1}; GN OrderedLocusNames=NMB1917 {ECO:0000313|EMBL:AAF42247.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42247.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42247.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42247.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42247.1; -; Genomic_DNA. DR PIR; D81029; D81029. DR RefSeq; NP_274911.1; NC_003112.2. DR RefSeq; WP_002225818.1; NC_003112.2. DR STRING; 122586.NMB1917; -. DR PaxDb; Q9JXR5; -. DR EnsemblBacteria; AAF42247; AAF42247; NMB1917. DR GeneID; 904245; -. DR KEGG; nme:NMB1917; -. DR PATRIC; 20359881; VBINeiMen85645_2445. DR eggNOG; ENOG4107QHA; Bacteria. DR eggNOG; COG3326; LUCA. DR HOGENOM; HOG000267103; -. DR OMA; PFRRWFF; -. DR OrthoDB; EOG6X6RHM; -. DR BioCyc; NMEN122586:GHGG-1974-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010718; DUF1294. DR Pfam; PF06961; DUF1294; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 111 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 135 AA; 14841 MW; 70B59B1E5981F6B3 CRC64; MKRQAFFKLM ACAAFLSAVS LRLPVLGACY AILSLYAFAL YGIDKRCAIR GQRRIPEHRL LLPALLGGWV GAYFGSMTFK HKTAKKRFVV LFRLTVSGNV LATLILIYSG LNLNQYGVAS PCRTICTVCG FVALS // ID Q9K0W5_NEIMB Unreviewed; 270 AA. AC Q9K0W5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Nitrilase {ECO:0000313|EMBL:AAF40879.1}; GN OrderedLocusNames=NMB0441 {ECO:0000313|EMBL:AAF40879.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40879.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40879.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40879.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40879.1; -; Genomic_DNA. DR PIR; B81199; B81199. DR RefSeq; NP_273489.1; NC_003112.2. DR RefSeq; WP_002222048.1; NC_003112.2. DR ProteinModelPortal; Q9K0W5; -. DR STRING; 122586.NMB0441; -. DR PaxDb; Q9K0W5; -. DR EnsemblBacteria; AAF40879; AAF40879; NMB0441. DR GeneID; 902557; -. DR KEGG; nme:NMB0441; -. DR PATRIC; 20356088; VBINeiMen85645_0559. DR eggNOG; ENOG4107QPI; Bacteria. DR eggNOG; COG0388; LUCA. DR HOGENOM; HOG000222700; -. DR KO; K01501; -. DR OMA; MCESNST; -. DR OrthoDB; EOG6CVV93; -. DR BioCyc; NMEN122586:GHGG-465-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; -; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR001110; UPF0012_CS. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. DR PROSITE; PS01227; UPF0012; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 270 CN hydrolase. FT {ECO:0000259|PROSITE:PS50263}. SQ SEQUENCE 270 AA; 29264 MW; 7E9F9B4E8BB7A3F8 CRC64; MDKIRVAAVQ MVSGVSPETN VAAMKRLVAR AAEQGADWVL LPEYWVLMGA NDTDKLALAE PLGGGRFQTA LSETAKECGV VLFGGTVPLQ SCEAGKVMNT LLVYGRDGVR TGLYHKMHLF GFSGLGERYA EADTIRAGGD VPHLSAEGVP VAAGICYDVR FPEFFRRQLP FDVLMLPAAF THTTGKAHWE LLLRARAVEN QCYVVAAAQG GLHENGRRTF GHSMIVDPWG DVLDVLPEGE GVVTADIDAN RLNSVRNRLP ALKYRVLDAV // ID Q9K0S1_NEIMB Unreviewed; 162 AA. AC Q9K0S1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40939.1}; GN OrderedLocusNames=NMB0507 {ECO:0000313|EMBL:AAF40939.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40939.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40939.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40939.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40939.1; -; Genomic_DNA. DR PIR; B81191; B81191. DR RefSeq; NP_273553.1; NC_003112.2. DR RefSeq; WP_002244018.1; NC_003112.2. DR STRING; 122586.NMB0507; -. DR PaxDb; Q9K0S1; -. DR EnsemblBacteria; AAF40939; AAF40939; NMB0507. DR GeneID; 902623; -. DR KEGG; nme:NMB0507; -. DR PATRIC; 20356260; VBINeiMen85645_0650. DR eggNOG; ENOG4105WS9; Bacteria. DR eggNOG; ENOG41123TY; LUCA. DR HOGENOM; HOG000218790; -. DR OMA; MATHREF; -. DR OrthoDB; EOG6G4W10; -. DR BioCyc; NMEN122586:GHGG-532-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 162 AA; 19568 MW; EB0828C477F38508 CRC64; MKKDIFYCEQ WSYGYKKLHK PFSEKQAEEK HLKGELYTAV IGSATQPEYV ITLREEVGFF SVHFFDKFGR DYLTHQFQKY SNSNYYFLSM AVWRDYITLE SHDLAEGYTY FFNENTDDCY VLKEDFINNE RYEKTELYSQ KDKVILFPKF GEYDLVLNPD II // ID Q9JZQ7_NEIMB Unreviewed; 278 AA. AC Q9JZQ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41344.1}; GN OrderedLocusNames=NMB0938 {ECO:0000313|EMBL:AAF41344.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41344.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41344.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41344.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41344.1; -; Genomic_DNA. DR PIR; G81139; G81139. DR RefSeq; NP_273976.1; NC_003112.2. DR RefSeq; WP_010980873.1; NC_003112.2. DR STRING; 122586.NMB0938; -. DR PaxDb; Q9JZQ7; -. DR EnsemblBacteria; AAF41344; AAF41344; NMB0938. DR GeneID; 903058; -. DR KEGG; nme:NMB0938; -. DR PATRIC; 20357349; VBINeiMen85645_1189. DR HOGENOM; HOG000218900; -. DR OMA; CTSLHPA; -. DR OrthoDB; EOG6V7BJZ; -. DR BioCyc; NMEN122586:GHGG-975-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 278 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329355. SQ SEQUENCE 278 AA; 31190 MW; 47DA082B1D14474C CRC64; MKNKTSSLLL WLTAIMLTAC SPSKDDKTKE VGASAASSSA SSAPSQTDLQ PTASAPDNVK QAESAPPSNC TSLHPATGID DLMQQIAEHI DSDCLFALSH HELETRFGLP DGGYDNIQRL LFPDIRPEDP DYHQKIILAI EDLRYGKRTI SRQAQNALME QERRLREATL LLIQGSQETR GQGEEPKRTR YFEVSATPAY SSRHNNGLGG NFQYISQLPG YLKIHGEMLE NQSLFRLSNR ERNPDKPFLD IHFDENGKIT RIVVYEKNIY FNPNTGRI // ID Q9JZZ6_NEIMB Unreviewed; 769 AA. AC Q9JZZ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:AAF41247.1}; GN Name=clpA {ECO:0000313|EMBL:AAF41247.1}; GN OrderedLocusNames=NMB0836 {ECO:0000313|EMBL:AAF41247.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41247.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41247.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41247.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. CC {ECO:0000256|RuleBase:RU004432}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41247.1; -; Genomic_DNA. DR PIR; D81153; D81153. DR RefSeq; NP_273877.1; NC_003112.2. DR RefSeq; WP_010980857.1; NC_003112.2. DR ProteinModelPortal; Q9JZZ6; -. DR SMR; Q9JZZ6; 179-370. DR STRING; 122586.NMB0836; -. DR PaxDb; Q9JZZ6; -. DR EnsemblBacteria; AAF41247; AAF41247; NMB0836. DR GeneID; 902950; -. DR KEGG; nme:NMB0836; -. DR PATRIC; 20357059; VBINeiMen85645_1048. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR HOGENOM; HOG000218210; -. DR KO; K03694; -. DR OMA; RTHLKNF; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; NMEN122586:GHGG-867-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR013461; ClpA. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR028299; ClpA/B_CS2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF02861; Clp_N; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR TIGRFAMs; TIGR02639; ClpA; 1. DR PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698, ECO:0000313|EMBL:AAF41247.1}; KW Chaperone {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00480820}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41247.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698, ECO:0000313|EMBL:AAF41247.1}; KW Protease {ECO:0000313|EMBL:AAF41247.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Repeat {ECO:0000256|SAAS:SAAS00417491}. FT DOMAIN 217 361 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 498 647 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 664 755 ClpB_D2-small. FT {ECO:0000259|SMART:SM01086}. SQ SEQUENCE 769 AA; 85080 MW; 264D4D4FC8978BA7 CRC64; MLAPELEQIL QQLYREARKA HYEFISLEHL LLVLIEEDAS VHNVLKLCGA DLKVVSEQLA ASVAENTPLI PEHLLDTVET RPTLGFQRVM QRAMVHTQSA GKAAVEPLDV LVALMSETDS HTVYFLKLQS VTRFEVLRCI AHGSPDEDED EDEDEDDGNY SSDGMDDDNG NRTKPGKNPL SAYTVNLNAE VKAGRIDPLI GRKHEMERLV QILCRRRKNN PLLVGEAGVG KTALAEGLAH QIVNGGIPDA LKDAEVYALD MGSLLAGTKY RGDFEARVKS VLKQLEKIPH AILFIDEIHT IIGAGSTSGG TMDASNLLKP ALAKGSLRCI GATTYDEYRT IFDKDHALSR RFQKIDVVEP TVSETVQILR GLKPMFEAFH QVRYTQGALE AAAELSARYI NERFLPDKAI DVMDEAGAEQ RILPKSKQKK VIGKAQIETV IAKVARIPEK TVSHDDKQVL QFLGRDLKNM VYGQENAIDA LVAAVKMSRS GLALPDKPIG SFLFSGPTGV GKTEVAKQLA YSMGVPLQRF DMSEYMERHA VSRLIGAPPG YVGFEQGGLL TEAINKQPHC VLLLDEIEKA HPDIFNVLLQ VMDAGKLTDN NGKSADFRNV ILIMTTNAGA ESLSRPSLGF TAKRERGDEM QAINKLFTPE FRNRLDAIIP FAPLSEPVIT KVVDKFLLQL EHRLLDKKVE AEFTSALHKY LAEKGFDPQM GARPMHRLIQ EKIRKPLADE LLFGKLSDGG FVRIDWDAAK EEAVLKFKKS KVKIKTASA // ID Q4W584_NEIMB Unreviewed; 225 AA. AC Q4W584; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 39. DE SubName: Full=Polysialic acid capsule biosynthesis protein SiaD, truncation disrupted by foreign ermC (NMB0066) cassette {ECO:0000313|EMBL:AAY52157.1}; GN OrderedLocusNames=NMB0067 {ECO:0000313|EMBL:AAY52157.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52157.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52157.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52157.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52157.1; -; Genomic_DNA. DR RefSeq; NP_273131.1; NC_003112.2. DR RefSeq; WP_010980749.1; NC_003112.2. DR STRING; 122586.NMB0067; -. DR PaxDb; Q4W584; -. DR EnsemblBacteria; AAY52157; AAY52157; NMB0067. DR GeneID; 903210; -. DR KEGG; nme:NMB0067; -. DR eggNOG; ENOG41060HX; Bacteria. DR eggNOG; ENOG41129DG; LUCA. DR OrthoDB; EOG6F2947; -. DR BioCyc; NMEN122586:GHGG-73-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010866; A-2_8-polyST. DR Pfam; PF07388; A-2_8-polyST; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 225 AA; 26411 MW; 10AC083AF47F34B8 CRC64; MLKKIKKALF QPKKFFQDSM WLTTSPFYLT PPRNNLFVIS NLGQLNQVQS LIKIQKLTNN LLVILYTSKN LKMPKLVHQS ANKNLFESIY LFELPRSPNN ITPKKLLYIY RSYKKILNII QPAHLYMLSF TGHYSYLISI AKKKNITTHL IDEGTGTYAP LLESFSYHPT KLERYLIGNN LNIKGYIDHF DILHVPFPEY AKKIFNAKKY NRFFAWRKGD VLQGD // ID Q9JZD0_NEIMB Unreviewed; 718 AA. AC Q9JZD0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41499.1}; GN OrderedLocusNames=NMB1108 {ECO:0000313|EMBL:AAF41499.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41499.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41499.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41499.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41499.1; -; Genomic_DNA. DR PIR; A81122; A81122. DR RefSeq; NP_274139.1; NC_003112.2. DR RefSeq; WP_010980892.1; NC_003112.2. DR STRING; 122586.NMB1108; -. DR PaxDb; Q9JZD0; -. DR EnsemblBacteria; AAF41499; AAF41499; NMB1108. DR GeneID; 903530; -. DR KEGG; nme:NMB1108; -. DR PATRIC; 20357782; VBINeiMen85645_1407. DR OMA; NGENAVQ; -. DR OrthoDB; EOG6MPWT9; -. DR BioCyc; NMEN122586:GHGG-1144-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 718 AA; 75544 MW; 17EA0017C905877A CRC64; MKLSLVLTAR DDGARRLLAD TQRQLDRTAK SRAQLERQSH TYALTGIRSE KQIQREIMLT QAAFNRLARS GKASQNDLAR AAVATRNRIR ELNAELKQGT GFADKMGKIG RFGAAAVAGG AAAYTVLKPA MDNRKQLDEN INRVSRQAFI EDNSKSAAWI ATEGAQQIKD LALELVEKNG GTHDKALDLI SGMMTTGLNF AQTKNEAQAA YAFALASEGS GEDTAKLIKT LKDGGMSGKD LQLGLEHVLQ SGLDGTFEVR DMVRELPSLL SAAQQAGMNG VGGLDYLLSL LQSAANKSGS PAEAATNVQN LLSKTLSPDT IGRLKKMANP NDPKKGVDWI GSVVQGKQNG ENAVQVLSRL ADAMLVKDKQ YQDYKKRAAA GDKTAAEQAN MLKGALLAQL LPDLQAKQGL LAATDMTQIR EYMASLAGVT LDNGKIAKNN EARMLSAAAQ QEQQESLAML RESLTGTLVD METSFKKLAA EYPNATLALQ ALTTAATAAS AAMLLTAGGG KGAGFLKDVG SKALGWGKAS AGGVAAGATA AGGKLLSWGK SAGSGLMNNP ALVKRAGLLG MLLYSESLGD GTLPKGLRGT KTTPEMINRL KNNGIRFEPA PKREQARGGV PQYLAAPSAQ PTDKMLSPLF STQTAAYQAA IQQQTAAYQA ALAQDTAAVT TGLAQVQSAM ASASQTINTN VSLNIDGRVI ANEVSRYQVA MFGRGAGQ // ID Q9K1J0_NEIMB Unreviewed; 85 AA. AC Q9K1J0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40593.1}; GN OrderedLocusNames=NMB0134 {ECO:0000313|EMBL:AAF40593.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40593.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40593.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40593.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40593.1; -; Genomic_DNA. DR PIR; G81233; G81233. DR RefSeq; NP_273192.1; NC_003112.2. DR RefSeq; WP_002224772.1; NC_003112.2. DR STRING; 122586.NMB0134; -. DR PaxDb; Q9K1J0; -. DR EnsemblBacteria; AAF40593; AAF40593; NMB0134. DR GeneID; 902242; -. DR KEGG; nme:NMB0134; -. DR PATRIC; 20355289; VBINeiMen85645_0174. DR HOGENOM; HOG000218663; -. DR OMA; SKNIFFM; -. DR OrthoDB; EOG6QP14J; -. DR BioCyc; NMEN122586:GHGG-144-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 85 AA; 9025 MW; B036A99522009A02 CRC64; MKPRNLFFAG CLLTSATFAE DIGVPVELIN VGNRIAMPSE GESLALLPFA EDVPPVRDAM PSEVPKSAAG GDVRGDRMRM PINIG // ID Q9JZS9_NEIMB Unreviewed; 208 AA. AC Q9JZS9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41320.1}; GN OrderedLocusNames=NMB0912 {ECO:0000313|EMBL:AAF41320.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41320.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41320.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41320.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41320.1; -; Genomic_DNA. DR PIR; B81142; B81142. DR RefSeq; NP_273952.1; NC_003112.2. DR RefSeq; WP_010980869.1; NC_003112.2. DR PaxDb; Q9JZS9; -. DR EnsemblBacteria; AAF41320; AAF41320; NMB0912. DR GeneID; 903033; -. DR KEGG; nme:NMB0912; -. DR PATRIC; 20357259; VBINeiMen85645_1143. DR HOGENOM; HOG000220735; -. DR OMA; GTHRFPT; -. DR OrthoDB; EOG6M0T67; -. DR BioCyc; NMEN122586:GHGG-950-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 65 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 105 139 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 208 AA; 23217 MW; 6827C33E6899821D CRC64; MGTHRFPTQQ PATQPDTDRN QEKRQNRVSA RAASLRSSEM DILLKYWKPV GVLLLIVLIF TAWHFDRAEK YRMGREAAAA EISNRLKDGY IEQAKQARSA EQKAAAAFAE RQTKLEEEKQ NAEKTVAAMR LELNRLRHYA AAQNRNRNLP ATATAATASD GASDSQGWLL FGQCAEKYAG LAETADGHAA DLREWQAYGH AVSSQRAE // ID Q9JZE4_NEIMB Unreviewed; 196 AA. AC Q9JZE4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41485.1}; GN OrderedLocusNames=NMB1093 {ECO:0000313|EMBL:AAF41485.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41485.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41485.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41485.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41485.1; -; Genomic_DNA. DR PIR; G81123; G81123. DR RefSeq; NP_274125.1; NC_003112.2. DR RefSeq; WP_002222513.1; NC_003112.2. DR STRING; 122586.NMB1093; -. DR PaxDb; Q9JZE4; -. DR EnsemblBacteria; AAF41485; AAF41485; NMB1093. DR GeneID; 903514; -. DR KEGG; nme:NMB1093; -. DR OrthoDB; EOG6716TR; -. DR BioCyc; NMEN122586:GHGG-1129-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 196 AA; 21593 MW; EFDF0CEF1A2C73B6 CRC64; MNWLNRGIQE KILRVLSDNY PNCLKATKVY NSLFPSSSLP ITSNIPVDKQ GLGLALTLGC EIQSQHLATL QSDEFQYFLK NIYYLEESGL IEITSIDSLH KNFDCKINHK GIDFLTDDGG LSAILGVVTV KLHSDTIQAL IAAKIDQAEI SDSEKSWLKK ELGKIKDTAL STLTENAINA IPAATLITLL KKFVGL // ID Q9K0P9_NEIMB Unreviewed; 459 AA. AC Q9K0P9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Na+/H+ antiporter {ECO:0000313|EMBL:AAF40965.1}; GN OrderedLocusNames=NMB0536 {ECO:0000313|EMBL:AAF40965.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40965.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40965.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40965.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40965.1; -; Genomic_DNA. DR PIR; G81187; G81187. DR RefSeq; NP_273581.1; NC_003112.2. DR RefSeq; WP_002225586.1; NC_003112.2. DR PaxDb; Q9K0P9; -. DR EnsemblBacteria; AAF40965; AAF40965; NMB0536. DR GeneID; 902651; -. DR KEGG; nme:NMB0536; -. DR PATRIC; 20356329; VBINeiMen85645_0683. DR eggNOG; ENOG4105DFD; Bacteria. DR eggNOG; COG1757; LUCA. DR HOGENOM; HOG000283662; -. DR KO; K03315; -. DR OMA; TCGAYMA; -. DR OrthoDB; EOG61GG5F; -. DR BioCyc; NMEN122586:GHGG-562-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015297; F:antiporter activity; IEA:InterPro. DR InterPro; IPR004770; Na/H_antiport_NhaC. DR InterPro; IPR018461; Na/H_Antiport_NhaC-like_C. DR Pfam; PF03553; Na_H_antiporter; 1. DR TIGRFAMs; TIGR00931; antiport_nhaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 233 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 315 337 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 432 454 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 162 454 Na_H_antiporter. FT {ECO:0000259|Pfam:PF03553}. SQ SEQUENCE 459 AA; 49445 MW; 3819498356544011 CRC64; MFAFKSLLDM PRGEALAVVV ALIAAMGYTI ISLEWLPHMS IIAAIVVLIL YGLARGLKYN DMQQGMIGAL NQGMGAIYLF FFIGLMVSAL MMSGAIPTLM YYGFGLISPT YFYFSSFALC SVIGVSIGSS LTTCATVGVA FMGMAAAFQA DMAMTAGAIV SGAFFGDKMS PLSDTTGISA SIVGIDLFEH IKNMMYTTIP AWLISAALML WLLPNVAAQD LNSVESFRSQ LEATGLVHGY SLIPFALLVI LALMRINAVV AMLFTVMVAV AVTYLHSTPD LRQLGAWFYG GYKLEGEAFK DVVKLISRGG LESMFFTQTI VILGMSLGGL LFALGVIPSL LEAIRTFLTN AGRATFSVAM TSVGVNFLIG EQYLSILLSG ETFKPVYDKL GLHSRNLSRT LEDAGTVINP LVPWSVCGVF ISHALGVPVW EYLPYAFFCY LSLALTLLFG WTGLTLSKK // ID Q9JZZ9_NEIMB Unreviewed; 128 AA. AC Q9JZZ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Type I restriction enzyme-related protein {ECO:0000313|EMBL:AAF41244.1}; GN OrderedLocusNames=NMB0833 {ECO:0000313|EMBL:AAF41244.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41244.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41244.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41244.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41244.1; -; Genomic_DNA. DR PIR; A81153; A81153. DR RefSeq; NP_273874.1; NC_003112.2. DR RefSeq; WP_002244075.1; NC_003112.2. DR STRING; 122586.NMB0833; -. DR PaxDb; Q9JZZ9; -. DR EnsemblBacteria; AAF41244; AAF41244; NMB0833. DR GeneID; 902947; -. DR KEGG; nme:NMB0833; -. DR PATRIC; 20357053; VBINeiMen85645_1045. DR eggNOG; COG0610; LUCA. DR OMA; SQCIANK; -. DR OrthoDB; EOG60CWZS; -. DR BioCyc; NMEN122586:GHGG-864-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR Pfam; PF04313; HSDR_N; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 29 114 HSDR_N. {ECO:0000259|Pfam:PF04313}. FT COILED 51 74 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 128 AA; 15065 MW; 4EFE8FFA8C7534D5 CRC64; MNLETKPIAE TPNFIVLDQY EKIEQSGSYQ SENRLEAELI ADLQNQGYEY RKDLNSQSRL LENLRAQLQR LNDVAFSDGE WARFLTEYLD RPSENITDKT RKIHDDHIYD FAFDDGPWIR ISSATLVY // ID Q9JZ71_NEIMB Unreviewed; 97 AA. AC Q9JZ71; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41642.1}; GN OrderedLocusNames=NMB1265 {ECO:0000313|EMBL:AAF41642.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41642.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41642.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41642.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41642.1; -; Genomic_DNA. DR PIR; C81102; C81102. DR RefSeq; NP_274286.1; NC_003112.2. DR RefSeq; WP_002222402.1; NC_003112.2. DR ProteinModelPortal; Q9JZ71; -. DR STRING; 122586.NMB1265; -. DR PaxDb; Q9JZ71; -. DR EnsemblBacteria; AAF41642; AAF41642; NMB1265. DR GeneID; 903687; -. DR KEGG; nme:NMB1265; -. DR PATRIC; 20358145; VBINeiMen85645_1584. DR eggNOG; ENOG4105VF2; Bacteria. DR eggNOG; COG1669; LUCA. DR HOGENOM; HOG000029676; -. DR KO; K07075; -. DR OMA; ARPIHEA; -. DR OrthoDB; EOG657JFW; -. DR BioCyc; NMEN122586:GHGG-1303-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 29 94 NTP_transf_2. {ECO:0000259|Pfam:PF01909}. SQ SEQUENCE 97 AA; 10622 MW; 3A22C63B9DB448CC CRC64; MKPSLLLQSR KKEILAVFGK YPLICNPRVF GSVSRGDDTE NSDIDLLVDA KTGTTLLDLG GLQEELQKLL GIKVDLLTPD DISAHFRDKV LTEAVAL // ID Q9JZ65_NEIMB Unreviewed; 47 AA. AC Q9JZ65; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41649.1}; GN OrderedLocusNames=NMB1272 {ECO:0000313|EMBL:AAF41649.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41649.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41649.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41649.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41649.1; -; Genomic_DNA. DR PIR; B81103; B81103. DR RefSeq; NP_274293.1; NC_003112.2. DR RefSeq; WP_010980914.1; NC_003112.2. DR STRING; 122586.NMB1272; -. DR PaxDb; Q9JZ65; -. DR EnsemblBacteria; AAF41649; AAF41649; NMB1272. DR GeneID; 903694; -. DR KEGG; nme:NMB1272; -. DR PATRIC; 20358161; VBINeiMen85645_1592. DR HOGENOM; HOG000027818; -. DR OrthoDB; EOG6997F5; -. DR BioCyc; NMEN122586:GHGG-1310-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 47 AA; 5500 MW; 580F194E7A07724B CRC64; MMLNQGFCEA FIVVVLMGIA AIMRKRPYFF KPPHRFRVCP SSRPDLQ // ID Q9K0Y5_NEIMB Unreviewed; 198 AA. AC Q9K0Y5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40857.1}; GN OrderedLocusNames=NMB0419 {ECO:0000313|EMBL:AAF40857.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40857.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40857.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40857.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40857.1; -; Genomic_DNA. DR PIR; F81200; F81200. DR RefSeq; NP_273467.1; NC_003112.2. DR RefSeq; WP_002220370.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y5; -. DR STRING; 122586.NMB0419; -. DR PaxDb; Q9K0Y5; -. DR EnsemblBacteria; AAF40857; AAF40857; NMB0419. DR GeneID; 902535; -. DR KEGG; nme:NMB0419; -. DR PATRIC; 20356032; VBINeiMen85645_0531. DR eggNOG; ENOG4105EUU; Bacteria. DR eggNOG; COG0790; LUCA. DR HOGENOM; HOG000003584; -. DR KO; K07126; -. DR OMA; HYPSQAR; -. DR OrthoDB; EOG6HJ27Z; -. DR BioCyc; NMEN122586:GHGG-443-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF08238; Sel1; 4. DR SMART; SM00671; SEL1; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 198 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329380. SQ SEQUENCE 198 AA; 22131 MW; 1A2D35C71E817813 CRC64; MKQTVKWLAA ALIALGLNRA VWADDVSDFR ENLQAAAQGN AAAQYNLGAM YYKGRGVRRD DAEAVRWYRQ AAEQGLAQAQ YNLGWMYANG RGVRQDDTEA VRWYRQAAAQ GVVQAQYNLG VIYAEGRGVR QDDVEAVRWF RQAAAQGVAQ AQNNLGVMYA ERRGVRQDRA LAQEWFGKAC QNGDQDGCDN DQRLKAGY // ID Q9JXZ7_NEIMB Unreviewed; 473 AA. AC Q9JXZ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAF42153.1}; GN OrderedLocusNames=NMB1818 {ECO:0000313|EMBL:AAF42153.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42153.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42153.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42153.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42153.1; -; Genomic_DNA. DR PIR; C81039; C81039. DR RefSeq; NP_274815.1; NC_003112.2. DR RefSeq; WP_002225655.1; NC_003112.2. DR STRING; 122586.NMB1818; -. DR PaxDb; Q9JXZ7; -. DR EnsemblBacteria; AAF42153; AAF42153; NMB1818. DR GeneID; 903282; -. DR KEGG; nme:NMB1818; -. DR PATRIC; 20359621; VBINeiMen85645_2316. DR eggNOG; ENOG4108NKX; Bacteria. DR eggNOG; COG2244; LUCA. DR HOGENOM; HOG000218779; -. DR OMA; LFCTLVE; -. DR OrthoDB; EOG6R87BG; -. DR BioCyc; NMEN122586:GHGG-1873-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 172 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 229 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 316 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 356 375 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 400 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 473 AA; 50747 MW; FE688CBA98D5E2E9 CRC64; MDTKEILGYA AGSIGSAVLA VIILPLLSWY FPADDIGRIV LMQTAAGLTV SVLCLGLDQA YVREYYATAD KDTLFKTLFL PPLLSAAAIA ALLLSRPSLP SEILFSLDDA AAGIGLVLFE LSFLPIRFLL LVLRMEGRAL AFSSAQLVPK LAILLLLPLT VGLLHFPANT AVLTAVYALA NLAAAAFLLF QNRCRLKAVR HAPFSPAVLH RGLRYGIPIA LSSIAYWGLA SADRLFLKKY AGLEQLGVYS MGISFGGAAL LFQSIFSTVW TPYIFRAIEE NAPPARLSAT AESAAALLAS ALCLTGIFSP LASLLLPENY AAVRFIVVSC MLPPLFCTLA EISGIGLNVV RKTRPIALAT LGALAANLLL LGLAVPSGGA RGAAVACAAS FWLFFAFKTE SSCRLWQPLK RLPLYLHTLF CLTSSAAYTC FGTPANYPLF AGVWAAYLAG CILRHRKDLH KLFHYLKKQG FPL // ID Q9JZN1_NEIMB Unreviewed; 127 AA. AC Q9JZN1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41383.1}; GN OrderedLocusNames=NMB0979 {ECO:0000313|EMBL:AAF41383.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41383.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41383.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41383.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41383.1; -; Genomic_DNA. DR PIR; E81134; E81134. DR RefSeq; NP_274016.1; NC_003112.2. DR RefSeq; WP_002225309.1; NC_003112.2. DR ProteinModelPortal; Q9JZN1; -. DR STRING; 122586.NMB0979; -. DR PaxDb; Q9JZN1; -. DR EnsemblBacteria; AAF41383; AAF41383; NMB0979. DR GeneID; 903099; -. DR KEGG; nme:NMB0979; -. DR PATRIC; 20357447; VBINeiMen85645_1238. DR eggNOG; ENOG4105QVA; Bacteria. DR eggNOG; COG3686; LUCA. DR HOGENOM; HOG000168796; -. DR OMA; NHFEAFP; -. DR OrthoDB; EOG6DRPJH; -. DR BioCyc; NMEN122586:GHGG-1016-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.550; -; 1. DR InterPro; IPR023352; MAPEG-like_dom. DR InterPro; IPR001129; Membr-assoc_MAPEG. DR Pfam; PF01124; MAPEG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 127 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327862. FT TRANSMEM 82 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 126 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 127 AA; 13572 MW; 6BF495901DF48CB9 CRC64; MTFAYWCILI ACLLPLFCAA YAKKAGGFRF KDNHNPRGFL AHTQGAAARA HAAQQNGFEA FAPFAAAVLT AHATGNAAQS TINTLACLFI LFRLAFIWCY IADKAAMRSL MWAGGFACTV GLFVAAA // ID Q9K0A1_NEIMB Unreviewed; 251 AA. AC Q9K0A1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41129.1}; GN OrderedLocusNames=NMB0714 {ECO:0000313|EMBL:AAF41129.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41129.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41129.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41129.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41129.1; -; Genomic_DNA. DR PIR; A81167; A81167. DR STRING; 122586.NMB0714; -. DR PaxDb; Q9K0A1; -. DR EnsemblBacteria; AAF41129; AAF41129; NMB0714. DR eggNOG; COG2354; LUCA. DR HOGENOM; HOG000244091; -. DR OMA; MPPETAQ; -. DR OrthoDB; EOG63FW29; -. DR BioCyc; NMEN122586:GHGG-742-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008526; YedI. DR Pfam; PF05661; DUF808; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 251 AA; 27888 MW; 2B4AA0112360050F CRC64; MAFASLFTLP DDITAVLDDV ALMTKAAAKK TAGVVGDDLA PNANRVTGVS AERELPIVWS MAKGSFSNKP VLVPAALLLS AFLPQLITPL LTAGGIYLCF EGVEKLLHKF LHRHDAHARN GGNRHRHDCF GVRNRCRHRQ TRRLRHAADA PPTNLFAQFG ANADCLYALL YARFERGRHA CHVSYRRRTG RPQPRPSARF PARATLGRWL GGVLRQPRCR AAFRFDCLRP RLAADESFRQ ALIPFSNTDA V // ID Q9JXU8_NEIMB Unreviewed; 671 AA. AC Q9JXU8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Prolyl oligopeptidase family protein {ECO:0000313|EMBL:AAF42211.1}; GN OrderedLocusNames=NMB1877 {ECO:0000313|EMBL:AAF42211.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42211.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42211.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42211.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42211.1; -; Genomic_DNA. DR PIR; C81033; C81033. DR RefSeq; NP_274873.1; NC_003112.2. DR RefSeq; WP_002225789.1; NC_003112.2. DR ProteinModelPortal; Q9JXU8; -. DR STRING; 122586.NMB1877; -. DR ESTHER; neime-NMB1877; S9N_PPCE_Peptidase_S9. DR PaxDb; Q9JXU8; -. DR EnsemblBacteria; AAF42211; AAF42211; NMB1877. DR GeneID; 904309; -. DR KEGG; nme:NMB1877; -. DR PATRIC; 20359785; VBINeiMen85645_2398. DR eggNOG; ENOG4108IE3; Bacteria. DR eggNOG; COG1505; LUCA. DR HOGENOM; HOG000238966; -. DR KO; K01322; -. DR OMA; YGPAWHQ; -. DR OrthoDB; EOG6VB6QV; -. DR BioCyc; NMEN122586:GHGG-1933-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR023302; Pept_S9A_N. DR InterPro; IPR001375; Peptidase_S9. DR InterPro; IPR002470; Peptidase_S9A. DR PANTHER; PTHR11757; PTHR11757; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR Pfam; PF02897; Peptidase_S9_N; 1. DR PRINTS; PR00862; PROLIGOPTASE. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 403 Peptidase_S9_N. FT {ECO:0000259|Pfam:PF02897}. FT DOMAIN 467 670 Peptidase_S9. {ECO:0000259|Pfam:PF00326}. SQ SEQUENCE 671 AA; 74663 MW; 76FFDED5F71F98BA CRC64; MKSYPDPYRH FENLDSAETQ NFAAEANAET RARFLENDKA RALSDGILAQ LQDTRQIPFC QEHRARMYHF HQDAEYPKGV YRVCTAATYR SGYPEWKILF SVADFDELLG DDVYLGGVSH LVEQPNRALL TLSKLGSDTA YTLEVDLEAG ELVEGGFHFP AGKNHVSWRD ENSVWVCPAW NERQLTQSGY PREVWLVERG KSFEESLPVY QIGEDGMMVN AWRYLDPQGS PIDLIEASDG FYTKTYLRVS AEGEAKPLNL PNDCDVVGYL AGHLLLTLRK DWNRANQSYP SGALVAVKLN RGELGAAQLL FAPDETQALE SVETTKRFVV ASLLENVQGR LKAWRFADGK WQEVELPRLP SGALEMTDQP WGGDVVYLAA SDFTTPLTLF ALDLNVMELT VMRRQPQQFD SDGINVQQFW TTSADGERIP YFHVGKNAAP DMPTLVYAYG GFGIPELPHY LGSIGKYWLE EGNAFVLANI RGGGEFGPRW HQAAQGISKH KSVDDLLAVV RDLSERGISS PEHIGLQGGS NGGLITAAAF VREPQSIGAL VCEVPLTDMI RYPLLSAGSS WTDEYGNPQK YEVCKRRLGE LSPYHNLSDG IDYPPALITT SLSDDRVHPA HALKFYAKLR ETSAQSWLYS PDGGGHTGNG TQRESADELA CVLLFLKEFL G // ID Q9K0P3_NEIMB Unreviewed; 67 AA. AC Q9K0P3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40971.1}; GN OrderedLocusNames=NMB0542 {ECO:0000313|EMBL:AAF40971.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40971.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40971.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40971.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40971.1; -; Genomic_DNA. DR PIR; D81186; D81186. DR RefSeq; NP_273587.1; NC_003112.2. DR RefSeq; WP_002225583.1; NC_003112.2. DR ProteinModelPortal; Q9K0P3; -. DR STRING; 122586.NMB0542; -. DR PaxDb; Q9K0P3; -. DR EnsemblBacteria; AAF40971; AAF40971; NMB0542. DR GeneID; 902657; -. DR KEGG; nme:NMB0542; -. DR PATRIC; 20356343; VBINeiMen85645_0690. DR eggNOG; COG4391; LUCA. DR HOGENOM; HOG000263985; -. DR OMA; PYCGTEY; -. DR OrthoDB; EOG6TTVTH; -. DR BioCyc; NMEN122586:GHGG-568-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.60.260.40; -; 1. DR InterPro; IPR019401; Znf_CHCC. DR Pfam; PF10276; zf-CHCC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 55 zf-CHCC. {ECO:0000259|Pfam:PF10276}. SQ SEQUENCE 67 AA; 7497 MW; B082AE6A3DB4B63C CRC64; MDNLNPQEIS VLPENLPLYC SGPGNEQWNG HPRVFLPLCE GESGSVACPY CGTRYRLDGK MPHHHYA // ID Q9JYR6_NEIMB Unreviewed; 207 AA. AC Q9JYR6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Putative transglycosylase {ECO:0000313|EMBL:AAF41821.1}; GN OrderedLocusNames=NMB1462 {ECO:0000313|EMBL:AAF41821.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41821.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41821.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41821.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41821.1; -; Genomic_DNA. DR PIR; C81080; C81080. DR RefSeq; NP_274473.1; NC_003112.2. DR RefSeq; WP_002219051.1; NC_003112.2. DR ProteinModelPortal; Q9JYR6; -. DR STRING; 122586.NMB1462; -. DR PaxDb; Q9JYR6; -. DR DNASU; 903884; -. DR EnsemblBacteria; AAF41821; AAF41821; NMB1462. DR GeneID; 903884; -. DR KEGG; nme:NMB1462; -. DR PATRIC; 20358671; VBINeiMen85645_1845. DR eggNOG; ENOG4108Y9W; Bacteria. DR eggNOG; COG0741; LUCA. DR HOGENOM; HOG000219015; -. DR OMA; QVMPFWT; -. DR OrthoDB; EOG6S52QZ; -. DR BioCyc; NMEN122586:GHGG-1502-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 207 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329344. FT DOMAIN 95 189 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 207 AA; 23488 MW; 0996EDC8D100EB5A CRC64; MRKPTDTLPV NLQRRRLLCA AGALLLSPLA HAGAQREETL ADDVASVMRS SVGSVNPPRL VFDNPKEGER WLSAMSARLA RFVPEEEERR RLLVNIQYES SRAGLDTQIV LGLIEVESAF RQYAISGVGA RGLMQVMPFW KNYIGKPAHN LFDIRTNLRY GCTILRHYRN LEKGNIVRAL ARFNGSLGSN KYPNAVLGAW RNRWQWR // ID Q9JZH8_NEIMB Unreviewed; 264 AA. AC Q9JZH8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41443.1}; GN OrderedLocusNames=NMB1045 {ECO:0000313|EMBL:AAF41443.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41443.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41443.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41443.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41443.1; -; Genomic_DNA. DR PIR; E81127; E81127. DR RefSeq; NP_274079.1; NC_003112.2. DR RefSeq; WP_010980885.1; NC_003112.2. DR STRING; 122586.NMB1045; -. DR PaxDb; Q9JZH8; -. DR EnsemblBacteria; AAF41443; AAF41443; NMB1045. DR GeneID; 903182; -. DR KEGG; nme:NMB1045; -. DR PATRIC; 20357627; VBINeiMen85645_1330. DR eggNOG; ENOG4105HJV; Bacteria. DR eggNOG; ENOG4111R92; LUCA. DR HOGENOM; HOG000218975; -. DR OMA; KVWVRKA; -. DR OrthoDB; EOG64XXP5; -. DR BioCyc; NMEN122586:GHGG-1082-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 264 AA; 29086 MW; 2986E103831D7480 CRC64; MTLPMQETRF SILLDELAAK QEAAIAPHLL ADGTKVWIRK AGRHNARWRY ALLGMVARYL KLGVLKPVPS LGGEPAIATE SKRLYELRSA GIAVPELLAV RKNALMFGNL EGIPLDAQIR QEAEAGKSDA WLAGLEAIAR VHKKRQFLSQ AFARNMMSDG KNISFLDFED DPSEVLTIAQ CQARDWLCYI HSTALILKNG GLLEAAAEKW GGVLSDQPAE IQKLIAATVK PILPIRRLEH PRWGRDALRL AASISLISLA DMPP // ID Q9K0S6_NEIMB Unreviewed; 540 AA. AC Q9K0S6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40931.1}; GN OrderedLocusNames=NMB0499 {ECO:0000313|EMBL:AAF40931.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40931.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40931.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40931.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40931.1; -; Genomic_DNA. DR PIR; D81192; D81192. DR RefSeq; NP_273545.1; NC_003112.2. DR RefSeq; WP_010980804.1; NC_003112.2. DR STRING; 122586.NMB0499; -. DR PaxDb; Q9K0S6; -. DR EnsemblBacteria; AAF40931; AAF40931; NMB0499. DR GeneID; 902615; -. DR KEGG; nme:NMB0499; -. DR PATRIC; 20356248; VBINeiMen85645_0644. DR eggNOG; ENOG4105XIU; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000027878; -. DR OMA; CQDGTIG; -. DR OrthoDB; EOG6RJV4N; -. DR BioCyc; NMEN122586:GHGG-524-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 132 283 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 312 348 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 540 AA; 57075 MW; DC7684A59DDB401B CRC64; MQVNIQIPCM LYRRGSVKPP LFEAPRLLPS FTDPVVPKLS APGGYIVDIP KGNLKTEIEK LAKQPEYAYL KQLQVAKNVN WNQVQLAYDK WDYKQEGLTR AGAAIIALAV TVVTAGAGVG AALGLNGAAA AAADAAFASL ASQASVSLIN NKGDVGKTLK ELGRSRTVKN LVVAAATAGV SNKLGASSLA TWSETPWVNN LNVNLANAGS AALINTAVNG GSLKDNLEAN ILAALVNTAH GEAASKIKGL DQHYVAHKIA HAVAGCAAAA ANKGKCQDGA IGAAVGEIVG EALVKNTDFS DMTPEQLDLE VKKITAYAKL AAGTVAGVTG GDVNTAAQTA QNAVENNAVK AVVTAAKVVY KVARKGLKNG KINVRDLKQT LKDEGYNLAD NLTTLFDETL DWNDAKAVID IVVGTELNRA NKGEAAQKVK EVLEKNRPYI PNKGAVPNMS TYMKNNPFGK QLAQISEKTT LPTQQGQSVF LVKRNQGLLK TGDRFYLDGQ HKNHLEVFDK NGNFKFVLNM DGSLNQMKTG AAKGRKLNLK // ID Q9JZC0_NEIMB Unreviewed; 98 AA. AC Q9JZC0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41510.1}; GN OrderedLocusNames=NMB1120 {ECO:0000313|EMBL:AAF41510.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41510.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41510.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41510.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41510.1; -; Genomic_DNA. DR PIR; B81120; B81120. DR RefSeq; NP_274150.1; NC_003112.2. DR RefSeq; WP_002225228.1; NC_003112.2. DR STRING; 122586.NMB1120; -. DR PaxDb; Q9JZC0; -. DR EnsemblBacteria; AAF41510; AAF41510; NMB1120. DR GeneID; 903542; -. DR KEGG; nme:NMB1120; -. DR PATRIC; 20357809; VBINeiMen85645_1420. DR eggNOG; ENOG41072V4; Bacteria. DR eggNOG; ENOG410YXRS; LUCA. DR HOGENOM; HOG000218949; -. DR OMA; RCYRGAV; -. DR OrthoDB; EOG6P8TRQ; -. DR BioCyc; NMEN122586:GHGG-1156-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 98 AA; 11432 MW; E5DC7F0CF6115EA3 CRC64; MDAKHRLKKY VYHLLVAIDQ LFNALTGGAA DETLSSRTYR RARLAQKPKT RWKILYTLIN GVFFDRHHCR QAYISELKGR QHDARFNQSR AAGEKGTR // ID Q9JXA2_NEIMB Unreviewed; 105 AA. AC Q9JXA2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42460.1}; GN OrderedLocusNames=NMB2152 {ECO:0000313|EMBL:AAF42460.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42460.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42460.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42460.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42460.1; -; Genomic_DNA. DR PIR; F81000; F81000. DR RefSeq; NP_275137.1; NC_003112.2. DR RefSeq; WP_002225742.1; NC_003112.2. DR STRING; 122586.NMB2152; -. DR PaxDb; Q9JXA2; -. DR EnsemblBacteria; AAF42460; AAF42460; NMB2152. DR GeneID; 903220; -. DR KEGG; nme:NMB2152; -. DR PATRIC; 20360500; VBINeiMen85645_2746. DR eggNOG; ENOG4106BJ2; Bacteria. DR eggNOG; ENOG410Y2AU; LUCA. DR HOGENOM; HOG000218686; -. DR OrthoDB; EOG6Z0QCR; -. DR BioCyc; NMEN122586:GHGG-2217-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025384; DUF4298. DR Pfam; PF14131; DUF4298; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 105 AA; 12652 MW; BCC3E2C788094171 CRC64; MQKRIDEIQS KYREWCHLLP QLEEDIRRWK HVVTLIRDMD NFYTHEYQAC HQAIEDGVEL DLSTEGEYSI MSEDALWNAL GEFHQLAWLY LRSSVDALDK YTQED // ID Q9JXJ7_NEIMB Unreviewed; 525 AA. AC Q9JXJ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=YhbX/YhjW/YijP/YjdB family protein {ECO:0000313|EMBL:AAF42335.1}; GN OrderedLocusNames=NMB2010 {ECO:0000313|EMBL:AAF42335.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42335.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42335.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42335.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42335.1; -; Genomic_DNA. DR PIR; F81017; F81017. DR RefSeq; NP_275002.1; NC_003112.2. DR RefSeq; WP_002223145.1; NC_003112.2. DR ProteinModelPortal; Q9JXJ7; -. DR STRING; 122586.NMB2010; -. DR PaxDb; Q9JXJ7; -. DR EnsemblBacteria; AAF42335; AAF42335; NMB2010. DR GeneID; 904111; -. DR KEGG; nme:NMB2010; -. DR PATRIC; 20360123; VBINeiMen85645_2566. DR eggNOG; ENOG4105G6F; Bacteria. DR eggNOG; COG2194; LUCA. DR HOGENOM; HOG000218728; -. DR OMA; WLMLKEI; -. DR OrthoDB; EOG6B35XZ; -. DR BioCyc; NMEN122586:GHGG-2067-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 155 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 214 465 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 525 AA; 59109 MW; ED7D1DB7961EF737 CRC64; MMKKSFLTLV LYSSLLTASE IAYRFVFGIE TLPAAKIAET FALTFVIAAL YLFARYKVTR LLIAVFFAFS IIANNVHYAV YQSWMTGINY WLMLKEVTEV GSAGASMLDK LWLPVLWGVL EVMLFCSLAK FRRKTHFSAD ILFAFLMLMI FVRSFDTKQE HGISPKPTYS RIKANYFSFG YFVGRVLPYQ LFDLSRIPAF KQPAPSKIGQ GSVQNIVLIM GESESAAHLK LFGYGRETSP FLTRLSQADF KPIVKQSYSA GFMTAVSLPS FFNAIPHANG LEQISGGDTN MFRLAKEQGY ETYFYSAQAE NEMAILNLIG KKWIDHLIQP TQLGYGNGDN MPDEKLLPLF DKINLQQGKH FIVLHQRGSH APYGALLQPQ DKVFGEADIV DKYDNTIHKT DQMIQTVFEQ LQKQPDGNWL FAYTSDHGQY VRQDIYNQGT VQPDSYLVPL VLYSPDKAVQ QAANQAFAPC EIAFHQQLST FLIHTLGYDM PVSGCREGSV TGNLITGDAG SLNIRDGKAE YVYPQ // ID Q9K1C3_NEIMB Unreviewed; 118 AA. AC Q9K1C3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE EC=1.6.5.11 {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394}; DE AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394}; GN Name=nuoA {ECO:0000256|HAMAP-Rule:MF_01394, GN ECO:0000313|EMBL:AAF40695.1}; GN OrderedLocusNames=NMB0241 {ECO:0000313|EMBL:AAF40695.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40695.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40695.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40695.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_01394}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01394}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU003639}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003639}. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40695.1; -; Genomic_DNA. DR PIR; G81221; G81221. DR RefSeq; NP_273297.1; NC_003112.2. DR RefSeq; WP_002224824.1; NC_003112.2. DR STRING; 122586.NMB0241; -. DR PaxDb; Q9K1C3; -. DR EnsemblBacteria; AAF40695; AAF40695; NMB0241. DR GeneID; 902352; -. DR KEGG; nme:NMB0241; -. DR PATRIC; 20355558; VBINeiMen85645_0303. DR eggNOG; ENOG4105KWU; Bacteria. DR eggNOG; COG0838; LUCA. DR HOGENOM; HOG000100119; -. DR KO; K00330; -. DR OMA; MKGALEW; -. DR OrthoDB; EOG6QVRQ6; -. DR BioCyc; NMEN122586:GHGG-256-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01394; NDH1_NuoA; 1. DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid. DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3. DR PANTHER; PTHR11058; PTHR11058; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003639, ECO:0000313|EMBL:AAF40695.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003639}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01394}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01394}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01394}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01394}. FT TRANSMEM 8 28 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01394}. FT TRANSMEM 64 84 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01394}. FT TRANSMEM 87 107 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01394}. SQ SEQUENCE 118 AA; 13598 MW; 21F58B3BAC579F84 CRC64; MLSAYFPVFV FILIGLAAGV LFILLGTILG PKRHYAEKDA PYECGFEAFE NARMKFDVRY YLVAILFILF DLEVAFMLPW AVVFKDLGAY GFWSMLVFIV VLTVGFVYEW KKGALEWE // ID Q9JY76_NEIMB Unreviewed; 252 AA. AC Q9JY76; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 75. DE SubName: Full=Beta-1,4-glucosyltransferase {ECO:0000313|EMBL:AAF42052.1}; GN Name=lgtF {ECO:0000313|EMBL:AAF42052.1}; GN OrderedLocusNames=NMB1704 {ECO:0000313|EMBL:AAF42052.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42052.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42052.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42052.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42052.1; -; Genomic_DNA. DR PIR; B81053; B81053. DR RefSeq; NP_274708.1; NC_003112.2. DR RefSeq; WP_002224973.1; NC_003112.2. DR ProteinModelPortal; Q9JY76; -. DR STRING; 122586.NMB1704; -. DR PaxDb; Q9JY76; -. DR EnsemblBacteria; AAF42052; AAF42052; NMB1704. DR GeneID; 903398; -. DR KEGG; nme:NMB1704; -. DR PATRIC; 20359365; VBINeiMen85645_2188. DR eggNOG; ENOG4106WTF; Bacteria. DR eggNOG; COG0463; LUCA. DR HOGENOM; HOG000262849; -. DR OMA; DWPGFGK; -. DR OrthoDB; EOG6W19MV; -. DR BioCyc; NMEN122586:GHGG-1760-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42052.1}. FT DOMAIN 5 123 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 252 AA; 29484 MW; A0AF1CCF076068D3 CRC64; MKKVSVLIVA KNEANHIQEC IESCRFDKEV IVIDDYSTDN TAEIAEGLGA KVFRRHLNGD FGAQKTFAIE QAGGEWVFLI DADERCTPEL SDEISKIVQT GDYAAYFVER RNLFPNHPAT HGAMRPDSVC RLMPKKDSSV QGKVHETVQT PYPKRRLKHF MYHYTYDNWE QYFNKFNKYT SISAEKYREQ GKPVRFVRDI ILRPIWGFFK IYILNKGFLD GKMGWIMSVN HSYYTMIKYV KLYYLYKSGG KF // ID Q9JYV3_NEIMB Unreviewed; 264 AA. AC Q9JYV3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41778.1}; GN OrderedLocusNames=NMB1417 {ECO:0000313|EMBL:AAF41778.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41778.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41778.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41778.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41778.1; -; Genomic_DNA. DR PIR; C81085; C81085. DR RefSeq; NP_274429.1; NC_003112.2. DR RefSeq; WP_002222307.1; NC_003112.2. DR ProteinModelPortal; Q9JYV3; -. DR STRING; 122586.NMB1417; -. DR PaxDb; Q9JYV3; -. DR EnsemblBacteria; AAF41778; AAF41778; NMB1417. DR GeneID; 903839; -. DR KEGG; nme:NMB1417; -. DR PATRIC; 20358519; VBINeiMen85645_1771. DR eggNOG; ENOG4106DFF; Bacteria. DR eggNOG; COG3298; LUCA. DR HOGENOM; HOG000261053; -. DR KO; K07501; -. DR OMA; HLDLMDV; -. DR OrthoDB; EOG6ZWJDD; -. DR BioCyc; NMEN122586:GHGG-1455-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR019288; 3'-5'_exonuclease_PolB-like. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF10108; DNA_pol_B_exo2; 1. DR SUPFAM; SSF53098; SSF53098; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 48 263 DNA_pol_B_exo2. FT {ECO:0000259|Pfam:PF10108}. SQ SEQUENCE 264 AA; 30545 MW; 11C7282B6D4DAFB3 CRC64; MTTILAFDIE TVPDVQGIRT LYELPSSLPD DEVVLFAQQK RRAQTGGDFM QHHLHQVVAI SCCMRWGQDK VHVGTIGEMD DGEEVVIAKF FELIEKHTPQ LVSWNGGGFD LPVLHYRSLI YGINAARYWD MGDGDFGDSR DFKWNNYISR YHQRHCDLMD LLALYQPRAN VPLDDMAKLC GFPGKLGMDG SKVWEAFHTG RLKEIRNYCE TDAANTYLMY LRFCLVSGRL DADEYEMEIK RMRNYLSAQA GEKPHWEEFV RAWE // ID Q9JZT5_NEIMB Unreviewed; 284 AA. AC Q9JZT5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41314.1}; GN OrderedLocusNames=NMB0906 {ECO:0000313|EMBL:AAF41314.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41314.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41314.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41314.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41314.1; -; Genomic_DNA. DR PIR; G81144; G81144. DR RefSeq; NP_273946.1; NC_003112.2. DR RefSeq; WP_002219433.1; NC_003112.2. DR STRING; 122586.NMB0906; -. DR PaxDb; Q9JZT5; -. DR EnsemblBacteria; AAF41314; AAF41314; NMB0906. DR GeneID; 903027; -. DR KEGG; nme:NMB0906; -. DR PATRIC; 20357247; VBINeiMen85645_1137. DR eggNOG; ENOG4105IIS; Bacteria. DR eggNOG; ENOG4112829; LUCA. DR HOGENOM; HOG000220717; -. DR OMA; ETRKSEF; -. DR OrthoDB; EOG63FVZP; -. DR BioCyc; NMEN122586:GHGG-944-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019276; DUF2303. DR Pfam; PF10065; DUF2303; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 284 AA; 32492 MW; D037D43C4B335298 CRC64; METQENMIKT ALQAAQKPFF EFAPNNTPLV FTPDQDGGWR YKSHPELMQN PYRKCGKFLM HDTASLIKFV QKHKQDGTQI YIDADFKSGR IDVTAVINGH TQQAPGWLDF YAVYTPQHTT SASNWLNNNA HRMNQMEFSH FLTNNARNIV SKNPGNENSV YPTAAEVLDF ALNLEYTEKT TFKQGYREQD GRINFTFQSE DSGQTEKNLK MFERFGIEFT PHQGGASYFV EALLKFRIDK NSGALVLWYE LQQIDAVIEQ AAKDISEAVQ KAFPEIDIYF GVIA // ID Q9JXC6_NEIMB Unreviewed; 118 AA. AC Q9JXC6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42432.1}; GN OrderedLocusNames=NMB2123 {ECO:0000313|EMBL:AAF42432.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42432.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42432.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42432.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3W1O} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX PubMed=23531546; DOI=10.1093/nar/gkt201; RA Wang H.C., Wu M.L., Ko T.P., Wang A.H.; RT "Neisseria conserved hypothetical protein DMP12 is a DNA mimic that RT binds to histone-like HU protein."; RL Nucleic Acids Res. 41:5127-5138(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42432.1; -; Genomic_DNA. DR PIR; C81005; C81005. DR RefSeq; NP_275109.1; NC_003112.2. DR RefSeq; WP_002218226.1; NC_003112.2. DR PDB; 3W1O; X-ray; 1.85 A; A/B=1-118. DR PDBsum; 3W1O; -. DR STRING; 122586.NMB2123; -. DR PaxDb; Q9JXC6; -. DR EnsemblBacteria; AAF42432; AAF42432; NMB2123. DR GeneID; 903432; -. DR KEGG; nme:NMB2123; -. DR PATRIC; 20360420; VBINeiMen85645_2706. DR HOGENOM; HOG000218701; -. DR OMA; KTIIFHF; -. DR OrthoDB; EOG63JRBD; -. DR BioCyc; NMEN122586:GHGG-2188-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR031891; DMP12. DR Pfam; PF16779; DMP12; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3W1O}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 118 AA; 13922 MW; 7E327231C14A31E3 CRC64; MNEHNLLIFC LKDNVSISEY TEMIDWAYKN IQSETVVEIT ENQIIEYQNR GLWRLVSEIT DNWLFGPSEG DWLIDKESIL AVKEKLQNSD FSTEPLVKNI IHVLEYAIKN EKTVIFHF // ID Q9JYZ3_NEIMB Unreviewed; 513 AA. AC Q9JYZ3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Putative oxalate/formate antiporter {ECO:0000313|EMBL:AAF41736.1}; GN OrderedLocusNames=NMB1362 {ECO:0000313|EMBL:AAF41736.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41736.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41736.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41736.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41736.1; -; Genomic_DNA. DR PIR; C81092; C81092. DR RefSeq; NP_274380.1; NC_003112.2. DR RefSeq; WP_002222334.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ3; -. DR STRING; 122586.NMB1362; -. DR PaxDb; Q9JYZ3; -. DR EnsemblBacteria; AAF41736; AAF41736; NMB1362. DR GeneID; 903784; -. DR KEGG; nme:NMB1362; -. DR PATRIC; 20358387; VBINeiMen85645_1705. DR eggNOG; ENOG4105FCD; Bacteria. DR eggNOG; ENOG410XQUK; LUCA. DR HOGENOM; HOG000058265; -. DR OMA; AWKTPQF; -. DR OrthoDB; EOG64XXNP; -. DR BioCyc; NMEN122586:GHGG-1400-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 266 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 311 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 323 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 403 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 423 442 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 487 506 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 19 447 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 513 AA; 54433 MW; 1BFB05D9A89AE27D CRC64; MKFLDREASI AKPGFNRWLV PPAALAVHLA IGQIYAYSVF NAPLTKLIGI TESAAGDWKL TTVGWIFSIA LAMLGASAAL FGTWMERVGP RKAIFAAACC FSLGFFVSAF GVRTHNLFLL YLGNGVIGGV GLGLGYIGPV STLMKWFPDK PGMATGLAIM GFGGGAMLAS PLSVSLMNTF SNAASVGVAE TFAVLGLLYL ALMMFGAFTI RVPADGWKPE GYTAPKTQNK LVSSNHVNVS QAMKTPQFWL LFWVLCLNVT AGIGVLGQAS VMIQELFSET SIGRQAAVGA GAAAGFVSLL SLFNMGGRFL WSSVSDKIGR KNTYTIFFVL GSLLYFAVPS IGEGGSKALF IIGFCVIISM YGGGFAAIPA YLKDLFGTYQ VGAIHGRILL AWSTAAVIGP VLVNYIRQSQ IDSGIPAAQA YSVTMYIMAC LLIIGLLCNL AVKSVHEKHH EKDIKTAAHS GNPDDETAIS DAYLVGEKVS GGGISVWWRW ALAVIPLAYG VVMVFVKALD LFS // ID Q9JXX6_NEIMB Unreviewed; 359 AA. AC Q9JXX6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040}; GN OrderedLocusNames=NMB1846 {ECO:0000313|EMBL:AAF42181.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42181.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42181.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42181.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to CC target apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP- CC Rule:MF_02040}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {ECO:0000256|HAMAP-Rule:MF_02040}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42181.1; -; Genomic_DNA. DR PIR; F81036; F81036. DR RefSeq; NP_274843.1; NC_003112.2. DR RefSeq; WP_002257287.1; NC_003112.2. DR ProteinModelPortal; Q9JXX6; -. DR STRING; 122586.NMB1846; -. DR PaxDb; Q9JXX6; -. DR EnsemblBacteria; AAF42181; AAF42181; NMB1846. DR GeneID; 903252; -. DR KEGG; nme:NMB1846; -. DR PATRIC; 20359699; VBINeiMen85645_2354. DR eggNOG; ENOG4105D1F; Bacteria. DR eggNOG; COG0489; LUCA. DR HOGENOM; HOG000079914; -. DR KO; K03593; -. DR OMA; ENNCLVP; -. DR OrthoDB; EOG64XXQJ; -. DR BioCyc; NMEN122586:GHGG-1902-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23264; PTHR23264; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02040}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02040}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT NP_BIND 104 111 ATP. {ECO:0000256|HAMAP-Rule:MF_02040}. SQ SEQUENCE 359 AA; 38577 MW; 2FBAC6960965C6A7 CRC64; MNIQNIRTLL DTVAVPNTAR TLGGEKAVRS VEQRSDGIHI ALHFGFPVAH IASETADRIQ EILMPETGDT HIHLSMDTEI GTHKVQPGVT TIKGVKNIIA VASGKGGVGK STTTANLAAA MARMGARVGV LDADLYGPSQ PTMLGVDDRK PDQKNQKLIP VESSDGIQVM SIGFLVDTDQ AVVWRGPMVS QALQQLMFQS EWDEVDYLFI DLPPGTGDIQ LTLSQRIPVT GSVIVTTPQD IALIDARKAV DMFRKVNIPI LGVLENMSVH ICTNCGHSEA LFGTDGGKDF AARLNVPLLG QLPLSLPVRE AMDGGTPAQL FDEHPAIARI YTDAAFQIAL SIADKGKDFS SRFPKIVVE // ID Q9K0S2_NEIMB Unreviewed; 506 AA. AC Q9K0S2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40938.1}; GN OrderedLocusNames=NMB0506 {ECO:0000313|EMBL:AAF40938.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40938.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40938.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40938.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40938.1; -; Genomic_DNA. DR PIR; A81191; A81191. DR RefSeq; NP_273552.2; NC_003112.2. DR STRING; 122586.NMB0506; -. DR PaxDb; Q9K0S2; -. DR EnsemblBacteria; AAF40938; AAF40938; NMB0506. DR GeneID; 902622; -. DR KEGG; nme:NMB0506; -. DR PATRIC; 20356258; VBINeiMen85645_0649. DR eggNOG; ENOG410647F; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000218789; -. DR OrthoDB; EOG6B8XH7; -. DR BioCyc; NMEN122586:GHGG-531-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 506 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327881. FT DOMAIN 73 231 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 248 293 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 506 AA; 52696 MW; A45ECDEA04046E5C CRC64; MTPAAAAVVV IVVTVLTYGA LSAPAAAGTA GAAGAGAGGA AAGTAAGTGV AAGTAATTGV AAGTSAAAIT TAAGKAALAS LASQAAVSLI NNKGDINHTL KELGKSSTVR QAATAAVTAG VLQGISGLNT QAAEAVSKHF HSPAAGKLTA NLINSTAAAS VHTAINGGSL KDNLGDAALG AIVSTVHGEV ASKIKFNLSE DYIAHKIAHA VAGCASAVAN KGKCRDGAIG AAVGEMVGET LLDGRDVGKL SPQERQKVIA YSQIIAGSAV ALVKGDVNTA ANAATVAVEN NSLLARRRVN IRWTSRQELE HEYAILEIQA ITNQIRRLDP KFNGIAIMRN PREPWTRHDV QTYRQYYNQL RESRGFAVDP IYRIRINNGN EFNRIMSSKY PYNELYVANP KSATGYFRVD SYNPATEEII SRKFTQFSQI QESTGIGYIK EAVRKYSPGA VISNVPSTPT TIRGRKLEGK LILEVPAQVN PIPQSVLRAA QEENVIIRDT TGRIYK // ID Q9JZK8_NEIMB Unreviewed; 207 AA. AC Q9JZK8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41409.1}; GN OrderedLocusNames=NMB1008 {ECO:0000313|EMBL:AAF41409.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41409.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41409.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41409.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41409.1; -; Genomic_DNA. DR PIR; A81131; A81131. DR RefSeq; NP_274043.1; NC_003112.2. DR RefSeq; WP_002222574.1; NC_003112.2. DR STRING; 122586.NMB1008; -. DR PaxDb; Q9JZK8; -. DR EnsemblBacteria; AAF41409; AAF41409; NMB1008. DR GeneID; 903146; -. DR KEGG; nme:NMB1008; -. DR eggNOG; ENOG41079JD; Bacteria. DR eggNOG; ENOG410Z6ER; LUCA. DR OMA; SYHIVEV; -. DR OrthoDB; EOG6XWVBW; -. DR BioCyc; NMEN122586:GHGG-1045-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 207 AA; 23890 MW; CD4B6A485EC4B3EC CRC64; MDQFELCQKE HVNPFALSKQ YLLVVTFVKS SSKNFQAALL WARSAKLFEN LEIGKETIYC CAFDKTAEQA GMAGVFLNYI ENWNGKQIYI NGRIHSGSIY DLLGVLDCYQ KSQSCPNPKS HCCFVSDDIF LWHGSRPTFE ISLDLTGKKK ETSSAKKFVM PCINFRHHRI EKETYLGNWN EQIAALAVKQ NIDWCPSFDI ENFRQYE // ID Q9K071_NEIMB Unreviewed; 188 AA. AC Q9K071; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41160.1}; GN OrderedLocusNames=NMB0747 {ECO:0000313|EMBL:AAF41160.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41160.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41160.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41160.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41160.1; -; Genomic_DNA. DR PIR; B81163; B81163. DR RefSeq; NP_273789.1; NC_003112.2. DR RefSeq; WP_002225444.1; NC_003112.2. DR ProteinModelPortal; Q9K071; -. DR STRING; 122586.NMB0747; -. DR PaxDb; Q9K071; -. DR EnsemblBacteria; AAF41160; AAF41160; NMB0747. DR GeneID; 902862; -. DR KEGG; nme:NMB0747; -. DR PATRIC; 20356865; VBINeiMen85645_0951. DR eggNOG; ENOG4108Z58; Bacteria. DR eggNOG; COG0500; LUCA. DR HOGENOM; HOG000027381; -. DR OMA; EPLNAAI; -. DR OrthoDB; EOG6R87KN; -. DR BioCyc; NMEN122586:GHGG-778-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR010719; rRNA_methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF06962; rRNA_methylase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 188 AA; 20857 MW; 206A4E0F8DACCA68 CRC64; MLLQNILPFA HCLLRKALPE GGNALDGTAG NGHDTLFLAQ TAGIRGKVWA FDIQPQALNN TRCRLQEAGY SNVRLILDGH ENLKQYIPKP LDAAIFNFGW LPGGDKSLTT RTETSIAALS ATLSLLKENG MLIAVLYPGH ENGKQEAEAI EQWAKNLPQE QFAVLRYGFT NRKNSPPYLL VFEKLRQK // ID Q7DDN4_NEIMB Unreviewed; 152 AA. AC Q7DDN4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40953.1}; GN OrderedLocusNames=NMB0521 {ECO:0000313|EMBL:AAF40953.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40953.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40953.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40953.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40953.1; -; Genomic_DNA. DR PIR; C81189; C81189. DR RefSeq; NP_273567.1; NC_003112.2. DR RefSeq; WP_002214429.1; NC_003112.2. DR STRING; 122586.NMB0521; -. DR PaxDb; Q7DDN4; -. DR EnsemblBacteria; AAF40953; AAF40953; NMB0521. DR GeneID; 902637; -. DR KEGG; nme:NMB0521; -. DR PATRIC; 20356283; VBINeiMen85645_0661. DR HOGENOM; HOG000218795; -. DR OrthoDB; EOG6384MQ; -. DR BioCyc; NMEN122586:GHGG-546-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 152 AA; 17866 MW; E3D5FEF70DDC12A4 CRC64; MLTKLKILLF LFLFVFVLAI NLLFFFFSSD IESFGNYQFE YVYDKGWPAN YILVMKDGNE GNFDKIISGL VLEYYKEDDN IYFSYIDGQG FASDSCYYKP EILYGKIILN KNHIININSM EKNNFLSEDK IMKGTRNWLA DPKNKCNIQT LD // ID Q9JZT3_NEIMB Unreviewed; 66 AA. AC Q9JZT3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41316.1}; GN OrderedLocusNames=NMB0908 {ECO:0000313|EMBL:AAF41316.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41316.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41316.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41316.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41316.1; -; Genomic_DNA. DR PIR; A81145; A81145. DR RefSeq; NP_273948.1; NC_003112.2. DR RefSeq; WP_002219431.1; NC_003112.2. DR STRING; 122586.NMB0908; -. DR PaxDb; Q9JZT3; -. DR EnsemblBacteria; AAF41316; AAF41316; NMB0908. DR GeneID; 903029; -. DR KEGG; nme:NMB0908; -. DR PATRIC; 20357251; VBINeiMen85645_1139. DR OrthoDB; EOG6SV5JJ; -. DR BioCyc; NMEN122586:GHGG-946-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 66 AA; 7136 MW; 2FD7AC9A40724C3D CRC64; METITIPKEN FDALLNLART AVALNENFIP KINYGASTIP AAGFAALNEF GIARSTVESL EILKIK // ID Q9K0Z2_NEIMB Unreviewed; 403 AA. AC Q9K0Z2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40848.1}; GN OrderedLocusNames=NMB0409 {ECO:0000313|EMBL:AAF40848.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40848.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40848.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40848.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40848.1; -; Genomic_DNA. DR PIR; F81201; F81201. DR RefSeq; NP_273458.1; NC_003112.2. DR RefSeq; WP_010980791.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z2; -. DR STRING; 122586.NMB0409; -. DR PaxDb; Q9K0Z2; -. DR EnsemblBacteria; AAF40848; AAF40848; NMB0409. DR GeneID; 902525; -. DR KEGG; nme:NMB0409; -. DR PATRIC; 20356005; VBINeiMen85645_0518. DR eggNOG; ENOG4105HD3; Bacteria. DR eggNOG; COG1565; LUCA. DR HOGENOM; HOG000265464; -. DR OMA; QHEMGEL; -. DR OrthoDB; EOG6716MX; -. DR BioCyc; NMEN122586:GHGG-433-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR003788; MidA. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR12049; PTHR12049; 1. DR Pfam; PF02636; Methyltransf_28; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 403 AA; 44515 MW; 4672C662EEE745A9 CRC64; MTAPVPTCNM SGNPINLHKL TLIMPLPSPE ARQFSLKLQT LIAEKIGKHG NWIPFSRFME LVLYAPQYGY YTGGSHKIGN TGDFITAPTL TSLFAQTLAR QLQELLSQTA GNIYEFGAGT GQLAADLLGS ISDGISRYYI IEISPELAAR QKNLIQARAP EASQKVVHLT ALPEAFDGII IGNEVLDAMP VEIVRKNEGG SFEHVGVCLD NDRFTYSARP LHDLQLSALA SLYFPQTDYP YTSELHPQQY AFIRTLASRL EHGCMIFIDY GFDAAQYYHP QRNQGTLIGH YRHHIIHNPF DFIGLADLTA HVNFTDIAQA GTDAGLDLIG YLPQSHFLLN LGITELLAQT GKTDSAAYIC EAAAVQKLID QHEMGELFKV IAFGKNIGID WAGFRFGDIC HKL // ID Q7DDN2_NEIMB Unreviewed; 260 AA. AC Q7DDN2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Thiol:disulfide interchange protein DsbC {ECO:0000313|EMBL:AAF40979.1}; GN Name=dsbC {ECO:0000313|EMBL:AAF40979.1}; GN OrderedLocusNames=NMB0550 {ECO:0000313|EMBL:AAF40979.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40979.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40979.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40979.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40979.1; -; Genomic_DNA. DR PIR; E81185; E81185. DR RefSeq; NP_273595.1; NC_003112.2. DR RefSeq; WP_002214390.1; NC_003112.2. DR ProteinModelPortal; Q7DDN2; -. DR STRING; 122586.NMB0550; -. DR PaxDb; Q7DDN2; -. DR EnsemblBacteria; AAF40979; AAF40979; NMB0550. DR GeneID; 902665; -. DR KEGG; nme:NMB0550; -. DR PATRIC; 20356363; VBINeiMen85645_0700. DR eggNOG; ENOG4105T95; Bacteria. DR eggNOG; COG1651; LUCA. DR HOGENOM; HOG000222078; -. DR KO; K03981; -. DR OMA; VWCAKDP; -. DR OrthoDB; EOG632D3W; -. DR BioCyc; NMEN122586:GHGG-576-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.450.70; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N. DR InterPro; IPR009094; DiS-bond_isomerase_DsbC_N. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10411; DsbC_N; 1. DR Pfam; PF13098; Thioredoxin_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF54423; SSF54423; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 98 260 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 260 AA; 28574 MW; 6084C613F4D1F6FF CRC64; MKTKLIKILT PFTVLPLLAC GQTPVSNANA EPAVKAESAG KSVAASLKAR LEKTYSAQDL KVLSVSETPV KGIYEVVVSG RQIIYTDAEG GYMFVGELIN IDTRKNLTEE RAADLNKIDF ASLPLDKAIK EVRGNGKLKV AVFSDPDCPF CKRLEHEFEK MTDVTVYSFM MPIAGLHPDA ARKAQILWCQ PDRAKAWTDW MRKGKFPVGG SICDNPVAET TSLGEQFGFN GTPTLVFPNG RSQSGYSPMP QLEEIIRKNQ // ID Q9JXX1_NEIMB Unreviewed; 129 AA. AC Q9JXX1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42186.1}; GN OrderedLocusNames=NMB1852 {ECO:0000313|EMBL:AAF42186.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42186.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42186.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42186.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42186.1; -; Genomic_DNA. DR PIR; A81035; A81035. DR RefSeq; NP_274848.1; NC_003112.2. DR RefSeq; WP_002214610.1; NC_003112.2. DR ProteinModelPortal; Q9JXX1; -. DR STRING; 122586.NMB1852; -. DR PaxDb; Q9JXX1; -. DR DNASU; 903246; -. DR EnsemblBacteria; AAF42186; AAF42186; NMB1852. DR GeneID; 903246; -. DR KEGG; nme:NMB1852; -. DR PATRIC; 20359727; VBINeiMen85645_2369. DR eggNOG; ENOG4105WDY; Bacteria. DR eggNOG; COG2852; LUCA. DR HOGENOM; HOG000218764; -. DR OMA; DFACHAK; -. DR OrthoDB; EOG6PKFM9; -. DR BioCyc; NMEN122586:GHGG-1908-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF04480; DUF559; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 121 DUF559. {ECO:0000259|Pfam:PF04480}. FT COILED 106 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 129 AA; 15009 MW; EB8B8CA199D10F10 CRC64; MSTHEKLLTA DNPVLHQRAK AMRQEMSEAE AKLWQHLRAG RLNGYKFRRQ QPMGNYIVDF MCVTPKLIVE ADGGQHAEQA VYDHARTAYL NSLGFTVLRF WNHEILQQTN DVLAEILRVL QELEKQYAQ // ID Q9K0U4_NEIMB Unreviewed; 94 AA. AC Q9K0U4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40904.1}; GN OrderedLocusNames=NMB0467 {ECO:0000313|EMBL:AAF40904.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40904.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40904.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40904.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40904.1; -; Genomic_DNA. DR PIR; H81195; H81195. DR RefSeq; NP_273514.1; NC_003112.2. DR RefSeq; WP_002224948.1; NC_003112.2. DR STRING; 122586.NMB0467; -. DR PaxDb; Q9K0U4; -. DR EnsemblBacteria; AAF40904; AAF40904; NMB0467. DR GeneID; 902583; -. DR KEGG; nme:NMB0467; -. DR PATRIC; 20356182; VBINeiMen85645_0612. DR HOGENOM; HOG000219089; -. DR OMA; AERQIYS; -. DR OrthoDB; EOG6B8XN5; -. DR BioCyc; NMEN122586:GHGG-491-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025711; PepSY. DR Pfam; PF13670; PepSY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 94 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327882. FT DOMAIN 4 90 PepSY. {ECO:0000259|Pfam:PF13670}. SQ SEQUENCE 94 AA; 10702 MW; A0E97D5FF7B6928D CRC64; MKKLLLAAVV SLSAAAAFAG DSAERQIYGD PHFEQNRTKA VKMLEQRGYQ VYDVDADDHW GKPVLEVEAY KDGREYDIVL SYPDLKIIKE QLDR // ID Q9JZC1_NEIMB Unreviewed; 201 AA. AC Q9JZC1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41509.1}; GN OrderedLocusNames=NMB1119 {ECO:0000313|EMBL:AAF41509.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41509.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41509.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41509.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41509.1; -; Genomic_DNA. DR PIR; A81120; A81120. DR RefSeq; NP_274149.1; NC_003112.2. DR RefSeq; WP_002225229.1; NC_003112.2. DR STRING; 122586.NMB1119; -. DR PaxDb; Q9JZC1; -. DR EnsemblBacteria; AAF41509; AAF41509; NMB1119. DR GeneID; 903541; -. DR KEGG; nme:NMB1119; -. DR PATRIC; 20357807; VBINeiMen85645_1419. DR eggNOG; ENOG4106D24; Bacteria. DR eggNOG; ENOG410Y78H; LUCA. DR HOGENOM; HOG000218948; -. DR OMA; ENEVQAW; -. DR OrthoDB; EOG65F8TJ; -. DR BioCyc; NMEN122586:GHGG-1155-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR020088; Uncharacterised_HI1402. DR ProDom; PD055258; Uncharacterised_HI1402; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 201 AA; 21810 MW; 459D37DFAAEBC5B5 CRC64; MTIYFKNGFY DDTLGGIPEG AVAVRAEEYA ALLAGQAQGG QIAADSDGRP VLTPPRPSDY HEWDGKKWKI SKAAAAARFA KQKTALAFRL AEKADELKNS LLAGYPQVEI DSFYRQEKEA LARQADNNAP TPMLAQIAAA RGVELDVLIE KVIEKSARLA VAAGAIIGKR QQLEDKLNTI ETAPGLDALE KEIEEWTLNI G // ID Q9JZJ3_NEIMB Unreviewed; 159 AA. AC Q9JZJ3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase {ECO:0000256|PIRNR:PIRNR006181}; DE EC=4.2.-.- {ECO:0000256|PIRNR:PIRNR006181}; GN OrderedLocusNames=NMB1026 {ECO:0000313|EMBL:AAF41426.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41426.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41426.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41426.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the prolyl-tRNA editing family. YbaK/EbsC CC subfamily. {ECO:0000256|PIRNR:PIRNR006181}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41426.1; -; Genomic_DNA. DR PIR; A81130; A81130. DR RefSeq; NP_274060.1; NC_003112.2. DR RefSeq; WP_002217103.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ3; -. DR STRING; 122586.NMB1026; -. DR PaxDb; Q9JZJ3; -. DR EnsemblBacteria; AAF41426; AAF41426; NMB1026. DR GeneID; 903164; -. DR KEGG; nme:NMB1026; -. DR PATRIC; 20357587; VBINeiMen85645_1310. DR eggNOG; ENOG4108Z66; Bacteria. DR eggNOG; COG2606; LUCA. DR HOGENOM; HOG000262089; -. DR OMA; EHPYDYV; -. DR OrthoDB; EOG6XDH1K; -. DR BioCyc; NMEN122586:GHGG-1063-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.90.960.10; -; 1. DR InterPro; IPR004369; Prolyl-tRNA_editing_YbaK/EbsC. DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom. DR Pfam; PF04073; tRNA_edit; 1. DR PIRSF; PIRSF006181; EbsC_YbaK; 1. DR SUPFAM; SSF55826; SSF55826; 1. DR TIGRFAMs; TIGR00011; YbaK_EbsC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|PIRNR:PIRNR006181}; KW Protein biosynthesis {ECO:0000256|PIRNR:PIRNR006181}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 36 147 tRNA_edit. {ECO:0000259|Pfam:PF04073}. SQ SEQUENCE 159 AA; 17669 MW; 4E2418D8536F33C8 CRC64; MSKHTYPITP AVRVLRENGI EFEPFTYAYE EHGGTAQFAR LFGKDEHLVI KTIVLQDENG KGLIVLMHGD KQISTRNLAR HLGAKHIEPA TPVQANKWTG YLVGGTTPFG IRTKLDIYVE QSVMDLETIY INGGKRGFII GIRPGDLNIL NPKTIQAAV // ID Q9JYL8_NEIMB Unreviewed; 275 AA. AC Q9JYL8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Phytoene synthase-related protein {ECO:0000313|EMBL:AAF41877.1}; GN OrderedLocusNames=NMB1521 {ECO:0000313|EMBL:AAF41877.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41877.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41877.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41877.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41877.1; -; Genomic_DNA. DR PIR; H81074; H81074. DR RefSeq; NP_274529.1; NC_003112.2. DR RefSeq; WP_009344762.1; NC_003112.2. DR ProteinModelPortal; Q9JYL8; -. DR STRING; 122586.NMB1521; -. DR PaxDb; Q9JYL8; -. DR EnsemblBacteria; AAF41877; AAF41877; NMB1521. DR GeneID; 904008; -. DR KEGG; nme:NMB1521; -. DR PATRIC; 20358838; VBINeiMen85645_1929. DR eggNOG; ENOG4105FBD; Bacteria. DR eggNOG; COG1562; LUCA. DR HOGENOM; HOG000003801; -. DR OMA; YAYCRIS; -. DR OrthoDB; EOG63FW00; -. DR BioCyc; NMEN122586:GHGG-1561-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR002060; Squ/phyt_synthse. DR InterPro; IPR017827; Squalene_synthase_HpnC. DR Pfam; PF00494; SQS_PSY; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR TIGRFAMs; TIGR03464; HpnC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 275 AA; 30613 MW; B8B2C2D77A549EA6 CRC64; MDGEGMSVGH YENFPVGSLI LPRRLRKPVH AVYAFARTAD DMADEGSMPS EARLAGLEGL QRELDVLASG GRSAHPLIAR LDAEAVVPFG LDLQPFYDLL SAFSQDVVKT RYGNFGELAD YCRRSANPVG RIMLALYGKT DAVCVAQSDG ICTALQLVNF WQDVAVDWQK GRVYIPQDDL LKFGVSEEQI AAGRADAAFQ RLMAYECRRA FRMLKAGSPL ARELNGRIGL ELRMIVLGAQ LILQKLDACR YDVFAQRPVL DKKDWLIMLK KALWK // ID Q7DDJ2_NEIMB Unreviewed; 591 AA. AC Q7DDJ2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Adhesin {ECO:0000313|EMBL:AAF41395.1}; GN Name=hsf {ECO:0000313|EMBL:AAF41395.1}; GN OrderedLocusNames=NMB0992 {ECO:0000313|EMBL:AAF41395.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41395.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41395.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41395.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41395.1; -; Genomic_DNA. DR RefSeq; NP_274028.1; NC_003112.2. DR RefSeq; WP_002222588.1; NC_003112.2. DR ProteinModelPortal; Q7DDJ2; -. DR STRING; 122586.NMB0992; -. DR PaxDb; Q7DDJ2; -. DR EnsemblBacteria; AAF41395; AAF41395; NMB0992. DR GeneID; 903112; -. DR KEGG; nme:NMB0992; -. DR PATRIC; 20357485; VBINeiMen85645_1257. DR eggNOG; COG5295; LUCA. DR HOGENOM; HOG000218916; -. DR KO; K12690; -. DR OMA; EDSNWAV; -. DR OrthoDB; EOG610441; -. DR BioCyc; NMEN122586:GHGG-1029-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR024973; ESPR. DR InterPro; IPR028230; TAA-Trp-ring. DR InterPro; IPR005594; YadA_C. DR Pfam; PF13018; ESPR; 1. DR Pfam; PF15401; TAA-Trp-ring; 1. DR Pfam; PF03895; YadA_anchor; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 51 {ECO:0000256|SAM:SignalP}. FT CHAIN 52 591 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287540. FT DOMAIN 1 24 ESPR. {ECO:0000259|Pfam:PF13018}. FT DOMAIN 259 317 TAA-Trp-ring. {ECO:0000259|Pfam:PF15401}. FT DOMAIN 514 591 YadA_anchor. {ECO:0000259|Pfam:PF03895}. SQ SEQUENCE 591 AA; 62112 MW; 7C22F3CAE7F73EC6 CRC64; MNKIYRIIWN SALNAWVVVS ELTRNHTKRA SATVKTAVLA TLLFATVQAS ANNEEQEEDL YLDPVQRTVA VLIVNSDKEG TGEKEKVEEN SDWAVYFNEK GVLTAREITL KAGDNLKIKQ NGTNFTYSLK KDLTDLTSVG TEKLSFSANG NKVNITSDTK GLNFAKETAG TNGDTTVHLN GIGSTLTDTL LNTGATTNVT NDNVTDDEKK RAASVKDVLN AGWNIKGVKP GTTASDNVDF VRTYDTVEFL SADTKTTTVN VESKDNGKKT EVKIGAKTSV IKEKDGKLVT GKDKGENGSS TDEGEGLVTA KEVIDAVNKA GWRMKTTTAN GQTGQADKFE TVTSGTNVTF ASGKGTTATV SKDDQGNITV MYDVNVGDAL NVNQLQNSGW NLDSKAVAGS SGKVISGNVS PSKGKMDETV NINAGNNIEI TRNGKNIDIA TSMTPQFSSV SLGAGADAPT LSVDGDALNV GSKKDNKPVR ITNVAPGVKE GDVTNVAQLK GVAQNLNNRI DNVDGNARAG IAQAIATAGL VQAYLPGKSM MAIGGGTYRG EAGYAIGYSS ISDGGNWIIK GTASGNSRGH FGASASVGYQ W // ID Q9K1G5_NEIMB Unreviewed; 375 AA. AC Q9K1G5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40645.1}; GN OrderedLocusNames=NMB0188 {ECO:0000313|EMBL:AAF40645.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40645.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40645.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40645.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40645.1; -; Genomic_DNA. DR PIR; A81227; A81227. DR RefSeq; NP_273246.1; NC_003112.2. DR RefSeq; WP_002226918.1; NC_003112.2. DR STRING; 122586.NMB0188; -. DR PaxDb; Q9K1G5; -. DR EnsemblBacteria; AAF40645; AAF40645; NMB0188. DR GeneID; 902295; -. DR KEGG; nme:NMB0188; -. DR PATRIC; 20355401; VBINeiMen85645_0230. DR eggNOG; ENOG4105DR8; Bacteria. DR eggNOG; COG1289; LUCA. DR HOGENOM; HOG000218658; -. DR OMA; TLGKRPY; -. DR OrthoDB; EOG6XWTZW; -. DR BioCyc; NMEN122586:GHGG-198-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR006726; PHBA_efflux_AaeB/fusaric-R. DR Pfam; PF04632; FUSC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 46 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 121 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 171 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 375 AA; 42383 MW; 41C6EAFAE06E635C CRC64; MNTSQRNRLV SRWLNSYERY RYRRLIHAVR LGGAVLFATA SARLLHLQHG EWIGMTVFVV LGMLQFQGAI YSKAVERMLG TVIGLGAGLG VLWLNQHYFH GNLLFYLTVG TASALAGWAA VGKNGYVPML AGLTMCMLIG DNGSEWLDSG LMRAMNVLIG AAIAIAAAKL LPLKSTLMWR FMLADNLADC SKMIAEISNG RRMTRERLEE NMAKMRQINA RMVKSRSHLA ATSGESRISP AMMEAMQHAH RKIVNTTELL LTTAAKLQSP KLNGSEIRLL DRHFTLLQTD LQQTVALING RHARRIRIDT AINPELEALA EHLHYQWQGF LWLSTNMRQE ISALVILLQR TRRKWLDAHE RQHLRQSLLE TREHG // ID Q9JXX2_NEIMB Unreviewed; 86 AA. AC Q9JXX2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42185.1}; GN OrderedLocusNames=NMB1851 {ECO:0000313|EMBL:AAF42185.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42185.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42185.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42185.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42185.1; -; Genomic_DNA. DR PIR; H81034; H81034. DR RefSeq; NP_274847.1; NC_003112.2. DR RefSeq; WP_002225776.1; NC_003112.2. DR STRING; 122586.NMB1851; -. DR PaxDb; Q9JXX2; -. DR EnsemblBacteria; AAF42185; AAF42185; NMB1851. DR GeneID; 903247; -. DR KEGG; nme:NMB1851; -. DR HOGENOM; HOG000220691; -. DR OrthoDB; EOG6Z9B4K; -. DR BioCyc; NMEN122586:GHGG-1907-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 86 AA; 9547 MW; 468455B2446EF22F CRC64; MPSPRPSPTG EGEGCSRFCG CRRFERQLRF AAVVSGHLKN KKQPAQPVFL AKPLIPTATT SSLPWERVRE RATNCKAYTN SNPTTE // ID Q4W590_NEIMB Unreviewed; 124 AA. AC Q4W590; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 44. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52141.1}; GN OrderedLocusNames=NMB0021 {ECO:0000313|EMBL:AAY52141.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52141.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52141.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52141.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52141.1; -; Genomic_DNA. DR RefSeq; WP_002221780.1; NC_003112.2. DR RefSeq; YP_338286.1; NC_003112.2. DR ProteinModelPortal; Q4W590; -. DR SMR; Q4W590; 1-115. DR PaxDb; Q4W590; -. DR EnsemblBacteria; AAY52141; AAY52141; NMB0021. DR GeneID; 902124; -. DR KEGG; nme:NMB0021; -. DR PATRIC; 20354983; VBINeiMen85645_0028. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR OMA; KTGTNKI; -. DR BioCyc; NMEN122586:GHGG-22-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 124 AA; 13238 MW; 122741610C4EAF7F CRC64; MVEGQKSAVT EYYLNHGEWP GDNSSAGVAT SSEIKGKYVK SVEVKNGVVT AQMASSNVNN EIKGKKLSLW AKRQNGSVKW FCGQPVTRDK AKDDAVTAAT GKGTANINTK HLPSTAPTRK STPN // ID Q9JYA6_NEIMB Unreviewed; 503 AA. AC Q9JYA6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=PqiA family protein {ECO:0000313|EMBL:AAF42019.1}; GN OrderedLocusNames=NMB1670 {ECO:0000313|EMBL:AAF42019.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42019.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42019.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42019.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42019.1; -; Genomic_DNA. DR PIR; H81056; H81056. DR RefSeq; NP_274675.1; NC_003112.2. DR RefSeq; WP_010980971.1; NC_003112.2. DR STRING; 122586.NMB1670; -. DR PaxDb; Q9JYA6; -. DR EnsemblBacteria; AAF42019; AAF42019; NMB1670. DR GeneID; 903440; -. DR KEGG; nme:NMB1670; -. DR PATRIC; 20359282; VBINeiMen85645_2149. DR eggNOG; ENOG4105F1S; Bacteria. DR eggNOG; COG2995; LUCA. DR HOGENOM; HOG000219070; -. DR KO; K03808; -. DR OMA; CRDEALP; -. DR OrthoDB; EOG661H80; -. DR BioCyc; NMEN122586:GHGG-1724-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005219; CHP00155. DR InterPro; IPR007498; PqiA. DR Pfam; PF04403; PqiA; 2. DR TIGRFAMs; TIGR00155; pqiA_fam; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 248 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 254 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 415 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 436 456 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 462 480 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 503 AA; 55928 MW; B8AF067E2C0A1E76 CRC64; MFLSRYFTIL YRIGILSNGF GSRRTTAQKI FLPDTKGLFI LPNLPVLHPD WVYRLFSFIM PPLIFATFPM KPFAENIPHS LRGNCCDEAL PPHTVDCPEC GCRADVPRLD SGEAAFCPRC GHKLFRVGRH PFSAPPAYAA ASLILMAFAY GMTYIEVGIP GAASVLSLPE MMRLMVFQDY GFLAEVMFVL TFGAPVLFLL LCLYVYAALI RKQAYPALRL ATRVMVRLRQ AMMVDVFFVS TLVAYIKLSS VAEVRFGPAF YLMFALSVML IRTSVSVPQH WVYFQIGRLT GDNAVQTASE GKTCCSRCLY FRDSAESPCG VCGAELYRRR PKSLSISSAF LTAAVILYFP ANILPIMISS NPAATEVNTI LNGIAYMWDE GDRLIAAVIF SASILVPVLK IAAMSVLIAS ARFALPTGAK KLSHLYRITE AVGRWSMIDI FVIIILMCSF HTYAARVIPG SAAVYFCLVV ILTMLSAYYF DPRLLWDKRA SDGIAFNETE KHD // ID Q4W574_NEIMB Unreviewed; 505 AA. AC Q4W574; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=Iron(III) ABC transporter, permease protein {ECO:0000313|EMBL:AAY52134.1}; GN Name=fbpB {ECO:0000313|EMBL:AAY52134.1}; GN OrderedLocusNames=NMB0633 {ECO:0000313|EMBL:AAY52134.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52134.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52134.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52134.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52134.1; -; Genomic_DNA. DR RefSeq; NP_273676.1; NC_003112.2. DR RefSeq; WP_002214251.1; NC_003112.2. DR ProteinModelPortal; Q4W574; -. DR STRING; 122586.NMB0633; -. DR PaxDb; Q4W574; -. DR EnsemblBacteria; AAY52134; AAY52134; NMB0633. DR GeneID; 903195; -. DR KEGG; nme:NMB0633; -. DR PATRIC; 20356563; VBINeiMen85645_0801. DR eggNOG; ENOG4107QVT; Bacteria. DR eggNOG; COG1178; LUCA. DR HOGENOM; HOG000238612; -. DR KO; K02011; -. DR OMA; SIHYAND; -. DR OrthoDB; EOG6FFS2H; -. DR BioCyc; NMEN122586:GHGG-659-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 29 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 57 78 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 90 111 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 117 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 179 198 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 218 239 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 269 293 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 313 335 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 347 369 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 375 393 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 427 448 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 478 499 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 53 237 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. FT DOMAIN 309 499 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 505 AA; 55888 MW; 685CF9569031679D CRC64; MSPKKIPIWL TGLILLIALP LTLPFLYVAM RSWQVGINRA VELLFRPRMW DLLSNTLTMM AGVTLISIVL GIACALLFQR YRFFGKTFFQ TAITLPLCIP AFVSCFTWIS LTFRVEGFWG TVMIMSLSSF PLAYLPVEAA LKRISLSYEE VSLSLGKSRL QTFFSAILPQ LKPAIGSSVL LIALHMLVEF GAVSILNYPT FTTAIFQEYE MSYNNNTAAL LSAVLMAVCG IVVFGESIFR GKAKIYHSGK GVARPYPVKT LKLPGQIGAI VFLSSLLTLG IIIPFGVLIH WMMVGTSGTF ALVSVFDAFI RSLSVSALGA ILTILCALPL VWASVRYRNF LTVWIDRLPF LLHAVPGLVI ALSLVYFSIN YTPAVYQTFI VVILAYFMLY LPMAQTTLRT SLEQLPKGME QVGATLGRGH FFIFRTLVLP SILPGITAAF ALVFLKLMKE LTATLLLTTD DVHTLSTAVW EYTSDAQYAA ATPYALMLVL FSGIPVFLLK KYAFK // ID Q9JXM8_NEIMB Unreviewed; 480 AA. AC Q9JXM8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Aldehyde dehydrogenase A {ECO:0000313|EMBL:AAF42297.1}; DE EC=1.2.1.22 {ECO:0000313|EMBL:AAF42297.1}; GN Name=aldA {ECO:0000313|EMBL:AAF42297.1}; GN OrderedLocusNames=NMB1968 {ECO:0000313|EMBL:AAF42297.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42297.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42297.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42297.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42297.1; -; Genomic_DNA. DR PIR; A81023; A81023. DR RefSeq; NP_274962.1; NC_003112.2. DR RefSeq; WP_002225842.1; NC_003112.2. DR ProteinModelPortal; Q9JXM8; -. DR SMR; Q9JXM8; 3-478. DR STRING; 122586.NMB1968; -. DR PaxDb; Q9JXM8; -. DR EnsemblBacteria; AAF42297; AAF42297; NMB1968. DR GeneID; 904174; -. DR KEGG; nme:NMB1968; -. DR PATRIC; 20359999; VBINeiMen85645_2504. DR eggNOG; ENOG4105C26; Bacteria. DR eggNOG; COG1012; LUCA. DR HOGENOM; HOG000271509; -. DR KO; K07248; -. DR OMA; WISIQHE; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NMEN122586:GHGG-2025-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003344, KW ECO:0000313|EMBL:AAF42297.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 21 474 Aldedh. {ECO:0000259|Pfam:PF00171}. SQ SEQUENCE 480 AA; 52257 MW; 35A72F5D1231F107 CRC64; MKQLAMYING RFENDFNGEW RDVLNPSTEE AIAREPKGGK ADVDRAVAAA RAAQPAWERL PAVERGAYLR KIAQGIRERA DELTDTIVAE GGKTKDLARV EVMFTADYLD YQAEWARRYE GEIIQSDRPR ENILLFKRPL GVIAGILPWN FPFFLIARKM GPALVTGNTI VVKPSSVTPI NCHIFAEIVD AVGLPAGVFN VVNGPGAEIG NALSAHPQVD MVSLTGSVEA GRQVMEAASA NITKVSLELG GKAPAIVLKD ADLDLAVKSI LASRVGNTGQ ICNCAERVYV HSSLKDAFIE KMTAAMKGVR YGNPAEAEAG ALEMGPLIEE RAVKAVAEKV ERAVKQGAKL VCGGKRAEGR GYFFEPTLLT DTDNSMDIMK EETFGPVLPV SAFDTLDQVI ALANDCEFGL TSSVYTTNLN EAFYVTRRLQ FGETYINREN FEAMQGFHAG WKKSGIGGAD GKHGLEEYLQ TQVVYLETDI // ID Q9K1P8_NEIMB Unreviewed; 175 AA. AC Q9K1P8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40503.1}; GN OrderedLocusNames=NMB0032 {ECO:0000313|EMBL:AAF40503.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40503.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40503.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40503.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40503.1; -; Genomic_DNA. DR PIR; C81246; C81246. DR RefSeq; NP_273098.1; NC_003112.2. DR RefSeq; WP_002221790.1; NC_003112.2. DR PaxDb; Q9K1P8; -. DR EnsemblBacteria; AAF40503; AAF40503; NMB0032. DR GeneID; 902135; -. DR KEGG; nme:NMB0032; -. DR PATRIC; 20355015; VBINeiMen85645_0044. DR HOGENOM; HOG000218695; -. DR OMA; CNGKPTL; -. DR OrthoDB; EOG68DD0V; -. DR BioCyc; NMEN122586:GHGG-33-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 136 163 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 175 AA; 19593 MW; 7422F626035FA72E CRC64; MEMKQMLLAV GVVAVLAGCG KDAGGYEGYW REKSDKKEGM IAVKKEKGNY FLNKIHVVTG KEESLLLSEK DGALSINTGI GEIPIKLSDD GKELYVERRQ YVKTDAAMKD KIIAHQKKCG QTAQAYRDAR NALPSNQTYQ QHLAAIEQLK RRFEAEFDEL EKEIKCNGRS PALLL // ID Q9JYG5_NEIMB Unreviewed; 68 AA. AC Q9JYG5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41949.1}; GN OrderedLocusNames=NMB1596 {ECO:0000313|EMBL:AAF41949.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41949.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41949.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41949.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41949.1; -; Genomic_DNA. DR PIR; G81063; G81063. DR STRING; 122586.NMB1596; -. DR PaxDb; Q9JYG5; -. DR EnsemblBacteria; AAF41949; AAF41949; NMB1596. DR BioCyc; NMEN122586:GHGG-1644-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 68 AA; 7918 MW; 8758ABC556B9CA65 CRC64; MQRGRLKGLV CRRLGRDPTN FVKYKNVGHD PTYLPFCTKR LSERPCLPYG GSRPSRFLLG YDPSYLLR // ID Q9K0B6_NEIMB Unreviewed; 229 AA. AC Q9K0B6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41115.1}; GN OrderedLocusNames=NMB0698 {ECO:0000313|EMBL:AAF41115.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41115.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41115.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41115.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41115.1; -; Genomic_DNA. DR PIR; A81169; A81169. DR RefSeq; NP_273740.1; NC_003112.2. DR RefSeq; WP_002225483.1; NC_003112.2. DR ProteinModelPortal; Q9K0B6; -. DR STRING; 122586.NMB0698; -. DR PaxDb; Q9K0B6; -. DR EnsemblBacteria; AAF41115; AAF41115; NMB0698. DR GeneID; 902810; -. DR KEGG; nme:NMB0698; -. DR PATRIC; 20356729; VBINeiMen85645_0886. DR eggNOG; ENOG4108SNQ; Bacteria. DR eggNOG; COG3663; LUCA. DR HOGENOM; HOG000218845; -. DR OMA; NDMWRIY; -. DR OrthoDB; EOG6P8TQ1; -. DR BioCyc; NMEN122586:GHGG-726-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.470.10; -; 1. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR SUPFAM; SSF52141; SSF52141; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 229 AA; 25368 MW; 446A31C74F26E5CE CRC64; MLFEGLPCLA VWCKNRLSAV LPVGGLNVSE NLLEIETHPF DPVLPPKAAV MMMGTFPPKE DKRAMQFHYP NFQNDMWRVY GLVFFNDAAH FQRLSEKAFD AEKIKAFLHE RGIASCPTVL KAVRQHGNAS DKFLKVVETV DLAAVLAKIP ECRHICTTGG KATEILLDIQ GGGIKMPKTG ETVPFPFAGR DLTLTRLPST SRAYPLSLAK KAAAYRAFFE MAGLCEKQL // ID Q9K039_NEIMB Unreviewed; 159 AA. AC Q9K039; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41196.1}; GN OrderedLocusNames=NMB0783 {ECO:0000313|EMBL:AAF41196.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41196.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41196.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41196.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41196.1; -; Genomic_DNA. DR PIR; D81158; D81158. DR RefSeq; NP_273825.1; NC_003112.2. DR RefSeq; WP_002222722.1; NC_003112.2. DR ProteinModelPortal; Q9K039; -. DR STRING; 122586.NMB0783; -. DR PaxDb; Q9K039; -. DR EnsemblBacteria; AAF41196; AAF41196; NMB0783. DR GeneID; 902898; -. DR KEGG; nme:NMB0783; -. DR PATRIC; 20356949; VBINeiMen85645_0993. DR eggNOG; ENOG4105X2M; Bacteria. DR eggNOG; COG3439; LUCA. DR HOGENOM; HOG000101109; -. DR OMA; CPAFPGR; -. DR OrthoDB; EOG6VB726; -. DR BioCyc; NMEN122586:GHGG-814-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.310.70; -; 1. DR InterPro; IPR005180; DUF302. DR Pfam; PF03625; DUF302; 1. DR SUPFAM; SSF103247; SSF103247; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 159 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327755. FT DOMAIN 67 127 DUF302. {ECO:0000259|Pfam:PF03625}. SQ SEQUENCE 159 AA; 17023 MW; BF9D29F8B9825594 CRC64; MKHILPLIAA SALCISTASA HPASEPSTQN ETAMTTHTLT SKYSFDETVS RLETAIKSKG MDIFAVIDHQ EAARRNGLTM QPAKVIVFGT PKAGTPLMVK DPAFALQLPL RVLVTETDGK VRAAYTDTRA LIAGSRIGFD EVANTLANAE KLIQKTVGE // ID Q9JZ94_NEIMB Unreviewed; 306 AA. AC Q9JZ94; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41613.1}; GN OrderedLocusNames=NMB1232 {ECO:0000313|EMBL:AAF41613.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41613.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41613.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41613.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41613.1; -; Genomic_DNA. DR PIR; A81107; A81107. DR ProteinModelPortal; Q9JZ94; -. DR STRING; 122586.NMB1232; -. DR PaxDb; Q9JZ94; -. DR EnsemblBacteria; AAF41613; AAF41613; NMB1232. DR PATRIC; 20358059; VBINeiMen85645_1542. DR eggNOG; COG2890; LUCA. DR HOGENOM; HOG000240391; -. DR OMA; WRGDFQN; -. DR OrthoDB; EOG6WT8C8; -. DR BioCyc; NMEN122586:GHGG-1269-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 119 263 MTS. {ECO:0000259|Pfam:PF05175}. SQ SEQUENCE 306 AA; 33439 MW; D9448EC4DA04E7ED CRC64; MKKRVRKPAA VRSDADIAAL FHAHRMKQAQ QSRILNMLAV EIRPGFVLDN KRAPDIRSAL LDVYGEADGK PFFLPLNLLL GFMGAHEWHK KGVAVPQLGG SIHVPFGVFS PLRGEYLDLL AHAPSTGFQT AFDIGTGSGV LAAILAKQGI PSVIGTDTNP KAVACARANI ARLGFEKQVE IRETDLFPEG FADLIVCNPP WLPAKPTSAV ESALYDPESA MLAAFLRDAP KHLNPDGEIR LIISDLAEHL HLRPSDFLDK AFAQAGLRVA DMMKTKPKHK KAANPSDPLA FARTRETTFL YRLKKA // ID Q9K0A6_NEIMB Unreviewed; 332 AA. AC Q9K0A6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=DNA polymerase III, delta subunit {ECO:0000313|EMBL:AAF41125.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAF41125.1}; GN Name=holA {ECO:0000313|EMBL:AAF41125.1}; GN OrderedLocusNames=NMB0708 {ECO:0000313|EMBL:AAF41125.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41125.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41125.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41125.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41125.1; -; Genomic_DNA. DR PIR; E81168; E81168. DR RefSeq; NP_273750.1; NC_003112.2. DR RefSeq; WP_002244058.1; NC_003112.2. DR ProteinModelPortal; Q9K0A6; -. DR STRING; 122586.NMB0708; -. DR PaxDb; Q9K0A6; -. DR EnsemblBacteria; AAF41125; AAF41125; NMB0708. DR GeneID; 902820; -. DR KEGG; nme:NMB0708; -. DR PATRIC; 20356763; VBINeiMen85645_0903. DR eggNOG; ENOG4105DJF; Bacteria. DR eggNOG; COG1466; LUCA. DR HOGENOM; HOG000256203; -. DR KO; K02340; -. DR OMA; RQQGFDE; -. DR OrthoDB; EOG6BCSPJ; -. DR BioCyc; NMEN122586:GHGG-736-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR032780; DNA_pol3_delt_C. DR InterPro; IPR010372; DNA_pol3_delta_N. DR InterPro; IPR005790; DNA_polIII_delta. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF14840; DNA_pol3_delt_C; 1. DR Pfam; PF06144; DNA_pol3_delta; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01128; holA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAF41125.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41125.1}. FT DOMAIN 18 186 DNA_pol3_delta. FT {ECO:0000259|Pfam:PF06144}. FT DOMAIN 216 328 DNA_pol3_delt_C. FT {ECO:0000259|Pfam:PF14840}. SQ SEQUENCE 332 AA; 36326 MW; A639AA7CE7CE92FF CRC64; MAAHIGRIDT DAPLKPLYVI HGEEELLRIE ALDALRAAAK KQGYLNREVY TADNAFDWNE LLQTAGSAGL FADLKLLELH IPNGKPGKTG GEALQDFAAR LPEDTVTLVL LPKLEKTQLQ SKWFAALAAK GEVWEAKPVG AAALPQWIRG RLDKIGLGIE ADALALFAER VEGNLLAARQ EIDKLGLLYP KGHTVNIDEA QTAVANVARF DAFQLAGAWM KGDVLRVCRL LDGLREEGEE PVLLLWAVAE DVRTLIRLAA ALKQGQSIQS VRNSLRLWGD KQTLAPLAVK RISVVRLLDA LKTCAQIDRI IKGAEDGDAW TVFKRLVVSL AE // ID Q9K0B9_NEIMB Unreviewed; 119 AA. AC Q9K0B9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41112.1}; GN OrderedLocusNames=NMB0695 {ECO:0000313|EMBL:AAF41112.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41112.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41112.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41112.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41112.1; -; Genomic_DNA. DR PIR; E81170; E81170. DR RefSeq; NP_273737.1; NC_003112.2. DR RefSeq; WP_010980826.1; NC_003112.2. DR STRING; 122586.NMB0695; -. DR PaxDb; Q9K0B9; -. DR EnsemblBacteria; AAF41112; AAF41112; NMB0695. DR GeneID; 902807; -. DR KEGG; nme:NMB0695; -. DR PATRIC; 20356719; VBINeiMen85645_0881. DR eggNOG; ENOG4106HVU; Bacteria. DR eggNOG; ENOG410Y4X4; LUCA. DR HOGENOM; HOG000218746; -. DR OMA; YLIPEMD; -. DR OrthoDB; EOG6WT8DD; -. DR BioCyc; NMEN122586:GHGG-723-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 119 AA; 14164 MW; C68D9E23B88FB776 CRC64; MYFVDRTAVV LKPTARFLEW LKSTDENMPD LTIEQLRANC SVFLVPQFDE PEAVVSYFDE RYRQIFEAEL AGWDIDKDKW PQDMGLKAFW EFFDIEIHDI VLNMEEAELN ITPVFDNMM // ID Q9K1P2_NEIMB Unreviewed; 90 AA. AC Q9K1P2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40510.1}; GN OrderedLocusNames=NMB0039 {ECO:0000313|EMBL:AAF40510.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40510.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40510.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40510.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40510.1; -; Genomic_DNA. DR PIR; A81245; A81245. DR STRING; 122586.NMB0039; -. DR PaxDb; Q9K1P2; -. DR EnsemblBacteria; AAF40510; AAF40510; NMB0039. DR PATRIC; 20355035; VBINeiMen85645_0054. DR HOGENOM; HOG000027825; -. DR OMA; MRKTFLF; -. DR OrthoDB; EOG6R87JH; -. DR BioCyc; NMEN122586:GHGG-40-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 90 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328389. SQ SEQUENCE 90 AA; 10456 MW; B32E3F5BC93AE300 CRC64; MRKTFLFLTA AAALLSGCAW ETYQDGNGKT AVRQKYPAGT PVYYQDGSYS KNMNYNQYRP ERHAVLPNQT GNNADEEHRQ HWQKPKFQNR // ID Q9JYY7_NEIMB Unreviewed; 462 AA. AC Q9JYY7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 98. DE SubName: Full=Putative ATP-dependent RNA helicase {ECO:0000313|EMBL:AAF41742.1}; GN OrderedLocusNames=NMB1368 {ECO:0000313|EMBL:AAF41742.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41742.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41742.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41742.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41742.1; -; Genomic_DNA. DR PIR; E81090; E81090. DR RefSeq; NP_274386.1; NC_003112.2. DR RefSeq; WP_002219125.1; NC_003112.2. DR ProteinModelPortal; Q9JYY7; -. DR STRING; 122586.NMB1368; -. DR PaxDb; Q9JYY7; -. DR EnsemblBacteria; AAF41742; AAF41742; NMB1368. DR GeneID; 903790; -. DR KEGG; nme:NMB1368; -. DR PATRIC; 20358401; VBINeiMen85645_1712. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR HOGENOM; HOG000268807; -. DR OMA; PMQAEDY; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; NMEN122586:GHGG-1406-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41742.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:AAF41742.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41742.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41742.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 31 Q_MOTIF. {ECO:0000259|PROSITE:PS51195}. FT DOMAIN 34 209 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 236 380 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 462 AA; 51366 MW; 9AD45742028CDCAE CRC64; MSIKFADLNL DKNILSAVSS EGYESPTPIQ AQAIPFALEG RDIMASAQTG SGKTAAFLLP TLQKLTKRSE KPGKGPRALV LTPTRELAAQ VEKNALAYAK NMRWFRTVSI VGGASFGYQT RALSKPVDLI VATPGRLMDL MQSGKVDFER LEVLILDEAD RMLDMGFIDD IETIVEATPS DRQTLLFSAT WDGAVGKLAR KLTKDPEIIE VERVDDQGKI EEQLLYCDDM RHKNRLLDHI LRDANIDQCV IFTSTKAMTE VIADELYEKG FAANCLHGDM PQGWRNRTLM DLRKGRCKIL VATDVAARGI DVPTITHVIN YDLPKQAEDY VHRIGRTGRA GRTGIAITFA EVNEYVKVHK IEKYINRKLP ELTIEGMEPT RKRKSAGGKP KGKGGWGDRK SGGWRGDHKP SKEGFGGKTR GEGFKKEGFK RDGFKKTGEG FKGKRKAGDS FAGKGERRYK DR // ID Q9JZ19_NEIMB Unreviewed; 78 AA. AC Q9JZ19; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41709.1}; GN OrderedLocusNames=NMB1334 {ECO:0000313|EMBL:AAF41709.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41709.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41709.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41709.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41709.1; -; Genomic_DNA. DR PIR; F81093; F81093. DR RefSeq; NP_274353.1; NC_003112.2. DR RefSeq; WP_010980924.1; NC_003112.2. DR STRING; 122586.NMB1334; -. DR PaxDb; Q9JZ19; -. DR EnsemblBacteria; AAF41709; AAF41709; NMB1334. DR GeneID; 903756; -. DR KEGG; nme:NMB1334; -. DR BioCyc; NMEN122586:GHGG-1372-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 78 AA; 8788 MW; 3B136472E840D2F3 CRC64; MPFAQSCAFF ARILAIGSNS LILCVIFSMP QRILCSDTQG STLSRIPYVA RFWERAPLQT KQALPLSRKT GIQPIRKF // ID Q9JY55_NEIMB Unreviewed; 167 AA. AC Q9JY55; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42078.1}; GN OrderedLocusNames=NMB1733 {ECO:0000313|EMBL:AAF42078.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42078.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42078.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42078.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42078.1; -; Genomic_DNA. DR PIR; D81049; D81049. DR RefSeq; NP_274736.1; NC_003112.2. DR RefSeq; WP_002227076.1; NC_003112.2. DR STRING; 122586.NMB1733; -. DR PaxDb; Q9JY55; -. DR EnsemblBacteria; AAF42078; AAF42078; NMB1733. DR GeneID; 903366; -. DR KEGG; nme:NMB1733; -. DR PATRIC; 20359429; VBINeiMen85645_2220. DR HOGENOM; HOG000218821; -. DR OrthoDB; EOG6K4010; -. DR BioCyc; NMEN122586:GHGG-1788-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR014478; UCP016195. DR PIRSF; PIRSF016195; UCP016195; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 159 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 167 AA; 19854 MW; 173631A183372CDE CRC64; MDAFDFFMQG NFKKIATEQG LDRKYFIFQY IVCNLSAISS FCLMKIIHTY TILYILIAVI GIINGFLLRS KVLSIVKNKQ KFLSDMFPLE MPFFFVEYKI PILARFLNRG MKWLYLPSFF CLVAICFSIY ILNEEGGWMP YFACYWFGLC YPVSTYYVFL SRDYKHI // ID Q9JYA1_NEIMB Unreviewed; 397 AA. AC Q9JYA1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Aromatic-amino-acid aminotransferase {ECO:0000313|EMBL:AAF42026.1}; DE EC=2.6.1.57 {ECO:0000313|EMBL:AAF42026.1}; GN Name=tyrB {ECO:0000313|EMBL:AAF42026.1}; GN OrderedLocusNames=NMB1678 {ECO:0000313|EMBL:AAF42026.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42026.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42026.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42026.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000479}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU000479}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42026.1; -; Genomic_DNA. DR PIR; H81054; H81054. DR RefSeq; NP_274682.1; NC_003112.2. DR RefSeq; WP_002224987.1; NC_003112.2. DR ProteinModelPortal; Q9JYA1; -. DR SMR; Q9JYA1; 1-396. DR STRING; 122586.NMB1678; -. DR PaxDb; Q9JYA1; -. DR EnsemblBacteria; AAF42026; AAF42026; NMB1678. DR GeneID; 903430; -. DR KEGG; nme:NMB1678; -. DR PATRIC; 20359307; VBINeiMen85645_2160. DR eggNOG; ENOG4105CGF; Bacteria. DR eggNOG; COG1448; LUCA. DR HOGENOM; HOG000185898; -. DR KO; K00832; -. DR OMA; FPDSGVW; -. DR OrthoDB; EOG6C2WBK; -. DR BioCyc; NMEN122586:GHGG-1733-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR000796; Asp_trans. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11879; PTHR11879; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00799; TRANSAMINASE. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAF42026.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAF42026.1}. FT DOMAIN 27 391 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 397 AA; 44749 MW; 163D6E7340362B94 CRC64; MYRHIEYYPG DPILSLVETF KNDPRPEKVN LSIGIYFDDE GKMPVLESVS RAETARAAAP APSPYLPMEG LDTYRSAVQH LLFGKDNPAL AQGRIVTVQT LGGSGALKVG ADFLHRWFPE ARAYVSDPTW DNHRGIFEGA GFEVGTYPYY DPATVGVKFD EMTAFFNTLP ENSVLILHPC CHNPTGVDMS ERQWDEVLHI IKTRKLIPFM DIAYQGFGGD LDSDAYAVRK AVEMELPLFV SNSFSKNLSL YGERVGGLSV VCPNKEEADL VFGQLKFTVR RIYSSPPAHG AYIAADVMNS PELYALWQNE VYMMRDRIRA MRQKLYDVLT AQIPNRDFTY FIKQRGMFGY TGLSVEQVRR LRDEFAVYLL DSGRMCVAGL NTSNTDYVAR AFAEVLK // ID Q9JYV7_NEIMB Unreviewed; 269 AA. AC Q9JYV7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=FrpC operon protein {ECO:0000313|EMBL:AAF41774.1}; GN OrderedLocusNames=NMB1412 {ECO:0000313|EMBL:AAF41774.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41774.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41774.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41774.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41774.1; -; Genomic_DNA. DR PIR; H81087; H81087. DR RefSeq; NP_274425.1; NC_003112.2. DR RefSeq; WP_002219097.1; NC_003112.2. DR STRING; 122586.NMB1412; -. DR PaxDb; Q9JYV7; -. DR EnsemblBacteria; AAF41774; AAF41774; NMB1412. DR GeneID; 903834; -. DR KEGG; nme:NMB1412; -. DR PATRIC; 20358503; VBINeiMen85645_1763. DR HOGENOM; HOG000219111; -. DR OMA; NNLEPMT; -. DR OrthoDB; EOG6TBHDH; -. DR BioCyc; NMEN122586:GHGG-1450-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010692; FrpC. DR Pfam; PF06901; FrpC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328332. SQ SEQUENCE 269 AA; 31327 MW; C7AEFDFDC1A02A59 CRC64; MRPYATTIYQ LFILFIGSVF TMTSCEPVNE KTDQKAVSAQ QAKEQTSFNN PEPMTGFEHT VTFDFQGTKM VIPYGYLARY TQDNATKWLS DTPGQDAYSI NLIEISVYYK KTDQGWVLEP YNQQNKAHFI QFLRDGLDSV DDIVIRKDAC SLSTTMGERL LTYGVKKMPS AYPEYEAYED KRHIPENPYF HEFYYIKKGE NPAIITHRNY HRYGENDYST SVGSCINGFT VRYYPFIREK QQLTQQELVG YHQQVEQLVQ SFVNNPSKK // ID Q9K0V7_NEIMB Unreviewed; 148 AA. AC Q9K0V7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40887.1}; GN OrderedLocusNames=NMB0450 {ECO:0000313|EMBL:AAF40887.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40887.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40887.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40887.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40887.1; -; Genomic_DNA. DR PIR; D81197; D81197. DR ProteinModelPortal; Q9K0V7; -. DR STRING; 122586.NMB0450; -. DR PaxDb; Q9K0V7; -. DR EnsemblBacteria; AAF40887; AAF40887; NMB0450. DR PATRIC; 20356114; VBINeiMen85645_0573. DR OMA; MVMYVVK; -. DR OrthoDB; EOG6SBT13; -. DR BioCyc; NMEN122586:GHGG-474-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR003819; TauD/TfdA-like. DR Pfam; PF02668; TauD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 144 TauD. {ECO:0000259|Pfam:PF02668}. SQ SEQUENCE 148 AA; 16759 MW; F0CAE17A43666E2E CRC64; MYVVKSANDG GNSLFLSSSD IVNQLSKTET GKKHLKTLTG NLYPFKTPAS FDKKQGVRWG NILSVNTQMI RFRSDCIYKG IEENRNKVSK EMVLALDYLI NVIKNASDIQ EFSAQDDGLI IIDNVNGLHA RTDYTDKNRH YIRARITV // ID Q9K1F8_NEIMB Unreviewed; 919 AA. AC Q9K1F8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Ribonuclease E {ECO:0000256|HAMAP-Rule:MF_00970}; DE Short=RNase E {ECO:0000256|HAMAP-Rule:MF_00970}; DE EC=3.1.26.12 {ECO:0000256|HAMAP-Rule:MF_00970}; GN Name=rne {ECO:0000256|HAMAP-Rule:MF_00970, GN ECO:0000313|EMBL:AAF40653.1}; GN OrderedLocusNames=NMB0196 {ECO:0000313|EMBL:AAF40653.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40653.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40653.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40653.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA CC processing and decay. Required for the maturation of 5S and 16S CC rRNAs and the majority of tRNAs. Also involved in the degradation CC of most mRNAs. {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of single-stranded CC RNA in A- and U-rich regions. {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00970}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970}; CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_00970}; CC -!- SUBUNIT: Homotetramer formed by a dimer of dimers. CC {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}. CC Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral CC membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic CC side {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP- CC Rule:MF_00970}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40653.1; -; Genomic_DNA. DR PIR; F81225; F81225. DR RefSeq; NP_273254.1; NC_003112.2. DR RefSeq; WP_010980758.1; NC_003112.2. DR ProteinModelPortal; Q9K1F8; -. DR SMR; Q9K1F8; 1-486. DR STRING; 122586.NMB0196; -. DR PaxDb; Q9K1F8; -. DR EnsemblBacteria; AAF40653; AAF40653; NMB0196. DR GeneID; 902304; -. DR KEGG; nme:NMB0196; -. DR PATRIC; 20355435; VBINeiMen85645_0246. DR eggNOG; ENOG4107QQB; Bacteria. DR eggNOG; COG1530; LUCA. DR HOGENOM; HOG000258027; -. DR KO; K08300; -. DR OMA; HVLRMVQ; -. DR OrthoDB; EOG6PCPTH; -. DR BioCyc; NMEN122586:GHGG-207-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00970; RNase_E; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR028878; RNase_E. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF10150; RNase_E_G; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00757; RNaseEG; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00970}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00970}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00970}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00970}. FT DOMAIN 39 117 S1 motif. {ECO:0000256|HAMAP- FT Rule:MF_00970, FT ECO:0000259|PROSITE:PS50126}. FT REGION 401 404 Required for zinc-mediated FT homotetramerization and catalytic FT activity. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 300 300 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 343 343 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 401 401 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. FT METAL 404 404 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. SQ SEQUENCE 919 AA; 101936 MW; 449937496BAC9DCB CRC64; MKRMLFNATQ AEELRVAIVD GQNLLDLDIE TLGKEQRKGN IYKGIITRIE PSLEACFVDY GTDRHGFLPF KEVSRSYFQD YEGGRARIQD VLKEGMEVIV QVEKDERGNK GAALTTFISL AGRYLVLMPN NPRGGGVSRR IEGEERQELK AAMAELDIPN GMSIIARTAG IGRSAEELEW DLNYLKQLWQ AIEEAGKAHH DPYLLFMESS LLIRAIRDYF RPDIGEILVD NQEVYDQVAE FMSYVMPGNI GRLKLYEDHT PLFSRFQIEH QIESAFSRSV SLPSGGAIVI DHTEALVSID VNSARATRGA DIEDTAFKTN MEAAEEVARQ MRLRDLGGLV VIDFIDMENP KHQRDVENVL RDALKKDRAR VQMGKLSRFG LLELSRQRLK PALGESSHVA CPRCAGTGVI RGIESTALHV LRIIQEEAMK DNTGEVRAQV PVDVATFLLN EKRAELFAME ERLDVNVVLI PNIHLENPHY EINRIRTDDV EEDGEPSYKR VAEPEEDESA KPFGGEKAKA ARPEPAVKGV RHTSPAPTAA PEKKTSWWDS FKAWLKRIFG GSETQAAPAA ETSEKRSTAN RSGSRANNRR QNPRRSKREG SKVEVREVAG KTAGQEARAD KAETRNNGNR RRNERGDRAA ERANEAEIQS RNVQPAATVA DAAPSETEVQ TGKRRRNGSR SERGQTAPET ATVAETTVQT AENTPSEPHT AEDKGSKPKS ERNRRERDSR DAKERRERNN QRDRRQNGKK RNIPSAAKIE QYLNIHDTAD KVRSAAAHVF GETDANAPIT VSIADPVAER DLPTASPAVS NGDAPVYDAA EKIRRATAAI LPEGATPKAE AQEMPSETAT FTAAAEQARE TAQTGGLVLI ETDPAALKAW AAQPEVQAGR GLRRSEQPKP SEVATVPAEE MIQVETRQG // ID Q9K1N7_NEIMB Unreviewed; 74 AA. AC Q9K1N7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40517.1}; GN OrderedLocusNames=NMB0046 {ECO:0000313|EMBL:AAF40517.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40517.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40517.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40517.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40517.1; -; Genomic_DNA. DR PIR; A81244; A81244. DR STRING; 122586.NMB0046; -. DR PaxDb; Q9K1N7; -. DR EnsemblBacteria; AAF40517; AAF40517; NMB0046. DR BioCyc; NMEN122586:GHGG-47-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 74 AA; 8786 MW; 4A45797EFF5053C3 CRC64; MPSENSRPMP SFPRRRESRP WDNGNIQRLS ESPRFWIPTF VGMTGCRFVG MTWCRFPYGW IRHSRAGGNL ERKI // ID Q9JYN1_NEIMB Unreviewed; 69 AA. AC Q9JYN1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41859.1}; GN OrderedLocusNames=NMB1503 {ECO:0000313|EMBL:AAF41859.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41859.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41859.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41859.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41859.1; -; Genomic_DNA. DR PIR; C81075; C81075. DR RefSeq; NP_274511.1; NC_003112.2. DR RefSeq; WP_010980949.1; NC_003112.2. DR STRING; 122586.NMB1503; -. DR PaxDb; Q9JYN1; -. DR EnsemblBacteria; AAF41859; AAF41859; NMB1503. DR GeneID; 903942; -. DR KEGG; nme:NMB1503; -. DR BioCyc; NMEN122586:GHGG-1543-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 69 AA; 8089 MW; 7971CC7A6FFFD3E6 CRC64; MPSEHLPDHI IRECRQIVFF CKLILKSTYR FTPCRPSLPH LHHPSTLSHG YSANPLPICP RICLFRPMH // ID Q9K1Q4_NEIMB Unreviewed; 78 AA. AC Q9K1Q4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40495.1}; GN OrderedLocusNames=NMB0016 {ECO:0000313|EMBL:AAF40495.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40495.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40495.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40495.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40495.1; -; Genomic_DNA. DR PIR; D81246; D81246. DR PaxDb; Q9K1Q4; -. DR EnsemblBacteria; AAF40495; AAF40495; NMB0016. DR BioCyc; NMEN122586:GHGG-17-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 78 AA; 8932 MW; 5CA11E82505DEA6D CRC64; MKNSFCGQFA CCANGILLFF TEWLPMSLRT GILWRFERKV CLELVEMVRC RHECLISAYR QSAHPNLCIS GGKNEICG // ID Q9JZT8_NEIMB Unreviewed; 97 AA. AC Q9JZT8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41311.1}; GN OrderedLocusNames=NMB0903 {ECO:0000313|EMBL:AAF41311.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41311.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41311.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41311.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41311.1; -; Genomic_DNA. DR PIR; D81144; D81144. DR RefSeq; NP_273943.1; NC_003112.2. DR RefSeq; WP_002220689.1; NC_003112.2. DR STRING; 122586.NMB0903; -. DR PaxDb; Q9JZT8; -. DR EnsemblBacteria; AAF41311; AAF41311; NMB0903. DR GeneID; 903024; -. DR KEGG; nme:NMB0903; -. DR PATRIC; 20357241; VBINeiMen85645_1134. DR OMA; HMRKLLV; -. DR OrthoDB; EOG661HCQ; -. DR BioCyc; NMEN122586:GHGG-941-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 97 AA; 10971 MW; 834A58264C32F5DB CRC64; MNFQEENENI KNDIEINLLH SAEADSVEAM MDLAVYGLAA MVAKHNKTRG EQLVLQAIAG HMRKLLAALP ETESLVQTGK VYRRLEDLIF KTYLPEQ // ID Q7DD44_NEIMB Unreviewed; 68 AA. AC Q7DD44; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42422.1}; GN OrderedLocusNames=NMB2108 {ECO:0000313|EMBL:AAF42422.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42422.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42422.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42422.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42422.1; -; Genomic_DNA. DR PIR; A81004; A81004. DR STRING; 122586.NMB2108; -. DR PaxDb; Q7DD44; -. DR EnsemblBacteria; AAF42422; AAF42422; NMB2108. DR PATRIC; 20360390; VBINeiMen85645_2691. DR HOGENOM; HOG000218646; -. DR OrthoDB; EOG6358GH; -. DR BioCyc; NMEN122586:GHGG-2173-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 68 AA; 7735 MW; D490F0DB2A34EBD0 CRC64; MNILSINNQN STISLTQDEV FVLRAILNEI YAGVCVDSRE FENVSGVRKH EVDNLQQQFA GIYKKMTT // ID Q9K050_NEIMB Unreviewed; 259 AA. AC Q9K050; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41184.1}; GN OrderedLocusNames=NMB0771 {ECO:0000313|EMBL:AAF41184.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41184.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41184.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41184.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41184.1; -; Genomic_DNA. DR PIR; H81159; H81159. DR RefSeq; NP_273813.1; NC_003112.2. DR RefSeq; WP_002225430.1; NC_003112.2. DR ProteinModelPortal; Q9K050; -. DR STRING; 122586.NMB0771; -. DR PaxDb; Q9K050; -. DR EnsemblBacteria; AAF41184; AAF41184; NMB0771. DR GeneID; 902886; -. DR KEGG; nme:NMB0771; -. DR PATRIC; 20356915; VBINeiMen85645_0976. DR eggNOG; ENOG4105F8V; Bacteria. DR eggNOG; COG0084; LUCA. DR HOGENOM; HOG000201520; -. DR KO; K03424; -. DR OMA; FFAIGAH; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; NMEN122586:GHGG-802-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR InterPro; IPR018228; DNase_TatD-rel_CS. DR InterPro; IPR015991; DNase_TatD-type. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005902; DNase_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00010; TIGR00010; 1. DR PROSITE; PS01137; TATD_1; 1. DR PROSITE; PS01091; TATD_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 259 AA; 28833 MW; D5046DFB3D32160A CRC64; MHIIDSHCHL NFEGLKERLP EVLSNMEANG VGQALAISVS RESFSEVFAI AEAHEHIYCT IGVHPDSKEA EEFSIAEMVE AAAHPKVVGI GETGLDYYWC KGDLSWQHKR FADHIEAANQ TGLPVIVHTR DAAADTLSIL KECRVNSGVI HCFSEDIGFA RAAMDLGLYI SFSGIVTFKN APLVQEAAKY VPDDRILVET DAPFLAPVPK RGRQNEPAFV RHTAEHIAKL RNQTLEQVAA YTTENFYRLF KKVPDMRTV // ID Q9JY29_NEIMB Unreviewed; 144 AA. AC Q9JY29; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42111.1}; GN OrderedLocusNames=NMB1771 {ECO:0000313|EMBL:AAF42111.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42111.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42111.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42111.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42111.1; -; Genomic_DNA. DR PIR; G81043; G81043. DR RefSeq; NP_274771.1; NC_003112.2. DR RefSeq; WP_010980984.1; NC_003112.2. DR STRING; 122586.NMB1771; -. DR PaxDb; Q9JY29; -. DR EnsemblBacteria; AAF42111; AAF42111; NMB1771. DR GeneID; 903328; -. DR KEGG; nme:NMB1771; -. DR BioCyc; NMEN122586:GHGG-1826-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 128 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 144 AA; 16615 MW; 229DEBF5BCB00423 CRC64; MNKNYLFYLI QNIKSIFLIG GVFFGLLIFS GLWGNDFKLS FLGVIDFIFG MVGGGFIVML WFLIPVILST LFRWVFQNQL AVSVILTFIV FYTYGYFSLF NSSERVGSFW YLVIPTIMFI GLSEWFIYKS SVHSLGENVT PRSN // ID Q9K0T2_NEIMB Unreviewed; 147 AA. AC Q9K0T2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40925.1}; GN OrderedLocusNames=NMB0491 {ECO:0000313|EMBL:AAF40925.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40925.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40925.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40925.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40925.1; -; Genomic_DNA. DR PIR; F81193; F81193. DR RefSeq; NP_273537.1; NC_003112.2. DR RefSeq; WP_010980803.1; NC_003112.2. DR STRING; 122586.NMB0491; -. DR PaxDb; Q9K0T2; -. DR EnsemblBacteria; AAF40925; AAF40925; NMB0491. DR GeneID; 902608; -. DR KEGG; nme:NMB0491; -. DR eggNOG; ENOG41073RS; Bacteria. DR eggNOG; ENOG410Z1I2; LUCA. DR HOGENOM; HOG000202537; -. DR BioCyc; NMEN122586:GHGG-516-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 147 AA; 17297 MW; 9FA0EF1E88F0D8AD CRC64; MAIFYFSSKK IERNIISSNL NRKQVRAIFS SDVQEIYKSS YSRVPMDVFP ELNIHCFYDD KNQLEAIEIF EPNKFFLEDI SFNWLGKIND EIISYLYKSG INDFEIDDLG IRLLNIPVST IINSIGKVEC CYLDFSNRDT KFYVKQV // ID Q9JXU1_NEIMB Unreviewed; 107 AA. AC Q9JXU1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42218.1}; GN OrderedLocusNames=NMB1884 {ECO:0000313|EMBL:AAF42218.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42218.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42218.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42218.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42218.1; -; Genomic_DNA. DR PIR; B81031; B81031. DR RefSeq; NP_274880.1; NC_003112.2. DR RefSeq; WP_002224094.1; NC_003112.2. DR ProteinModelPortal; Q9JXU1; -. DR STRING; 122586.NMB1884; -. DR PaxDb; Q9JXU1; -. DR EnsemblBacteria; AAF42218; AAF42218; NMB1884. DR GeneID; 904296; -. DR KEGG; nme:NMB1884; -. DR PATRIC; 20359803; VBINeiMen85645_2407. DR eggNOG; ENOG41082J7; Bacteria. DR eggNOG; COG0607; LUCA. DR HOGENOM; HOG000247776; -. DR OMA; EYELCHI; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-1940-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR001763; Rhodanese-like_dom. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 101 Rhodanese. {ECO:0000259|PROSITE:PS50206}. SQ SEQUENCE 107 AA; 12060 MW; 5929D1DB3551AE65 CRC64; MDIVQLGPAE LKAWMDEGRM FCLLDVRTDE ETAVCSLPNA LHIPMNLIPL RQNELPDDVP LVVYCHHGIR SLHTAMYLAD AGFENLYNLQ GGIDAWAAEI DGNMMRY // ID Q7DD87_NEIMB Unreviewed; 467 AA. AC Q7DD87; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Putative secretion protein {ECO:0000313|EMBL:AAF42081.1}; GN OrderedLocusNames=NMB1737 {ECO:0000313|EMBL:AAF42081.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42081.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42081.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42081.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42081.1; -; Genomic_DNA. DR RefSeq; NP_274739.1; NC_003112.2. DR RefSeq; WP_002212583.1; NC_003112.2. DR ProteinModelPortal; Q7DD87; -. DR STRING; 122586.NMB1737; -. DR PaxDb; Q7DD87; -. DR EnsemblBacteria; AAF42081; AAF42081; NMB1737. DR GeneID; 903362; -. DR KEGG; nme:NMB1737; -. DR PATRIC; 20359439; VBINeiMen85645_2225. DR eggNOG; ENOG4105DFG; Bacteria. DR eggNOG; COG1538; LUCA. DR HOGENOM; HOG000219082; -. DR KO; K12340; -. DR OMA; AMSQAEN; -. DR OrthoDB; EOG6JHRGC; -. DR BioCyc; NMEN122586:GHGG-1792-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR InterPro; IPR010130; T1SS_OMP_TolC. DR PANTHER; PTHR30026:SF3; PTHR30026:SF3; 1. DR Pfam; PF02321; OEP; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 467 AA; 52541 MW; A257682F52D2A411 CRC64; MTLLNLMIMQ DYGISVCLTL TPYLQHELFS AMKSYFSKYI LPVSLFTLPL SLSPSVSAFT LPEAWRAAQQ HSADFQASHY QRDAVRARQQ QAKAAFLPHV SANASYQRQP PSISSTRETQ GWSVQVGQTL FDAAKFAQYR QSRFDTQAAE QRFDAAREEL LLKVAESYFN VLLSRDTVAA HAAEKEAYAQ QVRQAQALFN KGAATALDIH EAKAGYDNAL AQEIAVLAEK QTYENQLNDY TDLDSKQIEA IDTANLLARY LPKLERYSLD EWQRIALSNN HEYRMQQLAL QSSGQALRAA QNSRYPTVSA HVGYQNNLYT SSAQNNDYHY RGKGMSVGVQ LNLPLYTGGE LSGKIHEAEA QYGAAEAQLT ATERHIKLAV RQAYTESGAA RYQIMAQERV LESSRLKLKS TETGQQYGIR NRLEVIRARQ EVAQAEQKLA QARYKFMLAY LRLVKESGLG LETVFAE // ID Q7DDQ3_NEIMB Unreviewed; 384 AA. AC Q7DDQ3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 78. DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369}; GN Name=pprC {ECO:0000313|EMBL:AAF40869.1}; GN OrderedLocusNames=NMB0431 {ECO:0000313|EMBL:AAF40869.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40869.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40869.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40869.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the citrate synthase family. CC {ECO:0000256|PIRNR:PIRNR001369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40869.1; -; Genomic_DNA. DR PIR; A81200; A81200. DR RefSeq; NP_273479.1; NC_003112.2. DR RefSeq; WP_002216540.1; NC_003112.2. DR ProteinModelPortal; Q7DDQ3; -. DR STRING; 122586.NMB0431; -. DR PaxDb; Q7DDQ3; -. DR EnsemblBacteria; AAF40869; AAF40869; NMB0431. DR GeneID; 902547; -. DR KEGG; nme:NMB0431; -. DR PATRIC; 20356062; VBINeiMen85645_0546. DR eggNOG; ENOG4105BZN; Bacteria. DR eggNOG; COG0372; LUCA. DR HOGENOM; HOG000021225; -. DR KO; K01659; -. DR OMA; SAYHYMG; -. DR OrthoDB; EOG6P8TP4; -. DR BioCyc; NMEN122586:GHGG-455-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046912; F:transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 1.10.230.10; -; 1. DR Gene3D; 1.10.580.10; -; 1. DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR019810; Citrate_synthase_AS. DR InterPro; IPR024176; Citrate_synthase_bac-typ. DR PANTHER; PTHR11739; PTHR11739; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PIRSF; PIRSF001369; Citrate_synth; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; SSF48256; 1. DR TIGRFAMs; TIGR01800; cit_synth_II; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:AAF40869.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF40869.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40869.1}. FT ACT_SITE 270 270 {ECO:0000256|PIRSR:PIRSR001369-1}. FT ACT_SITE 321 321 {ECO:0000256|PIRSR:PIRSR001369-1}. SQ SEQUENCE 384 AA; 42819 MW; 452B5D0031B37ECB CRC64; MTETTQTPTL KPKKSVALSG VAAGNTALCT VGRTGNDLSY RGYDILDLAQ KCEFEEVAHL LIHGHLPNKF ELAAYKTKLK SMRGLPIRVI KVLESLPAHT HPMDVMRTGV SMLGCVHPER ESHPESEARD IADKLIASLG SILLYWYQYS HNGKRIEVES DEETIGGHFL QLLHGKRPSE SHIKAMHVSL ILYAEHEFNA STFTARVIAG TGSDMYSSIT GAIGALKGPK HGGANEVAYD IQKRYRNADE AEADIRERIG RKEIVIGFGH PVYTISDPRN VVIKEVARGL SKETGDMRLF DIAERLESVM WEEKKMFPNL DWFSAVSYQK LGVPTAMFTP LFVISRTTGW SAHVLEQRKD GKIIRPSANY TGPEDLAFVE IEER // ID Q9JXF6_NEIMB Unreviewed; 64 AA. AC Q9JXF6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Thiamine biosynthesis protein ThiS {ECO:0000313|EMBL:AAF42389.1}; GN Name=thiS {ECO:0000313|EMBL:AAF42389.1}; GN OrderedLocusNames=NMB2070 {ECO:0000313|EMBL:AAF42389.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42389.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42389.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42389.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42389.1; -; Genomic_DNA. DR PIR; E81008; E81008. DR RefSeq; NP_275060.1; NC_003112.2. DR RefSeq; WP_002219965.1; NC_003112.2. DR ProteinModelPortal; Q9JXF6; -. DR STRING; 122586.NMB2070; -. DR PaxDb; Q9JXF6; -. DR EnsemblBacteria; AAF42389; AAF42389; NMB2070. DR GeneID; 903999; -. DR KEGG; nme:NMB2070; -. DR PATRIC; 20360300; VBINeiMen85645_2650. DR eggNOG; ENOG41067ZN; Bacteria. DR eggNOG; ENOG410XUTZ; LUCA. DR HOGENOM; HOG000248060; -. DR KO; K03154; -. DR OMA; NIEGAFA; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NMEN122586:GHGG-2133-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR010035; Thi_S. DR InterPro; IPR003749; ThiS/MoaD. DR Pfam; PF02597; ThiS; 1. DR SUPFAM; SSF54285; SSF54285; 1. DR TIGRFAMs; TIGR01683; thiS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 6657 MW; 25BBB49DE7B91BF2 CRC64; MNIILNGGPA ELHGTTVADL IAQTAPQKPF AVAVNTVFVP KGAYAETVLN ENDKIDIVRP VVGG // ID Q9K1R8_NEIMB Unreviewed; 163 AA. AC Q9K1R8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Putative acetyltransferase {ECO:0000313|EMBL:AAF40480.1}; GN OrderedLocusNames=NMB0001 {ECO:0000313|EMBL:AAF40480.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40480.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40480.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40480.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40480.1; -; Genomic_DNA. DR PIR; G81246; G81246. DR RefSeq; NP_273067.1; NC_003112.2. DR RefSeq; WP_002225747.1; NC_003112.2. DR ProteinModelPortal; Q9K1R8; -. DR STRING; 122586.NMB0001; -. DR PaxDb; Q9K1R8; -. DR EnsemblBacteria; AAF40480; AAF40480; NMB0001. DR GeneID; 902103; -. DR KEGG; nme:NMB0001; -. DR PATRIC; 20354929; VBINeiMen85645_0001. DR eggNOG; ENOG4105NPB; Bacteria. DR eggNOG; COG0454; LUCA. DR HOGENOM; HOG000218687; -. DR OMA; TIWHEVL; -. DR OrthoDB; EOG6GJC0M; -. DR BioCyc; NMEN122586:GHGG-1-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40480.1}. FT DOMAIN 18 161 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 163 AA; 18700 MW; ED332612AFA55FC3 CRC64; MNSLFVDNTV FITRLKAGHI GRLVQALFEE WHGFEPWSSV DKIHAYYGRC LKDDELPLAF AAVDDSGILL GSAAVKRHDM ESFPRYEYWL GDVFVLPEYR GKGIGRRLVA HCIGAARSLG IKFLYLYTPD VQIFYESFGW VVVGRHFHNG EWVTVMRLDV DKV // ID Q9JY11_NEIMB Unreviewed; 190 AA. AC Q9JY11; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42134.1}; GN OrderedLocusNames=NMB1796 {ECO:0000313|EMBL:AAF42134.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42134.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42134.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42134.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42134.1; -; Genomic_DNA. DR PIR; B81042; B81042. DR RefSeq; NP_274794.1; NC_003112.2. DR RefSeq; WP_002214471.1; NC_003112.2. DR ProteinModelPortal; Q9JY11; -. DR STRING; 122586.NMB1796; -. DR PaxDb; Q9JY11; -. DR EnsemblBacteria; AAF42134; AAF42134; NMB1796. DR GeneID; 903303; -. DR KEGG; nme:NMB1796; -. DR PATRIC; 20359559; VBINeiMen85645_2285. DR eggNOG; ENOG4108YYH; Bacteria. DR eggNOG; COG0431; LUCA. DR HOGENOM; HOG000263119; -. DR KO; K19784; -. DR OMA; NHHLRQC; -. DR OrthoDB; EOG6XHC2W; -. DR BioCyc; NMEN122586:GHGG-1851-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR005025; FMN_Rdtase-like. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 155 FMN_red. {ECO:0000259|Pfam:PF03358}. SQ SEQUENCE 190 AA; 20931 MW; 1081A8B36F909DA1 CRC64; MIMAKKISIL VGSLRRASFA RKVALNAAEM FPEGWQAEIV EIGHLPLYNF DYDDPAVEDV PLPESYTAFR ETIKASDGIL FVTSENNRTI PACLKNAVDI GSKPNADVAW KNKPAGIISH SVGKMGGYSS QKNLRLALSY FDMPVTGQPE VFLGNSPTLF DENGKLIDSA RDFVQSYINQ FVGLIERNAK // ID Q9JZL6_NEIMB Unreviewed; 1277 AA. AC Q9JZL6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:AAF41401.1}; GN OrderedLocusNames=NMB0998 {ECO:0000313|EMBL:AAF41401.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41401.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41401.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41401.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41401.1; -; Genomic_DNA. DR PIR; F81132; F81132. DR RefSeq; NP_274034.1; NC_003112.2. DR RefSeq; WP_002244102.1; NC_003112.2. DR ProteinModelPortal; Q9JZL6; -. DR STRING; 122586.NMB0998; -. DR PaxDb; Q9JZL6; -. DR EnsemblBacteria; AAF41401; AAF41401; NMB0998. DR GeneID; 903129; -. DR KEGG; nme:NMB0998; -. DR PATRIC; 20357513; VBINeiMen85645_1273. DR eggNOG; ENOG41066RF; Bacteria. DR eggNOG; COG0247; LUCA. DR eggNOG; COG0277; LUCA. DR HOGENOM; HOG000264473; -. DR OMA; FGLMGHE; -. DR OrthoDB; EOG6X9MH6; -. DR BioCyc; NMEN122586:GHGG-1035-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.43.10; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004017; Cys_rich_dom. DR InterPro; IPR021817; DUF3400. DR InterPro; IPR022153; DUF3683. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF02754; CCG; 2. DR Pfam; PF11880; DUF3400; 1. DR Pfam; PF12447; DUF3683; 1. DR Pfam; PF02913; FAD-oxidase_C; 2. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF55103; SSF55103; 2. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS51387; FAD_PCMH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 164 397 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. FT DOMAIN 803 833 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 865 894 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 1277 AA; 142030 MW; AFD3217160C31F5E CRC64; MTTTTAPQRI REIPYNYTSY TDREIVIRLL GDEAWQILQD LRGQRKTGRS ARMLFEVLGD IWVVVRNPYL VDDLLEHPKR RAALVREMRH RLNEIRKRRD DNRQVDVLVA AAEKAVERFD SSFDETSQKR RQILERLSKI TKPHNIMFDG LARVTHVTDA TDWRVEYPFV VVNPDTEAEI APLVRALIEL DLVIIPRGGG TGYTGGAIPL DANSAVINTE KLDKHRGVEY VELAGLDGKH PIIRCGAGVV TRRVEETAHQ AGLVFAVDPT SADASCVGGN VAMNAGGKKA VLWGTALDNL AYWNMVNPQG EWLRIERVRH NFGKIHDEET AVFDVHTLDS DGINIVKTER LEIPGHKFRK VGLGKDVTDK FLSGLPGVQK EGTDGIITSV AFVLHKMPKY TRTVCMEFFG TVATATPSIV EIRDFLLAHE SVRLAGLEHL DWRYVRAVGY ATKAAGKGRP KMVLLADVVS DDEAAVEAAA EHICELARAR DGEGFIAVSP EARKTFWLDR SRTAAIAKHT NAFKINEDVV IPLERLGEYS DGIERINIEL SIQNKLKLCA ALEQYLSGKL PIDKMGTDLP TAELLGERGK HALAHVSAVK TRWEWLLANL DTPLADYKAR YGAAVHAAPE AKNNESCFIA FRDFRLRVSV KADVMKPLSE IFSGKTDTKI IQGLGKIHAK TVRSRVFVAL HMHAGDGNVH TNIPVNSDDA EMLQTAYRSV ERIMKIARSL NGVISGEHGI GITKLEFLSD EEMQPFWDYK NQVDPKHTFN RHKLMKGSDL RNAYTPSFEL LGAESLIMEK SNLGTIADSV KDCLRCGKCK PVCSTHVPRA NLLYSPRNKI LGVGLLIEAF LYEEQTRRGV SIKHFEELMD IGDHCTVCHR CVKPCPVNID FGDVTVAVRN YLADSGHKRF APAAAMGMAF LNATGPKTIK ALRAAMIQIG FPAQNFAYKI GKLLPIGTKK QKAEPKATVG KAPIKEQVIH FINRPLPKNV PAKTPRSLLG IEDGKSIPII RNPAAPEDAE AVFYFPGCGS ERLFSQIGLA VQAMLWHVGV QTVLPPGYMC CGYPQDAGGN KAKAEEMSTN NRVAFHRMAN TLNYLDIKTV VVSCGTCYDQ LEKYRFEEIF PGCRIIDIHE YLLEKGVKLD GVKGQQYLYH DPCHTPIKTM NATQMASSLM GQKVVLSDRC CGESGMFAVK RPDIATQVKF RKQEEIEKNL KELPQGEPVK MLTSCPACLQ GLSRYADDNN MPADYIVIEM AKYILGENWL DEFVKKANNG GVEKVLL // ID Q9JYE2_NEIMB Unreviewed; 751 AA. AC Q9JYE2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Nitric oxide reductase {ECO:0000313|EMBL:AAF41974.1}; DE EC=1.7.99.- {ECO:0000313|EMBL:AAF41974.1}; GN Name=norB {ECO:0000313|EMBL:AAF41974.1}; GN OrderedLocusNames=NMB1622 {ECO:0000313|EMBL:AAF41974.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41974.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41974.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41974.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41974.1; -; Genomic_DNA. DR PIR; D81062; D81062. DR RefSeq; NP_274628.1; NC_003112.2. DR RefSeq; WP_010980966.1; NC_003112.2. DR STRING; 122586.NMB1622; -. DR PaxDb; Q9JYE2; -. DR EnsemblBacteria; AAF41974; AAF41974; NMB1622. DR GeneID; 904040; -. DR KEGG; nme:NMB1622; -. DR PATRIC; 20359144; VBINeiMen85645_2083. DR eggNOG; ENOG4105DSQ; Bacteria. DR eggNOG; COG3256; LUCA. DR HOGENOM; HOG000288072; -. DR KO; K04561; -. DR OMA; QGYEYID; -. DR OrthoDB; EOG6PW211; -. DR BioCyc; NMEN122586:GHGG-1671-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR Pfam; PF00115; COX1; 1. DR SUPFAM; SSF81442; SSF81442; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41974.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 306 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 361 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 373 398 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 418 439 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 451 472 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 484 510 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 522 545 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 551 571 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 592 615 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 635 657 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 669 697 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 729 747 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 751 AA; 84384 MW; 2995F665A5935F4D CRC64; MGQYKKLWYL LFAVLAVCFT ILGYMGSEVY KKAPPYPEQV VSASGKVLMT KDDILAGQSA WQTTGGMEVG SILGHGAYQA PDWTADWLHR ELVAWLDLTA QQTYGKKFDE VSPEEQAVLK TRLADEYRNQ SRVKEDGSVV ISDTRVKAIE SILPYYHGVY SDDPKFQTTR EHFAMKNNTL PSQEAREKLF NFFFWTSWSA STNRPDENFT YTNNWPHEPL INNVPTTENY MWSFTSVVLL LMGIGLLMWG YSFLTKHEEV EVPSEDPISK IQLTPSQKAL GKYVFLTVAL FVVQVLLGGL TAHYTVEGQG FYGIDEALGF EMSDWFPYAL TRTWHIQSAI FWIATGFLTA GLFLAPIVNG GKDPKFQRAG VNFLYIALFI VVGGSYAGNF FALTHILPPE FNFWFGHQGY EYLDLGRFWQ LLLMVGLLLW LFLMLRCTVS AFKEKGVDKN LLAIFVASMV GVGVFYAPGL FYGEKSPIAV MEYWRWWVVH LWVEGFFEVF ATAAFAFVFY NMGFVRRSTA TASTLAAAAI FMLGGVPGTL HHLYFSGSTS ASMAIGACFS ALEVVPLVLL GREAYEHWSY QHLSDWAKRL RWPLMCFVAV AFWNMIGAGV FGFLINPPIS LFYIQGLNTS AVHAHAALFG VYGFLALGFV LLVARYLKPN AQFDDKLMTW GFWLLNGGLA GMIAISLLPV GAIQAYASIT HGLWYARSEE FLQMEILDTL RWVRTAADLV FIGGAICVAI QATKIVFGRD K // ID Q9K0B8_NEIMB Unreviewed; 242 AA. AC Q9K0B8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 104. DE SubName: Full=Amino acid ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41113.1}; GN OrderedLocusNames=NMB0696 {ECO:0000313|EMBL:AAF41113.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41113.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41113.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41113.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41113.1; -; Genomic_DNA. DR PIR; G81168; G81168. DR RefSeq; NP_273738.1; NC_003112.2. DR RefSeq; WP_002233691.1; NC_003112.2. DR ProteinModelPortal; Q9K0B8; -. DR SMR; Q9K0B8; 1-239. DR STRING; 122586.NMB0696; -. DR PaxDb; Q9K0B8; -. DR EnsemblBacteria; AAF41113; AAF41113; NMB0696. DR GeneID; 902808; -. DR KEGG; nme:NMB0696; -. DR PATRIC; 20356721; VBINeiMen85645_0882. DR eggNOG; ENOG4105CDA; Bacteria. DR eggNOG; COG1126; LUCA. DR KO; K02028; -. DR OMA; VFFEGGK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-724-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030679; ABC_ATPase_HisP-typ. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41113.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41113.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 242 AA; 27011 MW; 00F59297739C6BA5 CRC64; MIKFKNVHKH FKDLHVINGV NLEIKKGEVV VVCGPSGSGK STLIRTVNQL ESIESGEIWV DGVNVADPKT DLNKIREEVG FVFQGFNLYP HLTVLENITL APMKVKGQNA EQAEKKAMEL LERVGLAHKK DAFPSQLSGG QQQRVAIARG LAMEPRVMLF DEPTSALDPE MVGEVLKVMK DLAESGMTMM CVTHEMGFAR EVADRVIFVD KGQILEDETP EAFFTNPKHE RAKQFLQQVM TH // ID Q9K017_NEIMB Unreviewed; 216 AA. AC Q9K017; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Transcriptional regulator, TetR family {ECO:0000313|EMBL:AAF41223.1}; GN OrderedLocusNames=NMB0810 {ECO:0000313|EMBL:AAF41223.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41223.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41223.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41223.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41223.1; -; Genomic_DNA. DR PIR; A81156; A81156. DR RefSeq; NP_273852.1; NC_003112.2. DR RefSeq; WP_010980850.1; NC_003112.2. DR ProteinModelPortal; Q9K017; -. DR STRING; 122586.NMB0810; -. DR PaxDb; Q9K017; -. DR EnsemblBacteria; AAF41223; AAF41223; NMB0810. DR GeneID; 902925; -. DR KEGG; nme:NMB0810; -. DR PATRIC; 20357007; VBINeiMen85645_1022. DR eggNOG; ENOG4108VVF; Bacteria. DR eggNOG; COG1309; LUCA. DR HOGENOM; HOG000262674; -. DR OMA; HYPAKDE; -. DR OrthoDB; EOG62ZJ03; -. DR BioCyc; NMEN122586:GHGG-841-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR025722; TetR. DR Pfam; PF13972; TetR; 1. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}; KW Transcription regulation {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}. FT DOMAIN 9 69 HTH tetR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50977}. SQ SEQUENCE 216 AA; 24832 MW; 350C72AAAF10597A CRC64; MPVTRPAKIN TYTRIIDASL ALFNEEGERN ISTNHIAAHL GISPGNLYYH FRNKDEIIVQ LFKRYSEALL AYLNEAVLPS DVEDSINYMA GIYDVMWEYR FLFSDVNTLL ARSAELLGEH NTFTQAKVSP LLVNLLTQLN GLNIIQADQT AMNDLAVNMW MVTKYWFDFD SSLRGRTKLT EDSKARGIRR TLSLLRPYLL PEHRKKYDRK IGNGNP // ID Q9JYK6_NEIMB Unreviewed; 335 AA. AC Q9JYK6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=IS1106 transposase {ECO:0000313|EMBL:AAF41894.1}; GN OrderedLocusNames=NMB1539 {ECO:0000313|EMBL:AAF41894.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41894.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41894.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41894.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41894.1; -; Genomic_DNA. DR PIR; G81072; G81072. DR RefSeq; NP_274546.1; NC_003112.2. DR RefSeq; WP_002225050.1; NC_003112.2. DR PaxDb; Q9JYK6; -. DR EnsemblBacteria; AAF41894; AAF41894; NMB1539. DR GeneID; 904074; -. DR KEGG; nme:NMB1539; -. DR PATRIC; 20358882; VBINeiMen85645_1950. DR eggNOG; ENOG4105F2I; Bacteria. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000218682; -. DR KO; K07481; -. DR OMA; RCGVLHC; -. DR OrthoDB; EOG6RZB5B; -. DR BioCyc; NMEN122586:GHGG-1580-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR002559; Transposase_11. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF01609; DDE_Tnp_1; 1. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 51 122 DUF772. {ECO:0000259|Pfam:PF05598}. FT DOMAIN 139 322 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 335 AA; 38507 MW; 2C2EDB04B04C7B1C CRC64; MSTFFQQTAQ AMIAKHIDRF PLLKLDQVID WQPIEQYLNR QRTRYLRDHR GRPAYPLLSM FKAVLLGQWH SLSDPELEHS LITRIDFNLF CRFDELSIPD YSTLCRYRNW LAQDDTLSEL LELINCQLTE KGLKVEKASA AVVDATIIQT AGSKQRQAIE VDEEGQVSGQ TTPSKDSDAR WIKKNGLYKL GYKQHTRTDA EGYIEKLHIT PANAHECKHL SPLLEGLPEG TTVYADKGYD SAENRQHLEE HQLQDGIMRK ACRNRPLSEV QTKRNRYLSK TRYVVEQSFG TLHRKFRYAR AAYFGLIKVS VQSHLKAMCL NLLKAANRLS APVAA // ID Q9K127_NEIMB Unreviewed; 128 AA. AC Q9K127; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40809.1}; GN OrderedLocusNames=NMB0367 {ECO:0000313|EMBL:AAF40809.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40809.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40809.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40809.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40809.1; -; Genomic_DNA. DR PIR; E81206; E81206. DR RefSeq; NP_273416.1; NC_003112.2. DR RefSeq; WP_009346283.1; NC_003112.2. DR STRING; 122586.NMB0367; -. DR PaxDb; Q9K127; -. DR EnsemblBacteria; AAF40809; AAF40809; NMB0367. DR GeneID; 902482; -. DR KEGG; nme:NMB0367; -. DR PATRIC; 20355891; VBINeiMen85645_0463. DR eggNOG; ENOG41077X7; Bacteria. DR eggNOG; ENOG410Z4X8; LUCA. DR HOGENOM; HOG000219105; -. DR OMA; KDIVNVQ; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NMEN122586:GHGG-389-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 128 AA; 15638 MW; CBB256E289E5A859 CRC64; MCIMCELKNF RRNITCFEGY DENSFIGKWY DDGVWDDEEY WKLENDLIEV RKKYPYPMDI PRYVVIGIGT IIDFLMVPNW KLFEIKASPW LPDSVGINER YERLKTMLRY IFTEKDIVNV QFDYYNKK // ID Q9JZT7_NEIMB Unreviewed; 86 AA. AC Q9JZT7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41312.1}; GN OrderedLocusNames=NMB0904 {ECO:0000313|EMBL:AAF41312.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41312.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41312.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41312.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41312.1; -; Genomic_DNA. DR PIR; E81144; E81144. DR RefSeq; NP_273944.1; NC_003112.2. DR RefSeq; WP_002223443.1; NC_003112.2. DR STRING; 122586.NMB0904; -. DR PaxDb; Q9JZT7; -. DR EnsemblBacteria; AAF41312; AAF41312; NMB0904. DR GeneID; 903025; -. DR KEGG; nme:NMB0904; -. DR PATRIC; 20357243; VBINeiMen85645_1135. DR HOGENOM; HOG000220715; -. DR OrthoDB; EOG632D6X; -. DR BioCyc; NMEN122586:GHGG-942-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 86 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327742. FT COILED 43 70 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 86 AA; 9512 MW; 4F3DEA2DCFCDF9BE CRC64; MKYLIRTALL AVAAAGIYAC QPQSEAAVQV KAENSLTAMR LAVADKQAEI DGLNAQIDAE IRQREAEELK DYRWIHGDAE VPELEK // ID Q7DDP1_NEIMB Unreviewed; 169 AA. AC Q7DDP1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40930.1}; GN OrderedLocusNames=NMB0498 {ECO:0000313|EMBL:AAF40930.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40930.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40930.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40930.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40930.1; -; Genomic_DNA. DR RefSeq; NP_273544.1; NC_003112.2. DR RefSeq; WP_002219760.1; NC_003112.2. DR STRING; 122586.NMB0498; -. DR PaxDb; Q7DDP1; -. DR EnsemblBacteria; AAF40930; AAF40930; NMB0498. DR GeneID; 902614; -. DR KEGG; nme:NMB0498; -. DR PATRIC; 20356246; VBINeiMen85645_0643. DR OrthoDB; EOG6FV84D; -. DR BioCyc; NMEN122586:GHGG-523-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 169 AA; 20334 MW; 9855906E25C7A930 CRC64; MSNFEKKYIL ELNDALSHLN HNSTSFDLLK VLISWLSNDI VIDKFKILGY DFSKYIEMNP DDYPVEKSIL NREEIIYLKN NIYRKISSGN FKFQYFVQYI RDILEYLFIE HIERVCPYCE WGEMQKLEEQ NTHETVYLCT QCGCAFYNDN SQFLLKTPLT IPMKRDEFK // ID Q7DDE0_NEIMB Unreviewed; 153 AA. AC Q7DDE0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41584.1}; GN OrderedLocusNames=NMB1202 {ECO:0000313|EMBL:AAF41584.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41584.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41584.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41584.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41584.1; -; Genomic_DNA. DR PIR; A81110; A81110. DR RefSeq; NP_274227.1; NC_003112.2. DR RefSeq; WP_002213539.1; NC_003112.2. DR STRING; 122586.NMB1202; -. DR PaxDb; Q7DDE0; -. DR EnsemblBacteria; AAF41584; AAF41584; NMB1202. DR GeneID; 903624; -. DR KEGG; nme:NMB1202; -. DR eggNOG; ENOG41072V0; Bacteria. DR eggNOG; ENOG410Z099; LUCA. DR HOGENOM; HOG000218957; -. DR OMA; LNTVFNS; -. DR OrthoDB; EOG6GJBTD; -. DR BioCyc; NMEN122586:GHGG-1239-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 153 AA; 17558 MW; AEC91F6FAB73D9F0 CRC64; MNIIMDSTRK FGILWEENSE CNGFIYGKIQ IIIGENIYPK ICPYGYFTLN AVFNSLKSSF EEKYYAGGNN GLDFGEQLFD IDKYNSLELC NIFSIDTTYM SGGGNCEIDC LVLEMGYSGE EERLFYSFDN GKNFKEIRYK KGTVESVIFQ LNL // ID Q9JZ33_NEIMB Unreviewed; 134 AA. AC Q9JZ33; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41692.1}; GN OrderedLocusNames=NMB1317 {ECO:0000313|EMBL:AAF41692.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41692.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41692.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41692.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41692.1; -; Genomic_DNA. DR PIR; D81096; D81096. DR RefSeq; NP_274336.1; NC_003112.2. DR RefSeq; WP_002219163.1; NC_003112.2. DR STRING; 122586.NMB1317; -. DR PaxDb; Q9JZ33; -. DR EnsemblBacteria; AAF41692; AAF41692; NMB1317. DR GeneID; 903739; -. DR KEGG; nme:NMB1317; -. DR PATRIC; 20358281; VBINeiMen85645_1652. DR HOGENOM; HOG000220747; -. DR OrthoDB; EOG6T1WSS; -. DR BioCyc; NMEN122586:GHGG-1355-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 134 AA; 14836 MW; 85373C3A3568F331 CRC64; MANRFQQRKS AYRRLSGKPL FSDGIAANLC GGRKTLSYNL SRFKISIRSE MQKISFNLLK PANSPKIGKR RPGLNGAPHI PMPSPRYLPA SPEMPGNNIH PAKIRNNTPG GRQSQTAPQS IRHQKNKPPP RASS // ID Q9JXU2_NEIMB Unreviewed; 96 AA. AC Q9JXU2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42217.1}; GN OrderedLocusNames=NMB1883 {ECO:0000313|EMBL:AAF42217.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42217.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42217.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42217.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42217.1; -; Genomic_DNA. DR PIR; A81031; A81031. DR RefSeq; NP_274879.1; NC_003112.2. DR RefSeq; WP_002223044.1; NC_003112.2. DR STRING; 122586.NMB1883; -. DR PaxDb; Q9JXU2; -. DR EnsemblBacteria; AAF42217; AAF42217; NMB1883. DR GeneID; 904298; -. DR KEGG; nme:NMB1883; -. DR OMA; GRGWQTE; -. DR BioCyc; NMEN122586:GHGG-1939-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 96 AA; 10879 MW; BBA125FB7146301A CRC64; MRQAFQTAFL KCVYLWCSKR SSESAASAKL KRGINEVKIC LNLKGSLHPN PLSRGRGLGR GGQTESLLGR HFQCAGCFYS GLTKIRTRRR SRRQYK // ID Q9JZT4_NEIMB Unreviewed; 119 AA. AC Q9JZT4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41315.1}; GN OrderedLocusNames=NMB0907 {ECO:0000313|EMBL:AAF41315.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41315.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41315.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41315.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41315.1; -; Genomic_DNA. DR PIR; H81144; H81144. DR RefSeq; NP_273947.1; NC_003112.2. DR RefSeq; WP_002219432.1; NC_003112.2. DR STRING; 122586.NMB0907; -. DR PaxDb; Q9JZT4; -. DR EnsemblBacteria; AAF41315; AAF41315; NMB0907. DR GeneID; 903028; -. DR KEGG; nme:NMB0907; -. DR PATRIC; 20357249; VBINeiMen85645_1138. DR eggNOG; ENOG41069QG; Bacteria. DR eggNOG; ENOG410XYUM; LUCA. DR HOGENOM; HOG000220718; -. DR OMA; TRTENQI; -. DR OrthoDB; EOG6C018B; -. DR BioCyc; NMEN122586:GHGG-945-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 119 AA; 12969 MW; E871B20B591CBD20 CRC64; METQEKKFVP ASKQIPTVNS GWLDRELGEA MSEAVRACLA HGKQSEITVK LKIQPQNIQS GTVKISHDVA TKLPKEKREG GIVFATPDGN IQADDPAQGK LKLKQVSNTS STLKMVRSN // ID Q9JYV4_NEIMB Unreviewed; 867 AA. AC Q9JYV4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 104. DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:AAF41777.1}; DE EC=3.4.11.2 {ECO:0000313|EMBL:AAF41777.1}; GN Name=pepN {ECO:0000313|EMBL:AAF41777.1}; GN OrderedLocusNames=NMB1416 {ECO:0000313|EMBL:AAF41777.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41777.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41777.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41777.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2GTQ} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ZINC. RX PubMed=17876832; DOI=10.1002/prot.21276; RA Nocek B., Mulligan R., Bargassa M., Collart F., Joachimiak A.; RT "Crystal structure of aminopeptidase N from human pathogen Neisseria RT meningitidis."; RL Proteins 70:273-279(2008). RN [3] {ECO:0000213|PDB:4QHP, ECO:0000213|PDB:4QIR, ECO:0000213|PDB:4QME} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-867 IN COMPLEX WITH ZINC. RX PubMed=25192493; DOI=10.1021/jm501071f; RA Vassiliou S., Weglarz-Tomczak E., Berlicki L., Pawelczak M., Nocek B., RA Mulligan R., Joachimiak A., Mucha A.; RT "Structure-guided, single-point modifications in the phosphinic RT dipeptide structure yield highly potent and selective inhibitors of RT neutral aminopeptidases."; RL J. Med. Chem. 57:8140-8151(2014). RN [4] {ECO:0000213|PDB:4PW4} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ZINC. RG Midwest Center for Structural Genomics (MCSG); RA Nocek B., Vassiliou S., Mulligan R., Weglarz-Tomczak E., Berlicki L., RA Pawelczak M., Joachimiak A., Mucha A.; RT "Crystal structure of Aminopeptidase N in complex with phosphonic RT analogs of homophenylalanine."; RL Submitted (MAR-2014) to the PDB data bank. RN [5] {ECO:0000213|PDB:4PVB} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC. RG Midwest Center for Structural Genomics (MCSG); RA Nocek B., Vassiliou S., Mulligan R., Weglarz-Tomczak E., Berlicki L., RA Pawelczak M., Mucha A., Joachimiak A.; RT "Crystal structure of Aminopeptidase N in complex with the phosphonic RT acid analogue of leucine (D-(S)-LeuP)."; RL Submitted (MAR-2014) to the PDB data bank. RN [6] {ECO:0000213|PDB:4PU2} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC. RG Midwest Center for Structural Genomics (MCSG); RA Nocek B., Vassiliou S., Mulligan R., Weglarz-Tomczak E., Berlicki L., RA Pawelczak M., Joachimiak A., Mucha A.; RT "Crystal structure of Aminopeptidase N in complex with the phosphonic RT acid analogue of leucine."; RL Submitted (MAR-2014) to the PDB data bank. RN [7] {ECO:0000213|PDB:5DYF} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RG Midwest Center for Structural Genomics (MCSG); RA Nocek B., Joachimiak A., Vassiliou S., Berlicki L., Mucha A.; RT "The crystal structure of Aminopeptidase N in complex with N-benzyl- RT 1,2-diaminoethylphosphonic acid."; RL Submitted (SEP-2015) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41777.1; -; Genomic_DNA. DR PIR; F81086; F81086. DR RefSeq; NP_274428.1; NC_003112.2. DR RefSeq; WP_002225125.1; NC_003112.2. DR PDB; 2GTQ; X-ray; 2.05 A; A=1-867. DR PDB; 4PU2; X-ray; 2.10 A; A=1-867. DR PDB; 4PVB; X-ray; 2.10 A; A=1-867. DR PDB; 4PW4; X-ray; 1.85 A; A=1-867. DR PDB; 4QHP; X-ray; 1.60 A; A=1-867. DR PDB; 4QIR; X-ray; 1.70 A; A=1-867. DR PDB; 4QME; X-ray; 1.60 A; A=2-867. DR PDB; 4QPE; X-ray; 2.00 A; A=1-867. DR PDB; 4QUO; X-ray; 1.65 A; A=3-867. DR PDB; 5DYF; X-ray; 1.85 A; A=1-867. DR PDBsum; 2GTQ; -. DR PDBsum; 4PU2; -. DR PDBsum; 4PVB; -. DR PDBsum; 4PW4; -. DR PDBsum; 4QHP; -. DR PDBsum; 4QIR; -. DR PDBsum; 4QME; -. DR PDBsum; 4QPE; -. DR PDBsum; 4QUO; -. DR PDBsum; 5DYF; -. DR ProteinModelPortal; Q9JYV4; -. DR SMR; Q9JYV4; 4-867. DR STRING; 122586.NMB1416; -. DR PaxDb; Q9JYV4; -. DR EnsemblBacteria; AAF41777; AAF41777; NMB1416. DR GeneID; 903838; -. DR KEGG; nme:NMB1416; -. DR PATRIC; 20358515; VBINeiMen85645_1769. DR eggNOG; ENOG4105CD8; Bacteria. DR eggNOG; COG0308; LUCA. DR HOGENOM; HOG000257670; -. DR KO; K01256; -. DR OMA; FKRWYSQ; -. DR OrthoDB; EOG693GJ0; -. DR BioCyc; NMEN122586:GHGG-1454-MONOMER; -. DR BRENDA; 3.4.11.2; 3593. DR EvolutionaryTrace; Q9JYV4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 1.25.50.10; -; 1. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_N. DR InterPro; IPR012779; Peptidase_M1_pepN. DR InterPro; IPR024601; Peptidase_M1_pepN_C. DR PANTHER; PTHR11533; PTHR11533; 2. DR Pfam; PF11940; DUF3458; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR TIGRFAMs; TIGR02414; pepN_proteo; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GTQ, ECO:0000213|PDB:4PU2, KW ECO:0000213|PDB:4PVB, ECO:0000213|PDB:4PW4}; KW Aminopeptidase {ECO:0000313|EMBL:AAF41777.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41777.1}; KW Metal-binding {ECO:0000213|PDB:2GTQ, ECO:0000213|PDB:4PU2, KW ECO:0000213|PDB:4PVB, ECO:0000213|PDB:4PW4}; KW Protease {ECO:0000313|EMBL:AAF41777.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000213|PDB:2GTQ, ECO:0000213|PDB:4PU2, KW ECO:0000213|PDB:4PVB, ECO:0000213|PDB:4PW4}. FT DOMAIN 102 380 Peptidase_M1. {ECO:0000259|Pfam:PF01433}. FT DOMAIN 454 824 DUF3458. {ECO:0000259|Pfam:PF11940}. FT METAL 293 293 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:2GTQ, FT ECO:0000213|PDB:4PU2, FT ECO:0000213|PDB:4PVB}. FT METAL 297 297 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:2GTQ, FT ECO:0000213|PDB:4PU2, FT ECO:0000213|PDB:4PVB}. FT METAL 316 316 Zinc. {ECO:0000213|PDB:2GTQ, FT ECO:0000213|PDB:4PU2, FT ECO:0000213|PDB:4PVB}. SQ SEQUENCE 867 AA; 97681 MW; 19D37D5A8F863C7D CRC64; MSKTVHYLKD YQTPAYHILK TDLHFDINEP QTVVKSRLTV EPQRVGEPLV LDGSAKLLSV KINGAAADYV LEGETLTIAG VPSERFTVEV ETEILPAENK SLMGLYASGG NLFTQCEPEG FRKITFYIDR PDVMSKFTTT IVADKKRYPV LLSNGNKIDG GEFSDGRHWV KWEDPFSKPS YLFALVAGDL AVTEDYFTTM SGRNVKIEFY TTEADKPKVG FAVESLKNAM KWDETRFGLE YDLDIFMVVA VGDFNMGAME NKGLNIFNTK FVLADSRTAT DTDFEGIESV VGHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFSGDR ASRAVRRIEN IRLLRQHQFP EDAGPTAHPV RPASYEEMNN FYTMTVYEKG AEVVRMYHTL LGEEGFQKGM KLYFQRHDGQ AVTCDDFRAA MADANGINLD QFALWYSQAG TPVLEAEGRL KNNIFELTVK QTVPPTPDMT DKQPMMIPVK VGLLNRNGEA VAFDYQGKRA TEAVLLLTEA EQTFLLEGVT EAVVPSLLRG FSAPVHLNYP YSDDDLLLLL AHDSDAFTRW EAAQTLYRRA VAANLATLSD GVELPKHEKL LAAVEKVISD DLLDNAFKAL LLGVPSEAEL WDGAENIDPL RYHQAREALL DTLAVHFLPK WHELNRQAAK QENQSYEYSP EAAGWRTLRN VCRAFVLRAD PAHIETVAEK YGEMAQNMTH EWGILSAVNG NESDTRNRLL AQFADKFSDD ALVMDKYFAL VGSSRRSDTL QQVRTALQHP KFSLENPNKA RSLIGSFSRN VPHFHAEDGS GYRFIADKVI EIDRFNPQVA ARLVQAFNLC NKLEPHRKNL VKQALQRIRA QEGLSKDVGE IVGKILD // ID Q7DDC3_NEIMB Unreviewed; 282 AA. AC Q7DDC3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=RpiR/YebK/YfhH family protein {ECO:0000313|EMBL:AAF41753.1}; GN OrderedLocusNames=NMB1389 {ECO:0000313|EMBL:AAF41753.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41753.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41753.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41753.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41753.1; -; Genomic_DNA. DR PIR; D81089; D81089. DR RefSeq; NP_274403.1; NC_003112.2. DR RefSeq; WP_002213148.1; NC_003112.2. DR ProteinModelPortal; Q7DDC3; -. DR STRING; 122586.NMB1389; -. DR PaxDb; Q7DDC3; -. DR EnsemblBacteria; AAF41753; AAF41753; NMB1389. DR GeneID; 903811; -. DR KEGG; nme:NMB1389; -. DR PATRIC; 20358461; VBINeiMen85645_1742. DR eggNOG; ENOG4106KNT; Bacteria. DR eggNOG; COG1737; LUCA. DR HOGENOM; HOG000027158; -. DR KO; K19337; -. DR OMA; GRTRDLM; -. DR OrthoDB; EOG6HMXHM; -. DR BioCyc; NMEN122586:GHGG-1427-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR000281; HTH_RpiR. DR InterPro; IPR001347; SIS. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01418; HTH_6; 1. DR Pfam; PF01380; SIS; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS51071; HTH_RPIR; 1. DR PROSITE; PS51464; SIS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 75 HTH rpiR-type DNA-binding. FT {ECO:0000259|PROSITE:PS51071}. FT DOMAIN 120 259 SIS. {ECO:0000259|PROSITE:PS51464}. SQ SEQUENCE 282 AA; 30382 MW; 6D80CFFA63C58252 CRC64; MLSKISESLA NLSGAERKVA ECALAEPKWF VHAAVAEIAE RASVSQPTVI RFCRSLGYKG LPEFKLALSA SIGHEGMPYV HEELNADDDM ASVVEKVLGN AAASLLGERR FLKESELENA IATLMHARRV EFYGVGNSGI VAQDAQHKFF RFGMSTVAYV DTHTQLMAAS VLSDQDVLVA ISNTGSSIEL LDAVSIAKEN GASVIALTRN DSPLAQLADC VLSVATQENA ELYTPMVSRL LQLAVIDILA IGLALRLGDA ASLQLQKSKK SIHNKHIDYD KD // ID Q9K0T5_NEIMB Unreviewed; 164 AA. AC Q9K0T5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40923.1}; GN OrderedLocusNames=NMB0488 {ECO:0000313|EMBL:AAF40923.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40923.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40923.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40923.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2GKP} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS). RA Osipiuk J., Volkart L., Bargassa M., Joachimiak A.; RT "X-ray crystal structure of hypothetical protein NMB0488 from RT Neisseria meningitidis."; RL Submitted (APR-2006) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40923.1; -; Genomic_DNA. DR PIR; D81193; D81193. DR RefSeq; NP_273534.1; NC_003112.2. DR RefSeq; WP_002222084.1; NC_003112.2. DR PDB; 2GKP; X-ray; 1.35 A; A=1-164. DR PDBsum; 2GKP; -. DR ProteinModelPortal; Q9K0T5; -. DR SMR; Q9K0T5; 1-164. DR STRING; 122586.NMB0488; -. DR PaxDb; Q9K0T5; -. DR EnsemblBacteria; AAF40923; AAF40923; NMB0488. DR GeneID; 902605; -. DR KEGG; nme:NMB0488; -. DR PATRIC; 20356230; VBINeiMen85645_0635. DR eggNOG; ENOG4105WEK; Bacteria. DR eggNOG; ENOG41123B4; LUCA. DR HOGENOM; HOG000220757; -. DR OMA; PRTDIWI; -. DR OrthoDB; EOG6423DR; -. DR BioCyc; NMEN122586:GHGG-513-MONOMER; -. DR EvolutionaryTrace; Q9K0T5; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1590.10; -; 1. DR InterPro; IPR009888; CdiI-o11. DR InterPro; IPR023127; NMB0488-like_domain. DR Pfam; PF07262; DUF1436; 1. DR SUPFAM; SSF160207; SSF160207; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GKP}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 164 AA; 18844 MW; B41D757E8EA9F4DF CRC64; MTFNQEQDYW AGYKANERAL IIQTWSGFGR YAPDHLYPPH ILPLDTDNET LGTTVLQALA NSRTFVYDSP EDQDFFDTEK IRQRYEDWVA KLCGNLGYKT RRALFKNMMS VDIWLHNGCL KISPSRHVKL EAWDAIDADD VILSLDNSPE EIGAGLKLAL SRCR // ID Q9K0L4_NEIMB Unreviewed; 206 AA. AC Q9K0L4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=Copper ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41007.1}; GN Name=nosF {ECO:0000313|EMBL:AAF41007.1}; GN OrderedLocusNames=NMB0579 {ECO:0000313|EMBL:AAF41007.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41007.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41007.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41007.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41007.1; -; Genomic_DNA. DR PIR; F81183; F81183. DR RefSeq; NP_273623.1; NC_003112.2. DR RefSeq; WP_002235538.1; NC_003112.2. DR ProteinModelPortal; Q9K0L4; -. DR STRING; 122586.NMB0579; -. DR PaxDb; Q9K0L4; -. DR EnsemblBacteria; AAF41007; AAF41007; NMB0579. DR GeneID; 902694; -. DR KEGG; nme:NMB0579; -. DR PATRIC; 20356439; VBINeiMen85645_0739. DR eggNOG; ENOG4105DVE; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K19340; -. DR OMA; DYFKRVT; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; NMEN122586:GHGG-605-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41007.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41007.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 205 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 206 AA; 22336 MW; 51A6E3AA7545A0A8 CRC64; MTTHHVELRK VTKRFGAQKA VNQVDLVLKA GESVGLAGHN GAGKSTIMKL ILGLITPTEG EVMLLGERTG SKAGARLRSQ IGYLPETVAL HPSLIGIETL DFYAKLKKQP LTQNRGLLER VGISQAAHRR VGTYSKGMRQ RLALAQALLG EPKVLLFDEP TTGLDPASRQ MFYEVVRELN GRGATVLLST HALAELDGHA DRIIVD // ID Q9K1A3_NEIMB Unreviewed; 618 AA. AC Q9K1A3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF40718.1}; GN OrderedLocusNames=NMB0264 {ECO:0000313|EMBL:AAF40718.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40718.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40718.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40718.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40718.1; -; Genomic_DNA. DR PIR; A81218; A81218. DR RefSeq; NP_273320.1; NC_003112.2. DR RefSeq; WP_010980767.1; NC_003112.2. DR ProteinModelPortal; Q9K1A3; -. DR STRING; 122586.NMB0264; -. DR PaxDb; Q9K1A3; -. DR EnsemblBacteria; AAF40718; AAF40718; NMB0264. DR GeneID; 902375; -. DR KEGG; nme:NMB0264; -. DR PATRIC; 20355608; VBINeiMen85645_0328. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K18893; -. DR OMA; IKFEHVD; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-279-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40718.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40718.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 206 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 267 294 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 44 316 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 364 603 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 618 AA; 67856 MW; 7DFF8DAE9E8CE199 CRC64; MLNKIFSWFE SRIDPYPEAA PKTPEKGLWR FVWSSMAGVR KWIAALAALT AGIGIMEALV FQFMGKIVEW LGKYAPAELF AEKSWELAAM AAMMVFSVAW AFAASNVRLQ TLQGVFPMRL RWNFHRLMLN QSLGFYQDEF AGRVSAKVMQ TALALRDAVM TVADMVVYVS VYFITSGVIL ASLDSWLLLP FIGWIVGFAS VMRLLIPKLG QTAAWQADAR SLMTGRITDA YSNIATVKLF SHGAREAAYA KQSMEEFMVT VRAQMRLATL LHSCSFIVNT SLTLSTAALG IWLWHNGQVG VGAVATATAM ALRVNGLSQY IMWESARLFE NIGTVGDGMA TLSKPHTILD KPRALPLNVP QGAIKFEHVD FSYEAGKPLL NGFNLTIRPG EKVGLIGRSG AGKSTIVNLL LRFYEPQSGT VSIDGQDISG VTQESLRAQI GLVTQDTSLL HRSVRDNIIY GRPDATDAEM VSAAERAEAA GFIPDLSDAK GRRGYDAHVG ERGVKLSGGQ RQRIAIARVM LKDAPILLLD EATSALDSEV EAAIQESLDK MMDGKTVIAI AHRLSTIAAM DRLVVLDKGR IIEEGTHAEL LEKRGLYAKL WAHQSGGFLN EHVEWQHD // ID Q7DDK5_NEIMB Unreviewed; 463 AA. AC Q7DDK5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Xanthine/uracil permease family protein {ECO:0000313|EMBL:AAF41337.1}; GN OrderedLocusNames=NMB0930 {ECO:0000313|EMBL:AAF41337.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41337.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41337.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41337.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41337.1; -; Genomic_DNA. DR PIR; E81141; E81141. DR RefSeq; NP_273969.1; NC_003112.2. DR RefSeq; WP_002225335.1; NC_003112.2. DR STRING; 122586.NMB0930; -. DR PaxDb; Q7DDK5; -. DR EnsemblBacteria; AAF41337; AAF41337; NMB0930. DR GeneID; 903051; -. DR KEGG; nme:NMB0930; -. DR PATRIC; 20357329; VBINeiMen85645_1179. DR eggNOG; ENOG4105C2W; Bacteria. DR eggNOG; COG2233; LUCA. DR HOGENOM; HOG000038198; -. DR KO; K16345; -. DR OMA; EGPAYLQ; -. DR OrthoDB; EOG6M6JJK; -. DR BioCyc; NMEN122586:GHGG-968-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006042; Xan_ur_permease. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR TIGRFAMs; TIGR00801; ncs2; 1. DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 190 207 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 239 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 259 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 342 364 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 391 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 463 AA; 48239 MW; 936BBDFB7606A0C9 CRC64; MSGQLGKGAD APDLVYGLED RPPFGNALLS AVTHLLAIFV PMITPALIVG GALELPVEMT AYLVSMAMVA SGVGTYLQVN RFGPVGSGML SIQSVNFSFV TVMIALGAGM KEGGLTKDAM ISTLLGVSFV GAFLVCFSAW LLPYLKKVIT PTVSGVVVML IGLSLVHVGI TDFGGGFGAK ADGTFGSMEN LGLASLVLLI VLVFNCMKNP LLRMSGIAVG LIAGYIVALF LGKVDFSALQ NLPLVTLPVP FKYGFAFDWH AFIVAGAIFL LSVFEAVGDL TATAMVSDQP IEGEEYTKRL RGGVLADGLV SVIATALGSL PLTTFAQNNG VIQMTGVASR HVGKYIAVIL VLLGLFPVVG RAFTTIPSPV LGGAMVLMFG LIAIAGVRIL VSHGIRRREA VIAATSVGLG LGVAFEPEVF KNLPVLFQNS ISAGGITAVL LNLVLPEDKT EAAVKFDTDH LEH // ID Q9K019_NEIMB Unreviewed; 188 AA. AC Q9K019; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41221.1}; GN OrderedLocusNames=NMB0808 {ECO:0000313|EMBL:AAF41221.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41221.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41221.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41221.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41221.1; -; Genomic_DNA. DR PIR; G81155; G81155. DR RefSeq; NP_273850.1; NC_003112.2. DR RefSeq; WP_002217565.1; NC_003112.2. DR STRING; 122586.NMB0808; -. DR PaxDb; Q9K019; -. DR EnsemblBacteria; AAF41221; AAF41221; NMB0808. DR GeneID; 902923; -. DR KEGG; nme:NMB0808; -. DR PATRIC; 20357003; VBINeiMen85645_1020. DR eggNOG; COG3165; LUCA. DR HOGENOM; HOG000218866; -. DR OMA; VERFCHE; -. DR OrthoDB; EOG6BS8R4; -. DR BioCyc; NMEN122586:GHGG-839-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 188 AA; 19978 MW; C5DFA06FCDE8DCF0 CRC64; MSALLPIINR LILQSPDSRS ELAAFAGKTL TLNIAGLKLA GRITEDGLLS AGNGFADTEI TFRNSAVQKI LQGGEPGAGD IGLEGDLILG IAVLSLLGSL RSRASDELAR IFGTQADIGS RAADIGHGIK QIGRNIAEQI GGFSRESESA NIGNEALADC LDEISRLRDG VERLNERLDR LERDIWID // ID Q9JZK4_NEIMB Unreviewed; 57 AA. AC Q9JZK4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41414.1}; GN OrderedLocusNames=NMB1013 {ECO:0000313|EMBL:AAF41414.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41414.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41414.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41414.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41414.1; -; Genomic_DNA. DR PIR; F81131; F81131. DR STRING; 122586.NMB1013; -. DR PaxDb; Q9JZK4; -. DR EnsemblBacteria; AAF41414; AAF41414; NMB1013. DR HOGENOM; HOG000152759; -. DR OMA; HRKSGVA; -. DR BioCyc; NMEN122586:GHGG-1050-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 57 AA; 6298 MW; A5C0438041FD48E9 CRC64; MSKKSLIALM TAAMQPDFSH SDLGIRYAMP TQGCWTQAHR KSGVAAAKRA AKKKRHK // ID Q9K106_NEIMB Unreviewed; 111 AA. AC Q9K106; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Multidrug resistance protein {ECO:0000313|EMBL:AAF40833.1}; GN OrderedLocusNames=NMB0393 {ECO:0000313|EMBL:AAF40833.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40833.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40833.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40833.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU003942}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003942}. CC -!- SIMILARITY: Belongs to the small multidrug resistance (SMR) CC protein family. {ECO:0000256|RuleBase:RU003942}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40833.1; -; Genomic_DNA. DR PIR; A81204; A81204. DR RefSeq; NP_273442.1; NC_003112.2. DR RefSeq; WP_002222011.1; NC_003112.2. DR ProteinModelPortal; Q9K106; -. DR STRING; 122586.NMB0393; -. DR PaxDb; Q9K106; -. DR EnsemblBacteria; AAF40833; AAF40833; NMB0393. DR GeneID; 902508; -. DR KEGG; nme:NMB0393; -. DR PATRIC; 20355949; VBINeiMen85645_0492. DR eggNOG; ENOG410814C; Bacteria. DR eggNOG; COG2076; LUCA. DR HOGENOM; HOG000268006; -. DR KO; K03297; -. DR OMA; MGIVMVS; -. DR OrthoDB; EOG69WFSW; -. DR BioCyc; NMEN122586:GHGG-415-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR000390; Small_multidrug_res. DR Pfam; PF00893; Multi_Drug_Res; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00489003}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00488994, KW ECO:0000256|SAAS:SAAS00489003, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00488994, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00488994, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00488979}. FT TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 105 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 111 AA; 11853 MW; 501F68D086BA609D CRC64; MQMHWLFLTV AILSEVCGSS MLKLSGGFSK LWPSIGVVVS FSVCFWALSM TLKTMPLATA YAIWAGVGLV LTALVSVVFF GEKADFIGIV SIGLILLGVV LLNTMSHMSG H // ID Q9JXI8_NEIMB Unreviewed; 461 AA. AC Q9JXI8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Gluconate permease {ECO:0000313|EMBL:AAF42350.1}; GN Name=gntP {ECO:0000313|EMBL:AAF42350.1}; GN OrderedLocusNames=NMB2027 {ECO:0000313|EMBL:AAF42350.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42350.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42350.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42350.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42350.1; -; Genomic_DNA. DR PIR; F81015; F81015. DR RefSeq; NP_275019.1; NC_003112.2. DR RefSeq; WP_002223160.1; NC_003112.2. DR STRING; 122586.NMB2027; -. DR PaxDb; Q9JXI8; -. DR EnsemblBacteria; AAF42350; AAF42350; NMB2027. DR GeneID; 904076; -. DR KEGG; nme:NMB2027; -. DR PATRIC; 20360169; VBINeiMen85645_2584. DR eggNOG; ENOG4105C6Z; Bacteria. DR eggNOG; COG2610; LUCA. DR HOGENOM; HOG000237114; -. DR KO; K03299; -. DR OMA; PVILGCW; -. DR OrthoDB; EOG6B8XPC; -. DR BioCyc; NMEN122586:GHGG-2089-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003474; Glcn_transporter. DR Pfam; PF02447; GntP_permease; 1. DR PIRSF; PIRSF002746; Gluconate_transporter; 1. DR TIGRFAMs; TIGR00791; gntP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 278 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 316 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 370 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 376 394 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 444 460 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 461 AA; 47570 MW; 8CDAE9799C7768B3 CRC64; MDGWTQTLSA QTLLGISAAA IILILILIVK FRIHALLTLV IVSLLTALAT GLPTGSIVND ILVKNFGGTL GGVALLVGLG AMLGRLVETS GGAQSLADAL IRMFGEKRAP FALGVASLIF GFPIFFDAGL IVMLPIVFAT ARRMKQDVLP FALASIGAFS VMHVFLPPHP GPIAASEFYG ANIGQVLILG LPTAFITWYF SGYMLGKVLG RTIHVPVPEL LSGGTQDNDL PKEPAKAGTV VAIMLIPMLL IFLNTGVSAL ISEKLVSADE TWVQTAKIIG STPIALLISV LVALFVLGRK RGESGSALEK TVDGALAPVC SVILITGAGG MFGGVLRASG IGKALADSMA DLGIPVLLGC FLVALALRIA QGSATVALTT AAALMAPAVA AAGFTDWQLA CIVLATAAGS VGCSHFNDSG FWLVGRLLDM DVPTTLKTWT VNQTLIALIG FALSALLFAI V // ID Q9JYD7_NEIMB Unreviewed; 100 AA. AC Q9JYD7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41980.1}; GN OrderedLocusNames=NMB1630 {ECO:0000313|EMBL:AAF41980.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41980.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41980.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41980.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41980.1; -; Genomic_DNA. DR PIR; H81060; H81060. DR RefSeq; NP_274636.1; NC_003112.2. DR RefSeq; WP_010980969.1; NC_003112.2. DR STRING; 122586.NMB1630; -. DR PaxDb; Q9JYD7; -. DR EnsemblBacteria; AAF41980; AAF41980; NMB1630. DR GeneID; 903998; -. DR KEGG; nme:NMB1630; -. DR PATRIC; 20359164; VBINeiMen85645_2093. DR HOGENOM; HOG000219039; -. DR OMA; EKWVLNG; -. DR OrthoDB; EOG67HK3D; -. DR BioCyc; NMEN122586:GHGG-1679-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 100 AA; 11285 MW; 5638C5DF3CE0F960 CRC64; MGYRVGINCF DTRLHADDYL LSSLPPTVTQ DGKIIRPERV GEKWVLNGKP VMLSYPKCSN FEQIKQGSYV GSTVLILFVV IYGFRLLINF LKDMGKVGID // ID Q7DDL0_NEIMB Unreviewed; 336 AA. AC Q7DDL0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41242.1}; GN OrderedLocusNames=NMB0830 {ECO:0000313|EMBL:AAF41242.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41242.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41242.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41242.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41242.1; -; Genomic_DNA. DR PIR; G81152; G81152. DR RefSeq; NP_273872.1; NC_003112.2. DR RefSeq; WP_002213929.1; NC_003112.2. DR STRING; 122586.NMB0830; -. DR PaxDb; Q7DDL0; -. DR EnsemblBacteria; AAF41242; AAF41242; NMB0830. DR GeneID; 902944; -. DR KEGG; nme:NMB0830; -. DR PATRIC; 20357047; VBINeiMen85645_1042. DR eggNOG; ENOG4105C60; Bacteria. DR eggNOG; COG3943; LUCA. DR HOGENOM; HOG000003496; -. DR OMA; KEIFTMA; -. DR OrthoDB; EOG6QVRJM; -. DR BioCyc; NMEN122586:GHGG-861-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011204; Virulence_RhuM-like. DR Pfam; PF13310; Virulence_RhuM; 1. DR PIRSF; PIRSF015268; Virulence_RhuM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 336 AA; 38443 MW; 9DDAF7F03B12F954 CRC64; MSIILYTAND GTAQFALQEF GGQLWLTQAD MAELYQTTKQ NISKHIKTIL AEQELEEKAT VNFQLTVQNE NGRKVNRKIA HYSLPMIIAV GYRVRSARGI QFRQWATERL DEYLTKGFAI DDERLKGTGG GDYWKELLNR IRDIRSSEKA LYRQVLDLYA TSQDYNPKSS ESQTFFAAVQ NKLHYAASRQ TAAELIYSRA DSSKDFMGLT TFQGAIPTLN EAKIAKNYLT EDELFRLNRL VSAFFDLAEI KAQEQSPMYM RDWIAELDKF SGLYGQGTLQ GAGSISRKQA EQKAEREYRA YEARILSPVE QAYLESVKAL EKTAVQQIKQ KKDRTK // ID Q9JYP1_NEIMB Unreviewed; 29 AA. AC Q9JYP1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41847.1}; GN OrderedLocusNames=NMB1491 {ECO:0000313|EMBL:AAF41847.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41847.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41847.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41847.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41847.1; -; Genomic_DNA. DR PIR; A81078; A81078. DR RefSeq; NP_274499.1; NC_003112.2. DR RefSeq; WP_010980947.1; NC_003112.2. DR STRING; 122586.NMB1491; -. DR PaxDb; Q9JYP1; -. DR EnsemblBacteria; AAF41847; AAF41847; NMB1491. DR GeneID; 903913; -. DR KEGG; nme:NMB1491; -. DR BioCyc; NMEN122586:GHGG-1531-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 29 AA; 3152 MW; 869D458B4084850B CRC64; MKQCACRDLC LMPASNSAGM RAHKTLNAE // ID Q4W566_NEIMB Unreviewed; 177 AA. AC Q4W566; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41794.1}; GN OrderedLocusNames=NMB1433 {ECO:0000313|EMBL:AAF41794.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41794.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41794.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41794.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41794.1; -; Genomic_DNA. DR PIR; B81085; B81085. DR RefSeq; NP_274445.1; NC_003112.2. DR RefSeq; WP_002219084.1; NC_003112.2. DR ProteinModelPortal; Q4W566; -. DR STRING; 122586.NMB1433; -. DR MEROPS; C40.006; -. DR PaxDb; Q4W566; -. DR EnsemblBacteria; AAF41794; AAF41794; NMB1433. DR GeneID; 903133; -. DR KEGG; nme:NMB1433; -. DR PATRIC; 20358579; VBINeiMen85645_1801. DR eggNOG; ENOG4105K4H; Bacteria. DR eggNOG; COG0791; LUCA. DR HOGENOM; HOG000229978; -. DR OMA; KMARFAF; -. DR OrthoDB; EOG6GTZPF; -. DR BioCyc; NMEN122586:GHGG-1471-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.1720.10; -; 1. DR InterPro; IPR000064; NLP_P60_dom. DR Pfam; PF00877; NLPC_P60; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 65 171 NLPC_P60. {ECO:0000259|Pfam:PF00877}. SQ SEQUENCE 177 AA; 19394 MW; E7E55E15575BC4FB CRC64; MFPPDKTLFL CLSALLLASC GTTSGKHRQP KPKQTVRQIQ AVRISHIDRT QGSQELMLHS LGLIGTPYKW GGSSTATGFD CSGMIQFVYK NALNVKLPRT ARDMAAASRK IPDSRLKAGD LVFFNTGGAH RYSHVGLYIG NGEFIHAPSS GKTIKTEKLS TPFYAKNYLG AHTFFTE // ID Q9JXX9_NEIMB Unreviewed; 166 AA. AC Q9JXX9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Putative 4-hydroxyphenylacetate 3-hydroxylase, small subunit {ECO:0000313|EMBL:AAF42177.1}; GN OrderedLocusNames=NMB1842 {ECO:0000313|EMBL:AAF42177.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42177.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42177.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42177.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42177.1; -; Genomic_DNA. DR PIR; B81036; B81036. DR RefSeq; NP_274839.1; NC_003112.2. DR RefSeq; WP_002244300.1; NC_003112.2. DR ProteinModelPortal; Q9JXX9; -. DR STRING; 122586.NMB1842; -. DR PaxDb; Q9JXX9; -. DR EnsemblBacteria; AAF42177; AAF42177; NMB1842. DR GeneID; 903257; -. DR KEGG; nme:NMB1842; -. DR PATRIC; 20359691; VBINeiMen85645_2351. DR eggNOG; ENOG4108VQN; Bacteria. DR eggNOG; COG1853; LUCA. DR HOGENOM; HOG000115783; -. DR KO; K00484; -. DR OMA; WFDRGYH; -. DR OrthoDB; EOG6T1WSH; -. DR BioCyc; NMEN122586:GHGG-1897-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0042537; P:benzene-containing compound metabolic process; IEA:InterPro. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR002563; Flavin_Rdtase-like_dom. DR InterPro; IPR011982; HPA_mOase_red. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR Pfam; PF01613; Flavin_Reduct; 1. DR SMART; SM00903; Flavin_Reduct; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR02296; HpaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 164 Flavin_Reduct. FT {ECO:0000259|SMART:SM00903}. SQ SEQUENCE 166 AA; 18434 MW; AC42701FB9FADB98 CRC64; MADLQKNFQT SFRDAMASCA AGVHVITTDG AAGRYGITMT AVAPVTDEPP TVMLCINRSA RIIPILSENG SLCINTLADE HQDVAEHFAG LTGLSPEERF AYHIWHRGKT GQLEIEGALA HLHGHIVGKH EIGTHFVFYV RLDEIKNCGC KRPALLYFRR QFRFLD // ID Q4W579_NEIMB Unreviewed; 91 AA. AC Q4W579; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 39. DE SubName: Full=Iron-regulated protein FrpC, truncation {ECO:0000313|EMBL:AAY52167.1}; GN OrderedLocusNames=NMB0365 {ECO:0000313|EMBL:AAY52167.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52167.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52167.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52167.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52167.1; -; Genomic_DNA. DR STRING; 122586.NMB0365; -. DR PaxDb; Q4W579; -. DR EnsemblBacteria; AAY52167; AAY52167; NMB0365. DR PATRIC; 20355887; VBINeiMen85645_0461. DR eggNOG; COG2931; LUCA. DR HOGENOM; HOG000219109; -. DR OrthoDB; EOG690MC5; -. DR BioCyc; NMEN122586:GHGG-387-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 91 AA; 10228 MW; 5917497E655F2DDA CRC64; MNEGEVVLTP EQIQTLRGYA SRGDTYGGWR YLANLGDRYA DDAAAIVGKD ANLNGLNLWM KKGVENLWDD TVGKKTRLMC ISVFWIVVFN L // ID Q9JXB9_NEIMB Unreviewed; 71 AA. AC Q9JXB9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42439.1}; GN OrderedLocusNames=NMB2131 {ECO:0000313|EMBL:AAF42439.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42439.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42439.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42439.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42439.1; -; Genomic_DNA. DR PIR; D81003; D81003. DR RefSeq; NP_275116.1; NC_003112.2. DR RefSeq; WP_002248798.1; NC_003112.2. DR STRING; 122586.NMB2131; -. DR PaxDb; Q9JXB9; -. DR EnsemblBacteria; AAF42439; AAF42439; NMB2131. DR GeneID; 903373; -. DR KEGG; nme:NMB2131; -. DR PATRIC; 20360438; VBINeiMen85645_2715. DR HOGENOM; HOG000218698; -. DR OMA; WFSFIEA; -. DR OrthoDB; EOG6W45X5; -. DR BioCyc; NMEN122586:GHGG-2196-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 55 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 71 AA; 8091 MW; 4A25DBB87621F66B CRC64; MFKLGVYTCL GLFAGWVLLL IVQLWFSFLE AELFFKITLT MAGLFVIILA ALLVCGQYFS EKKMKDDGFI N // ID Q9JZF6_NEIMB Unreviewed; 222 AA. AC Q9JZF6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41470.1}; GN OrderedLocusNames=NMB1075 {ECO:0000313|EMBL:AAF41470.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41470.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41470.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41470.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41470.1; -; Genomic_DNA. DR PIR; F81124; F81124. DR RefSeq; NP_274108.1; NC_003112.2. DR RefSeq; WP_002225254.1; NC_003112.2. DR ProteinModelPortal; Q9JZF6; -. DR STRING; 122586.NMB1075; -. DR PaxDb; Q9JZF6; -. DR EnsemblBacteria; AAF41470; AAF41470; NMB1075. DR GeneID; 903494; -. DR KEGG; nme:NMB1075; -. DR PATRIC; 20357707; VBINeiMen85645_1370. DR eggNOG; ENOG4108RXW; Bacteria. DR eggNOG; COG0560; LUCA. DR HOGENOM; HOG000250087; -. DR OMA; ATNRFIT; -. DR OrthoDB; EOG61ZTM8; -. DR BioCyc; NMEN122586:GHGG-1112-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like. DR InterPro; IPR006385; HAD-SF_hydro_IB_PSP-like_bac. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1. DR TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 222 AA; 25327 MW; 9B01A88AA9281100 CRC64; MKNLAIFDLD NTLINTDSDH AWPQYLIKKG LVDAAETEAQ NEKFYRDYQN GCLDIDAFLK FHLAPLARYS KEELAEFHRE FMAEYIIPHI SPMQRMLVQS HQMAGDETLV ISSTNEFIIT PVCHLFGITN IIGTQLETGS DGRYTGNYIG TPSLKEGKIT RLNQWLAERG ETLQSYGKTY FYSDSKNDLP LLRLVSEPVA VNPDAELEKE AKEKGWPVLN FK // ID Q9JYG7_NEIMB Unreviewed; 376 AA. AC Q9JYG7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574}; GN Name=potD-3 {ECO:0000313|EMBL:AAF41947.1}; GN OrderedLocusNames=NMB1594 {ECO:0000313|EMBL:AAF41947.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41947.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41947.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41947.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine. {ECO:0000256|PIRNR:PIRNR019574}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR019574}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein CC PotD/PotF family. {ECO:0000256|PIRNR:PIRNR019574}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41947.1; -; Genomic_DNA. DR PIR; D81066; D81066. DR RefSeq; NP_274600.1; NC_003112.2. DR RefSeq; WP_002223553.1; NC_003112.2. DR ProteinModelPortal; Q9JYG7; -. DR STRING; 122586.NMB1594; -. DR PaxDb; Q9JYG7; -. DR EnsemblBacteria; AAF41947; AAF41947; NMB1594. DR GeneID; 904275; -. DR KEGG; nme:NMB1594; -. DR PATRIC; 20359070; VBINeiMen85645_2047. DR eggNOG; ENOG4107RUE; Bacteria. DR eggNOG; COG0687; LUCA. DR HOGENOM; HOG000263815; -. DR KO; K11073; -. DR OMA; VEYYIPK; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NMEN122586:GHGG-1642-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1. DR PRINTS; PR00909; SPERMDNBNDNG. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Periplasm {ECO:0000256|PIRNR:PIRNR019574}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|PIRNR:PIRNR019574}. SQ SEQUENCE 376 AA; 41922 MW; 883B6A59862FCA53 CRC64; MTKHLPLAVL TALLLAACGG SDKPPAEKPA PAENQNVLKI YNWSEYVDPE TVADFEKKNG IKVTYDVYDS DETLESKVLT GKSGYDIVAP SNAFVGRQIK AGAYQKIDKS LIPNYKHLNP EMMRLMDGVD PGHEYAVPFY WGTNTFAINT ERVKKALGTD KLPDNQWDLV FDPEYTSKLK QCGISYLDSA AEIYPMVLNY LGKNPNSSNT EDIREATALL KKNRPNIKRF TSSGFIDDLA RGDTCVTIGF GGDLNIAKRR AEEAGGKEKI RVMMPKEGVG IWVDSFVIPK DAKNVANAHK YINDFLDPEV SAKNGNFVTY APSSKPAREL MEDEFKNDNT IFPTEEDLKN SFIMVPIQPA ALKFMVRQWQ DVKAGK // ID Q9K1D2_NEIMB Unreviewed; 215 AA. AC Q9K1D2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40685.1}; GN OrderedLocusNames=NMB0230 {ECO:0000313|EMBL:AAF40685.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40685.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40685.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40685.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40685.1; -; Genomic_DNA. DR PIR; G81223; G81223. DR RefSeq; NP_273287.1; NC_003112.2. DR RefSeq; WP_002224820.1; NC_003112.2. DR ProteinModelPortal; Q9K1D2; -. DR STRING; 122586.NMB0230; -. DR PaxDb; Q9K1D2; -. DR EnsemblBacteria; AAF40685; AAF40685; NMB0230. DR GeneID; 902341; -. DR KEGG; nme:NMB0230; -. DR PATRIC; 20355536; VBINeiMen85645_0292. DR eggNOG; ENOG4105P4J; Bacteria. DR eggNOG; COG2049; LUCA. DR HOGENOM; HOG000265714; -. DR OMA; QPGFAYM; -. DR OrthoDB; EOG6VTK1C; -. DR BioCyc; NMEN122586:GHGG-245-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR003833; CT_C_D. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR010016; KipI_fam. DR Pfam; PF02682; AHS1; 1. DR SMART; SM00796; AHS1; 1. DR SUPFAM; SSF50891; SSF50891; 1. DR TIGRFAMs; TIGR00370; TIGR00370; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 200 AHS1. {ECO:0000259|SMART:SM00796}. SQ SEQUENCE 215 AA; 23560 MW; 0A4CA1F8936EF907 CRC64; MRIEITPISE SALVYRLNAP SELGKQQKLW AFAAALGQHD RIEEVVVGMN NLTVFTRFDT DLATLADELQ YVWEHTAVTD HQGKLVEIPV CYGGEYGPDL AEVAAFHQTV ISEIVRRHTA QTYTVFMMGF QPGFPYLGGL PEALHTPRRA VPRTSVPAGS VGIGGSQTGV YPFASPGGWQ IIGRTELPLF RADLNPPTLL AAGDQVRFVA ERIEP // ID Q9JYQ7_NEIMB Unreviewed; 404 AA. AC Q9JYQ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Aminotransferase, class I {ECO:0000313|EMBL:AAF41830.1}; DE EC=2.6.1.- {ECO:0000313|EMBL:AAF41830.1}; GN OrderedLocusNames=NMB1473 {ECO:0000313|EMBL:AAF41830.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41830.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41830.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41830.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41830.1; -; Genomic_DNA. DR PIR; G81078; G81078. DR RefSeq; NP_274482.1; NC_003112.2. DR RefSeq; WP_002225095.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ7; -. DR STRING; 122586.NMB1473; -. DR PaxDb; Q9JYQ7; -. DR PRIDE; Q9JYQ7; -. DR EnsemblBacteria; AAF41830; AAF41830; NMB1473. DR GeneID; 903895; -. DR KEGG; nme:NMB1473; -. DR PATRIC; 20358711; VBINeiMen85645_1865. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR HOGENOM; HOG000223042; -. DR KO; K14260; -. DR OMA; RIVFLPH; -. DR OrthoDB; EOG6X9MJ6; -. DR BioCyc; NMEN122586:GHGG-1513-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 4: Predicted; KW Aminotransferase {ECO:0000313|EMBL:AAF41830.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41830.1}. FT DOMAIN 56 381 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 404 AA; 45475 MW; 4F296A941799B87C CRC64; MDKFPKSAKL DHVCYDIRGP VHKKALQLEE EGNKILKLNI GNPAPFGFEA PDEILVDVIR NLPTSQGYCD SKGLYSARKA IVHYYQTKGL RDITVDDVYI GNGVSELITM SMQALLNDGD EILIPAPDYP LWTAAATLAG GTVRHYLCDE ENGWFPNLAD MEAKITPKTK AIVVINPNNP TGAVYSREIL LEIAELARKH GLIIFADEIY DKILYDGAVH HHIAALAPDL LTVTFNGLSK AYRVAGFRQG WMVLNGPKHH AKGYIEGLDM LSSMRLCANT PMQHAIQTAL GGYQSINEFI LPGGRLLEQR NRAWELVNQI PGVSCVKPMG AMYMFPKIDT EMYRIRDDMK FVYDLLVREK VLLVQGTGFN WIKPDHFRIV TLPYVHQIEE AMGRLARFLQ TYRQ // ID Q9JZN5_NEIMB Unreviewed; 57 AA. AC Q9JZN5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41374.1}; GN OrderedLocusNames=NMB0969 {ECO:0000313|EMBL:AAF41374.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41374.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41374.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41374.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41374.1; -; Genomic_DNA. DR PIR; C81136; C81136. DR PaxDb; Q9JZN5; -. DR DNASU; 903089; -. DR EnsemblBacteria; AAF41374; AAF41374; NMB0969. DR PATRIC; 20357427; VBINeiMen85645_1228. DR eggNOG; COG3676; LUCA. DR HOGENOM; HOG000218644; -. DR OMA; HLKKFQW; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NMEN122586:GHGG-1006-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 57 AA; 6825 MW; 3D3DF2F594D766D0 CRC64; MLPIIRKKVK PDGIVYTDTF RSYDVLDISE FSHLRKFNGI PKEHLGLHLK KCQWHFK // ID Q9K1A1_NEIMB Unreviewed; 108 AA. AC Q9K1A1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40720.1}; GN OrderedLocusNames=NMB0266 {ECO:0000313|EMBL:AAF40720.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40720.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40720.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40720.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40720.1; -; Genomic_DNA. DR PIR; C81218; C81218. DR RefSeq; NP_273322.1; NC_003112.2. DR RefSeq; WP_002221923.1; NC_003112.2. DR STRING; 122586.NMB0266; -. DR PaxDb; Q9K1A1; -. DR EnsemblBacteria; AAF40720; AAF40720; NMB0266. DR GeneID; 902377; -. DR KEGG; nme:NMB0266; -. DR PATRIC; 20355614; VBINeiMen85645_0331. DR eggNOG; ENOG4106849; Bacteria. DR eggNOG; COG3212; LUCA. DR HOGENOM; HOG000285676; -. DR OMA; DHGHSKQ; -. DR OrthoDB; EOG6N3D0B; -. DR BioCyc; NMEN122586:GHGG-281-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025711; PepSY. DR Pfam; PF03413; PepSY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 108 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328377. FT DOMAIN 47 104 PepSY. {ECO:0000259|Pfam:PF03413}. SQ SEQUENCE 108 AA; 11781 MW; B5F357FE27D346F1 CRC64; MNIKHLLLTS AATALLSISA PALAHHDGHG DDDHGHAAHQ HNKQDKIISR AQAEKAALAR VGGKITDIDL EHDNGRPHYD VEIVKNGQEY KVVVDARTGR VISSRRDD // ID Q9JZL4_NEIMB Unreviewed; 291 AA. AC Q9JZL4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41403.1}; GN OrderedLocusNames=NMB1002 {ECO:0000313|EMBL:AAF41403.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41403.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41403.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41403.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41403.1; -; Genomic_DNA. DR PIR; H81132; H81132. DR RefSeq; NP_274037.1; NC_003112.2. DR RefSeq; WP_002221070.1; NC_003112.2. DR STRING; 122586.NMB1002; -. DR PaxDb; Q9JZL4; -. DR EnsemblBacteria; AAF41403; AAF41403; NMB1002. DR GeneID; 903138; -. DR KEGG; nme:NMB1002; -. DR PATRIC; 20357537; VBINeiMen85645_1285. DR eggNOG; ENOG4108QNS; Bacteria. DR eggNOG; ENOG410XWY9; LUCA. DR HOGENOM; HOG000218921; -. DR OMA; ENEPHGD; -. DR OrthoDB; EOG62ZHS3; -. DR BioCyc; NMEN122586:GHGG-1039-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR021451; DUF3102. DR Pfam; PF11300; DUF3102; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 291 AA; 32518 MW; 478554B072F65D8A CRC64; MNTEIEIIAT DKVSNQAAMR SVLVMEQWGN GETYSEERWV ERGRQAVRQT MEGMFELGRA LIILKEHTEH GRFMEIVKSQ FGLGIAETSR LMSATRRFAT PQMQKAAPKL MDLGKSKLLE LLVEEDVTLV GLAEGEEVNG MTFDDVDRMT VRELRVALRE SRENLAAKDE VMKTKTAKID ELAEKLAKKQ TVVREPKAED VGSELAMQLT SLEVGIRSQV SRLKDLFDQL NAHSEAHGIS HQAKMVGTLN QIILDCEQLR ESYALPTEAP TDNVPEWLGG ETGEGDESGN D // ID Q9JZL7_NEIMB Unreviewed; 563 AA. AC Q9JZL7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE RecName: Full=D-lactate dehydrogenase {ECO:0000256|PIRNR:PIRNR000101}; DE EC=1.1.1.28 {ECO:0000256|PIRNR:PIRNR000101}; GN Name=dld {ECO:0000313|EMBL:AAF41400.1}; GN OrderedLocusNames=NMB0997 {ECO:0000313|EMBL:AAF41400.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41400.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41400.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41400.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: First component of the membrane-bound D-lactate oxidase, CC which is believed to play an important role in the energization of CC the active transport of a variety of sugars and amino acids. CC {ECO:0000256|PIRNR:PIRNR000101}. CC -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH. CC {ECO:0000256|PIRNR:PIRNR000101}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRNR:PIRNR000101}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41400.1; -; Genomic_DNA. DR PIR; D81134; D81134. DR RefSeq; NP_274033.1; NC_003112.2. DR RefSeq; WP_002222583.1; NC_003112.2. DR ProteinModelPortal; Q9JZL7; -. DR SMR; Q9JZL7; 4-561. DR STRING; 122586.NMB0997; -. DR PaxDb; Q9JZL7; -. DR EnsemblBacteria; AAF41400; AAF41400; NMB0997. DR GeneID; 903128; -. DR KEGG; nme:NMB0997; -. DR PATRIC; 20357509; VBINeiMen85645_1271. DR eggNOG; ENOG4105CXG; Bacteria. DR eggNOG; COG0277; LUCA. DR HOGENOM; HOG000122232; -. DR KO; K03777; -. DR OMA; RDRYEHH; -. DR OrthoDB; EOG6Z3KJX; -. DR BioCyc; NMEN122586:GHGG-1034-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006089; P:lactate metabolic process; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR Gene3D; 3.30.1370.20; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.30.70.610; -; 2. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016172; D-lactate_DH_C-sub1. DR InterPro; IPR016173; D-lactate_DH_C-sub2. DR InterPro; IPR012256; D_lactate_DH. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR015409; Lactate_DH_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF09330; Lact-deh-memb; 1. DR PIRSF; PIRSF000101; D-lactate_dh; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|PIRNR:PIRNR000101}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000101}; KW NAD {ECO:0000256|PIRNR:PIRNR000101}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000101, KW ECO:0000313|EMBL:AAF41400.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 36 266 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. SQ SEQUENCE 563 AA; 63402 MW; 405212B58E6B08CE CRC64; MSASQLLSRL TQTVGEKYII TDPAKTEQYR QGYRFGEGKA LAVVRPGSIL EMWKILQACV EADVIVITQA ANTGLTGGST PDGNDYDRDI VIVNTMRMNI IQTINNNEQV VCLPGSTLNQ LELLLKPLGR EPHSVIGSSC IGASVLGGVC NNSGGALVQR GPAYTEMALF AQINEEGRLE LVNHLGIDLG NTPEEILTNL QGHHYQNKDI TQDAGKGHDH AYCEHVRQVD EPTAARFNAD PARHYEASGC AGKLMVFAVR LDTFPQEKQT AVFYIGTNDI NELTDIRRAA LGEFESLPVS GEYIHRHAFD IADVYGKDTF YVIKKFGTHQ LPKLFDLKAR VDRFGKKVSF LPKHFSDKAM QFVSKFLPDH LPKSMRDYRD KYEHHLILKM GGKGVDEARA FLKEYFAHHG GAFFECNAEE TQAAMLHRFA VASAAIRYRA VHDDEVEDLV ALDIALRRDD RDWFEKLPPE IDNKIIHKLY YGHFMCHVFH QDYIIKKGND CMALEHEMLH LLDQRGAQYP AEHNVGHLYE AKPALKQFYR KLDPTNSFNP GVGKTSKKKN WAE // ID Q7DDJ0_NEIMB Unreviewed; 123 AA. AC Q7DDJ0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41399.1}; GN OrderedLocusNames=NMB0996 {ECO:0000313|EMBL:AAF41399.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41399.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41399.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41399.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41399.1; -; Genomic_DNA. DR PIR; C81134; C81134. DR RefSeq; NP_274032.1; NC_003112.2. DR RefSeq; WP_002213703.1; NC_003112.2. DR STRING; 122586.NMB0996; -. DR PaxDb; Q7DDJ0; -. DR EnsemblBacteria; AAF41399; AAF41399; NMB0996. DR GeneID; 903125; -. DR KEGG; nme:NMB0996; -. DR PATRIC; 20357505; VBINeiMen85645_1269. DR eggNOG; ENOG4106EWW; Bacteria. DR eggNOG; ENOG410XV71; LUCA. DR HOGENOM; HOG000218919; -. DR OMA; MTGAMFV; -. DR OrthoDB; EOG679TDC; -. DR BioCyc; NMEN122586:GHGG-1033-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR024399; DUF2628. DR Pfam; PF10947; DUF2628; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 83 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 123 AA; 13364 MW; 93B7E357778AEF79 CRC64; MKPYKIYTHP ALPPQAVKQG WSWPGLLFGT LWACFKRMWG LGLGLTGAIF VLAVFAQLVY GDTPATDSAF NVLGLAVSVW FGAKGNSLYA RHLLSRGYTE LPETVEAANP QAALAQYFGR GGR // ID Q9JZX8_NEIMB Unreviewed; 218 AA. AC Q9JZX8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative bacteriocin resistance protein {ECO:0000313|EMBL:AAF41266.1}; GN OrderedLocusNames=NMB0855 {ECO:0000313|EMBL:AAF41266.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41266.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41266.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41266.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41266.1; -; Genomic_DNA. DR PIR; B81150; B81150. DR RefSeq; NP_273896.1; NC_003112.2. DR RefSeq; WP_010980860.1; NC_003112.2. DR ProteinModelPortal; Q9JZX8; -. DR STRING; 122586.NMB0855; -. DR PaxDb; Q9JZX8; -. DR EnsemblBacteria; AAF41266; AAF41266; NMB0855. DR GeneID; 902969; -. DR KEGG; nme:NMB0855; -. DR PATRIC; 20357101; VBINeiMen85645_1069. DR eggNOG; ENOG4108VMT; Bacteria. DR eggNOG; COG3271; LUCA. DR HOGENOM; HOG000218674; -. DR KO; K06992; -. DR OMA; EENPIAY; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NMEN122586:GHGG-886-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF03412; Peptidase_C39; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332281. FT DOMAIN 53 176 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 218 AA; 24865 MW; A557A50204CD3B7E CRC64; MMKFKYVFLL ACVVVSLSYR LNAAPMFNDN PVVYGKIKVQ SWKARRDFNI VKQDLDFSCG AASVATLLNN FYGQTLTEEE VLKKLDKEQM RASFEDMRRI MPDLGFEAKG YALSFEQLAQ LKIPVIVYLK YRKDDHFSVL RGIDGNTVLL ADPSLGHVSM SRAQFLDAWQ TREGNLAGKI LAVIPKKAET ISNKLFFTQH PKRQTEFTVG QIRQARAE // ID Q9K158_NEIMB Unreviewed; 49 AA. AC Q9K158; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40765.1}; GN OrderedLocusNames=NMB0320 {ECO:0000313|EMBL:AAF40765.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40765.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40765.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40765.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40765.1; -; Genomic_DNA. DR PIR; C81212; C81212. DR STRING; 122586.NMB0320; -. DR PaxDb; Q9K158; -. DR EnsemblBacteria; AAF40765; AAF40765; NMB0320. DR BioCyc; NMEN122586:GHGG-340-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 49 AA; 5715 MW; 9CFFBFC30C4D7BA8 CRC64; MQQFPKSAII APHLFRTCKR STDATIGRII RAKQPFFFKT LELTLFFVV // ID Q9JXR0_NEIMB Unreviewed; 127 AA. AC Q9JXR0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42252.1}; GN OrderedLocusNames=NMB1923 {ECO:0000313|EMBL:AAF42252.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42252.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42252.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42252.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42252.1; -; Genomic_DNA. DR PIR; F81026; F81026. DR ProteinModelPortal; Q9JXR0; -. DR SMR; Q9JXR0; 5-123. DR STRING; 122586.NMB1923; -. DR PaxDb; Q9JXR0; -. DR EnsemblBacteria; AAF42252; AAF42252; NMB1923. DR PATRIC; 20359893; VBINeiMen85645_2451. DR eggNOG; ENOG4105K5B; Bacteria. DR eggNOG; COG3012; LUCA. DR HOGENOM; HOG000252587; -. DR OMA; DEGRAPN; -. DR OrthoDB; EOG6WMJ4X; -. DR BioCyc; NMEN122586:GHGG-1980-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.450.50; -; 1. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR004027; SEC_C_motif. DR Pfam; PF02810; SEC-C; 1. DR SUPFAM; SSF54427; SSF54427; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 127 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327686. SQ SEQUENCE 127 AA; 14291 MW; E06E3A0ECAC10C50 CRC64; MYCLRLRRLV LIFVNPLYII ATTVPAQQAF LDAAELMQWS IETEGLGLNV ISHKILGKDH AQVEFEAYFR DGQHRSAHHE LSGFVNIGGQ WYFIDPTVPH PAMKQPCICG SGKKFKACCG KYLKPVA // ID Q9JY36_NEIMB Unreviewed; 595 AA. AC Q9JY36; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Putative hemolysin activation protein HecB {ECO:0000313|EMBL:AAF42103.1}; GN OrderedLocusNames=NMB1762 {ECO:0000313|EMBL:AAF42103.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42103.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42103.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42103.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42103.1; -; Genomic_DNA. DR PIR; H81044; H81044. DR RefSeq; NP_274762.1; NC_003112.2. DR RefSeq; WP_002225623.1; NC_003112.2. DR ProteinModelPortal; Q9JY36; -. DR STRING; 122586.NMB1762; -. DR PaxDb; Q9JY36; -. DR EnsemblBacteria; AAF42103; AAF42103; NMB1762. DR GeneID; 903336; -. DR KEGG; nme:NMB1762; -. DR PATRIC; 20359489; VBINeiMen85645_2250. DR eggNOG; ENOG4105D5K; Bacteria. DR eggNOG; COG2831; LUCA. DR HOGENOM; HOG000218787; -. DR OMA; HWLPLQR; -. DR OrthoDB; EOG6TBHBP; -. DR BioCyc; NMEN122586:GHGG-1817-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR InterPro; IPR005565; Hemolysn_activator_HlyB. DR InterPro; IPR013686; Polypept-transport_assoc_ShlB. DR InterPro; IPR027282; TPS. DR Pfam; PF08479; POTRA_2; 1. DR Pfam; PF03865; ShlB; 1. DR PIRSF; PIRSF029745; FhaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 87 165 POTRA_2. {ECO:0000259|Pfam:PF08479}. FT DOMAIN 193 546 ShlB. {ECO:0000259|Pfam:PF03865}. SQ SEQUENCE 595 AA; 67075 MW; 338628EF270C9FEC CRC64; MKLPLSYLPN IRFLSWCCLL AGIIAPATLL ASPNPAEIRM QQDIQQRQRE EQLRQTMQPE SDVRLHQKNT GETVNQLMGD DSSQPCFAIN EVVLEGEHHA RFQFALKRAL RETGFQAGKC LHAGNINQIM SLAQNALIGR GYTTTRILAA PQDLNSGKLQ LTLIPSYLRS IRIDRSNDDQ THAGRIAAFQ NKFPTRSNDL LNLRDLEQGL ENLKRLPTAE ADLQIVPVEG EPNQSDVVVQ WRQRLLPYRV SVGMDNSGSE ATGKYQGNIT FSADNPLGLS DMFYVNYGRS IGGTPDEESF DGHRKEGGSN NYAVHYSAPF GKWTWAFNHN GYRYHQAVSG LSEVYDYNGK SYNTDFGFNR LLYRDAKRKT YLGVKLWMRE TKSYIDDAEL TVQRRKTAGW LAELSHKEYI GRSTADFKLK YKRGTGMKDA LRAPEEAFGE GTSRMKIWTA SADVNTPFQI GKQLFAYDTS VHAQWNKTPL TSQDKLAIGG HHTVRGFDGE MSLSAERGWY WRNDLSWQFK PGHQLYLGAD VGHVSGQSAK WLSGQTLVGT AIGIRGQIKL GGNLHYDIFT GRALKKPEFF QSRKWASGFQ VGYTF // ID Q9K102_NEIMB Unreviewed; 95 AA. AC Q9K102; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40837.1}; GN OrderedLocusNames=NMB0397 {ECO:0000313|EMBL:AAF40837.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40837.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40837.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40837.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40837.1; -; Genomic_DNA. DR PIR; E81204; E81204. DR RefSeq; NP_273446.1; NC_003112.2. DR RefSeq; WP_009346305.1; NC_003112.2. DR STRING; 122586.NMB0397; -. DR PaxDb; Q9K102; -. DR EnsemblBacteria; AAF40837; AAF40837; NMB0397. DR GeneID; 902512; -. DR KEGG; nme:NMB0397; -. DR PATRIC; 20355957; VBINeiMen85645_0496. DR OrthoDB; EOG6XQ3WH; -. DR BioCyc; NMEN122586:GHGG-419-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 95 AA; 10134 MW; 79199888400AAC5A CRC64; MSGKEPLNPN PVIASGRKCR LKDSSDGIFR KGRDALEKTA FQAGILFARQ RGGIGRAGKR TGGGSFMPSE SPPLRLFAKK VGKGTYNPVQ SSINI // ID Q9JXJ5_NEIMB Unreviewed; 214 AA. AC Q9JXJ5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42337.1}; GN OrderedLocusNames=NMB2013 {ECO:0000313|EMBL:AAF42337.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42337.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42337.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42337.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42337.1; -; Genomic_DNA. DR PIR; B81016; B81016. DR RefSeq; NP_275005.1; NC_003112.2. DR RefSeq; WP_002223148.1; NC_003112.2. DR STRING; 122586.NMB2013; -. DR PaxDb; Q9JXJ5; -. DR EnsemblBacteria; AAF42337; AAF42337; NMB2013. DR GeneID; 904109; -. DR KEGG; nme:NMB2013; -. DR HOGENOM; HOG000027849; -. DR OrthoDB; EOG6Z9B44; -. DR BioCyc; NMEN122586:GHGG-2070-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 214 AA; 24366 MW; 5AC1491CF0B9D2F6 CRC64; MVEFALSEPF PFEVGEIVEQ QNSDIALSEI SKYLSQEMLK EIVLTAHNNI QDKAALSDRN TLGMYRQAEI TFALRVYLSK DGWTLEPWSG GAFLCLSPCR TKSIIVATAT SDVGRHHGMP MTTARKGKGF EEAIRNSKLD LPDTVQFWVL LFHWKYNKVQ LELSLPSGFV SHQITGYKQR IILADVDLTK FDELERKQPV EEYEPLVERK QKAG // ID Q7DDB2_NEIMB Unreviewed; 62 AA. AC Q7DDB2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=FixS protein {ECO:0000313|EMBL:AAF41872.1}; GN Name=fixS {ECO:0000313|EMBL:AAF41872.1}; GN OrderedLocusNames=NMB1516 {ECO:0000313|EMBL:AAF41872.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41872.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41872.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41872.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41872.1; -; Genomic_DNA. DR PIR; C81074; C81074. DR RefSeq; NP_274524.1; NC_003112.2. DR RefSeq; WP_002220582.1; NC_003112.2. DR STRING; 122586.NMB1516; -. DR PaxDb; Q7DDB2; -. DR EnsemblBacteria; AAF41872; AAF41872; NMB1516. DR GeneID; 903990; -. DR KEGG; nme:NMB1516; -. DR PATRIC; 20358820; VBINeiMen85645_1920. DR eggNOG; ENOG41067U2; Bacteria. DR eggNOG; COG3197; LUCA. DR HOGENOM; HOG000277965; -. DR OMA; AILMDDD; -. DR OrthoDB; EOG6H1Q79; -. DR BioCyc; NMEN122586:GHGG-1556-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004714; Cyt_oxidase_maturation_cbb3. DR Pfam; PF03597; FixS; 1. DR TIGRFAMs; TIGR00847; ccoS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 62 AA; 7276 MW; 862568A869BA6079 CRC64; MMESMFILVP ISIILAFVIG WFFWWSGKNG QFDDLEGPAH RILMDDDSTS KLIEKEREND VR // ID Q9JY88_NEIMB Unreviewed; 297 AA. AC Q9JY88; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Chorismate mutase-related protein {ECO:0000313|EMBL:AAF42040.1}; GN OrderedLocusNames=NMB1692 {ECO:0000313|EMBL:AAF42040.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42040.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42040.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42040.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42040.1; -; Genomic_DNA. DR PIR; E81054; E81054. DR RefSeq; NP_274696.1; NC_003112.2. DR RefSeq; WP_002222124.1; NC_003112.2. DR ProteinModelPortal; Q9JY88; -. DR STRING; 122586.NMB1692; -. DR PaxDb; Q9JY88; -. DR EnsemblBacteria; AAF42040; AAF42040; NMB1692. DR GeneID; 903413; -. DR KEGG; nme:NMB1692; -. DR PATRIC; 20359337; VBINeiMen85645_2175. DR eggNOG; COG2876; LUCA. DR HOGENOM; HOG000027872; -. DR OMA; HEHEFAE; -. DR OrthoDB; EOG690MBS; -. DR BioCyc; NMEN122586:GHGG-1747-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR Pfam; PF00793; DAHP_synth_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00456513}. FT DOMAIN 148 293 DAHP_synth_1. {ECO:0000259|Pfam:PF00793}. SQ SEQUENCE 297 AA; 32143 MW; 988BF83F7EB03ED5 CRC64; MIIVMSRRAA EADIAGVVAF IRSRGLREHI SHGDERTVIG AIGDDRVLSV REVQTLPEVE KAVRILDTWK TVSRENRAED SRVAAKGVAF GGGETVRIAA EPSVWRNADA VFLDPFFTSA NLYDTSSADE GRGRCRRLAE QTASAHDAGK PVLVRVRNVR HVEAALNAGA DILYLGGGLM SDLAVLNEAG NLNIPLVLCK DKHHSAEDWL NAAEYVVSRG NRHLILGESG VLNHTKGHPY RLDVESIVKV RQISHLPVIA NITGLWNRDM PQEILYGLAK AAGACGIVGT CFEKSGG // ID Q9JZB7_NEIMB Unreviewed; 603 AA. AC Q9JZB7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=GTP-binding protein TypA {ECO:0000313|EMBL:AAF41581.1}; GN Name=typA {ECO:0000313|EMBL:AAF41581.1}; GN OrderedLocusNames=NMB1199 {ECO:0000313|EMBL:AAF41581.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41581.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41581.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41581.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41581.1; -; Genomic_DNA. DR PIR; H81111; H81111. DR RefSeq; NP_274224.1; NC_003112.2. DR RefSeq; WP_002219266.1; NC_003112.2. DR ProteinModelPortal; Q9JZB7; -. DR STRING; 122586.NMB1199; -. DR PaxDb; Q9JZB7; -. DR EnsemblBacteria; AAF41581; AAF41581; NMB1199. DR GeneID; 903618; -. DR KEGG; nme:NMB1199; -. DR PATRIC; 20357979; VBINeiMen85645_1505. DR eggNOG; ENOG4105CI3; Bacteria. DR eggNOG; COG1217; LUCA. DR HOGENOM; HOG000282351; -. DR KO; K06207; -. DR OMA; SMLFTIN; -. DR OrthoDB; EOG67HJSM; -. DR BioCyc; NMEN122586:GHGG-1233-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR006298; TypA_GTP-bd. DR PANTHER; PTHR23115:SF14; PTHR23115:SF14; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR TIGRFAMs; TIGR01394; TypA_BipA; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW GTP-binding {ECO:0000256|RuleBase:RU000323}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000323}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 197 Tr-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51722}. SQ SEQUENCE 603 AA; 67259 MW; BC0AE94B3F5EAF8D CRC64; MKQIRNIAII AHVDHGKTTL VDQLLRQSGT FRANQQVDER VMDSNDLEKE RGITILAKNT AIDYEGYHIN IVDTPGHADF GGEVERVLGM VDCVVLLVDA QEGPMPQTRF VTKKALALGL KPIVVINKID KPSARPSWVI DQTFELFDNL GATDEQLDFP IVYASGLSGF AKLEETDESN DMRPLFDTIL KYTPAPSGSA DETLQLQISQ LDYDNYTGRL GIGRILNGRI KPGQTVAVMN HDQQIAQGRI NQLLGFKGLE RVPLEEAEAG DIVIISGIED IGIGVTITDK DNPKGLPMLS VDEPTLTMDF MVNTSPLAGT EGKFVTSRQI RDRLQKELLT NVALRVEDTA DADVFRVSGR GELHLTILLE NMRREGYELA VGKPRVVYRD IDGQKCEPYE NLTVDVPDDN QGAVMEELGR RRGELTNMES DGNGRTRLEY HIPARGLIGF QGEFMTLTRG VGLMSHVFDD YAPVKPDMPG RHNGVLVSQE QGEAVAYALW NLEDRGRMFV SPNDKIYEGM IIGIHSRDND LVVNPLKGKK LTNIRASGTD EAVRLTTPIK LTLEGAVEFI DDDELVEITP QSIRLRKRYL SELERRRHFK KLD // ID Q9JXN1_NEIMB Unreviewed; 196 AA. AC Q9JXN1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42292.1}; GN OrderedLocusNames=NMB1963 {ECO:0000313|EMBL:AAF42292.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42292.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42292.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42292.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42292.1; -; Genomic_DNA. DR PIR; D81022; D81022. DR RefSeq; NP_274957.1; NC_003112.2. DR RefSeq; WP_002225840.1; NC_003112.2. DR ProteinModelPortal; Q9JXN1; -. DR STRING; 122586.NMB1963; -. DR PaxDb; Q9JXN1; -. DR EnsemblBacteria; AAF42292; AAF42292; NMB1963. DR GeneID; 904186; -. DR KEGG; nme:NMB1963; -. DR PATRIC; 20359987; VBINeiMen85645_2498. DR eggNOG; ENOG4105E3I; Bacteria. DR eggNOG; COG2854; LUCA. DR KO; K07323; -. DR OMA; QTQFADQ; -. DR OrthoDB; EOG6X10ZT; -. DR BioCyc; NMEN122586:GHGG-2020-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.10.640; -; 2. DR Gene3D; 3.10.450.50; -; 2. DR InterPro; IPR008869; MlaC/ttg2D. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR023094; Tol_tolerance_alpha. DR Pfam; PF05494; MlaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 196 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329317. SQ SEQUENCE 196 AA; 21083 MW; BEA39AC78CE0EF72 CRC64; MKKSSLISAL GIGILSIGMA FAAPADAVSQ IRQNATQVLS ILKNGDANTA RQKAEAYAIP YFDFQRMTAL AVGNPWRTAS DAQKQALAKE FQTLLIRTYS GTMLKLKNAN VNVKDNPIVN KGGKEIIVRA EVGVPGQKPV NMDFTTYQSG GKYRTYNVAI EGASLVTVYR NQFGEIIKAK GVDGLIAELK AKNGGK // ID Q9JZW1_NEIMB Unreviewed; 508 AA. AC Q9JZW1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=L-threonine dehydratase {ECO:0000256|RuleBase:RU362012}; DE EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012}; DE AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012}; GN Name=ilvA {ECO:0000256|RuleBase:RU362012, GN ECO:0000313|EMBL:AAF41289.1}; GN OrderedLocusNames=NMB0878 {ECO:0000313|EMBL:AAF41289.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41289.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41289.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41289.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate CC and ammonia from threonine in a two-step reaction. The first step CC involved a dehydration of threonine and a production of enamine CC intermediates (aminocrotonate), which tautomerizes to its imine CC form (iminobutyrate). Both intermediates are unstable and short- CC lived. The second step is the nonenzymatic hydrolysis of the CC enamine/imine intermediates to form 2-ketobutyrate and free CC ammonia. In the low water environment of the cell, the second step CC is accelerated by RidA. {ECO:0000256|RuleBase:RU362012}. CC -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3). CC {ECO:0000256|RuleBase:RU362012}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU362012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from L-threonine: step 1/1. CC {ECO:0000256|RuleBase:RU362012}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU362012}. CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. CC {ECO:0000256|RuleBase:RU362012}. CC -!- SIMILARITY: Contains 2 ACT-like domains. CC {ECO:0000256|RuleBase:RU362012}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41289.1; -; Genomic_DNA. DR PIR; A81147; A81147. DR RefSeq; NP_273919.1; NC_003112.2. DR RefSeq; WP_002225371.1; NC_003112.2. DR ProteinModelPortal; Q9JZW1; -. DR SMR; Q9JZW1; 2-508. DR STRING; 122586.NMB0878; -. DR PaxDb; Q9JZW1; -. DR EnsemblBacteria; AAF41289; AAF41289; NMB0878. DR GeneID; 902997; -. DR KEGG; nme:NMB0878; -. DR PATRIC; 20357161; VBINeiMen85645_1094. DR eggNOG; ENOG4105C7B; Bacteria. DR eggNOG; COG1171; LUCA. DR HOGENOM; HOG000046975; -. DR KO; K01754; -. DR OMA; DEVCAAM; -. DR OrthoDB; EOG6ZSP7D; -. DR BioCyc; NMEN122586:GHGG-914-MONOMER; -. DR UniPathway; UPA00047; UER00054. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001721; ACT-like_dom. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR005787; Thr_deHydtase_biosynth. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR Pfam; PF00585; Thr_dehydrat_C; 2. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1. DR PROSITE; PS51672; ACT_LIKE; 2. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|RuleBase:RU362012}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012}; KW Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:AAF41289.1}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 334 405 ACT-like. {ECO:0000259|PROSITE:PS51672}. FT DOMAIN 428 499 ACT-like. {ECO:0000259|PROSITE:PS51672}. SQ SEQUENCE 508 AA; 55193 MW; 087DB8CF41810353 CRC64; MNTPLPYSDY LIRILTASVY DVAVETPLEP ARSLSVRLKN NILLKREDLQ PVFSFKIRGA YNKMSKLPKD ALACGVIAAS AGNHAQGVAL SAQRLGCRAV IVMPETTPKI KVDAVKSHGG EVVLRGVSYN DAYDYAMELA EKEGLTYIAP FDDPDVIAGQ GTVGMEIVSQ HPDPIRAVFV PIGGGGLAAG VAAFIKQVRP EIKVIGVQTN DSCCMKQSVE AGEIVHLKDV GLFSDGTAVK VVGNETFRLC KELLDEIITV DTDAVCGAVK DIFDDTRSIT EPAGALALAG LKAYIAREGA ENQTLIAVTS GANMNFHRLR HVSERSELGE GNEGIFAVTI PEERGSFLKF VNILGNRNIT EFNYRYGDDE KAHIFVGLQA AGPQDLAVIG SRLDEAGLPN VDLTNNEIAK IHIRYMVGGR TDKVENERLV SFEFPERPGA LARFLNHMQG GWNITLFHYR NHGADYGRIL VGIDVPPHDA AAFDGFLESL GYSYHEETQN AAYKLFLA // ID Q9JZ89_NEIMB Unreviewed; 542 AA. AC Q9JZ89; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41621.1}; GN OrderedLocusNames=NMB1240 {ECO:0000313|EMBL:AAF41621.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41621.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41621.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41621.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41621.1; -; Genomic_DNA. DR PIR; E81105; E81105. DR RefSeq; NP_274264.1; NC_003112.2. DR RefSeq; WP_002222421.1; NC_003112.2. DR ProteinModelPortal; Q9JZ89; -. DR STRING; 122586.NMB1240; -. DR PaxDb; Q9JZ89; -. DR EnsemblBacteria; AAF41621; AAF41621; NMB1240. DR GeneID; 903662; -. DR KEGG; nme:NMB1240; -. DR PATRIC; 20358077; VBINeiMen85645_1551. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR HOGENOM; HOG000271629; -. DR OMA; WSENAKI; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NMEN122586:GHGG-1277-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAF41621.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000313|EMBL:AAF41621.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 252 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 321 541 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT COILED 242 275 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 542 AA; 60779 MW; 1EACB1DC50077CE9 CRC64; MISTNGITMQ FGAKPLFENV SVKFGEGNRY GLIGANGSGK STFMKILGGD LEQTAGEVAI ENGVRLGKLR QDQFAYEDMR VLDVVMMGHT EMWAAMTERD AIYANPEATE DDYMKAAELE AKFAEYDGYT AEARAAELLS GVGISEDLHN AKMAEVAPGF KLRVLLAQAL FSKPDVLLLD EPTNNLDINT IRWLEGVLNQ YDSTMIIISH DRHFLNEVCT HMADLDYNTI TIYPGNYDDY MLASAQSRER ALKDNAKAKE KLQELQEFVA RFSANKSKAR QATSRLKQAD KIKSEMVEVK PSTRQNPYIR FEADEKAKLH RQAVEVEKLA KRFETQLFKN LNFILEAGQR LAIIGPNGAG KSTLLKLLAG AYNPEYSDGL LPDEGTIKWA EKASVGYYPQ DHENDFDVDM DLSEWMRQWG QEGDDEQVIR GTLGRLLFGS NDVVKKVKVL SGGEKGRMLY GKLLLLKPNV LVMDEPTNHM DMESIESLNM ALEKYNGTLI FVSHDRQFVS SLATQIIELD GKGGYEHYLG DYESYLEKKG VA // ID Q9K133_NEIMB Unreviewed; 427 AA. AC Q9K133; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=AmpG-related protein {ECO:0000313|EMBL:AAF40803.1}; GN OrderedLocusNames=NMB0360 {ECO:0000313|EMBL:AAF40803.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40803.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40803.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40803.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40803.1; -; Genomic_DNA. DR PIR; G81208; G81208. DR RefSeq; NP_273409.1; NC_003112.2. DR RefSeq; WP_002243984.1; NC_003112.2. DR ProteinModelPortal; Q9K133; -. DR STRING; 122586.NMB0360; -. DR PaxDb; Q9K133; -. DR EnsemblBacteria; AAF40803; AAF40803; NMB0360. DR GeneID; 902476; -. DR KEGG; nme:NMB0360; -. DR PATRIC; 20355877; VBINeiMen85645_0456. DR eggNOG; ENOG4105EYM; Bacteria. DR eggNOG; COG0477; LUCA. DR HOGENOM; HOG000217208; -. DR KO; K08218; -. DR OMA; GYFSWIA; -. DR OrthoDB; EOG6PS5R8; -. DR BioCyc; NMEN122586:GHGG-382-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004752; AmpG_permease/AT-1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00901; 2A0125; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 252 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 272 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 354 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 366 388 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 412 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 427 AA; 46310 MW; 7E7D4881FE4F4933 CRC64; MTASKSGFIG QIFSRNMLVC IFTGFTSGLP LYFLINLIPA WLRSEQVDLK SIGLMALIGL PFTWKFLWSP LMDAVRLPVL GRRRGWMLLT QAGLLAALAV YAFLNPRNHL PLIAGLSVLV AFFSASQDIV LDAFRREILS DEELGLGNSV HVNAYRIAAL IPGSLSLVLA DRMPWLEVFV ITSLFMLPGL LMTLFLAREP VLPPAVPKTL KQTVVEPFKE FFTRKGIASA VCVLLFIFLY KLGDSMATAL ATPFYLDMGF SKTDIGLIAK NAGLWPAVAA GILGGVWMLK IGVNKALWLF GAVQAVTVLG FVWLAGFGPF DTVGTGERLM LAAVIGAEAV GVGLGTAAFV SYMARETNPA FTATQLALFT SLSAVPRTVI NSFAGYLIEW LGYVPFFQLC FALALPGMLL LLKVAPWNGE KTQDAGR // ID Q9K010_NEIMB Unreviewed; 127 AA. AC Q9K010; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41230.1}; GN OrderedLocusNames=NMB0817 {ECO:0000313|EMBL:AAF41230.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41230.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41230.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41230.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41230.1; -; Genomic_DNA. DR PIR; H81153; H81153. DR RefSeq; NP_273859.1; NC_003112.2. DR RefSeq; WP_010980854.1; NC_003112.2. DR STRING; 122586.NMB0817; -. DR PaxDb; Q9K010; -. DR EnsemblBacteria; AAF41230; AAF41230; NMB0817. DR GeneID; 902932; -. DR KEGG; nme:NMB0817; -. DR HOGENOM; HOG000218660; -. DR OrthoDB; EOG65XN8C; -. DR BioCyc; NMEN122586:GHGG-848-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007929; DUF723. DR Pfam; PF05265; DUF723; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 127 AA; 14180 MW; 5693E6482A7FA844 CRC64; MPKSLSLQDV QLRFSSKFPD KTVLKFTKNY EPVTIQCPLH GSVVYGNLQA AMKSSTGCPE CTRNPEKPSP NAVAIRLEDT ETGEIYEFAS TLAASKFIGC SNSTLAVRLS GRTPFDRLIR YRYRLVK // ID Q9K0B3_NEIMB Unreviewed; 84 AA. AC Q9K0B3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41118.1}; GN OrderedLocusNames=NMB0701 {ECO:0000313|EMBL:AAF41118.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41118.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41118.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41118.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41118.1; -; Genomic_DNA. DR PIR; D81169; D81169. DR PaxDb; Q9K0B3; -. DR EnsemblBacteria; AAF41118; AAF41118; NMB0701. DR BioCyc; NMEN122586:GHGG-729-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 84 AA; 9732 MW; B04C1F77AB6D1788 CRC64; MTNPSVRKPA PRHSHEPPSR HYHESGNLGL RVKKTYIPSF PQKQKTKIRN LKSRHSRKSG NPKTKSRRNL TEEPNPENRL PAFA // ID Q9JY43_NEIMB Unreviewed; 114 AA. AC Q9JY43; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42096.1}; GN OrderedLocusNames=NMB1755 {ECO:0000313|EMBL:AAF42096.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42096.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42096.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42096.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42096.1; -; Genomic_DNA. DR PIR; B81046; B81046. DR STRING; 122586.NMB1755; -. DR PaxDb; Q9JY43; -. DR EnsemblBacteria; AAF42096; AAF42096; NMB1755. DR HOGENOM; HOG000152754; -. DR OMA; HYYKTVQ; -. DR BioCyc; NMEN122586:GHGG-1810-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 114 AA; 13185 MW; 75C791CD480842D4 CRC64; MANRCRLKPY NRRQNNACSN RTHTLPANGL RNLRLLDLRT KVTELKHIGG QSTAAIADLA GEMRRLAKKS KMLLKGLWPF LSSTISAFKI NQSLFKHYYK TVQLLNCKHR KKNY // ID Q4W582_NEIMB Unreviewed; 218 AA. AC Q4W582; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=UDP-glucose 4-epimerase, truncation {ECO:0000313|EMBL:AAY52155.1}; GN OrderedLocusNames=NMB0078 {ECO:0000313|EMBL:AAY52155.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52155.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52155.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52155.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52155.1; -; Genomic_DNA. DR ProteinModelPortal; Q4W582; -. DR STRING; 122586.NMB0078; -. DR PaxDb; Q4W582; -. DR EnsemblBacteria; AAY52155; AAY52155; NMB0078. DR PATRIC; 20355159; VBINeiMen85645_0113. DR eggNOG; COG1087; LUCA. DR HOGENOM; HOG000168001; -. DR OMA; HIVAMEK; -. DR OrthoDB; EOG6WHNS9; -. DR BioCyc; NMEN122586:GHGG-84-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01179; galE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 142 Epimerase. {ECO:0000259|Pfam:PF01370}. SQ SEQUENCE 218 AA; 24220 MW; F79E93E54B8962AE CRC64; MAFTLMRRAM IRKMPYTEDM RPGDTANPYG ASKAMVERML TDIQKADPRW SMILLRYFNP IGAHESGLIG EQPNGIPNNL LPYICQVAAG KLPQLAVFGD DYPTPDGTGM RDYIHVMDLA EGHVAAMQAK SNVAGTHLLN LGSGRASSVL EIIRAFEAAS GLTIPYEVKP RRAGDLACFY ADPSYTKAQI GWQTQRDLTQ MMEDSWRWVS NNPNGYDD // ID Q7DD41_NEIMB Unreviewed; 100 AA. AC Q7DD41; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42426.1}; GN OrderedLocusNames=NMB2113 {ECO:0000313|EMBL:AAF42426.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42426.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42426.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42426.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42426.1; -; Genomic_DNA. DR PIR; E81004; E81004. DR RefSeq; NP_275100.1; NC_003112.2. DR RefSeq; WP_002215106.1; NC_003112.2. DR PaxDb; Q7DD41; -. DR EnsemblBacteria; AAF42426; AAF42426; NMB2113. DR GeneID; 903519; -. DR KEGG; nme:NMB2113; -. DR PATRIC; 20360400; VBINeiMen85645_2696. DR HOGENOM; HOG000218704; -. DR OMA; NSINKAM; -. DR OrthoDB; EOG6D2M23; -. DR BioCyc; NMEN122586:GHGG-2178-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR029080; Imm40. DR Pfam; PF15569; Imm40; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 91 Imm40. {ECO:0000259|Pfam:PF15569}. SQ SEQUENCE 100 AA; 11695 MW; 0FF23D4163B23EB9 CRC64; MLNEIFEIYS RQGESLIGIG IREAALPVPI AIDILNLFIN ERILVLGGDI YIKKDNYFYQ TYDNWYYEGS NLFNSIDKAM HYLSQIKLEN AYVSFVLKFI // ID Q9K0J5_NEIMB Unreviewed; 107 AA. AC Q9K0J5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=HitA protein {ECO:0000313|EMBL:AAF41029.1}; GN Name=hitA {ECO:0000313|EMBL:AAF41029.1}; GN OrderedLocusNames=NMB0602 {ECO:0000313|EMBL:AAF41029.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41029.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41029.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41029.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41029.1; -; Genomic_DNA. DR PIR; F81181; F81181. DR RefSeq; NP_273646.1; NC_003112.2. DR RefSeq; WP_002222846.1; NC_003112.2. DR ProteinModelPortal; Q9K0J5; -. DR STRING; 122586.NMB0602; -. DR PaxDb; Q9K0J5; -. DR EnsemblBacteria; AAF41029; AAF41029; NMB0602. DR GeneID; 902716; -. DR KEGG; nme:NMB0602; -. DR PATRIC; 20356489; VBINeiMen85645_0764. DR eggNOG; ENOG4105K59; Bacteria. DR eggNOG; COG0537; LUCA. DR HOGENOM; HOG000061064; -. DR KO; K02503; -. DR OMA; CNPYPDG; -. DR OrthoDB; EOG69GZSV; -. DR BioCyc; NMEN122586:GHGG-628-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR23089; PTHR23089; 1. DR Pfam; PF01230; HIT; 1. DR PRINTS; PR00332; HISTRIAD. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 107 HIT. {ECO:0000259|PROSITE:PS51084}. SQ SEQUENCE 107 AA; 11572 MW; 9DC3275793B6BDCA CRC64; MDNCIFCKIA AKDIPAQTVY EDGEMVCFKD INPAAPVHLL LIPKVHFDSL AHAAPEHQML LGKMMLKVPE IAKAAGLADG FKTLINTGKG GGQEVFHLHI HIMGTPV // ID Q9JYM3_NEIMB Unreviewed; 244 AA. AC Q9JYM3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=DNA polymerase III, epsilon subunit {ECO:0000313|EMBL:AAF41870.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAF41870.1}; GN Name=dnaQ-2 {ECO:0000313|EMBL:AAF41870.1}; GN OrderedLocusNames=NMB1514 {ECO:0000313|EMBL:AAF41870.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41870.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41870.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41870.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41870.1; -; Genomic_DNA. DR PIR; A81074; A81074. DR RefSeq; NP_274522.1; NC_003112.2. DR RefSeq; WP_002219026.1; NC_003112.2. DR ProteinModelPortal; Q9JYM3; -. DR STRING; 122586.NMB1514; -. DR PaxDb; Q9JYM3; -. DR EnsemblBacteria; AAF41870; AAF41870; NMB1514. DR GeneID; 903984; -. DR KEGG; nme:NMB1514; -. DR PATRIC; 20358816; VBINeiMen85645_1918. DR eggNOG; ENOG4108JDX; Bacteria. DR eggNOG; COG0847; LUCA. DR HOGENOM; HOG000258616; -. DR KO; K02342; -. DR OMA; FHVYLNP; -. DR OrthoDB; EOG696BTR; -. DR BioCyc; NMEN122586:GHGG-1554-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR006309; DnaQ_proteo. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. DR TIGRFAMs; TIGR01406; dnaQ_proteo; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAF41870.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41870.1}. FT DOMAIN 4 178 Exonuclease. {ECO:0000259|SMART:SM00479}. SQ SEQUENCE 244 AA; 27134 MW; 01585BA8770B6A6E CRC64; MTTRQIILDT ETTGLYADGG DRLVEFAGLE MVNRQMTDKN LHLYVHPERD MPEEAARVHG LTIQVLEGKN APPFAEVGRQ IADFLRGAEL IIHNAKFDVG FLNMEFRRMG LPTVEELGCT VTDTLAMARE MFPGQKASLD ALCNRFSVDR SKRVLHGALI DCELLGEVYL AMTRRQFDLM GAAAEEKMET KPVVHTETKR SGKLKVIRAD ENELAAHGQY LDGLGEACIW RKEAVPSENG GTDA // ID Q9JY62_NEIMB Unreviewed; 1069 AA. AC Q9JY62; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486}; DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486}; DE AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486}; GN Name=recC {ECO:0000256|HAMAP-Rule:MF_01486, GN ECO:0000313|EMBL:AAF42066.1}; GN OrderedLocusNames=NMB1720 {ECO:0000313|EMBL:AAF42066.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42066.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42066.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42066.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit recognizes the wild- CC type Chi sequence, and when added to isolated RecB increases its CC ATP-dependent helicase processivity. {ECO:0000256|HAMAP- CC Rule:MF_01486}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01486}. CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}. CC -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP- CC Rule:MF_01486}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42066.1; -; Genomic_DNA. DR PIR; A81050; A81050. DR RefSeq; NP_274723.1; NC_003112.2. DR RefSeq; WP_010980978.1; NC_003112.2. DR ProteinModelPortal; Q9JY62; -. DR STRING; 122586.NMB1720; -. DR PaxDb; Q9JY62; -. DR EnsemblBacteria; AAF42066; AAF42066; NMB1720. DR GeneID; 903381; -. DR KEGG; nme:NMB1720; -. DR PATRIC; 20359401; VBINeiMen85645_2206. DR eggNOG; ENOG4105DSY; Bacteria. DR eggNOG; COG1330; LUCA. DR HOGENOM; HOG000258319; -. DR KO; K03583; -. DR OMA; ERDNIEM; -. DR OrthoDB; EOG61P6M4; -. DR BioCyc; NMEN122586:GHGG-1775-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01486; RecC; 1. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006697; RecC. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR PIRSF; PIRSF000980; RecC; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR01450; recC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01486}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01486}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01486}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01486}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01486}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01486}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 1069 AA; 120579 MW; E633FF844F681EDE CRC64; MFYLYQSNRL ETLAALFARI QKVKPLKSAL QPEQIIVQSQ GMRRYLNTCL ARDLGVAANL SFSLPAGLTW KLMKKLIPGI PELSPFAPEV MRWRLLDLFR SEAFRNTAEF EDVRNVLQDY LGSGESADYQ LAGQLADIFD QYLVYRPQWI DAWQQGRRLG LGDDEIWQSK LWRYLDDGRQ SAPHRVALWE KLLESLSSDK LPERYFVFGI STMAPMYLQL LHKLSEHCDV FVFALNPSGM YWGNVIEAAQ ILKGGGDPDL TQAGHPLLAS LGKQGRDFFD FLNEMEIEGE TPVFEEGGRD TLLHALQTDI QNLKMPSEMA GSVNTGDGSI RIVSAHSPLR ELQILKDKLL KILHEHPDWQ PHDIAVLTPN IESYTPFIEA VFGQAQPGAQ ALPYSVSDVK ISRRQPLFHA LSCLFDLLES RFEVDKVLVL LETAPVLRRF GLTEDDLPLL HDMVADLNVH WGLDGEMRGG TDQLFTWKQA VERMILGWML PKGGNPMWQD VSAWYADVNQ TAMFGRFAAF LETLTDIVRI WRQPATVGEW VARCRDLLET LFQAEADDQK SVQNLENEWV KWQAETELAQ FSGQLPPHTV IRHIRRFLDS ESEAGFLRGG ITFCSMVPMR SLPFKVICLL GLNDGDFPRN TKAAVFDLIA KHPAKGDRAR RDDDRYLFLE ALISAREILY LSYIGRDIRK DEELAPSSLL GELIDTVAAM AGIGSRQLAQ NLIEQHPLQA FSRRYFQEGG RSDGIFGTRT DYAAALGQTP EPPQPFFDQP VENAEPVAEI GQDEFIRFWR NPVKVWLQQQ LAWSEPHIGE AWEPAEPFEP QHADQIAEIY IEARCEGRDF AQTAARIGAE SLLPSGELGR LWQQDFQTAA KQIDTAVLNS PKLPPLSYAI PSDGQILKGS LGNLYRCGQV FYAYGKPNAP QRIAFLLEHL IFCAVMPSEA EMRQTFIVQS GETEILAEIA QDRALQLLSE WMAFFNIGQN RPLPFFAKTS LATAEAFAQK QDWEAALKKA QTAYHGSKVS KGQKDYTEVA LVFGNASQNP LEQPLFENLV RLLADTLAAA EKKEEAGEA // ID Q9JYS1_NEIMB Unreviewed; 65 AA. AC Q9JYS1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41815.1}; GN OrderedLocusNames=NMB1456 {ECO:0000313|EMBL:AAF41815.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41815.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41815.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41815.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41815.1; -; Genomic_DNA. DR PIR; A81082; A81082. DR STRING; 122586.NMB1456; -. DR PaxDb; Q9JYS1; -. DR EnsemblBacteria; AAF41815; AAF41815; NMB1456. DR HOGENOM; HOG000027845; -. DR OMA; FVYELAP; -. DR OrthoDB; EOG6TJ84R; -. DR BioCyc; NMEN122586:GHGG-1496-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7316 MW; 68CA339DFF7C4409 CRC64; MLSRKGRTRG KAAAGDRRGR IFDLRAKPAI IPFEIKSYRL CAGLSIAFVY ELAPSVLPIW GCRFF // ID Q9JY26_NEIMB Unreviewed; 34 AA. AC Q9JY26; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42116.1}; GN OrderedLocusNames=NMB1776 {ECO:0000313|EMBL:AAF42116.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42116.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42116.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42116.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42116.1; -; Genomic_DNA. DR PIR; D81044; D81044. DR RefSeq; NP_274776.1; NC_003112.2. DR RefSeq; WP_010980986.1; NC_003112.2. DR STRING; 122586.NMB1776; -. DR PaxDb; Q9JY26; -. DR EnsemblBacteria; AAF42116; AAF42116; NMB1776. DR GeneID; 903323; -. DR KEGG; nme:NMB1776; -. DR BioCyc; NMEN122586:GHGG-1831-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 3593 MW; A37C09225AEA6D69 CRC64; MPWKISTTTN LTPVPSANLS ALPTTRCTTP PPTP // ID Q9K088_NEIMB Unreviewed; 161 AA. AC Q9K088; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41143.1}; GN OrderedLocusNames=NMB0730 {ECO:0000313|EMBL:AAF41143.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41143.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41143.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41143.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41143.1; -; Genomic_DNA. DR PIR; E81166; E81166. DR RefSeq; NP_273772.1; NC_003112.2. DR RefSeq; WP_002225457.1; NC_003112.2. DR STRING; 122586.NMB0730; -. DR PaxDb; Q9K088; -. DR EnsemblBacteria; AAF41143; AAF41143; NMB0730. DR GeneID; 902843; -. DR KEGG; nme:NMB0730; -. DR PATRIC; 20356817; VBINeiMen85645_0929. DR eggNOG; COG3030; LUCA. DR HOGENOM; HOG000218854; -. DR KO; K07113; -. DR OMA; TIDGEYH; -. DR OrthoDB; EOG6742Z1; -. DR BioCyc; NMEN122586:GHGG-759-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007313; FxsA. DR Pfam; PF04186; FxsA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 101 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 161 AA; 17514 MW; B7925D7F3FFB8E04 CRC64; MRFFGIGFLV LLFLEIMSIV WVADWLGGGW TLFLMAAGFA AGVLMLRHTG LSGLLLAGAA MRSGGRVSVY QMLWPIRYTV AAVCLMSPGF VSSVLAVLLL LPFKGGAVLQ AGGAENFFNM NQSGRKEGFS RDDDIIEGEY TVEEPYGGNR SRNAIEHKKD E // ID Q9JY22_NEIMB Unreviewed; 580 AA. AC Q9JY22; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Putative hemolysin activation protein HecB {ECO:0000313|EMBL:AAF42120.1}; GN OrderedLocusNames=NMB1780 {ECO:0000313|EMBL:AAF42120.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42120.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42120.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42120.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42120.1; -; Genomic_DNA. DR PIR; F81042; F81042. DR RefSeq; NP_274780.1; NC_003112.2. DR RefSeq; WP_002225635.1; NC_003112.2. DR ProteinModelPortal; Q9JY22; -. DR STRING; 122586.NMB1780; -. DR TCDB; 1.B.20.1.5; the two-partner secretion (tps) family. DR PaxDb; Q9JY22; -. DR EnsemblBacteria; AAF42120; AAF42120; NMB1780. DR GeneID; 903319; -. DR KEGG; nme:NMB1780; -. DR PATRIC; 20359515; VBINeiMen85645_2263. DR eggNOG; ENOG4105D5K; Bacteria. DR eggNOG; COG2831; LUCA. DR HOGENOM; HOG000218787; -. DR OMA; FSYETAI; -. DR OrthoDB; EOG6TBHBP; -. DR BioCyc; NMEN122586:GHGG-1835-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR InterPro; IPR005565; Hemolysn_activator_HlyB. DR InterPro; IPR013686; Polypept-transport_assoc_ShlB. DR InterPro; IPR027282; TPS. DR Pfam; PF08479; POTRA_2; 1. DR Pfam; PF03865; ShlB; 1. DR PIRSF; PIRSF029745; FhaC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 580 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332238. FT DOMAIN 85 150 POTRA_2. {ECO:0000259|Pfam:PF08479}. FT DOMAIN 177 519 ShlB. {ECO:0000259|Pfam:PF03865}. SQ SEQUENCE 580 AA; 65696 MW; 1FCD5EA9800DBB0C CRC64; MKFFPAPCLL VILAVIPLKT LAADENDAEL IRSMQRQQHI DAELLTDANV RFEQPLEKNN YVLSEDETPC TRVNYISLDD KTVRKFSFLP SVLMKETAFK TGMCLGSNNL SRLQKAAQQI LIVRGYLTSQ AIIQPQNMDS GILKLRVSAG EIGDIRYEEK RDGKSAEGSI SAFNNKFPLY RNKILNLRDV EQGLENLRRL PSVKTDIQII PSEEEGKSDL QIKWQQNKPI RFSIGIDDAG GKTTGKYQGN VALSFDNPLG LSDLFYVSYG RGLAHKTDLT DATGTETESG SRSYSVHYSV PVKKWLFSFN HNGHRYHEAT EGYSVNYDYN GKQYQSSLAA ERMLWRNRLH KTSVGMKLWT RQTYKYIDDA EIEVQRRRSA GWEAELRHRA YLNRWQLDGK LSYKRGTGMR QSMPAPEENG GDILPGTSRM KIITASLDAA APFILGKQQF FYATAIQAQW NKTPLVAQDK LSIGSRYTVR GFDGEQSLFG ERGFYWQNTL TWYFHPNHQF YLGADYGRVS GESAQYVSGK QLMGAVVGFR GGHKVGGMFA YDLFAGKPLH KPKGFQTTNT VYGFNLNYSF // ID Q9JZH3_NEIMB Unreviewed; 70 AA. AC Q9JZH3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41453.1}; GN OrderedLocusNames=NMB1056 {ECO:0000313|EMBL:AAF41453.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41453.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41453.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41453.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41453.1; -; Genomic_DNA. DR PIR; C81126; C81126. DR STRING; 122586.NMB1056; -. DR PaxDb; Q9JZH3; -. DR EnsemblBacteria; AAF41453; AAF41453; NMB1056. DR PATRIC; 20357653; VBINeiMen85645_1343. DR eggNOG; ENOG4107079; Bacteria. DR eggNOG; ENOG410Z0C4; LUCA. DR HOGENOM; HOG000027803; -. DR OMA; NLPFNVL; -. DR OrthoDB; EOG66B43D; -. DR BioCyc; NMEN122586:GHGG-1093-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 70 AA; 7827 MW; 22A760368B6821E7 CRC64; MVYQRVMADK DVVGAGYLID FAQTAENLPF NVLLLISLVL NKGNETLKTS MLNKLPDNAK ENLRIMGYLP // ID Q9JZA0_NEIMB Unreviewed; 133 AA. AC Q9JZA0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41605.1}; GN OrderedLocusNames=NMB1224 {ECO:0000313|EMBL:AAF41605.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41605.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41605.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41605.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41605.1; -; Genomic_DNA. DR PIR; A81108; A81108. DR RefSeq; NP_274248.1; NC_003112.2. DR RefSeq; WP_010980909.1; NC_003112.2. DR STRING; 122586.NMB1224; -. DR PaxDb; Q9JZA0; -. DR EnsemblBacteria; AAF41605; AAF41605; NMB1224. DR GeneID; 903646; -. DR KEGG; nme:NMB1224; -. DR HOGENOM; HOG000218958; -. DR OMA; FSRIVHT; -. DR OrthoDB; EOG6GTZK1; -. DR BioCyc; NMEN122586:GHGG-1261-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 133 AA; 15050 MW; E83F751D3B420225 CRC64; MMKKQRHILC VGCLYIILKV NVFPNTGWME ASKGMQGMSF STFGYADAPG YTFSRIGHTL IFLLGKTTGT RTTVSDSSHN VYYVKLYICA NNSKALSCCL MLCQFGRKLS ICAIKRALRW RSSKWVSSWT TTY // ID Q9K104_NEIMB Unreviewed; 312 AA. AC Q9K104; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40835.1}; GN OrderedLocusNames=NMB0395 {ECO:0000313|EMBL:AAF40835.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40835.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40835.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40835.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40835.1; -; Genomic_DNA. DR PIR; C81204; C81204. DR RefSeq; NP_273444.1; NC_003112.2. DR RefSeq; WP_002222013.1; NC_003112.2. DR ProteinModelPortal; Q9K104; -. DR STRING; 122586.NMB0395; -. DR PaxDb; Q9K104; -. DR DNASU; 902510; -. DR EnsemblBacteria; AAF40835; AAF40835; NMB0395. DR GeneID; 902510; -. DR KEGG; nme:NMB0395; -. DR PATRIC; 20355953; VBINeiMen85645_0494. DR eggNOG; ENOG4107QMI; Bacteria. DR eggNOG; COG4111; LUCA. DR HOGENOM; HOG000219101; -. DR OMA; GHRTLQS; -. DR OrthoDB; EOG62RS8R; -. DR BioCyc; NMEN122586:GHGG-417-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.90.79.10; -; 2. DR InterPro; IPR011213; NMN_biosyn. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PIRSF; PIRSF019423; NMN_biosyn; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 312 AA; 35440 MW; 14938F68460BA813 CRC64; MDAYPEAEAP PQSIVELVPV LIAVTDGGLR VLTVAQGMLL PNGPLSPLRN SLQAGVKLWV AKQTSQPMGY VEQLYTFVDT HRRNEHGMPV LYVSYLGLVR EAADSILHPD AKWQDCYGYF PWEDLRTDGG QRDAVVGRLR IWANSADTEE VRQKRLKRIH LCWGVEPENW SEEYVLQRYE MLYESGLIAE AAEPQANFDF ALTGQPMRHD HRRVLATALS RLRAKIKYRP VIFELMPPEF TLLQLQNSVE AISGRLLHKQ NFRRQIQQQN LIEPSDTGVS GSKGRPAQLC RFRDDVLPDR LISDIGLPLG SR // ID Q9K0F7_NEIMB Unreviewed; 74 AA. AC Q9K0F7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41070.1}; GN OrderedLocusNames=NMB0649 {ECO:0000313|EMBL:AAF41070.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41070.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41070.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41070.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41070.1; -; Genomic_DNA. DR PIR; D81173; D81173. DR RefSeq; NP_273691.1; NC_003112.2. DR RefSeq; WP_002222817.1; NC_003112.2. DR STRING; 122586.NMB0649; -. DR PaxDb; Q9K0F7; -. DR EnsemblBacteria; AAF41070; AAF41070; NMB0649. DR GeneID; 902761; -. DR KEGG; nme:NMB0649; -. DR PATRIC; 20356597; VBINeiMen85645_0817. DR eggNOG; ENOG410686Y; Bacteria. DR eggNOG; ENOG410XVI2; LUCA. DR HOGENOM; HOG000218829; -. DR OMA; IPNYTWH; -. DR OrthoDB; EOG63JR5W; -. DR BioCyc; NMEN122586:GHGG-676-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR InterPro; IPR024622; Colicin/pyocin_DNase_dom. DR Pfam; PF12639; Colicin-DNase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 66 Colicin-DNase. FT {ECO:0000259|Pfam:PF12639}. SQ SEQUENCE 74 AA; 8605 MW; E2C6B81567CC3C42 CRC64; MRLATKDLAE AIRKGQVRKS SFNTEQLRAI EKGESKIPDY TWHHHQDTGR MQLIREGLHH DTGHIGWEAM NKGR // ID Q9JX97_NEIMB Unreviewed; 211 AA. AC Q9JX97; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Putative pyrazinamidase/nicotinamidase PncA {ECO:0000313|EMBL:AAF42465.1}; GN OrderedLocusNames=NMB2157 {ECO:0000313|EMBL:AAF42465.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42465.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42465.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42465.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42465.1; -; Genomic_DNA. DR PIR; C81001; C81001. DR RefSeq; NP_275142.1; NC_003112.2. DR RefSeq; WP_002223229.1; NC_003112.2. DR ProteinModelPortal; Q9JX97; -. DR STRING; 122586.NMB2157; -. DR PaxDb; Q9JX97; -. DR EnsemblBacteria; AAF42465; AAF42465; NMB2157. DR GeneID; 903215; -. DR KEGG; nme:NMB2157; -. DR PATRIC; 20360510; VBINeiMen85645_2751. DR eggNOG; ENOG4108RWI; Bacteria. DR eggNOG; COG1335; LUCA. DR HOGENOM; HOG000078666; -. DR KO; K08281; -. DR OMA; GACYHDL; -. DR OrthoDB; EOG615VP6; -. DR BioCyc; NMEN122586:GHGG-2222-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.50.850; -; 1. DR InterPro; IPR000868; Isochorismatase-like. DR Pfam; PF00857; Isochorismatase; 1. DR SUPFAM; SSF52499; SSF52499; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 202 Isochorismatase. FT {ECO:0000259|Pfam:PF00857}. SQ SEQUENCE 211 AA; 23368 MW; C2FE40AC63A6CCDA CRC64; MIVSIDVDAQ KTFTPLCPDE LPVNEGHLIV EELNAQAALA DLRVMTKDAH HMVAKWLVDN PVDMLKPTGL PDADLTWVAH AMVGTRGYEL LDGLPSAKEY DYCVWKGVDP ELHPYGACFH DIEEKLSTGL IEWLRCQNTD TVIIGGLATD YCVKTTVLQL LKGGRWQVVV NEAACRGIAP ETIETAWQEM HSAGAIILKN ADEINKYINN Q // ID Q9K0H7_NEIMB Unreviewed; 176 AA. AC Q9K0H7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41050.1}; GN OrderedLocusNames=NMB0625 {ECO:0000313|EMBL:AAF41050.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41050.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41050.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41050.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41050.1; -; Genomic_DNA. DR PIR; E81176; E81176. DR RefSeq; NP_273668.1; NC_003112.2. DR RefSeq; WP_002225532.1; NC_003112.2. DR ProteinModelPortal; Q9K0H7; -. DR PaxDb; Q9K0H7; -. DR EnsemblBacteria; AAF41050; AAF41050; NMB0625. DR GeneID; 902738; -. DR KEGG; nme:NMB0625; -. DR PATRIC; 20356545; VBINeiMen85645_0792. DR eggNOG; ENOG4108Z0R; Bacteria. DR eggNOG; COG0663; LUCA. DR HOGENOM; HOG000049430; -. DR OMA; FFPYSAG; -. DR OrthoDB; EOG65XN5M; -. DR BioCyc; NMEN122586:GHGG-651-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 2. DR SUPFAM; SSF51161; SSF51161; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 176 AA; 18986 MW; EBEF11CDBAEF07E1 CRC64; MNAIRTFQNR TPEIHETCMI DEACVVIGEV SLAEDVSVWP CAVLRGDVNS ITVGARSNIQ DGSVLHVSHK TAAKPEGSPL VIGEDVTVGH KVMLHGCRIG NRVLVGMGTT VLDDAVIEDE VMIGAGSLVP PRKRLAGGYL YVGSPVRQVR VLTDEEKAFL KYSAAHYVKL SKQYGM // ID Q9K1P5_NEIMB Unreviewed; 421 AA. AC Q9K1P5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40507.1}; GN OrderedLocusNames=NMB0036 {ECO:0000313|EMBL:AAF40507.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40507.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40507.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40507.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40507.1; -; Genomic_DNA. DR PIR; F81244; F81244. DR RefSeq; NP_273102.1; NC_003112.2. DR RefSeq; WP_002243924.1; NC_003112.2. DR ProteinModelPortal; Q9K1P5; -. DR STRING; 122586.NMB0036; -. DR PaxDb; Q9K1P5; -. DR EnsemblBacteria; AAF40507; AAF40507; NMB0036. DR GeneID; 902139; -. DR KEGG; nme:NMB0036; -. DR PATRIC; 20355027; VBINeiMen85645_0050. DR eggNOG; ENOG4105DBE; Bacteria. DR eggNOG; COG2837; LUCA. DR HOGENOM; HOG000236941; -. DR KO; K16301; -. DR OMA; VERWDRT; -. DR OrthoDB; EOG6F55G9; -. DR BioCyc; NMEN122586:GHGG-37-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro. DR GO; GO:0015684; P:ferrous iron transport; IEA:InterPro. DR GO; GO:0033212; P:iron assimilation; IEA:InterPro. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR006314; Dyp_peroxidase. DR InterPro; IPR006313; EfeB. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF04261; Dyp_perox; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1. DR TIGRFAMs; TIGR01412; tat_substr_1; 1. DR PROSITE; PS51404; DYP_PEROXIDASE; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 421 AA; 46118 MW; 1488F54783D74337 CRC64; MSKKQPAQPT RRTLFKTAIA AGAVGAIGGY LGGKKQGETA ERTAESQHSP QAYPCYGEHQ AGIVTPQQAF SIMCAFDVTA QSAKQLENLF RTLTARIEFL TQGGEYQDGD DKLPPAGSGI LGKAFNPDGL TVTVGVGSSL FDGRFGLKDK KPIHLQEMRD FSNDKLQKSW CDGDLSLQIC AFTPETCQAA LRDIIKHTVQ TAVIRWSIDG WQPKSEPGAM AARNLLGFRD GTGNPKVSDP KTADEVLWTG VAANSLDEPE WAKNGSYQAV RLIRHFVEFW DRTPLQEQTD IFGRRKYSGA PMDGKKEADQ PDFAKDPEGD ITPKDSHIRL ANPRDPEFLK KHRLFRRAYS YSRGLASSGQ LDVGLVFVCY QANLADGFIF VQNLLNGEPL EEYISPFGGG YFFVLPGVEK GGFLGQGLLG V // ID Q9K1L2_NEIMB Unreviewed; 172 AA. AC Q9K1L2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40561.1}; GN OrderedLocusNames=NMB0102 {ECO:0000313|EMBL:AAF40561.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40561.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40561.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40561.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40561.1; -; Genomic_DNA. DR PIR; E81237; E81237. DR RefSeq; NP_273160.1; NC_003112.2. DR RefSeq; WP_002232242.1; NC_003112.2. DR STRING; 122586.NMB0102; -. DR PaxDb; Q9K1L2; -. DR EnsemblBacteria; AAF40561; AAF40561; NMB0102. DR GeneID; 902206; -. DR KEGG; nme:NMB0102; -. DR PATRIC; 20355213; VBINeiMen85645_0140. DR HOGENOM; HOG000218675; -. DR OMA; RPDIAFN; -. DR OrthoDB; EOG6HQSPF; -. DR BioCyc; NMEN122586:GHGG-108-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 150 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 172 AA; 18161 MW; 1DB2696FD70D5AD7 CRC64; MWRVLSALPI GVVFFDLIYG FVLNVLQGLD LQRAVPDSEG VLAVTPDIAF NSLQIVANGG MAAVVCFGLA VVFLLNRSVR RRQVLEIGVF RMLGLVAVLA FSAPSVWEWA NALPLLLKGA DVVNTGNARY VLTALCMPFP AVSCVIGLVG RFRLQTASGR AAKSGGAGKA DG // ID Q9K090_NEIMB Unreviewed; 216 AA. AC Q9K090; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026}; DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026}; GN OrderedLocusNames=NMB0727 {ECO:0000313|EMBL:AAF41140.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41140.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41140.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41140.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000256|RuleBase:RU362026}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41140.1; -; Genomic_DNA. DR PIR; B81166; B81166. DR RefSeq; NP_273769.1; NC_003112.2. DR RefSeq; WP_002217650.1; NC_003112.2. DR ProteinModelPortal; Q9K090; -. DR STRING; 122586.NMB0727; -. DR PaxDb; Q9K090; -. DR EnsemblBacteria; AAF41140; AAF41140; NMB0727. DR GeneID; 902840; -. DR KEGG; nme:NMB0727; -. DR eggNOG; ENOG4107WH3; Bacteria. DR eggNOG; COG0863; LUCA. DR HOGENOM; HOG000032246; -. DR KO; K00571; -. DR OMA; CEIAYCS; -. DR OrthoDB; EOG6FZ4GH; -. DR BioCyc; NMEN122586:GHGG-756-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0006306; P:DNA methylation; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF41140.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41140.1}. FT DOMAIN 113 193 N6_N4_Mtase. {ECO:0000259|Pfam:PF01555}. SQ SEQUENCE 216 AA; 25398 MW; 13B808D49C92FE2C CRC64; MITISNEDNM ILMSRYPDKY FDLAIVDPPY GILNKTKRGG DYKFNMNEYS QWDIKPDQTY FNELFRVSKN QIIWGGNYFG ELWLRSEYNK GFIIWDKNQP ETLNNFSMAE MAWSSFDRPS KIFRFSVRKN RNKTHPTQKP VELYQWLLKM YAKQGDKILD THLGSGTLAI ACCIAQFDLT ACEINSDYYQ QSIEKIKNNL PEARISFGHP GYCIIE // ID Q9JZ85_NEIMB Unreviewed; 242 AA. AC Q9JZ85; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461}; DE EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461}; GN Name=rpe {ECO:0000313|EMBL:AAF41625.1}; GN OrderedLocusNames=NMB1244 {ECO:0000313|EMBL:AAF41625.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41625.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41625.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41625.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5- CC phosphate. {ECO:0000256|PIRNR:PIRNR001461}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000256|PIRSR:PIRSR001461-2}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. CC {ECO:0000256|PIRNR:PIRNR001461}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41625.1; -; Genomic_DNA. DR PIR; A81106; A81106. DR RefSeq; NP_274268.1; NC_003112.2. DR RefSeq; WP_002213492.1; NC_003112.2. DR ProteinModelPortal; Q9JZ85; -. DR STRING; 122586.NMB1244; -. DR PaxDb; Q9JZ85; -. DR EnsemblBacteria; AAF41625; AAF41625; NMB1244. DR GeneID; 903666; -. DR KEGG; nme:NMB1244; -. DR PATRIC; 20358085; VBINeiMen85645_1555. DR eggNOG; ENOG4105DJV; Bacteria. DR eggNOG; COG0036; LUCA. DR HOGENOM; HOG000259347; -. DR KO; K01783; -. DR OMA; GANYITF; -. DR OrthoDB; EOG67HK17; -. DR BioCyc; NMEN122586:GHGG-1281-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR026019; Ribul_P_3_epim. DR InterPro; IPR000056; Ribul_P_3_epim-like. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR11749; PTHR11749; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01163; rpe; 1. DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1. DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461}; KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|PIRNR:PIRNR001461, KW ECO:0000313|EMBL:AAF41625.1}; KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}. FT REGION 143 146 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT REGION 202 203 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT ACT_SITE 36 36 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR001461-1}. FT ACT_SITE 180 180 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001461-1}. FT METAL 34 34 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 36 36 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 67 67 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 180 180 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT BINDING 9 9 Substrate. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT BINDING 67 67 Substrate. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT BINDING 182 182 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR001461-3}. SQ SEQUENCE 242 AA; 26289 MW; AD37D414E37B037C CRC64; MTTYRIAPSI LSADFARLGE EVESVIAAGA DLIHFDVMDN HYVPNLTFGP MVCAALKPYA SVPIDVHLMV EPVDDLIQSF AKAGASIITF HPEASRHIDR SLSLIRDMGC QAGLVLNPAT PVYLLENVLD RLDMVLLMSV NPGFGGQSFI PHTLEKIRRV RAMLDRYEAQ SGRHIAIEVD GGIKTDNIAA VARAGADTFV AGSAIFGKPD YKAVIDAMRA ELEKSGRLNL APMIEIEMPS EN // ID Q9K0Z8_NEIMB Unreviewed; 30 AA. AC Q9K0Z8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40842.1}; GN OrderedLocusNames=NMB0403 {ECO:0000313|EMBL:AAF40842.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40842.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40842.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40842.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40842.1; -; Genomic_DNA. DR PIR; H81202; H81202. DR RefSeq; NP_273452.1; NC_003112.2. DR RefSeq; WP_010980790.1; NC_003112.2. DR STRING; 122586.NMB0403; -. DR PaxDb; Q9K0Z8; -. DR EnsemblBacteria; AAF40842; AAF40842; NMB0403. DR GeneID; 902517; -. DR KEGG; nme:NMB0403; -. DR BioCyc; NMEN122586:GHGG-425-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 30 AA; 3285 MW; 94819EDA30756E7D CRC64; MPSENGRRII GKTYRASFAV AKLHLKTPAA // ID Q9JYU7_NEIMB Unreviewed; 342 AA. AC Q9JYU7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41785.1}; GN OrderedLocusNames=NMB1424 {ECO:0000313|EMBL:AAF41785.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41785.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41785.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41785.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41785.1; -; Genomic_DNA. DR PIR; B81086; B81086. DR RefSeq; NP_274436.1; NC_003112.2. DR RefSeq; WP_002237161.1; NC_003112.2. DR ProteinModelPortal; Q9JYU7; -. DR PaxDb; Q9JYU7; -. DR EnsemblBacteria; AAF41785; AAF41785; NMB1424. DR GeneID; 903846; -. DR KEGG; nme:NMB1424; -. DR PATRIC; 20358543; VBINeiMen85645_1783. DR HOGENOM; HOG000219012; -. DR OMA; MCPADED; -. DR OrthoDB; EOG6FBWW2; -. DR BioCyc; NMEN122586:GHGG-1462-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR007929; DUF723. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF05265; DUF723; 1. DR SUPFAM; SSF51306; SSF51306; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 342 AA; 37323 MW; 24999CEFF45922DB CRC64; MARRSKTFEE AAAEVEERFG HRGIKLVEFE GTAKPCVINC PKHGNQTCSR YSNMFIGSSW GCPSCGNEQA AKAGIATLRK NHIALEMLKQ AVTGMTKQER ITTQAYNEMT KSVAGSNSIV LNDVQGDTTI NNHHTHTHNH SDADGKALSM RLTPRPLLSD RQAAAFARTG KLTGSFDLFA SVVAPSQYTF AVAMPDTSMS PVIEKGDLLV VEPRMCPADE DIALIELSDK RLVVAHLVID IAGRMLIYQT GRPSEAFDLP EGSTILGVVL ESKNGLCPPH RQEGVLIRIT APDVWTVGMI SASKTSCTRP TAARKSAVCF LRFWQATRGI PKTRSWRNPN NA // ID Q7DD63_NEIMB Unreviewed; 287 AA. AC Q7DD63; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 57. DE RecName: Full=Lipoprotein {ECO:0000256|PIRNR:PIRNR002854}; GN OrderedLocusNames=NMB1946 {ECO:0000313|EMBL:AAF42275.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42275.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42275.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42275.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the nlpA lipoprotein family. CC {ECO:0000256|PIRNR:PIRNR002854}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42275.1; -; Genomic_DNA. DR RefSeq; NP_274940.1; NC_003112.2. DR RefSeq; WP_002225833.1; NC_003112.2. DR ProteinModelPortal; Q7DD63; -. DR STRING; 122586.NMB1946; -. DR PaxDb; Q7DD63; -. DR EnsemblBacteria; AAF42275; AAF42275; NMB1946. DR GeneID; 904205; -. DR KEGG; nme:NMB1946; -. DR PATRIC; 20359943; VBINeiMen85645_2476. DR eggNOG; ENOG4107F8V; Bacteria. DR eggNOG; COG1464; LUCA. DR HOGENOM; HOG000222927; -. DR KO; K02073; -. DR OMA; PHTIVFG; -. DR OrthoDB; EOG6P073X; -. DR BioCyc; NMEN122586:GHGG-2003-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR004872; Lipoprotein_NlpA. DR PANTHER; PTHR30429; PTHR30429; 1. DR Pfam; PF03180; Lipoprotein_9; 1. DR PIRSF; PIRSF002854; MetQ; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000256|PIRNR:PIRNR002854, KW ECO:0000313|EMBL:AAF42275.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 287 Lipoprotein. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287189. SQ SEQUENCE 287 AA; 31221 MW; 87AABC2C93E03B01 CRC64; MKTFFKTLSA AALALILAAC GGQKDSAPAA SASAAADNGA AKKEIVFGTT VGDFGDMVKE QIQAELEKKG YTVKLVEFTD YVRPNLALAE GELDINVFQH KPYLDDFKKE HNLDITEVFQ VPTAPLGLYP GKLKSLEEVK DGSTVSAPND PSNFARVLVM LDELGWIKLK DGINPLTASK ADIAENLKNI KIVELEAAQL PRSRADVDFA VVNGNYAISS GMKLTEALFQ EPSFAYVNWS AVKTADKDSQ WLKDVTEAYN SDAFKAYAHK RFEGYKSPAA WNEGAAK // ID Q4W565_NEIMB Unreviewed; 704 AA. AC Q4W565; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=DNA polymerase III, subunits gamma and tau {ECO:0000313|EMBL:AAY52154.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAY52154.1}; GN Name=dnaX {ECO:0000313|EMBL:AAY52154.1}; GN OrderedLocusNames=NMB1443 {ECO:0000313|EMBL:AAY52154.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52154.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52154.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52154.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52154.1; -; Genomic_DNA. DR RefSeq; NP_274455.1; NC_003112.2. DR RefSeq; WP_002244171.1; NC_003112.2. DR ProteinModelPortal; Q4W565; -. DR SMR; Q4W565; 3-361. DR STRING; 122586.NMB1443; -. DR PaxDb; Q4W565; -. DR EnsemblBacteria; AAY52154; AAY52154; NMB1443. DR GeneID; 903132; -. DR KEGG; nme:NMB1443; -. DR PATRIC; 20358601; VBINeiMen85645_1812. DR eggNOG; ENOG4107QMP; Bacteria. DR eggNOG; COG2812; LUCA. DR HOGENOM; HOG000083934; -. DR KO; K02343; -. DR OMA; NDCPVED; -. DR OrthoDB; EOG6WQD76; -. DR BioCyc; NMEN122586:GHGG-1481-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR022754; DNA_pol_III_gamma-3. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR021029; DNA_pol_III_tau_dom-5. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF12169; DNA_pol3_gamma3; 1. DR Pfam; PF12170; DNA_pol3_tau_5; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02397; dnaX_nterm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAY52154.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAY52154.1}. FT DOMAIN 37 179 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 704 AA; 76261 MW; 8A26572B6F8F7241 CRC64; MAYQVLARKW RPKTFADLVG QEHVVKALQN ALDEGRLHHA YLLTGTRGVG KTTIARILAK SLNCENAQHG EPCGVCESCT QIDAGRYVDL LEIDAASNTG IDNIREVLEN AQYAPTAGKY KVYIIDEVHM LSKSAFNAML KTLEEPPEHV KFILATTDPH KVPVTVLSRC LQFVLRNMTA QQVADHLAHV LDSEKIAYEP AALQLLGRAA AGSMRDALSL LDQAIALGSG KVAENDVRQM IGAVDKQYLY ELLTGIINQD GAALTAKAQE MAACAVGFDN ALGELAILLQ HLALIQAVPN ALAHDDPDSD ILHRLAQTIS GEQIQLYYQI AVHGKRDLSL APDEYAGFMM TLLRMLAFAP LAAASCDANA VIENTELKSP SAQTAEKETA AKKPQPRPEA ETAQTPVQTA SAAAMPSEGK TAEPVTNQEN NDIPPWEDAP DETAAGTAQA SAKSIQTASE AGTPPKNQVS KNEAADNETD APLSEVPSEN PIQATPNNEA LETEAFAHEA PAKPFNGYSF PNDDYLVEDG AEIPPPDWEH AAPADAEEEN NADESSNNED HTPYAPPPEF STENWAAIVR HFARKLGAAQ MPAQHSAWTE YHPDTGLMVL AMTAEARATA DKKRLDKIRD TLAQAYGLQL TLQTQDWRDE AGRETPAMQD KRVQAEDRQK AQALLEADPA AQKILQAFGA QWQPESLELA ANRP // ID Q9JYA5_NEIMB Unreviewed; 172 AA. AC Q9JYA5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42021.1}; GN OrderedLocusNames=NMB1672 {ECO:0000313|EMBL:AAF42021.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42021.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42021.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42021.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42021.1; -; Genomic_DNA. DR PIR; B81057; B81057. DR RefSeq; NP_274677.1; NC_003112.2. DR RefSeq; WP_002222138.1; NC_003112.2. DR ProteinModelPortal; Q9JYA5; -. DR STRING; 122586.NMB1672; -. DR PaxDb; Q9JYA5; -. DR EnsemblBacteria; AAF42021; AAF42021; NMB1672. DR GeneID; 903438; -. DR KEGG; nme:NMB1672; -. DR PATRIC; 20359286; VBINeiMen85645_2151. DR eggNOG; ENOG410639K; Bacteria. DR eggNOG; COG3009; LUCA. DR HOGENOM; HOG000283606; -. DR KO; K09857; -. DR OMA; IKRPFNI; -. DR OrthoDB; EOG6PZXDB; -. DR BioCyc; NMEN122586:GHGG-1726-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.10610; -; 1. DR InterPro; IPR005586; ABC_trans_aux. DR Pfam; PF03886; ABC_trans_aux; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 172 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332247. SQ SEQUENCE 172 AA; 18812 MW; FE32830428245567 CRC64; MRLFPIAAAL SLAACGTVQS TQYFVLPDSR YIRPATQGGE TAVEVRLAEP LKRGGLVYQT DPYRLNTAQN HVWADTLDDM LEAALSNAFN RLDSTRIFVP ASRSGSTEKW TVYIDAFQGS YTGKTLISGY AVLPDGTNRP FHIETEQQGD GYAAMTAALE QGLKQAAQQM VE // ID Q9JZQ1_NEIMB Unreviewed; 54 AA. AC Q9JZQ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41351.1}; GN OrderedLocusNames=NMB0945 {ECO:0000313|EMBL:AAF41351.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41351.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41351.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41351.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41351.1; -; Genomic_DNA. DR PIR; F81140; F81140. DR STRING; 122586.NMB0945; -. DR PaxDb; Q9JZQ1; -. DR EnsemblBacteria; AAF41351; AAF41351; NMB0945. DR PATRIC; 20357371; VBINeiMen85645_1200. DR HOGENOM; HOG000071281; -. DR OMA; AGKFSHC; -. DR OrthoDB; EOG6PCQ35; -. DR BioCyc; NMEN122586:GHGG-982-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 54 AA; 6151 MW; DBFA14FBFE47C7E2 CRC64; MNKYRLKAFQ TVFCPDLRRK GAVAGKSFHC SLFFSNSALY VGNRQIGVVF DSFK // ID Q9K178_NEIMB Unreviewed; 201 AA. AC Q9K178; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40743.1}; GN OrderedLocusNames=NMB0292 {ECO:0000313|EMBL:AAF40743.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40743.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40743.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40743.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40743.1; -; Genomic_DNA. DR PIR; C81215; C81215. DR RefSeq; NP_273346.1; NC_003112.2. DR RefSeq; WP_002230218.1; NC_003112.2. DR ProteinModelPortal; Q9K178; -. DR STRING; 122586.NMB0292; -. DR PaxDb; Q9K178; -. DR DNASU; 902403; -. DR EnsemblBacteria; AAF40743; AAF40743; NMB0292. DR GeneID; 902403; -. DR KEGG; nme:NMB0292; -. DR PATRIC; 20355684; VBINeiMen85645_0366. DR eggNOG; ENOG4108RTX; Bacteria. DR eggNOG; COG3560; LUCA. DR HOGENOM; HOG000089187; -. DR KO; K07078; -. DR OMA; YFEDSEV; -. DR OrthoDB; EOG6SV5D7; -. DR BioCyc; NMEN122586:GHGG-307-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 178 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. SQ SEQUENCE 201 AA; 22094 MW; 6DAFBB45FB8D6B9B CRC64; MTRQSLQQAA ESRRSIYSLN KNLPVGKDEV VQIVEHAVLH TPSSFNSQSA RVVVLFGEEH DKVWQFVEDA LRAVVPADSF EPTAQKLNLF KAGAATILFY EDQNVVKGLQ EQFPAYAANF PVWADQANAM VQYAVWTTLA AVGVGANLQH YNPLPDAAIA KAWNIPENWL LRAQMVIGGI EGAAGEKTFE PVAERLKVFG A // ID Q9K1D6_NEIMB Unreviewed; 72 AA. AC Q9K1D6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40679.1}; GN OrderedLocusNames=NMB0223 {ECO:0000313|EMBL:AAF40679.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40679.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40679.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40679.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40679.1; -; Genomic_DNA. DR PIR; A81223; A81223. DR STRING; 122586.NMB0223; -. DR PaxDb; Q9K1D6; -. DR EnsemblBacteria; AAF40679; AAF40679; NMB0223. DR PATRIC; 20355520; VBINeiMen85645_0284. DR OMA; IMGFWGS; -. DR OrthoDB; EOG6P338J; -. DR BioCyc; NMEN122586:GHGG-238-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 72 AA; 7950 MW; 6EA0AA7F470CE1C9 CRC64; MIMGFWNGVA KAAKAVGEGM IEAGNEHKAL KMEYAEKSSE ELHEIVKSDG FFKNSTREKS AAYAILKERG EV // ID Q9K0D3_NEIMB Unreviewed; 290 AA. AC Q9K0D3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE EC=6.4.1.2 {ECO:0000256|HAMAP-Rule:MF_01395}; GN Name=accD {ECO:0000256|HAMAP-Rule:MF_01395, GN ECO:0000313|EMBL:AAF41097.1}; GN OrderedLocusNames=NMB0679 {ECO:0000313|EMBL:AAF41097.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41097.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41097.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41097.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. Biotin carboxylase (BC) catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the transcarboxylase to acetyl-CoA to form malonyl- CC CoA. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01395}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) CC and two subunits each of ACCase subunit alpha (AccA) and ACCase CC subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_01395, CC ECO:0000256|SAAS:SAAS00521812}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395, CC ECO:0000256|SAAS:SAAS00505673}. CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP- CC Rule:MF_01395}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41097.1; -; Genomic_DNA. DR PIR; E81171; E81171. DR RefSeq; NP_273721.1; NC_003112.2. DR RefSeq; WP_002225500.1; NC_003112.2. DR ProteinModelPortal; Q9K0D3; -. DR SMR; Q9K0D3; 27-281. DR STRING; 122586.NMB0679; -. DR PaxDb; Q9K0D3; -. DR EnsemblBacteria; AAF41097; AAF41097; NMB0679. DR GeneID; 902791; -. DR KEGG; nme:NMB0679; -. DR PATRIC; 20356667; VBINeiMen85645_0851. DR eggNOG; ENOG4107QTG; Bacteria. DR eggNOG; COG0777; LUCA. DR HOGENOM; HOG000021670; -. DR KO; K01963; -. DR OMA; PEGLWIK; -. DR OrthoDB; EOG6HQSSF; -. DR BioCyc; NMEN122586:GHGG-707-MONOMER; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1. DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su. DR InterPro; IPR000022; Carboxyl_trans. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011762; COA_CT_N. DR Pfam; PF01039; Carboxyl_trans; 1. DR PRINTS; PR01070; ACCCTRFRASEB. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00515; accD; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395, KW ECO:0000256|SAAS:SAAS00505665}; KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01395, ECO:0000313|EMBL:AAF41097.1}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41097.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 33 260 Carboxyltransferase. FT {ECO:0000259|PROSITE:PS50980}. FT ZN_FING 31 53 C4-type. {ECO:0000256|HAMAP- FT Rule:MF_01395}. FT METAL 31 31 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 34 34 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 50 50 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 53 53 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. SQ SEQUENCE 290 AA; 31709 MW; D42789DAE262B02C CRC64; MSWLDKILPP KIKNRGKDGS SNVPEGLWHK CPSCSATVYS TELQQNNQVC PKCNHHNPLS ARQRLNLLLD EDGREEVAGN VKPTDPLKFK DGKKYPDRLS AARKLTGEDD ALVVMKGKMN GLPVVVAAFE FRFIGGSMGS VVGERFVQGI RRAVADNCPF VCVAASGGAR MQEGVNSLMQ MTKTSAALHL LTEKRLPFIS VLTDPTMGGV SASFAFLGDV VLAEPNALIG FAGPRVIEQT VRETLPEGFQ RAEFLLEKGA IDQIVDRRDM KRRISDLITL LCRQDKVSAA // ID Q9JYK1_NEIMB Unreviewed; 100 AA. AC Q9JYK1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41902.1}; GN OrderedLocusNames=NMB1547 {ECO:0000313|EMBL:AAF41902.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41902.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41902.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41902.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41902.1; -; Genomic_DNA. DR PIR; F81071; F81071. DR RefSeq; NP_274554.1; NC_003112.2. DR RefSeq; WP_002223128.1; NC_003112.2. DR STRING; 122586.NMB1547; -. DR PaxDb; Q9JYK1; -. DR EnsemblBacteria; AAF41902; AAF41902; NMB1547. DR GeneID; 904091; -. DR KEGG; nme:NMB1547; -. DR PATRIC; 20358928; VBINeiMen85645_1978. DR HOGENOM; HOG000219039; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-1588-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 100 AA; 11217 MW; CB3D858DA1458DF0 CRC64; MGYRVGINCF DTRLQADDYL LSSLPPTVTQ DGKIIRPERV GDKWILNGKP VTLSYPECSN FEQIKQGSYV GSTVLILFVV IYGFRLLINF LKDIGKVGTD // ID Q9JZV5_NEIMB Unreviewed; 468 AA. AC Q9JZV5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 105. DE RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085}; GN Name=dnaB {ECO:0000313|EMBL:AAF41296.1}; GN OrderedLocusNames=NMB0885 {ECO:0000313|EMBL:AAF41296.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41296.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41296.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41296.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Participates in initiation and elongation during CC chromosome replication; it exhibits DNA-dependent ATPase activity CC and contains distinct active sites for ATP binding, DNA binding, CC and interaction with DnaC protein, primase, and other prepriming CC proteins. {ECO:0000256|RuleBase:RU362085}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|RuleBase:RU362085}. CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily. CC {ECO:0000256|RuleBase:RU362085}. CC -!- SIMILARITY: Contains 1 SF4 helicase domain. CC {ECO:0000256|RuleBase:RU362085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41296.1; -; Genomic_DNA. DR PIR; E81145; E81145. DR RefSeq; NP_273926.1; NC_003112.2. DR RefSeq; WP_002225362.1; NC_003112.2. DR ProteinModelPortal; Q9JZV5; -. DR STRING; 122586.NMB0885; -. DR PaxDb; Q9JZV5; -. DR EnsemblBacteria; AAF41296; AAF41296; NMB0885. DR GeneID; 903004; -. DR KEGG; nme:NMB0885; -. DR PATRIC; 20357177; VBINeiMen85645_1102. DR eggNOG; ENOG4105CDU; Bacteria. DR eggNOG; COG0305; LUCA. DR HOGENOM; HOG000113196; -. DR KO; K02314; -. DR OMA; SELMEHT; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; NMEN122586:GHGG-921-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007692; DNA_helicase_DnaB. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00772; DnaB; 1. DR Pfam; PF03796; DnaB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48024; SSF48024; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00665; DnaB; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAF41296.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA replication {ECO:0000256|RuleBase:RU362085, KW ECO:0000256|SAAS:SAAS00435671}; KW DNA-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000256|SAAS:SAAS00435659}; KW Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:AAF41296.1}; KW Hydrolase {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAF41296.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAF41296.1}; KW Primosome {ECO:0000256|RuleBase:RU362085}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 194 461 SF4 helicase. FT {ECO:0000259|PROSITE:PS51199}. SQ SEQUENCE 468 AA; 52088 MW; E556BDD33269D113 CRC64; MNDYAAMPSE DREVGALSLP PHSMEAEQSV LGGLMLENPA WDRIADVVSG EDFYRHEHRL IFRSIAKLIN ESRPADVITV QEDLQRNEEL EAAGGFEYLI TLAQNTPSAA NIRRYAEIVR ERSIMRQLAE VGTEIARSAY NPQGRDAGQL LDEAENKVFQ IAESTAKSKQ GFLEMPDLLK EVVQRIDMLY SRDNPDEVTG VPTGFIDLDK KTSGLQPGDL IIVAGRPSMG KTAFSINIAE HVAVEGRLPV AVFSMEMGGA QLVMRMLGSV GRLDQSVLKT GRLEDEHWGR LNEAVVKLSD APVYIDETPG LTALELRARA RRLARQFNNK LGLIVIDYLQ LMAGSGRSDN RASELGEISR SLKALAKELQ VPIIALSQLS RTVESRTDKR PMMSDLRESG AIEQDADLIM FMYRDEYYNQ DSPMKGLAEC IIGKHRNGPV GKIFLTWTGQ FTKFDNAAYI PEEAKIED // ID Q9JXE8_NEIMB Unreviewed; 176 AA. AC Q9JXE8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42398.1}; GN OrderedLocusNames=NMB2080 {ECO:0000313|EMBL:AAF42398.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42398.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42398.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42398.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42398.1; -; Genomic_DNA. DR PIR; F81009; F81009. DR RefSeq; NP_275069.1; NC_003112.2. DR RefSeq; WP_002225715.1; NC_003112.2. DR STRING; 122586.NMB2080; -. DR PaxDb; Q9JXE8; -. DR DNASU; 903975; -. DR EnsemblBacteria; AAF42398; AAF42398; NMB2080. DR GeneID; 903975; -. DR KEGG; nme:NMB2080; -. DR PATRIC; 20360328; VBINeiMen85645_2661. DR HOGENOM; HOG000218714; -. DR OMA; HGWAQRQ; -. DR OrthoDB; EOG64JFP2; -. DR BioCyc; NMEN122586:GHGG-2146-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR010662; Hydrolase_RBBP9/YdeN. DR Pfam; PF06821; Ser_hydrolase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 176 AA; 19635 MW; 21CBFAF08EB3F1FA CRC64; MQGFELEDLT LWLIRDAGED QMWIDRWAIS YPVVQMSEAS AGQSIGEWQA GLQTAFERIR GKYVAVVAHG AGAAAFLAWL YQADILTRKK IANIILVPQR PDIFPDDAEH AFQRVRCPCR AALVVPEHGG VPHGWAQKQA DLWNARLLVS PHSGSLNGML GGWQWGMKLM QEMLLA // ID Q9JZD2_NEIMB Unreviewed; 121 AA. AC Q9JZD2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41497.1}; GN OrderedLocusNames=NMB1106 {ECO:0000313|EMBL:AAF41497.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41497.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41497.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41497.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41497.1; -; Genomic_DNA. DR PIR; G81121; G81121. DR RefSeq; NP_274137.1; NC_003112.2. DR RefSeq; WP_002217234.1; NC_003112.2. DR STRING; 122586.NMB1106; -. DR PaxDb; Q9JZD2; -. DR EnsemblBacteria; AAF41497; AAF41497; NMB1106. DR GeneID; 903528; -. DR KEGG; nme:NMB1106; -. DR PATRIC; 20357776; VBINeiMen85645_1404. DR BioCyc; NMEN122586:GHGG-1142-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 121 AA; 13220 MW; 772FC2DA7476DCB0 CRC64; MITVKLTHGL TYNGKVVSEL RLKPLTVGGE LAAFALIDDL PELPENATKA ELLQRDVLET LTYWSQQIEA QGIPSDILTA QWLMENLSTE DYHTVMAAQE DLRLKPSAAT ASPDAPSAAE Q // ID Q9JXC8_NEIMB Unreviewed; 114 AA. AC Q9JXC8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42428.1}; GN OrderedLocusNames=NMB2116 {ECO:0000313|EMBL:AAF42428.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42428.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42428.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42428.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42428.1; -; Genomic_DNA. DR PIR; G81004; G81004. DR RefSeq; NP_275103.1; NC_003112.2. DR RefSeq; WP_002215110.1; NC_003112.2. DR PaxDb; Q9JXC8; -. DR EnsemblBacteria; AAF42428; AAF42428; NMB2116. DR GeneID; 903511; -. DR KEGG; nme:NMB2116; -. DR PATRIC; 20360406; VBINeiMen85645_2699. DR HOGENOM; HOG000220774; -. DR OrthoDB; EOG6BS8SP; -. DR BioCyc; NMEN122586:GHGG-2181-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 114 AA; 13277 MW; 2D861B6B63A5C807 CRC64; MIIEHNGNIH KIARMTGNKN NFLEIILSDI HENIKIKPLT IKVKGENVIN ILPEEVSFYV KQGVDLIYEK YKRKFFISEI SFCQSDSRPS SIYAFLTFHL LEDIIKNESP SNYT // ID Q9JZ76_NEIMB Unreviewed; 436 AA. AC Q9JZ76; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41636.1}; GN OrderedLocusNames=NMB1258 {ECO:0000313|EMBL:AAF41636.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41636.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41636.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41636.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41636.1; -; Genomic_DNA. DR PIR; E81103; E81103. DR RefSeq; NP_274280.1; NC_003112.2. DR RefSeq; WP_002222407.1; NC_003112.2. DR ProteinModelPortal; Q9JZ76; -. DR STRING; 122586.NMB1258; -. DR PaxDb; Q9JZ76; -. DR EnsemblBacteria; AAF41636; AAF41636; NMB1258. DR GeneID; 903680; -. DR KEGG; nme:NMB1258; -. DR PATRIC; 20358129; VBINeiMen85645_1576. DR eggNOG; ENOG4105D1H; Bacteria. DR eggNOG; COG2256; LUCA. DR HOGENOM; HOG000017623; -. DR KO; K07478; -. DR OMA; YRYDHDE; -. DR OrthoDB; EOG64FKG0; -. DR BioCyc; NMEN122586:GHGG-1296-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032423; AAA_assoc_2. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR021886; MgsA_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008824; RuvB_N. DR Pfam; PF16193; AAA_assoc_2; 1. DR Pfam; PF12002; MgsA_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 46 162 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 436 AA; 48460 MW; 978F20874DF896EE CRC64; MTDLFAREPD APLAERLRPH TLDDVVGQEH LIGEGKPLRV AVEGGKPHSM LLWGPPGVGK TTLARILAQS FNAQFLPVSA VFSGVKDIRE AIDKAEIALQ QGRATILFVD EVHRFNKAQQ DAFLPHVESG LLTFIGATTE NPSFEVNPAL LSRAQVYVLQ PLSSDDLKKL IAKVLALPEY QEFTIETDAQ KLLVNTADGD ARRLLNLLEQ LLRAADTRRL KNLTAEFLAD SLGAQIRRFD KGGESFYNQI SALHKSVRGS HPNAALYWFC RMLDGGTDPR YLARRIVRIA WEDIGLADPR AFQIANDAAA TFERLGSPEG ELALAQAVLY LAAAAKSNAG YKAYNQMRHF VKENASDEVP VHLRNAPTKL MKELGYGREY RYAHDEPNAY SAGESYMPDG LDEPDFYQPV PRGLEIKIGE KLEWLKSLDE EVLKAK // ID Q9K0Q3_NEIMB Unreviewed; 506 AA. AC Q9K0Q3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40961.1}; GN OrderedLocusNames=NMB0531 {ECO:0000313|EMBL:AAF40961.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40961.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40961.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40961.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40961.1; -; Genomic_DNA. DR PIR; C81190; C81190. DR RefSeq; NP_273576.1; NC_003112.2. DR RefSeq; WP_002236747.1; NC_003112.2. DR STRING; 122586.NMB0531; -. DR PaxDb; Q9K0Q3; -. DR EnsemblBacteria; AAF40961; AAF40961; NMB0531. DR GeneID; 902647; -. DR KEGG; nme:NMB0531; -. DR PATRIC; 20356313; VBINeiMen85645_0675. DR eggNOG; ENOG4107S6Z; Bacteria. DR eggNOG; COG1757; LUCA. DR HOGENOM; HOG000276345; -. DR OMA; LVPISSW; -. DR OrthoDB; EOG6CGC8T; -. DR BioCyc; NMEN122586:GHGG-557-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR018461; Na/H_Antiport_NhaC-like_C. DR Pfam; PF03553; Na_H_antiporter; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 206 225 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 278 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298 318 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 351 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 371 395 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 457 474 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 480 498 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 165 476 Na_H_antiporter. FT {ECO:0000259|Pfam:PF03553}. SQ SEQUENCE 506 AA; 53515 MW; 52E14FBA4DEA2A36 CRC64; MQLIDYSHSF FSVVPPFLAL ALAVITRRVL LSLGIGILVG VAFLVGGNPV DGLTHLKDMV VGLAWSDGDW SLGKPKILVF LILLGIFTSL LTYSGSNQAF ADWAKRHIKN RRGAKMLTAC LVFVTFIDDY FHSLAVGAIA RPVTDKFKVS RTKLAYILDS TAAPMCVLMP VSSWGASIIA TLAGLLVTYK ITEYTPMGTF VAMSLMNYYA LFALIMVFVV AWFSFDIGSM ARFEQAALNE AHDETAVSDA TKGRVYALII PVLALIASTV SAMIYTGAQA SETFSILGAF ENTDVNTSLV FGGTCGVLAV VLCTLGTIKT ADYPKAVWQG AKSMFGAIAI LILAWLISTV VGEMHTGDYL STLVAGNIHP GFLPVILFLL ASVMAFATGT SWGTFGIMLP IAAAMAVKVE PALIIPCMSA VMAGAVCGDH CSPISDTTIL SSTGARCNHI DHVTSQLPYA LTVAAAAASG YLALGLTKSA LLGFGTTGIV LAVLIFLLKD KKRANA // ID Q9JX98_NEIMB Unreviewed; 322 AA. AC Q9JX98; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Heptosyltransferase I {ECO:0000313|EMBL:AAF42464.1}; GN Name=rfaC {ECO:0000313|EMBL:AAF42464.1}; GN OrderedLocusNames=NMB2156 {ECO:0000313|EMBL:AAF42464.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42464.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42464.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42464.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42464.1; -; Genomic_DNA. DR PIR; B81001; B81001. DR RefSeq; NP_275141.1; NC_003112.2. DR RefSeq; WP_002218264.1; NC_003112.2. DR ProteinModelPortal; Q9JX98; -. DR STRING; 122586.NMB2156; -. DR PaxDb; Q9JX98; -. DR EnsemblBacteria; AAF42464; AAF42464; NMB2156. DR GeneID; 903216; -. DR KEGG; nme:NMB2156; -. DR PATRIC; 20360508; VBINeiMen85645_2750. DR eggNOG; ENOG4105D16; Bacteria. DR eggNOG; COG0859; LUCA. DR HOGENOM; HOG000257134; -. DR KO; K02841; -. DR OMA; LFYNRRH; -. DR OrthoDB; EOG6WQD45; -. DR BioCyc; NMEN122586:GHGG-2221-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008920; F:lipopolysaccharide heptosyltransferase activity; IEA:InterPro. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR InterPro; IPR002201; Glyco_trans_9. DR InterPro; IPR011908; LipoPS_heptosylTferase-I. DR Pfam; PF01075; Glyco_transf_9; 1. DR TIGRFAMs; TIGR02193; heptsyl_trn_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42464.1}. SQ SEQUENCE 322 AA; 36198 MW; FAD48F2D05C6CC71 CRC64; MKILLVRLSS MGDLIHTLPA IEDLARQCPD VELHWLCEAG FADIARLHPF VKKIHVMKWR QWRKHLFRAE TWREMGHLKQ TLRQEVFDFV LDSQGLIKSA CFAKMAKSPI CGLDKNSARE GWAALAYVKT YAVPKGKNAV WRNRELFAQV FGYVMPETQV FGLTVPEAGR LKNLAQPYYA ALHATSRDSK LWPVENWRSL LQKLNEEQQC NIYLPWGNED EKTRAKQIAD GLPFAIVCDK INLLQAAYLL KYAVGIVGVD TGLLHLANAL EKPVVGIYTD TDPIKTGVQV SPIAKNLGNI GQIPTADLVY QALMDCVAAD KG // ID Q9JZE9_NEIMB Unreviewed; 181 AA. AC Q9JZE9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 75. DE SubName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AAF41477.1}; GN OrderedLocusNames=NMB1085 {ECO:0000313|EMBL:AAF41477.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41477.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41477.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41477.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3CZX} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ZINC. RA Zhang R., Zhou M., Bargassa M., Joachimiak A.; RT "The crystal structure of the putative N-acetylmuramoyl-L-alanine RT amidase from Neisseria meningitidis."; RL Submitted (APR-2008) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41477.1; -; Genomic_DNA. DR PIR; G81122; G81122. DR RefSeq; NP_274117.1; NC_003112.2. DR RefSeq; WP_002248849.1; NC_003112.2. DR PDB; 3CZX; X-ray; 1.60 A; A/B/C/D=1-181. DR PDBsum; 3CZX; -. DR ProteinModelPortal; Q9JZE9; -. DR STRING; 122586.NMB1085; -. DR PaxDb; Q9JZE9; -. DR EnsemblBacteria; AAF41477; AAF41477; NMB1085. DR GeneID; 903502; -. DR KEGG; nme:NMB1085; -. DR PATRIC; 20357725; VBINeiMen85645_1379. DR eggNOG; ENOG4105QMG; Bacteria. DR eggNOG; COG0860; LUCA. DR HOGENOM; HOG000218907; -. DR KO; K01448; -. DR OrthoDB; EOG60KN2C; -. DR BioCyc; NMEN122586:GHGG-1121-MONOMER; -. DR EvolutionaryTrace; Q9JZE9; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.40.630.40; -; 1. DR InterPro; IPR002508; CW_Hdrlase/autolysin_cat. DR Pfam; PF01520; Amidase_3; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3CZX}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Metal-binding {ECO:0000213|PDB:3CZX}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000213|PDB:3CZX}. FT DOMAIN 5 173 Ami_3. {ECO:0000259|Pfam:PF01520}. FT METAL 11 11 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3CZX}. FT METAL 25 25 Zinc. {ECO:0000213|PDB:3CZX}. FT METAL 77 77 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:3CZX}. SQ SEQUENCE 181 AA; 19306 MW; 57B968873FCDEEA4 CRC64; MSKIICLTAG HSNTDPGAVN GSDREADLAQ DMRNIVASIL RNDYGLTVKT DGTGKGNMPL RDAVKLIRGS DVAIEFHTNA AANKTATGIE ALSTPKNKRW CQVLGKAVAK KTGWKLRGED GFKPDNAGQH SRLAYAQAGG IVFEPFFISN DTDLALFKTT KWGICRAIAD AIAMELGAAK V // ID Q9JZS1_NEIMB Unreviewed; 741 AA. AC Q9JZS1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Isocitrate dehydrogenase, NADP-dependent, monomeric type {ECO:0000313|EMBL:AAF41328.1}; DE EC=1.1.1.42 {ECO:0000313|EMBL:AAF41328.1}; GN Name=icd {ECO:0000313|EMBL:AAF41328.1}; GN OrderedLocusNames=NMB0920 {ECO:0000313|EMBL:AAF41328.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41328.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41328.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41328.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRSR:PIRSR009407-3}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41328.1; -; Genomic_DNA. DR PIR; B81143; B81143. DR RefSeq; NP_273960.1; NC_003112.2. DR RefSeq; WP_002225341.1; NC_003112.2. DR ProteinModelPortal; Q9JZS1; -. DR SMR; Q9JZS1; 7-741. DR STRING; 122586.NMB0920; -. DR PaxDb; Q9JZS1; -. DR PRIDE; Q9JZS1; -. DR EnsemblBacteria; AAF41328; AAF41328; NMB0920. DR GeneID; 903041; -. DR KEGG; nme:NMB0920; -. DR PATRIC; 20357285; VBINeiMen85645_1156. DR eggNOG; ENOG4105E9K; Bacteria. DR eggNOG; COG2838; LUCA. DR HOGENOM; HOG000240860; -. DR KO; K00031; -. DR OMA; RDSGKMW; -. DR OrthoDB; EOG6DVJPP; -. DR BioCyc; NMEN122586:GHGG-958-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.40.718.10; -; 3. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR TIGRFAMs; TIGR00178; monomer_idh; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41328.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT REGION 133 140 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR009407-2}. FT METAL 351 351 Magnesium or manganese. FT {ECO:0000256|PIRSR:PIRSR009407-3}. FT METAL 549 549 Magnesium or manganese. FT {ECO:0000256|PIRSR:PIRSR009407-3}. FT METAL 553 553 Magnesium or manganese. FT {ECO:0000256|PIRSR:PIRSR009407-3}. FT BINDING 146 146 Substrate. FT {ECO:0000256|PIRSR:PIRSR009407-2}. FT BINDING 548 548 Substrate. FT {ECO:0000256|PIRSR:PIRSR009407-2}. FT SITE 256 256 Critical for catalysis. FT {ECO:0000256|PIRSR:PIRSR009407-1}. FT SITE 421 421 Critical for catalysis. FT {ECO:0000256|PIRSR:PIRSR009407-1}. SQ SEQUENCE 741 AA; 80163 MW; 18FB6AF911226D31 CRC64; MTQKSTIVYT HTDEAPALAT QSLLPIVQAF ARHADIDVKT SDISLSGRIL AAFPEYLTEA QRVPDALAEL GELVKQPDAN VIKLPNISAS VPQLTAAIKE LQSKGFAVPD YPADPQTDEE KAVRERYDRI KGSAVNPVLR EGNSDRRAPK AVKNFAKKNP HSMGAWTKDS KTHVATMQSG DFFHNEQSVI VPEATSVSIV FTDKQGNKKE LREPVALKAG EIIDATVMSK KALLAFLAEQ VKDAKAKGVL FSLHMKATMM KVSDPIIFGH AVKVFFAPVF EKFGDKLAAA GVNVNNGFGN LLANLDKLDA DTRTAVEAEI AAVYAANPDL AMVDSDKGIT NLHVPSDVIV DASMPAMIRN SGRMWDKNGK AQDTKAVIPD SSYAGVYQAT IDFCREHGAF DPTTMGTVPN VGLMAQAAEE YGSHNKTFEI EADGQVQVID AAGKVLMQHD VEAGDIWRMC QTKDAPVKDW VQLAVNRARL SNTPAVFWLD ENRPHDKSLL AKVKAYLAEL DTNGLDIRVL APEEAAKFSL GRLKNGEDTI SVTGNVLRDY LTDLFPILEL GTSAKMLSIV PLMNGGGMFE TGAGGSAPKH VQQFLEENHL RWDSLGEFLA LAVSFEHLAQ KTGNAKAQVL ADTLDAATEK LLLNDKSPKR KAGELDNRGS HFYLTLYWAQ ELAAQDKDAE LKAAFTPLAA ALTADEAKIV AELSAVQGKA ADIGGYYAAN PEKAAQVMRP SVTFNQALNA L // ID Q9K0Z6_NEIMB Unreviewed; 498 AA. AC Q9K0Z6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Competence protein ComM {ECO:0000313|EMBL:AAF40844.1}; GN Name=comM {ECO:0000313|EMBL:AAF40844.1}; GN OrderedLocusNames=NMB0405 {ECO:0000313|EMBL:AAF40844.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40844.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40844.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40844.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40844.1; -; Genomic_DNA. DR PIR; B81203; B81203. DR RefSeq; NP_273454.1; NC_003112.2. DR RefSeq; WP_002224914.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z6; -. DR STRING; 122586.NMB0405; -. DR PaxDb; Q9K0Z6; -. DR EnsemblBacteria; AAF40844; AAF40844; NMB0405. DR GeneID; 902519; -. DR KEGG; nme:NMB0405; -. DR PATRIC; 20355993; VBINeiMen85645_0514. DR eggNOG; ENOG4105C0P; Bacteria. DR eggNOG; COG0606; LUCA. DR HOGENOM; HOG000246698; -. DR KO; K07391; -. DR OMA; CRCTPDQ; -. DR OrthoDB; EOG6ZWJFW; -. DR BioCyc; NMEN122586:GHGG-427-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR004482; Mg_chelat-rel. DR InterPro; IPR025158; Mg_chelat-rel_C. DR InterPro; IPR000523; Mg_chelatse_chII_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR32039:SF7; PTHR32039:SF7; 1. DR Pfam; PF01078; Mg_chelatase; 1. DR Pfam; PF13335; Mg_chelatase_C; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00368; TIGR00368; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 212 393 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 498 AA; 53617 MW; 5A1A94B375662251 CRC64; MSLALVYSRA LSGMNAPLVE VEAHLANGLP HFNIVGLPDM EVKESRDRVR AAIIQSGFEF PAKKITVNLA PADLPKESGR FDLPIAIGIL AASGQVAPEK LEEYEFAGEL ALSGLLRPVR GALAMAWQGM QAKRAFVLPE ENAGQAAVMR GITVYGARSL GEVAAHLNGI EPLAQTECQV PQMPFEHGGQ PDLCDVKGQH TARLALEIAA AGGHSLLMMG PPGTGKSMLS QRLPGILPPL TEDELVEVWA LRSLLPNHQQ QLDSNRPFRS PHHSASAAAM VGGGSDPRPG EISLAHHGVL FLDELPEFDR KVLEVLREPL ENGEIHISRA ARQAVYPAKF QLVAAMNPCP CGYLGHPVKP CRCTPESVAR YRSKISGPLL DRIDLTIEVP SLSAAELMQQ EAGESSASVL ERVIAARDKQ YARQGKVNAA LSVSELDTSA RIQKEAQEAL GGLLEKLSLS ARSFHRIMRV ARTLADLAGD EEVGRSHVMK AIGFRRAL // ID Q7DD67_NEIMB Unreviewed; 83 AA. AC Q7DD67; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42244.1}; GN OrderedLocusNames=NMB1914 {ECO:0000313|EMBL:AAF42244.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42244.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42244.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42244.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42244.1; -; Genomic_DNA. DR PIR; A81029; A81029. DR RefSeq; NP_274908.1; NC_003112.2. DR RefSeq; WP_002244315.1; NC_003112.2. DR STRING; 122586.NMB1914; -. DR PaxDb; Q7DD67; -. DR EnsemblBacteria; AAF42244; AAF42244; NMB1914. DR GeneID; 904249; -. DR KEGG; nme:NMB1914; -. DR PATRIC; 20359873; VBINeiMen85645_2441. DR HOGENOM; HOG000218753; -. DR OMA; DILCTYI; -. DR OrthoDB; EOG6GN75X; -. DR BioCyc; NMEN122586:GHGG-1971-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 83 AA; 9932 MW; C71D05FD77AA623D CRC64; MKTLEKRMKA LDKRIMKFGK SLEGRLDARL IESALDYIHY SERFLAFEIL CTYIEDFDVR LTEQESREIS FINKEFEIES TSD // ID Q9K0L2_NEIMB Unreviewed; 180 AA. AC Q9K0L2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative bacteriocin resistance protein {ECO:0000313|EMBL:AAF41010.1}; GN OrderedLocusNames=NMB0582 {ECO:0000313|EMBL:AAF41010.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41010.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41010.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41010.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41010.1; -; Genomic_DNA. DR PIR; H81181; H81181. DR RefSeq; NP_273626.1; NC_003112.2. DR RefSeq; WP_002222865.1; NC_003112.2. DR ProteinModelPortal; Q9K0L2; -. DR PaxDb; Q9K0L2; -. DR EnsemblBacteria; AAF41010; AAF41010; NMB0582. DR GeneID; 902697; -. DR KEGG; nme:NMB0582; -. DR PATRIC; 20356447; VBINeiMen85645_0743. DR eggNOG; ENOG4108VMT; Bacteria. DR eggNOG; COG3271; LUCA. DR HOGENOM; HOG000218674; -. DR KO; K06992; -. DR OMA; MNNFHGQ; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NMEN122586:GHGG-608-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF03412; Peptidase_C39; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 138 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 180 AA; 20526 MW; 909DAF569D6FE00B CRC64; MQSWKERRDF NIVKQDLDFS CGAASVVTLL NNFYGQKLTE EDVLKKLDKE QMPASFEDMR RIMPDLGFEA KGYALSFEQL AQLQIPVIVY LKYRKDDHFS VLRGIDGNTV LLADPSLGHV SMSRAQFLDA WQTREGNLAG KILAVVPKGR DAGGDKAFFT RSPKRQTEFA VGQVKWWRAY // ID Q9JZG7_NEIMB Unreviewed; 178 AA. AC Q9JZG7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41460.1}; GN OrderedLocusNames=NMB1064 {ECO:0000313|EMBL:AAF41460.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41460.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41460.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41460.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41460.1; -; Genomic_DNA. DR PIR; B81127; B81127. DR RefSeq; NP_274097.1; NC_003112.2. DR RefSeq; WP_002225264.1; NC_003112.2. DR ProteinModelPortal; Q9JZG7; -. DR STRING; 122586.NMB1064; -. DR PaxDb; Q9JZG7; -. DR EnsemblBacteria; AAF41460; AAF41460; NMB1064. DR GeneID; 903481; -. DR KEGG; nme:NMB1064; -. DR PATRIC; 20357671; VBINeiMen85645_1352. DR eggNOG; ENOG4108YZ4; Bacteria. DR eggNOG; COG0494; LUCA. DR HOGENOM; HOG000045854; -. DR KO; K01515; -. DR OMA; EEPIECA; -. DR OrthoDB; EOG6VMTQG; -. DR BioCyc; NMEN122586:GHGG-1101-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 39 170 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 178 AA; 19739 MW; 54DE79496DBC5047 CRC64; MDLREVKLGG ETIYEGGFVS ISRDKVRLPN GNEGQRIVIR HPGAACVLAV TDEGKVVLVR QWRYAANQAT LELPAGKLDV AGEDMAACAL RELAEETPYT ADSVRLLYSF YTAVGFCNEK MYLFEAEGVR LGSTLANDED EITETVLMSK EEVRQALAND EIKDGKTLIG LQYWLMKD // ID Q9JYH4_NEIMB Unreviewed; 288 AA. AC Q9JYH4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41939.1}; GN OrderedLocusNames=NMB1586 {ECO:0000313|EMBL:AAF41939.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41939.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41939.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41939.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41939.1; -; Genomic_DNA. DR PIR; D81065; D81065. DR RefSeq; NP_274592.1; NC_003112.2. DR RefSeq; WP_002225028.1; NC_003112.2. DR ProteinModelPortal; Q9JYH4; -. DR STRING; 122586.NMB1586; -. DR PaxDb; Q9JYH4; -. DR EnsemblBacteria; AAF41939; AAF41939; NMB1586. DR GeneID; 904238; -. DR KEGG; nme:NMB1586; -. DR PATRIC; 20359038; VBINeiMen85645_2037. DR eggNOG; ENOG4105EPE; Bacteria. DR eggNOG; ENOG410XRCD; LUCA. DR HOGENOM; HOG000219034; -. DR OMA; LERDNHF; -. DR OrthoDB; EOG6GTZFW; -. DR BioCyc; NMEN122586:GHGG-1628-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR InterPro; IPR011527; ABC1_TM_dom. DR Pfam; PF13748; ABC_membrane_3; 1. DR SUPFAM; SSF90123; SSF90123; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 241 ABC transmembrane type-1. FT {ECO:0000259|Pfam:PF13748}. SQ SEQUENCE 288 AA; 32796 MW; DCB8F4DC6AC414CC CRC64; MWKMLKHIAQ THRKRLIGTF SLVGLENLLM LVYPVFGGRA INAVIAGEVW QALLYALVVL LMWLVGAVRR IADTRTFTRI YTEIAVPVVL EQRQRQVPHS AVTARVALSR EFVSFFEEHL PIAATSVVSI FGACIMLLVL EFWVGVSAVG ILALFLWLLP RFAAISENLY FRLNNSLERD NHFIRKGDRR QLYRHYGLLA RLRVLISNRE AFGYLCVGTA MGILFGFAFV MMTLKGYSSA GHVYSVGTYL WMFAMSLDDV PRLVEQYSNL KDIGQRIEWS ERNIKAGT // ID Q9JZY5_NEIMB Unreviewed; 57 AA. AC Q9JZY5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41258.1}; GN OrderedLocusNames=NMB0847 {ECO:0000313|EMBL:AAF41258.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41258.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41258.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41258.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41258.1; -; Genomic_DNA. DR PIR; D81152; D81152. DR STRING; 122586.NMB0847; -. DR PaxDb; Q9JZY5; -. DR EnsemblBacteria; AAF41258; AAF41258; NMB0847. DR BioCyc; NMEN122586:GHGG-878-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 57 AA; 6531 MW; AE90F4F06D544693 CRC64; MPEPLHVLVI PSWYPQSEQD VDGIFFKIRH WHCRGKASKP PCLHRCSATC GKKQQAS // ID Q9JYL1_NEIMB Unreviewed; 169 AA. AC Q9JYL1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41887.1}; GN OrderedLocusNames=NMB1532 {ECO:0000313|EMBL:AAF41887.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41887.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41887.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41887.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2P0N} RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH MANGANESE. RA Osipiuk J., Li H., Bargassa M., Joachimiak A.; RT "X-ray crystal structure of NMB1532 protein of unknown function from RT Neisseria meningitidis."; RL Submitted (FEB-2007) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41887.1; -; Genomic_DNA. DR PIR; H81071; H81071. DR RefSeq; NP_274539.1; NC_003112.2. DR RefSeq; WP_002220565.1; NC_003112.2. DR PDB; 2P0N; X-ray; 1.41 A; A/B=1-169. DR PDBsum; 2P0N; -. DR ProteinModelPortal; Q9JYL1; -. DR SMR; Q9JYL1; 9-169. DR STRING; 122586.NMB1532; -. DR PaxDb; Q9JYL1; -. DR EnsemblBacteria; AAF41887; AAF41887; NMB1532. DR GeneID; 904056; -. DR KEGG; nme:NMB1532; -. DR PATRIC; 20358870; VBINeiMen85645_1944. DR eggNOG; ENOG4105NSG; Bacteria. DR eggNOG; ENOG4111WZE; LUCA. DR HOGENOM; HOG000219026; -. DR OMA; NQAVKND; -. DR OrthoDB; EOG6B09V1; -. DR BioCyc; NMEN122586:GHGG-1573-MONOMER; -. DR EvolutionaryTrace; Q9JYL1; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF01814; Hemerythrin; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2P0N}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Manganese {ECO:0000213|PDB:2P0N}; KW Metal-binding {ECO:0000213|PDB:2P0N}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 14 141 Hemerythrin. {ECO:0000259|Pfam:PF01814}. FT METAL 22 22 Manganese 1; via tele nitrogen. FT {ECO:0000213|PDB:2P0N}. FT METAL 66 66 Manganese 1; via tele nitrogen. FT {ECO:0000213|PDB:2P0N}. FT METAL 70 70 Manganese 1. {ECO:0000213|PDB:2P0N}. FT METAL 70 70 Manganese 2. {ECO:0000213|PDB:2P0N}. FT METAL 96 96 Manganese 2; via tele nitrogen. FT {ECO:0000213|PDB:2P0N}. FT METAL 136 136 Manganese 2; via tele nitrogen. FT {ECO:0000213|PDB:2P0N}. FT METAL 140 140 Manganese 1. {ECO:0000213|PDB:2P0N}. FT METAL 140 140 Manganese 2. {ECO:0000213|PDB:2P0N}. SQ SEQUENCE 169 AA; 19336 MW; 3122FB04FD53FAB9 CRC64; MNPFETKSVT FAEPIEMLYA CHGKVRRFCG QVAMLSDYIA ENGCNQIVLQ TIRQIAQYFN VAAPLHHEDE EENFFPLLLQ YAPQAQESVD ELLRQHIGLH DNWAAVSAEF AKLEADNAYV PDEEAFKRFV AGYDVHLAIE EPLFDMGNTF IPKEKLTEIG EIMAARRRK // ID Q9JYV9_NEIMB Unreviewed; 179 AA. AC Q9JYV9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41772.1}; GN OrderedLocusNames=NMB1410 {ECO:0000313|EMBL:AAF41772.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41772.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41772.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41772.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41772.1; -; Genomic_DNA. DR PIR; F81087; F81087. DR RefSeq; NP_274423.1; NC_003112.2. DR RefSeq; WP_002218396.1; NC_003112.2. DR PaxDb; Q9JYV9; -. DR EnsemblBacteria; AAF41772; AAF41772; NMB1410. DR GeneID; 903832; -. DR KEGG; nme:NMB1410; -. DR BioCyc; NMEN122586:GHGG-1448-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 179 AA; 20624 MW; CF91AD39E584A0F5 CRC64; MDFLEIFIMS AFRKILLIIS CLLIASCSFV ETIFYMAISP EPVVVDFPLG KKTKRSIELK QKIGKPYAIS LGTNFIHYDP KQGERWIDDK LNYPYNISVK IFKVEEDGKK LIIDELLTER SRKLGGGVFG AGGKYSMHIY DFYLPEGEYL FEISDNSEYI PLYDEINNSI RIVVNARIQ // ID Q9K0A0_NEIMB Unreviewed; 106 AA. AC Q9K0A0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62319.1}; GN OrderedLocusNames=NMB0715 {ECO:0000313|EMBL:AAF62319.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62319.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62319.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62319.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62319.1; -; Genomic_DNA. DR RefSeq; NP_273757.1; NC_003112.2. DR RefSeq; WP_002222763.1; NC_003112.2. DR STRING; 122586.NMB0715; -. DR PaxDb; Q9K0A0; -. DR EnsemblBacteria; AAF62319; AAF62319; NMB0715. DR GeneID; 902827; -. DR KEGG; nme:NMB0715; -. DR PATRIC; 20356779; VBINeiMen85645_0911. DR HOGENOM; HOG000220709; -. DR OrthoDB; EOG6KDKW4; -. DR BioCyc; NMEN122586:GHGG-743-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 68 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 106 AA; 11435 MW; 043E3A3AA5A52F31 CRC64; MDWMGSLFLP GGALLFLSVV STTLSARLGM PLLLVSPANV LDRAAEALAI AAFLMLVARP SAVFGGLWKF NYSLREKAYS RIEMQSDTVL QAGIWRGTSC PTARSI // ID Q9JZJ5_NEIMB Unreviewed; 288 AA. AC Q9JZJ5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41424.1}; GN OrderedLocusNames=NMB1024 {ECO:0000313|EMBL:AAF41424.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41424.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41424.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41424.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the GcvT family. CC {ECO:0000256|RuleBase:RU003980}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41424.1; -; Genomic_DNA. DR PIR; G81129; G81129. DR RefSeq; NP_274058.1; NC_003112.2. DR RefSeq; WP_002225281.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ5; -. DR STRING; 122586.NMB1024; -. DR PaxDb; Q9JZJ5; -. DR EnsemblBacteria; AAF41424; AAF41424; NMB1024. DR GeneID; 903162; -. DR KEGG; nme:NMB1024; -. DR PATRIC; 20357583; VBINeiMen85645_1308. DR eggNOG; ENOG4106XY2; Bacteria. DR eggNOG; COG0354; LUCA. DR HOGENOM; HOG000261299; -. DR KO; K06980; -. DR OMA; WRKTGTI; -. DR OrthoDB; EOG6QP0ZT; -. DR BioCyc; NMEN122586:GHGG-1061-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR017703; YgfZ/GcvT_CS. DR Pfam; PF01571; GCV_T; 1. DR TIGRFAMs; TIGR03317; ygfZ_signature; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 70 GCV_T. {ECO:0000259|Pfam:PF01571}. SQ SEQUENCE 288 AA; 31151 MW; 42E07169A101491E CRC64; MMKTLLPFFG VVRVSGEDRQ TFLHGQLSND INHLQTGQAC YATYNTPKGR VIANMIVVNR GGDLLLIMAQ DLLEATVKRL RMFVLRAKAV FEILEDYAVG AELEASAEPL AAQEPSLAFT AECGSDGICS VVLPHRGILH IAPKNALPPY DAAAENAWRL HEIRSGYPWI CAATKETAVA QMLNQHIIGG VHFKKGCYPG QEIIARAQYR GQVKRGLAVL SGNSAVEAGT LLTADGEEAG IVLDSVQDSE NFTALTVIKF SAAQKTLTVP NGGIFKAVHL FFKTENAE // ID Q9K036_NEIMB Unreviewed; 302 AA. AC Q9K036; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41199.1}; GN OrderedLocusNames=NMB0786 {ECO:0000313|EMBL:AAF41199.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41199.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41199.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41199.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41199.1; -; Genomic_DNA. DR PIR; G81158; G81158. DR RefSeq; NP_273828.1; NC_003112.2. DR RefSeq; WP_002217584.1; NC_003112.2. DR ProteinModelPortal; Q9K036; -. DR STRING; 122586.NMB0786; -. DR PaxDb; Q9K036; -. DR EnsemblBacteria; AAF41199; AAF41199; NMB0786. DR GeneID; 902901; -. DR KEGG; nme:NMB0786; -. DR PATRIC; 20356957; VBINeiMen85645_0997. DR eggNOG; ENOG4105EZR; Bacteria. DR eggNOG; COG2837; LUCA. DR HOGENOM; HOG000151980; -. DR KO; K07223; -. DR OMA; CAEPNLH; -. DR OrthoDB; EOG6N682X; -. DR BioCyc; NMEN122586:GHGG-817-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR006314; Dyp_peroxidase. DR Pfam; PF04261; Dyp_perox; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1. DR PROSITE; PS51404; DYP_PEROXIDASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 302 AA; 32787 MW; 401DCEA563106E85 CRC64; MNTPQSAIIP DHAQAGIFIE ADFAANRLND IKAACRASLD ALTALKARFP DDILGLTIAF GSKAWATFGH TDEGSEIKPF SEMGNGLAPS TQHDMSIHIQ SFRQNAAYAL AQSVLGAFGD SICVASEEHG LRLYQDRGLD GFVDGTENPQ GDENVREVAI IPEGKPDAGG SYVLLQKYLH DLKKWDAVPV AEQEASVGRG KETDDEFGRD VRLPDSHLGR VNLKENGVGL KIVRRSLPFG KISGEHGLMF TAYCRTLHNI EAQLLSMFGD TDGKTDLLLR HLSAAVSGGY YYAPSVERLQ NL // ID Q7DD62_NEIMB Unreviewed; 127 AA. AC Q7DD62; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42288.1}; GN OrderedLocusNames=NMB1959 {ECO:0000313|EMBL:AAF42288.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42288.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42288.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42288.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42288.1; -; Genomic_DNA. DR PIR; H81021; H81021. DR RefSeq; NP_274953.1; NC_003112.2. DR RefSeq; WP_002214837.1; NC_003112.2. DR ProteinModelPortal; Q7DD62; -. DR STRING; 122586.NMB1959; -. DR PaxDb; Q7DD62; -. DR EnsemblBacteria; AAF42288; AAF42288; NMB1959. DR GeneID; 904191; -. DR KEGG; nme:NMB1959; -. DR PATRIC; 20359979; VBINeiMen85645_2494. DR eggNOG; ENOG410835Z; Bacteria. DR eggNOG; COG0824; LUCA. DR HOGENOM; HOG000004132; -. DR KO; K12500; -. DR OMA; ANININY; -. DR OrthoDB; EOG6JQH7N; -. DR BioCyc; NMEN122586:GHGG-2016-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR029069; HotDog_dom. DR SUPFAM; SSF54637; SSF54637; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 127 AA; 14278 MW; 709C29A81B9E0A48 CRC64; MKLTVRNYHL DGYGHVNNAR YLEFFEEARW AFFEERGLLH ELAGLILIVA RIDIRYSRPA VEGDVLQFSC RLKTPGTRRI VLTQTITLPN GKTAAEADIT LMPVHAATQR TVSLPATLAR ALEALSE // ID Q9JZR9_NEIMB Unreviewed; 152 AA. AC Q9JZR9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Cytochrome c {ECO:0000313|EMBL:AAF41331.1}; GN OrderedLocusNames=NMB0923 {ECO:0000313|EMBL:AAF41331.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41331.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41331.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41331.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41331.1; -; Genomic_DNA. DR PIR; E81143; E81143. DR RefSeq; NP_273963.1; NC_003112.2. DR RefSeq; WP_002222632.1; NC_003112.2. DR ProteinModelPortal; Q9JZR9; -. DR STRING; 122586.NMB0923; -. DR PaxDb; Q9JZR9; -. DR EnsemblBacteria; AAF41331; AAF41331; NMB0923. DR GeneID; 903044; -. DR KEGG; nme:NMB0923; -. DR PATRIC; 20357295; VBINeiMen85645_1161. DR eggNOG; ENOG4105T86; Bacteria. DR eggNOG; COG3909; LUCA. DR HOGENOM; HOG000288835; -. DR OMA; SCEACHK; -. DR OrthoDB; EOG64N9ZS; -. DR BioCyc; NMEN122586:GHGG-961-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR Gene3D; 1.20.120.10; -; 1. DR InterPro; IPR010980; Cyt_c/b562. DR InterPro; IPR002321; Cyt_c_II. DR InterPro; IPR012127; Cyt_c_prime. DR InterPro; IPR015984; Cyt_c_prime_subgr. DR Pfam; PF01322; Cytochrom_C_2; 1. DR PIRSF; PIRSF000027; Cytc_c_prime; 1. DR PRINTS; PR00608; CYTCHROMECII. DR SUPFAM; SSF47175; SSF47175; 1. DR PROSITE; PS51009; CYTCII; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Heme {ECO:0000256|PIRSR:PIRSR000027-2}; KW Iron {ECO:0000256|PIRSR:PIRSR000027-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000027-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 152 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327863. FT METAL 145 145 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR000027-1}. FT BINDING 141 141 Heme (covalent). FT {ECO:0000256|PIRSR:PIRSR000027-2}. FT BINDING 144 144 Heme (covalent). FT {ECO:0000256|PIRSR:PIRSR000027-2}. SQ SEQUENCE 152 AA; 16191 MW; 4121D35F3B5C53F8 CRC64; MKTQISLAAA AITLLLSACG GSGIPSQPKG EISENRTAAF KSMMPEFTRM GKMVKDEEPY DVEKFKQAAA SFAESSKKPF TLFESDPQGN GRALPAVWSD GAKFEAEKTK FAAAVEKLNA AAQTGKLDEI KAAYGETGAS CKSCHDSFRA PE // ID Q9K1L4_NEIMB Unreviewed; 47 AA. AC Q9K1L4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40559.1}; GN OrderedLocusNames=NMB0099 {ECO:0000313|EMBL:AAF40559.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40559.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40559.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40559.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40559.1; -; Genomic_DNA. DR PIR; C81237; C81237. DR PaxDb; Q9K1L4; -. DR EnsemblBacteria; AAF40559; AAF40559; NMB0099. DR PATRIC; 20355205; VBINeiMen85645_0136. DR OrthoDB; EOG6MWNNN; -. DR BioCyc; NMEN122586:GHGG-105-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5858 MW; F145BA1E0CD44786 CRC64; MEWAENETVK LAQKWEQEQK KQQIQQKKET EKSPKHKASR DDWEMER // ID Q9JZD9_NEIMB Unreviewed; 321 AA. AC Q9JZD9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41490.1}; GN OrderedLocusNames=NMB1099 {ECO:0000313|EMBL:AAF41490.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41490.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41490.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41490.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41490.1; -; Genomic_DNA. DR PIR; H81120; H81120. DR RefSeq; NP_274130.1; NC_003112.2. DR RefSeq; WP_002225241.1; NC_003112.2. DR ProteinModelPortal; Q9JZD9; -. DR STRING; 122586.NMB1099; -. DR PaxDb; Q9JZD9; -. DR EnsemblBacteria; AAF41490; AAF41490; NMB1099. DR GeneID; 903521; -. DR KEGG; nme:NMB1099; -. DR PATRIC; 20357762; VBINeiMen85645_1397. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; EFAGHET; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-1135-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 37976 MW; 892C52A7AF127FBA CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLV P // ID Q9K0G1_NEIMB Unreviewed; 154 AA. AC Q9K0G1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41066.1}; GN OrderedLocusNames=NMB0644 {ECO:0000313|EMBL:AAF41066.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41066.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41066.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41066.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41066.1; -; Genomic_DNA. DR PIR; H81175; H81175. DR RefSeq; NP_273687.1; NC_003112.2. DR RefSeq; WP_002217740.1; NC_003112.2. DR STRING; 122586.NMB0644; -. DR PaxDb; Q9K0G1; -. DR EnsemblBacteria; AAF41066; AAF41066; NMB0644. DR GeneID; 902756; -. DR KEGG; nme:NMB0644; -. DR HOGENOM; HOG000220701; -. DR OrthoDB; EOG6WX4PS; -. DR BioCyc; NMEN122586:GHGG-671-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 154 AA; 18305 MW; 150DBD22279E1294 CRC64; MAIWNYRYYL IPSAAIRNKF NANKDIILDE YRSNGFQNFN ENKSFENYFI DNDVILLSII NEAKKQLKLK ESWDKDAIMF CDNFGNSLTV WPDDIECELD LRFDYTKFIQ KTIDWAIKYN CLLVIEKTGN VVSPNINNLM YEIKAYLESK PWPI // ID Q9JZ45_NEIMB Unreviewed; 658 AA. AC Q9JZ45; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:AAF41673.1}; GN OrderedLocusNames=NMB1297 {ECO:0000313|EMBL:AAF41673.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41673.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41673.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41673.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41673.1; -; Genomic_DNA. DR PIR; D81099; D81099. DR RefSeq; NP_274317.1; NC_003112.2. DR RefSeq; WP_002225171.1; NC_003112.2. DR ProteinModelPortal; Q9JZ45; -. DR STRING; 122586.NMB1297; -. DR PaxDb; Q9JZ45; -. DR EnsemblBacteria; AAF41673; AAF41673; NMB1297. DR GeneID; 903719; -. DR KEGG; nme:NMB1297; -. DR PATRIC; 20358223; VBINeiMen85645_1623. DR eggNOG; ENOG4105E9H; Bacteria. DR eggNOG; COG0741; LUCA. DR HOGENOM; HOG000258639; -. DR KO; K08307; -. DR OMA; IVPQNDM; -. DR OrthoDB; EOG6038ZC; -. DR BioCyc; NMEN122586:GHGG-1335-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.10.350.10; -; 3. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01476; LysM; 3. DR Pfam; PF01464; SLT; 1. DR SMART; SM00257; LysM; 3. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF54106; SSF54106; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 658 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332266. FT DOMAIN 329 372 LysM. {ECO:0000259|SMART:SM00257}. FT DOMAIN 558 601 LysM. {ECO:0000259|SMART:SM00257}. FT DOMAIN 614 656 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 658 AA; 72053 MW; 9F0E5D14F17A8FA8 CRC64; MSKLKTIALT ASGLSVCPGF LYAQNTSSHQ IGLAIMRLNS SILDLPPTKQ YFQSGSLWGE LRQGFRMGEV NPELVRRHES KFIASHSYFN RVINRSRPYM YHIANEVKKR NMPAEAALLP FIESAFVTKA KSHVGASGLW QFMPATGRHY GLEKTPVYDG RHDVYAATDA ALNYLQYLYG LFGDWPLAFA AYNWGEGNVG RAINRARAQG LEPTYENLRM PNETRNYVPK LLAVRNIIAT PQSFGMNISD IDNKPYFQAV EPDRPLDNEA IARLAGITQS ELLALNPAFN VPAFIPKSKR KLLLPVASVQ TFQSNYLNAA PDSLFSWEVY TPAAKTSLSD ISTATGMSIA DIKRLNNLNG NLVNAGRSIL VAKNGKTLQT ASESVVSIDI DNTPDTYRSN MPAGTVNVGI ARIRPAAAQT ADITVAPLPQ KTVRTEPDPL VRIAEPALAT AAAQPQTEKQ TAMPSETQTA TLAQIIPQND MQAADELMQL VARNNLRRQA EETISAVIGT PDTVAEHKIS ASPQHTAAAD GKRRVRLETR VAKAADGEAE ISPLHASIHR VVEGDTLFNI AKRYNVSVAD LIVANNIKGN TIQKGQVLRL AQAAPAQTRI EKVSYTARKG DTFKSIAARF NIHIDDIRRL NPNLNTINPG QRVKLIGS // ID Q9JZU6_NEIMB Unreviewed; 395 AA. AC Q9JZU6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Aminotransferase, class I {ECO:0000313|EMBL:AAF41303.1}; GN OrderedLocusNames=NMB0894 {ECO:0000313|EMBL:AAF41303.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41303.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41303.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41303.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41303.1; -; Genomic_DNA. DR PIR; D81146; D81146. DR RefSeq; NP_273935.1; NC_003112.2. DR RefSeq; WP_002225352.1; NC_003112.2. DR ProteinModelPortal; Q9JZU6; -. DR STRING; 122586.NMB0894; -. DR PaxDb; Q9JZU6; -. DR EnsemblBacteria; AAF41303; AAF41303; NMB0894. DR GeneID; 903013; -. DR KEGG; nme:NMB0894; -. DR PATRIC; 20357209; VBINeiMen85645_1120. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR HOGENOM; HOG000223059; -. DR KO; K14267; -. DR OMA; DECYLEL; -. DR OrthoDB; EOG6CP3SM; -. DR BioCyc; NMEN122586:GHGG-930-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR019878; DapC_beta/gammaproteobac. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03538; DapC_gpp; 1. PE 4: Predicted; KW Aminotransferase {ECO:0000313|EMBL:AAF41303.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41303.1}. FT DOMAIN 33 385 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 395 AA; 44012 MW; 7240556D6E4C034F CRC64; MNTLLNQLKP YPFARLREAM QGISAPEGLE AVPLHIGEPK HPTPKVITDA LTASLHELEK YPLTAGLPEL RQACANWLKR RYDGLTVDAD NEILPVLGSR EALFSFVQTV LNPVSDGIKP AIVSPNPFYQ IYEGATLLGG GEIHFANCPA PSFNPDWRSI SEEVWKRTKL VFVCSPNNPS GSVLDLDGWK EVFDLQDKYG FIIASDECYS EIYFDGNKPL GCLQAAAQLG RSRQKLLMFT SLSKRSNVPG LRSGFVAGDA ELLKNFLLYR TYHGSAMSIP VQRASIAAWD DEQHVIDNRR MYQEKFERVI PILQQVFDVK LPDASFYIWL KVPDGDDLAL ARNLWQKAAI QVLPGRFLAR DTEQGNPGEG YVRIALVADV ATCVKAAETI VSLYR // ID Q9JYX7_NEIMB Unreviewed; 73 AA. AC Q9JYX7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62331.1}; GN OrderedLocusNames=NMB1382 {ECO:0000313|EMBL:AAF62331.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62331.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62331.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62331.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62331.1; -; Genomic_DNA. DR RefSeq; NP_274398.1; NC_003112.2. DR RefSeq; WP_002213166.1; NC_003112.2. DR STRING; 122586.NMB1382; -. DR PaxDb; Q9JYX7; -. DR EnsemblBacteria; AAF62331; AAF62331; NMB1382. DR GeneID; 903804; -. DR KEGG; nme:NMB1382; -. DR PATRIC; 20358443; VBINeiMen85645_1733. DR eggNOG; COG3036; LUCA. DR HOGENOM; HOG000000578; -. DR KO; K09890; -. DR OMA; MANIRVN; -. DR OrthoDB; EOG6V1M8M; -. DR BioCyc; NMEN122586:GHGG-1420-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005589; DUF331. DR Pfam; PF03889; DUF331; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 73 AA; 8570 MW; 4DF78FDC504082F2 CRC64; MGGKVQHNKG KIRDNALKAL VKSDLFRHKV ERKRKGKGSY NRQEAKKWRD GFDTVPPFLC LKRGSFRRSR RSL // ID Q9JXK8_NEIMB Unreviewed; 252 AA. AC Q9JXK8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 102. DE SubName: Full=Iron(III) ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF42320.1}; GN OrderedLocusNames=NMB1993 {ECO:0000313|EMBL:AAF42320.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42320.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42320.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42320.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42320.1; -; Genomic_DNA. DR PIR; H81018; H81018. DR RefSeq; NP_274985.1; NC_003112.2. DR RefSeq; WP_002226767.1; NC_003112.2. DR ProteinModelPortal; Q9JXK8; -. DR STRING; 122586.NMB1993; -. DR PaxDb; Q9JXK8; -. DR EnsemblBacteria; AAF42320; AAF42320; NMB1993. DR GeneID; 904135; -. DR KEGG; nme:NMB1993; -. DR PATRIC; 20360083; VBINeiMen85645_2546. DR eggNOG; ENOG4108IPW; Bacteria. DR eggNOG; COG4604; LUCA. DR KO; K02013; -. DR OMA; EQDHQVV; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NMEN122586:GHGG-2050-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42320.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42320.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 252 AA; 28263 MW; EC2205B14F3321B8 CRC64; MITIRNVSYR IGTRPILDNV SLDIPEGGIT ALVGPNGAGK STLFSFMARL RPLESGSIAY RGKNLADTPT AELAKTLSIL TQENSIMSRI TVRDLLMFGR YPYHQGRPTA ECRRIVNGAI EEFHLQDLSD RYLTELSGGQ RQRAMIAMVF CQSTDYVLLD EPLNNLDMYH ARSLMQILRR LTDEHKRTTV VVLHDINQAA AYADHVVAMK NGQVAMQGKP NDIFTAANIK TLFDMDVDVL DYEGKKLVIH HI // ID Q9JXQ9_NEIMB Unreviewed; 231 AA. AC Q9JXQ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Inositol monophosphatase family protein {ECO:0000313|EMBL:AAF42253.1}; GN OrderedLocusNames=NMB1924 {ECO:0000313|EMBL:AAF42253.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42253.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42253.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42253.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42253.1; -; Genomic_DNA. DR PIR; G81026; G81026. DR RefSeq; NP_274918.1; NC_003112.2. DR RefSeq; WP_010981008.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ9; -. DR STRING; 122586.NMB1924; -. DR PaxDb; Q9JXQ9; -. DR EnsemblBacteria; AAF42253; AAF42253; NMB1924. DR GeneID; 904231; -. DR KEGG; nme:NMB1924; -. DR PATRIC; 20359895; VBINeiMen85645_2452. DR eggNOG; ENOG4105ECY; Bacteria. DR eggNOG; COG0483; LUCA. DR HOGENOM; HOG000282238; -. DR KO; K01092; -. DR OMA; YLHGGQK; -. DR OrthoDB; EOG6QK4W4; -. DR BioCyc; NMEN122586:GHGG-1981-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PROSITE; PS00629; IMP_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 231 AA; 25492 MW; 693539D5BE887D13 CRC64; MLSEADIAAQ TAFAAALPLL IDSPMLGEEM SRQEQSALWE QYSGEKGLWI VDPIDGTNNF VNGLPHFAVS VAFVRNGRAE LGVIYNPVSG ECFYAERGQG AFLNGTRLPL RLVDKKLNEA IAGVEIKYLR SGKLSSRMST LAPFGTIRSM GSSTLDWCYL ACGRYDVYVH GGQKLWDYAA GALIFEEAGG RLTTLEGDGF WSGEHVFKRS VVAALEPKLF ERWVGWIREN Q // ID Q7DDM2_NEIMB Unreviewed; 174 AA. AC Q7DDM2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Outer membrane protein NspA {ECO:0000313|EMBL:AAF41081.1}; GN Name=nspA {ECO:0000313|EMBL:AAF41081.1}; GN OrderedLocusNames=NMB0663 {ECO:0000313|EMBL:AAF41081.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41081.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41081.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41081.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41081.1; -; Genomic_DNA. DR RefSeq; NP_273705.1; NC_003112.2. DR RefSeq; WP_002225511.1; NC_003112.2. DR ProteinModelPortal; Q7DDM2; -. DR SMR; Q7DDM2; 20-174. DR STRING; 122586.NMB0663; -. DR PaxDb; Q7DDM2; -. DR EnsemblBacteria; AAF41081; AAF41081; NMB0663. DR GeneID; 902774; -. DR KEGG; nme:NMB0663; -. DR PATRIC; 20356625; VBINeiMen85645_0831. DR eggNOG; COG3637; LUCA. DR HOGENOM; HOG000218831; -. DR OMA; LNRASAH; -. DR OrthoDB; EOG6H1Q21; -. DR BioCyc; NMEN122586:GHGG-690-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0015288; F:porin activity; IEA:InterPro. DR Gene3D; 2.40.160.20; -; 1. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 174 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287195. FT DOMAIN 52 174 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 174 AA; 18397 MW; E8B02767DDC6E109 CRC64; MKKALATLIA LALPAAALAE GASGFYVQAD AAHAKASSSL GSAKGFSPRI SAGYRINDLR FAVDYTRYKN YKAPSTDFKL YSIGASAIYD FDTQSPVKPY LGARLSLNRA SVDLGGSDSF SQTSIGLGVL TGVSYAVTPN VDLDAGYRYN YIGKVNTVKN VRSGELSAGV RVKF // ID Q9JXV4_NEIMB Unreviewed; 320 AA. AC Q9JXV4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42204.1}; GN OrderedLocusNames=NMB1870 {ECO:0000313|EMBL:AAF42204.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42204.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42204.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42204.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2W80, ECO:0000213|PDB:2W81} RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 71-320. RX PubMed=19225461; DOI=10.1038/nature07769; RA Schneider M.C., Prosser B.E., Caesar J.J., Kugelberg E., Li S., RA Zhang Q., Quoraishi S., Lovett J.E., Deane J.E., Sim R.B., Roversi P., RA Johnson S., Tang C.M., Lea S.M.; RT "Neisseria meningitidis recruits factor H using protein mimicry of RT host carbohydrates."; RL Nature 458:890-893(2009). RN [3] {ECO:0000213|PDB:2Y7S} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 73-320. RX PubMed=21753121; DOI=10.1126/SCITRANSLMED.3002234; RA Scarselli M., Arico B., Brunelli B., Savino S., Di Marcello F., RA Palumbo E., Veggi D., Ciucchi L., Cartocci E., Bottomley M.J., RA Malito E., Lo Surdo P., Comanducci M., Giuliani M.M., Cantini F., RA Dragonetti S., Colaprico A., Doro F., Giannetti P., Pallaoro M., RA Brogioni B., Tontini M., Hilleringmann M., Nardi-Dei V., Banci L., RA Pizza M., Rappuoli R.; RT "Rational design of a meningococcal antigen inducing broad protective RT immunity."; RL Sci. Transl. Med. 3:91ra62-91ra62(2011). RN [4] {ECO:0000213|PDB:4AYD, ECO:0000213|PDB:4AYE} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 73-320. RX PubMed=23133374; DOI=10.1371/journal.ppat.1002981; RA Johnson S., Tan L., van der Veen S., Caesar J., RA Goicoechea De Jorge E., Harding R.J., Bai X., Exley R.M., Ward P.N., RA Ruivo N., Trivedi K., Cumber E., Jones R., Newham L., Staunton D., RA Ufret-Vincenty R., Borrow R., Pickering M.C., Lea S.M., Tang C.M.; RT "Design and evaluation of meningococcal vaccines through structure- RT based modification of host and pathogen molecules."; RL PLoS Pathog. 8:e1002981-e1002981(2012). RN [5] {ECO:0000213|PDB:2YPV} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 69-320. RX PubMed=23396847; DOI=10.1073/pnas.1222845110; RA Malito E., Faleri A., Lo Surdo P., Veggi D., Maruggi G., Grassi E., RA Cartocci E., Bertoldi I., Genovese A., Santini L., Romagnoli G., RA Borgogni E., Brier S., Lo Passo C., Domina M., Castellino F., RA Felici F., van der Veen S., Johnson S., Lea S.M., Tang C.M., Pizza M., RA Savino S., Norais N., Rappuoli R., Bottomley M.J., Masignani V.; RT "Defining a protective epitope on factor H binding protein, a key RT meningococcal virulence factor and vaccine antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 110:3304-3309(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42204.1; -; Genomic_DNA. DR PIR; D81032; D81032. DR RefSeq; NP_274866.1; NC_003112.2. DR RefSeq; WP_010981001.1; NC_003112.2. DR PDB; 2W80; X-ray; 2.35 A; C/D/F/H=71-320. DR PDB; 2W81; X-ray; 2.35 A; C/D/F=71-320. DR PDB; 2Y7S; X-ray; 1.90 A; A/B=73-320. DR PDB; 2YPV; X-ray; 1.80 A; A=69-320. DR PDB; 4AYD; X-ray; 2.40 A; C/D/F=73-320. DR PDB; 4AYE; X-ray; 2.80 A; C/D/F=73-320. DR PDBsum; 2W80; -. DR PDBsum; 2W81; -. DR PDBsum; 2Y7S; -. DR PDBsum; 2YPV; -. DR PDBsum; 4AYD; -. DR PDBsum; 4AYE; -. DR ProteinModelPortal; Q9JXV4; -. DR SMR; Q9JXV4; 166-320. DR DIP; DIP-59745N; -. DR STRING; 122586.NMB1870; -. DR PaxDb; Q9JXV4; -. DR EnsemblBacteria; AAF42204; AAF42204; NMB1870. DR GeneID; 904318; -. DR KEGG; nme:NMB1870; -. DR PATRIC; 20359769; VBINeiMen85645_2390. DR HOGENOM; HOG000218761; -. DR OMA; PLDHKDK; -. DR OrthoDB; EOG69GZJZ; -. DR BioCyc; NMEN122586:GHGG-1926-MONOMER; -. DR EvolutionaryTrace; Q9JXV4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR014902; Lipoprot_GNA1870-rel_C. DR InterPro; IPR011250; OMP/PagP_b-brl. DR Pfam; PF08794; Lipoprot_C; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2W80, ECO:0000213|PDB:2W81, KW ECO:0000213|PDB:2Y7S, ECO:0000213|PDB:2YPV}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 166 320 Lipoprot_C. {ECO:0000259|Pfam:PF08794}. SQ SEQUENCE 320 AA; 34286 MW; 8CA166BCAC1B005C CRC64; MPSEPPFGRH LIFASLTCLI DAVCKKRYHN QNVYILSILR MTRSKPVNRT AFCCLSLTTA LILTACSSGG GGVAADIGAG LADALTAPLD HKDKGLQSLT LDQSVRKNEK LKLAAQGAEK TYGNGDSLNT GKLKNDKVSR FDFIRQIEVD GQLITLESGE FQVYKQSHSA LTAFQTEQIQ DSEHSGKMVA KRQFRIGDIA GEHTSFDKLP EGGRATYRGT AFGSDDAGGK LTYTIDFAAK QGNGKIEHLK SPELNVDLAA ADIKPDGKRH AVISGSVLYN QAEKGSYSLG IFGGKAQEVA GSAEVKTVNG IRHIGLAAKQ // ID Q9JZY7_NEIMB Unreviewed; 317 AA. AC Q9JZY7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=PhoH-related protein {ECO:0000313|EMBL:AAF41256.1}; GN OrderedLocusNames=NMB0845 {ECO:0000313|EMBL:AAF41256.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41256.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41256.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41256.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41256.1; -; Genomic_DNA. DR PIR; B81152; B81152. DR RefSeq; NP_273886.1; NC_003112.2. DR RefSeq; WP_002219479.1; NC_003112.2. DR ProteinModelPortal; Q9JZY7; -. DR SMR; Q9JZY7; 109-312. DR STRING; 122586.NMB0845; -. DR PaxDb; Q9JZY7; -. DR DNASU; 902959; -. DR EnsemblBacteria; AAF41256; AAF41256; NMB0845. DR GeneID; 902959; -. DR KEGG; nme:NMB0845; -. DR PATRIC; 20357079; VBINeiMen85645_1058. DR eggNOG; ENOG4105C9A; Bacteria. DR eggNOG; COG1702; LUCA. DR HOGENOM; HOG000015043; -. DR KO; K06217; -. DR OMA; FDITFGI; -. DR OrthoDB; EOG6F81S0; -. DR BioCyc; NMEN122586:GHGG-876-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003714; PhoH. DR Pfam; PF02562; PhoH; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 109 312 PhoH. {ECO:0000259|Pfam:PF02562}. SQ SEQUENCE 317 AA; 35424 MW; 4E6916CE8770C1CC CRC64; MTHTVHLHLE ETDNLALQRL CGSFDNNLDL LAKALDIHIS RRFEHFTFNG AFAHAGKRAL LKLLETAQTR DLNDGDIRLA AVEAQTEDAG HQEKNHDHAY YFRTKRGSIG GRTPRQNGYI RALLNHDIVF GLGPAGTGKT YLAVAAAVDA MEKHQVERII LVRPAVEAGE KLGFLPGDLT QKVDPYLRPL YDALYDLMGF DRVTKLIEKG LIEIAPLAYM RGRTLNGAYI ILDEAQNTTP EQMKMFLTRI GFGAKAVITG DTSQIDLPKN IKSGLKDARE KLHNVEGLYF HTFTGEDVVR HPLVQKIVEA YESAEHD // ID Q9JYS2_NEIMB Unreviewed; 39 AA. AC Q9JYS2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41814.1}; GN OrderedLocusNames=NMB1455 {ECO:0000313|EMBL:AAF41814.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41814.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41814.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41814.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41814.1; -; Genomic_DNA. DR PIR; H81081; H81081. DR RefSeq; NP_274466.1; NC_003112.2. DR RefSeq; WP_002212983.1; NC_003112.2. DR STRING; 122586.NMB1455; -. DR PaxDb; Q9JYS2; -. DR EnsemblBacteria; AAF41814; AAF41814; NMB1455. DR GeneID; 903877; -. DR KEGG; nme:NMB1455; -. DR PATRIC; 20358653; VBINeiMen85645_1836. DR BioCyc; NMEN122586:GHGG-1495-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 39 AA; 4810 MW; 0F97AA4F378AA72C CRC64; MYPPHTSGRR IKLYNSGNIF WEKRIFSKLE TQRLKKQEK // ID Q9K049_NEIMB Unreviewed; 71 AA. AC Q9K049; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41185.1}; GN OrderedLocusNames=NMB0772 {ECO:0000313|EMBL:AAF41185.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41185.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41185.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41185.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41185.1; -; Genomic_DNA. DR PIR; A81160; A81160. DR RefSeq; NP_273814.1; NC_003112.2. DR RefSeq; WP_002225429.1; NC_003112.2. DR STRING; 122586.NMB0772; -. DR PaxDb; Q9K049; -. DR EnsemblBacteria; AAF41185; AAF41185; NMB0772. DR GeneID; 902887; -. DR KEGG; nme:NMB0772; -. DR PATRIC; 20356917; VBINeiMen85645_0977. DR eggNOG; COG3042; LUCA. DR HOGENOM; HOG000137695; -. DR KO; K09712; -. DR OMA; MFLSRAP; -. DR OrthoDB; EOG622PTX; -. DR BioCyc; NMEN122586:GHGG-803-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005590; DUF333. DR Pfam; PF03891; DUF333; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 71 AA; 8032 MW; 7C0CB64550299C3A CRC64; MKAIHPYACP RCCRLPANTF RTGMANSASK FCIAKGGRRE AKKDESGGGY ALCHLPDSRI VEEWEYFRSQ Y // ID Q9JYT4_NEIMB Unreviewed; 237 AA. AC Q9JYT4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41801.1}; GN OrderedLocusNames=NMB1440 {ECO:0000313|EMBL:AAF41801.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41801.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41801.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41801.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41801.1; -; Genomic_DNA. DR PIR; H81083; H81083. DR RefSeq; NP_274452.1; NC_003112.2. DR RefSeq; WP_002222287.1; NC_003112.2. DR ProteinModelPortal; Q9JYT4; -. DR STRING; 122586.NMB1440; -. DR PaxDb; Q9JYT4; -. DR EnsemblBacteria; AAF41801; AAF41801; NMB1440. DR GeneID; 903861; -. DR KEGG; nme:NMB1440; -. DR PATRIC; 20358593; VBINeiMen85645_1808. DR eggNOG; ENOG4105SNY; Bacteria. DR eggNOG; COG1729; LUCA. DR HOGENOM; HOG000219013; -. DR OMA; PTQENAS; -. DR OrthoDB; EOG6PCPVX; -. DR BioCyc; NMEN122586:GHGG-1478-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13174; TPR_6; 1. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 237 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329346. FT COILED 53 80 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 237 AA; 25920 MW; 2CE9AFE28990991B CRC64; MKIKLPLFII WLSVSASCAS VSPVPAGSQT EMSTRENASD GIPYPVPTLQ DRLDYLEGKI VRLSNEVETL NGKVKALEHA KTHSSGRAYV QKLDDRKLKE HYLNTEGGSA SAHTVETAQN LYNQALKHYK SGKFSAAASL LKGADGGDGG SIAQRSMYLL LQSRARMGNC ESVIEIGGRY ANRFKDSPTA PEAMFKIGEC QYRLQQKDIA RATWRSLIQT YPGSPAAKRA AAAVRKR // ID Q9JXL9_NEIMB Unreviewed; 139 AA. AC Q9JXL9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42308.1}; GN OrderedLocusNames=NMB1980 {ECO:0000313|EMBL:AAF42308.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42308.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42308.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42308.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42308.1; -; Genomic_DNA. DR PIR; E81020; E81020. DR RefSeq; NP_274973.1; NC_003112.2. DR RefSeq; WP_002225853.1; NC_003112.2. DR STRING; 122586.NMB1980; -. DR PaxDb; Q9JXL9; -. DR EnsemblBacteria; AAF42308; AAF42308; NMB1980. DR GeneID; 904158; -. DR KEGG; nme:NMB1980; -. DR PATRIC; 20360035; VBINeiMen85645_2522. DR eggNOG; ENOG4108VBH; Bacteria. DR eggNOG; COG4316; LUCA. DR HOGENOM; HOG000130289; -. DR OMA; CTIAELC; -. DR OrthoDB; EOG6DZF1M; -. DR BioCyc; NMEN122586:GHGG-2037-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014449; UCP007050_HI0931. DR Pfam; PF10008; DUF2251; 1. DR PIRSF; PIRSF007050; UPC007050; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 139 AA; 15633 MW; 3CC5574547C060B9 CRC64; MAQLPLYLTS EIKDFTVGTP KVLESFSKHI PYGVVFEDDG DTGYFYAASQ DGILDALHIY NVEDVSDKHI PNHVLILWDD ACTIAALCIN DYIHAVYDFV EQAGYCRNGF PEAGGEWVKV ENRVLDDELL DKILSRKST // ID Q9JXA6_NEIMB Unreviewed; 36 AA. AC Q9JXA6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42454.1}; GN OrderedLocusNames=NMB2146 {ECO:0000313|EMBL:AAF42454.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42454.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42454.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42454.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42454.1; -; Genomic_DNA. DR PIR; H81002; H81002. DR RefSeq; NP_275131.1; NC_003112.2. DR RefSeq; WP_010981033.1; NC_003112.2. DR STRING; 122586.NMB2146; -. DR PaxDb; Q9JXA6; -. DR EnsemblBacteria; AAF42454; AAF42454; NMB2146. DR GeneID; 903226; -. DR KEGG; nme:NMB2146; -. DR BioCyc; NMEN122586:GHGG-2211-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 36 AA; 4131 MW; E793F718BA2AF08B CRC64; MYKYAKYEGC INLPYLLYLP YFTDGATPPA QPVLSE // ID Q9JZM5_NEIMB Unreviewed; 143 AA. AC Q9JZM5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41389.1}; GN OrderedLocusNames=NMB0986 {ECO:0000313|EMBL:AAF41389.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41389.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41389.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41389.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41389.1; -; Genomic_DNA. DR PIR; C81135; C81135. DR RefSeq; NP_274022.1; NC_003112.2. DR RefSeq; WP_002225301.1; NC_003112.2. DR ProteinModelPortal; Q9JZM5; -. DR STRING; 122586.NMB0986; -. DR PaxDb; Q9JZM5; -. DR EnsemblBacteria; AAF41389; AAF41389; NMB0986. DR GeneID; 903106; -. DR KEGG; nme:NMB0986; -. DR PATRIC; 20357469; VBINeiMen85645_1249. DR eggNOG; ENOG4107J8K; Bacteria. DR eggNOG; ENOG4112B19; LUCA. DR HOGENOM; HOG000218905; -. DR OMA; YIPRCEV; -. DR OrthoDB; EOG64FKJF; -. DR BioCyc; NMEN122586:GHGG-1023-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR014875; Mor_transcription_activator. DR Pfam; PF08765; Mor; 1. DR SUPFAM; SSF46689; SSF46689; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 54 137 Mor. {ECO:0000259|Pfam:PF08765}. SQ SEQUENCE 143 AA; 15958 MW; 9888B3E6C8427B64 CRC64; MMGFEKVEHL LPDTVLDIVD VIGLAATEQL VKAIGGARFK FGKGKVDTER LAILVEAIGE VKTHELLQVY GGEELYVPRC GKALIQLRNH RFYQEFVKLR DIDKKSGLMA MTKLCPKYGI SSRTGYTIIN EMSRPAAQQA ALF // ID Q9K0T4_NEIMB Unreviewed; 293 AA. AC Q9K0T4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40924.1}; GN OrderedLocusNames=NMB0489 {ECO:0000313|EMBL:AAF40924.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40924.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40924.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40924.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40924.1; -; Genomic_DNA. DR PIR; E81193; E81193. DR STRING; 122586.NMB0489; -. DR PaxDb; Q9K0T4; -. DR EnsemblBacteria; AAF40924; AAF40924; NMB0489. DR PATRIC; 20356232; VBINeiMen85645_0636. DR eggNOG; ENOG4107FEK; Bacteria. DR eggNOG; ENOG410XTP6; LUCA. DR OrthoDB; EOG6B360B; -. DR BioCyc; NMEN122586:GHGG-514-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 293 AA; 31606 MW; 185EE3A6B7EEBD8C CRC64; MRTDAFKYGT WNSLNDIRSS YDRAATKIKG AGNMGLGATT FVGSGAIGGG LCSTGIGCAA GGLIATAGMT GGYTQASEGS RQLFGTYQSD FGKKVVLSLG TPIEYESPLV SDAKNLAVWG LETLITRKLG NLATGVKTSL TPKTADVQRN ILSQSEVGIK WGKGIEGQGM PWEDYVGKGL SANARLPKNF KTFDYFDRGT GTAISAKTLD TQTTARLSKP EQLYSTMKGY IDKTANFKSY ELSEVPLRAD MIKQREIHLA IPAQTNKEQR LQLQRVVEYG KSQNITVKIT EIE // ID Q9K043_NEIMB Unreviewed; 407 AA. AC Q9K043; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41192.1}; GN OrderedLocusNames=NMB0779 {ECO:0000313|EMBL:AAF41192.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41192.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41192.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41192.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41192.1; -; Genomic_DNA. DR PIR; H81160; H81160. DR RefSeq; NP_273821.1; NC_003112.2. DR RefSeq; WP_002225425.1; NC_003112.2. DR ProteinModelPortal; Q9K043; -. DR STRING; 122586.NMB0779; -. DR PaxDb; Q9K043; -. DR EnsemblBacteria; AAF41192; AAF41192; NMB0779. DR GeneID; 902894; -. DR KEGG; nme:NMB0779; -. DR PATRIC; 20356935; VBINeiMen85645_0986. DR eggNOG; ENOG4108KBV; Bacteria. DR eggNOG; COG3071; LUCA. DR HOGENOM; HOG000263403; -. DR KO; K02498; -. DR OMA; MACETLL; -. DR OrthoDB; EOG6MPWRV; -. DR BioCyc; NMEN122586:GHGG-810-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042168; P:heme metabolic process; IEA:InterPro. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005254; Heme_biosyn_assoc_TPR_pro. DR InterPro; IPR010817; HemY_N. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF07219; HemY_N; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR00540; TPR_hemY_coli; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 66 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 26 134 HemY_N. {ECO:0000259|Pfam:PF07219}. SQ SEQUENCE 407 AA; 45602 MW; 6BD14BA447EF552B CRC64; MKTVVWIVVL FAAAVGLALA SGIYTGDVYI VLGQTMLRIN LHAFVLGSLI AVVVWYFLFK FIIGVLNIPE KMQRFGSARK GRKAALALNK AGLAYFEGRF EKAELEASRV LVNKEAGDNR TLALMLGAHA AGQMENIELR DRYLAEIAKL PEKQQLSRYL LLAESALNRR DYEAAEANLH AAAKMNANLT RLVRLQLRYA FDRGDALQVL AKTEKLSKAG ALGKSEMERY QNWAYRRQLA DAADAAALKT CLKRIPDSLK NGELSVSVAE KYERLGLYAD AVKWVKQHYP HNRRPELLEA FVESVRFLGE REQQKAIDFA DAWLKEQPDN ALLLMYLGRL AYGRKLWGKA KGYLEASIAL KPSISARLVL AKVFDEIGEP QKAEAQRNLV LEAVSDDERH AALEQHS // ID Q9K157_NEIMB Unreviewed; 394 AA. AC Q9K157; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=UbiH family protein {ECO:0000313|EMBL:AAF40768.1}; GN OrderedLocusNames=NMB0323 {ECO:0000313|EMBL:AAF40768.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40768.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40768.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40768.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40768.1; -; Genomic_DNA. DR PIR; F81212; F81212. DR RefSeq; NP_273372.1; NC_003112.2. DR RefSeq; WP_002243976.1; NC_003112.2. DR ProteinModelPortal; Q9K157; -. DR STRING; 122586.NMB0323; -. DR PaxDb; Q9K157; -. DR EnsemblBacteria; AAF40768; AAF40768; NMB0323. DR GeneID; 902439; -. DR KEGG; nme:NMB0323; -. DR PATRIC; 20355779; VBINeiMen85645_0409. DR eggNOG; ENOG4105EAK; Bacteria. DR eggNOG; COG0654; LUCA. DR HOGENOM; HOG000255771; -. DR OMA; NKHMLHA; -. DR OrthoDB; EOG6G20HJ; -. DR BioCyc; NMEN122586:GHGG-343-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR010971; UbiH/COQ6. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR01988; Ubi-OHases; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 346 FAD_binding_3. FT {ECO:0000259|Pfam:PF01494}. SQ SEQUENCE 394 AA; 43638 MW; 2C2F2B542891E2EC CRC64; MSLHSDILVV GAGPAGLSFA AELAGSGLKV TLIERSPLTV LQNPPYDGRE IALTHFSREI MQRLGMWDKI PENEIYPLRD AKVLNGRSDY QLHFPQPTEA RGEPADCLGY LISNHNIRRA AYEVVSQLDN VSILTDTVVK EVKTSDNEAQ VILENGKILT ARLLLAADSR FSQTRRQLGI SSDMHDYSRT MFVCRMKHTL SNQHTAYECF HYGRTIALLP LEEHLTNTVI TVDTDKINSV QNLSPEELAA SVKEQLKGRL GDMELVSSIH HYPLVGMIAK RFYGKRSALI GDAAVGMHPV TAHGFNLGLS SADILAKLIL EAEQRGQDIG ASSLLEKYSS KHMLHAHPLY HGTNMMLKLF TNETAPAKLL RGLVLRASNN FPPLKKLITK QLTG // ID Q9K1E8_NEIMB Unreviewed; 343 AA. AC Q9K1E8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160}; GN Name=gapA-1 {ECO:0000313|EMBL:AAF40664.1}; GN OrderedLocusNames=NMB0207 {ECO:0000313|EMBL:AAF40664.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40664.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40664.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40664.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {ECO:0000256|RuleBase:RU361160}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40664.1; -; Genomic_DNA. DR PIR; H81224; H81224. DR RefSeq; NP_273265.1; NC_003112.2. DR RefSeq; WP_002236620.1; NC_003112.2. DR ProteinModelPortal; Q9K1E8; -. DR SMR; Q9K1E8; 3-330. DR STRING; 122586.NMB0207; -. DR PaxDb; Q9K1E8; -. DR EnsemblBacteria; AAF40664; AAF40664; NMB0207. DR GeneID; 902315; -. DR KEGG; nme:NMB0207; -. DR PATRIC; 20355455; VBINeiMen85645_0256. DR eggNOG; ENOG4105C17; Bacteria. DR eggNOG; COG0057; LUCA. DR HOGENOM; HOG000071679; -. DR KO; K00134; -. DR OMA; NDQNNID; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; NMEN122586:GHGG-218-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160, KW ECO:0000313|EMBL:AAF40664.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 155 Gp_dh_N. {ECO:0000259|SMART:SM00846}. FT ACT_SITE 155 155 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR000149-1}. FT SITE 182 182 Activates thiol group during catalysis. FT {ECO:0000256|PIRSR:PIRSR000149-4}. SQ SEQUENCE 343 AA; 36963 MW; E8262081E2A87BAC CRC64; MGIKVAINGY GRIGRQVLRA IYDYQIQDQL QIVAVNASGS LETNAHLTKF DTVHGRFEAD VSHDGGNLIV NGDKIPFFST RNPAELPWKE LGVDLVMECT GAFTSKEKAK IHLESGAKKV LISAPGGDDV DATVVYGVND SVLTADMTVV SNASCTTNCL SPVAKVLSES VGIVKGAMTT IHALTNDQTV TDVRHKDLRR ARSGVENMIP TKTGAAKAVG LVLPELKGRL DGLAIRVPTV NVSLVDLSFQ AARDTTVEEI NALMKAASEA GPLKGVLGYN TLPLVSMDFN HTTEASHFDA TLTKVVDGNM VKVFAWYDNE WGFSCQMLNT ARRMFGLEVR PLK // ID Q9K0J7_NEIMB Unreviewed; 256 AA. AC Q9K0J7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000256|HAMAP-Rule:MF_00902}; GN Name=tatC {ECO:0000256|HAMAP-Rule:MF_00902}; GN OrderedLocusNames=NMB0599 {ECO:0000313|EMBL:AAF41027.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41027.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41027.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41027.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. CC Together with TatB, TatC is part of a receptor directly CC interacting with Tat signal peptides. {ECO:0000256|HAMAP- CC Rule:MF_00902}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000256|HAMAP-Rule:MF_00902}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00902}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00902}. CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP- CC Rule:MF_00902}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41027.1; -; Genomic_DNA. DR PIR; D81181; D81181. DR RefSeq; NP_273643.1; NC_003112.2. DR RefSeq; WP_002222849.1; NC_003112.2. DR STRING; 122586.NMB0599; -. DR PaxDb; Q9K0J7; -. DR EnsemblBacteria; AAF41027; AAF41027; NMB0599. DR GeneID; 902714; -. DR KEGG; nme:NMB0599; -. DR PATRIC; 20356483; VBINeiMen85645_0761. DR eggNOG; ENOG4105DCX; Bacteria. DR eggNOG; COG0805; LUCA. DR HOGENOM; HOG000245379; -. DR KO; K03118; -. DR OMA; ATQIYKF; -. DR OrthoDB; EOG60SCQS; -. DR BioCyc; NMEN122586:GHGG-625-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00902; TatC; 1. DR InterPro; IPR002033; TatC. DR PANTHER; PTHR30371:SF0; PTHR30371:SF0; 1. DR Pfam; PF00902; TatC; 1. DR PRINTS; PR01840; TATCFAMILY. DR TIGRFAMs; TIGR00945; tatC; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00902}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00902}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_00902}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_00902}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00902}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00902}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00902}. FT TRANSMEM 29 49 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 68 88 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 121 141 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 161 181 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 198 218 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 220 240 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. SQ SEQUENCE 256 AA; 28527 MW; 8A88365A9CF1B5C7 CRC64; MSETQNEQPV QPLVEHLIEL RRRLMWTVVG ILVCFFGLMP FAQQLYTFIA DPLMANLPKD TSMIATDVIA PFFVPVKVTL MAAFLISLPH TLYQIWAFVA PALYQNEKRL ITPLVLSSVS LFFIGMAFAY FLVFPVIFKF LASVTPVGVN MATDIDKYLS FILGMFVAFG TTFEVPIVVI LLTKIGVVTT GQLKRARPYV IVGAFVIAAI ITPPDVISQT LLAIPLILLY EAGIWFGRFF TPRSEQDGDI RPPATT // ID Q9JZD5_NEIMB Unreviewed; 65 AA. AC Q9JZD5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41494.1}; GN OrderedLocusNames=NMB1103 {ECO:0000313|EMBL:AAF41494.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41494.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41494.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41494.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41494.1; -; Genomic_DNA. DR PIR; D81121; D81121. DR RefSeq; NP_274134.1; NC_003112.2. DR RefSeq; WP_002225238.1; NC_003112.2. DR STRING; 122586.NMB1103; -. DR PaxDb; Q9JZD5; -. DR EnsemblBacteria; AAF41494; AAF41494; NMB1103. DR GeneID; 903525; -. DR KEGG; nme:NMB1103; -. DR PATRIC; 20357770; VBINeiMen85645_1401. DR HOGENOM; HOG000219053; -. DR OMA; VEDSIYY; -. DR OrthoDB; EOG6FNHW4; -. DR BioCyc; NMEN122586:GHGG-1139-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR024400; DUF2635. DR Pfam; PF10948; DUF2635; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7242 MW; 2639C2CDB4BA1F59 CRC64; MSKIKVTAAD GLRVPTEHNP HEYIGQEPVE VDGNSLYYRR MIDDGDLVVV EDAAPNTKTR NTKGE // ID Q9JXT4_NEIMB Unreviewed; 70 AA. AC Q9JXT4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42226.1}; GN OrderedLocusNames=NMB1892 {ECO:0000313|EMBL:AAF42226.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42226.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42226.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42226.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42226.1; -; Genomic_DNA. DR PIR; E81029; E81029. DR RefSeq; NP_274888.1; NC_003112.2. DR RefSeq; WP_002225797.1; NC_003112.2. DR STRING; 122586.NMB1892; -. DR PaxDb; Q9JXT4; -. DR EnsemblBacteria; AAF42226; AAF42226; NMB1892. DR GeneID; 904285; -. DR KEGG; nme:NMB1892; -. DR HOGENOM; HOG000071336; -. DR OMA; LQGVGFK; -. DR OrthoDB; EOG6GJBZC; -. DR BioCyc; NMEN122586:GHGG-1949-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 70 AA; 7313 MW; 11FD2D5718F38590 CRC64; MPDRIKPSRN GGGADDIARQ QGTAQTGAKP ETSPTARYGD FLRPLQGGIG FKRRGLEGKT GGAQNCLNAV // ID Q9JZG5_NEIMB Unreviewed; 226 AA. AC Q9JZG5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41462.1}; GN OrderedLocusNames=NMB1066 {ECO:0000313|EMBL:AAF41462.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41462.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41462.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41462.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41462.1; -; Genomic_DNA. DR PIR; D81125; D81125. DR RefSeq; NP_274099.1; NC_003112.2. DR RefSeq; WP_002225261.1; NC_003112.2. DR STRING; 122586.NMB1066; -. DR PaxDb; Q9JZG5; -. DR EnsemblBacteria; AAF41462; AAF41462; NMB1066. DR GeneID; 903483; -. DR KEGG; nme:NMB1066; -. DR PATRIC; 20357677; VBINeiMen85645_1355. DR eggNOG; ENOG4105P7V; Bacteria. DR eggNOG; COG3235; LUCA. DR HOGENOM; HOG000218930; -. DR OMA; SERGIWL; -. DR OrthoDB; EOG69D3CQ; -. DR BioCyc; NMEN122586:GHGG-1103-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 204 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 226 AA; 24548 MW; 680E486E2E03FDD2 CRC64; MIFQTVWFSD MVLSVSWIVL ILILAASAPS AFRSLARYRS ALPLCTVIFS AAWCLNASAG GGQLAQMNYH LLAVNLVALM MGTSAALWLA ALLMLPYCLL FAGSVGAYPP NALVLILPAL TVNRLSRMLV NRLPPNIFIF IFVNGFLASA AGILLTGLVL TGILDAANAF PSEILWTTAL PVFILLAWAE AFLSGISTAI FVALKPHWIN TFDDNRYLKS DRGIWR // ID Q9JYF1_NEIMB Unreviewed; 83 AA. AC Q9JYF1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41963.1}; GN OrderedLocusNames=NMB1611 {ECO:0000313|EMBL:AAF41963.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41963.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41963.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41963.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41963.1; -; Genomic_DNA. DR PIR; A81063; A81063. DR RefSeq; NP_274617.1; NC_003112.2. DR RefSeq; WP_002218963.1; NC_003112.2. DR STRING; 122586.NMB1611; -. DR PaxDb; Q9JYF1; -. DR EnsemblBacteria; AAF41963; AAF41963; NMB1611. DR GeneID; 904311; -. DR KEGG; nme:NMB1611; -. DR PATRIC; 20359110; VBINeiMen85645_2067. DR HOGENOM; HOG000219046; -. DR OrthoDB; EOG6J1DHR; -. DR BioCyc; NMEN122586:GHGG-1659-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 83 AA; 9546 MW; 2C6AED3708E1EFFF CRC64; MGSIEQRLEY LEEANDVLRM QNHVLSTAFK ALIRALPAET AEIAVESIQL AFEDALAELS YEDSPHTDLF HDVTYAFFRE KER // ID Q9JXF8_NEIMB Unreviewed; 366 AA. AC Q9JXF8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:AAF42387.1}; DE EC=1.4.3.19 {ECO:0000313|EMBL:AAF42387.1}; GN Name=thiO {ECO:0000313|EMBL:AAF42387.1}; GN OrderedLocusNames=NMB2068 {ECO:0000313|EMBL:AAF42387.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42387.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42387.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42387.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42387.1; -; Genomic_DNA. DR PIR; H81010; H81010. DR RefSeq; NP_275058.1; NC_003112.2. DR RefSeq; WP_002225707.1; NC_003112.2. DR ProteinModelPortal; Q9JXF8; -. DR STRING; 122586.NMB2068; -. DR PaxDb; Q9JXF8; -. DR EnsemblBacteria; AAF42387; AAF42387; NMB2068. DR GeneID; 904004; -. DR KEGG; nme:NMB2068; -. DR PATRIC; 20360296; VBINeiMen85645_2648. DR eggNOG; ENOG4107S07; Bacteria. DR eggNOG; COG0665; LUCA. DR HOGENOM; HOG000042042; -. DR KO; K03153; -. DR OMA; PRYPIYI; -. DR OrthoDB; EOG622PM9; -. DR BioCyc; NMEN122586:GHGG-2131-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42387.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 337 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 366 AA; 40566 MW; E20CFFAC386CE06F CRC64; MTRIAILGGG LSGRLTALQL AEQGYQIALF DKGCRRGEHA AAYVAAAMLA PAAEAVEATP EVVRLGRQSI PLWRGIRCRL NTHTMMQENG SLIVWHGQDK PLSSEFVRHL KRGGVADDEI VRWRADDIAE REPQLGGRFS DGIYLPTEGQ LDGRQILSAL ADALDELNVP CHWEHECVPE GLQAQYDWLI DCRGYGAKTA WNQSPEHTST LRGIRGEVAR VYTPEITLNR PVRLLHPRYP LYIAPKENHV FVIGATQIES ESQAPASVRS GLELLSALYA IHPAFGEADI LEIATGLRPT LNHHNPEIRY NRARRLIEIN GLFRHGFMIS PAVTAAAARL AVALFDGKDA PERDKESGLA YIRRQD // ID Q7DDN7_NEIMB Unreviewed; 90 AA. AC Q7DDN7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40940.1}; GN OrderedLocusNames=NMB0508 {ECO:0000313|EMBL:AAF40940.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40940.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40940.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40940.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40940.1; -; Genomic_DNA. DR RefSeq; NP_273554.1; NC_003112.2. DR RefSeq; WP_002214440.1; NC_003112.2. DR STRING; 122586.NMB0508; -. DR PaxDb; Q7DDN7; -. DR EnsemblBacteria; AAF40940; AAF40940; NMB0508. DR GeneID; 902624; -. DR KEGG; nme:NMB0508; -. DR PATRIC; 20356262; VBINeiMen85645_0651. DR HOGENOM; HOG000218791; -. DR OrthoDB; EOG6TR0HJ; -. DR BioCyc; NMEN122586:GHGG-533-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 90 AA; 10808 MW; 6FFF7D4D0CF691B9 CRC64; MNKRMKMCPA CQQGYLYHSK PKYLHDEIIL CDECDAVWLK GMNIFYGEYE KDFYSYVPFM ESQGITSECI WEGDLFDHPY YEDENSNDMD // ID Q9JYN8_NEIMB Unreviewed; 64 AA. AC Q9JYN8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41851.1}; GN OrderedLocusNames=NMB1495 {ECO:0000313|EMBL:AAF41851.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41851.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41851.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41851.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41851.1; -; Genomic_DNA. DR PIR; E81078; E81078. DR RefSeq; NP_274503.1; NC_003112.2. DR RefSeq; WP_002212913.1; NC_003112.2. DR STRING; 122586.NMB1495; -. DR PaxDb; Q9JYN8; -. DR EnsemblBacteria; AAF41851; AAF41851; NMB1495. DR GeneID; 903917; -. DR KEGG; nme:NMB1495; -. DR PATRIC; 20358756; VBINeiMen85645_1887. DR BioCyc; NMEN122586:GHGG-1535-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7606 MW; DA8609EF18D0CB8B CRC64; MNPSQYLFID LNFDKIPDTR LCCFSIFQPT VNLKQPVHAM LQFLFLSADC FDKELKIHFM HLKI // ID Q9K0L6_NEIMB Unreviewed; 190 AA. AC Q9K0L6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=NosR-related protein {ECO:0000313|EMBL:AAF41005.1}; GN OrderedLocusNames=NMB0577 {ECO:0000313|EMBL:AAF41005.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41005.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41005.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41005.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41005.1; -; Genomic_DNA. DR PIR; D81183; D81183. DR RefSeq; NP_273621.1; NC_003112.2. DR RefSeq; WP_010980814.1; NC_003112.2. DR STRING; 122586.NMB0577; -. DR PaxDb; Q9K0L6; -. DR EnsemblBacteria; AAF41005; AAF41005; NMB0577. DR GeneID; 902692; -. DR KEGG; nme:NMB0577; -. DR PATRIC; 20356435; VBINeiMen85645_0737. DR eggNOG; COG3901; LUCA. DR HOGENOM; HOG000218806; -. DR KO; K19339; -. DR OMA; FRARITV; -. DR OrthoDB; EOG6VXFB0; -. DR BioCyc; NMEN122586:GHGG-603-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 190 AA; 20615 MW; 334F771621296946 CRC64; MIHIISILKS IGISGIVMSC FSIKRMSAFR ARITAFFAAF VFLTAALPAY AERLPDFLAK IQPSEIFPGA DRYGKPEGKP MVARVYKGDE QLGLVYITTD AVNTRGYSSK PIDTLMVLAN DGTIAGAKLV DHHEPIMLIG IPHLPAPGRA IRSNWLPAYI KPNFTLTNRL RLKGLPTVPQ PSKATGAGVP // ID Q9JYL3_NEIMB Unreviewed; 271 AA. AC Q9JYL3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41884.1}; GN OrderedLocusNames=NMB1529 {ECO:0000313|EMBL:AAF41884.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41884.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41884.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41884.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41884.1; -; Genomic_DNA. DR PIR; E81073; E81073. DR RefSeq; NP_274536.1; NC_003112.2. DR RefSeq; WP_002225059.1; NC_003112.2. DR ProteinModelPortal; Q9JYL3; -. DR SMR; Q9JYL3; 83-117. DR STRING; 122586.NMB1529; -. DR PaxDb; Q9JYL3; -. DR EnsemblBacteria; AAF41884; AAF41884; NMB1529. DR GeneID; 904043; -. DR KEGG; nme:NMB1529; -. DR eggNOG; COG1881; LUCA. DR KO; K06910; -. DR OMA; HRSRIIK; -. DR OrthoDB; EOG6N681K; -. DR BioCyc; NMEN122586:GHGG-1570-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.280.10; -; 1. DR InterPro; IPR008914; PtdEtn-bd_prot_PEBP. DR Pfam; PF01161; PBP; 1. DR SUPFAM; SSF49777; SSF49777; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 271 AA; 31220 MW; 1253191A6A2A2702 CRC64; MTAYNESTYS SSKGIIYANP HPLRRTAGFF NRCLCRGRIH AAIRQPVRRR RLHAKPAFER ALRLLLFRRQ CFARAVVEKS ARRDKSFVLT VYDKDAPTGL GWMHRVVADI PADVHRRNAT SLQLSRCANI ADRTGLDALG GRRHSRRCPP PQRGLAAIKP LRQHRRRPVR SHIGGNQFAD LPHQVDAFVH GKTDAVMLQP RQHAAKRGLR SIVRHFFIRQ YRSLIIKRRA HTPGIRQLYR IAHCLRRPVL CGEPFYGFLF ESNPLRLIEA V // ID Q9JZC4_NEIMB Unreviewed; 175 AA. AC Q9JZC4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41506.1}; GN OrderedLocusNames=NMB1116 {ECO:0000313|EMBL:AAF41506.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41506.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41506.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41506.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41506.1; -; Genomic_DNA. DR PIR; F81119; F81119. DR STRING; 122586.NMB1116; -. DR PaxDb; Q9JZC4; -. DR EnsemblBacteria; AAF41506; AAF41506; NMB1116. DR OrthoDB; EOG6ZPT33; -. DR BioCyc; NMEN122586:GHGG-1152-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 175 AA; 19249 MW; DA0D6524459B6392 CRC64; MPRQSCHSSS FPPLSSFPRK RESRPPDATG IYRKNRNPRH RHSRESGNPA PKRGRNLSEK TETPAAVIPA QAGIQTPNAA GIYRKKQKSP PPSFPRRRES RPQTRQESIG KNRPPATVIP AQAGIQTPNA AGIYRKRLKP NGLDSRLRGN DGGRGFGIPA FAGMTESGGN NERRE // ID Q9K1A7_NEIMB Unreviewed; 128 AA. AC Q9K1A7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40714.1}; GN OrderedLocusNames=NMB0260 {ECO:0000313|EMBL:AAF40714.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40714.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40714.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40714.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40714.1; -; Genomic_DNA. DR PIR; G81220; G81220. DR STRING; 122586.NMB0260; -. DR PaxDb; Q9K1A7; -. DR EnsemblBacteria; AAF40714; AAF40714; NMB0260. DR BioCyc; NMEN122586:GHGG-275-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 128 AA; 14407 MW; AFFFD969E79ECFC6 CRC64; MPFRNAVQTA SPPTTPKQKA HHDRIHVHPF GLGTHLCQRP LPHDQTVRRG RTQAQTFRTP HDRAGGRFRA DRRSCLHPRI PCRIGTRSGL GVLCHSRLPV PDFCVSMFCV AVFLAHAQQG IDKHRNAV // ID Q9JZN2_NEIMB Unreviewed; 461 AA. AC Q9JZN2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204}; DE EC=1.6.1.2 {ECO:0000256|PIRNR:PIRNR000204}; DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204}; GN Name=pntB {ECO:0000313|EMBL:AAF41382.1}; GN OrderedLocusNames=NMB0978 {ECO:0000313|EMBL:AAF41382.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41382.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41382.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41382.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane. {ECO:0000256|PIRNR:PIRNR000204}. CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC {ECO:0000256|PIRNR:PIRNR000204}. CC -!- SIMILARITY: Belongs to the PNT beta subunit family. CC {ECO:0000256|PIRNR:PIRNR000204}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41382.1; -; Genomic_DNA. DR PIR; C81137; C81137. DR RefSeq; NP_274015.1; NC_003112.2. DR RefSeq; WP_002217354.1; NC_003112.2. DR ProteinModelPortal; Q9JZN2; -. DR SMR; Q9JZN2; 293-459. DR STRING; 122586.NMB0978; -. DR PaxDb; Q9JZN2; -. DR EnsemblBacteria; AAF41382; AAF41382; NMB0978. DR GeneID; 903098; -. DR KEGG; nme:NMB0978; -. DR PATRIC; 20357445; VBINeiMen85645_1237. DR eggNOG; ENOG4105C15; Bacteria. DR eggNOG; COG1282; LUCA. DR HOGENOM; HOG000243958; -. DR KO; K00325; -. DR OMA; HHAEVFI; -. DR OrthoDB; EOG6WDSHK; -. DR BioCyc; NMEN122586:GHGG-1015-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR012136; NADH_DH_b. DR Pfam; PF02233; PNTB; 1. DR PIRSF; PIRSF000204; PNTB; 1. DR SUPFAM; SSF52467; SSF52467; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR000204}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR000204}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|PIRNR:PIRNR000204, ECO:0000256|SAM:Phobius}; KW NAD {ECO:0000256|PIRNR:PIRNR000204}; KW NADP {ECO:0000256|PIRNR:PIRNR000204}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000204, KW ECO:0000313|EMBL:AAF41382.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 230 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 236 256 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 461 AA; 48533 MW; 5FA1C084CB944507 CRC64; MSSGLVTAAY IVAAILFIFS LAGLSKQETA KQGCYSGIAG MAVALFVTVF SDNTHGLGWI IIAMLIGAAI GIYKAKKVEM TEMPELIALL HSFVGLAAVL VGFNSYIAPG NVSHDMHTIH LVEVYLGIFI GAVTFTGSLV AFGKLNGKIS SSPLQLPAKH KLNALALAVS FVLLLVFVGI DGSGFILLIM TLIALAFGWH LVASIGGADM PVVVSMLNSY SGWAAAAAGF MLSNDLLIVT GALVGSSGAI LSYIMCKAMN RSFVSVIAGG FGSDSGTLSS GSQEIGEYRE VKAADIAEML KGANNVIITP GYGMAVAQAQ YPVAEITELL RKNGTEVRFG IHPVAGRLPG HMNVLLAEAK VPYDIVLEMD EINDDFPETD VVLVIGANDT VNPAAQTDPN SPIAGMPVLE VWKAKEVVVF KRSMNTGYAG VQNPLFFNEN SVMCFGDAKK TVDDILSELK K // ID Q7DDP5_NEIMB Unreviewed; 110 AA. AC Q7DDP5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40918.1}; GN OrderedLocusNames=NMB0481 {ECO:0000313|EMBL:AAF40918.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40918.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40918.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40918.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40918.1; -; Genomic_DNA. DR PIR; G81192; G81192. DR RefSeq; NP_273528.1; NC_003112.2. DR RefSeq; WP_010980801.1; NC_003112.2. DR STRING; 122586.NMB0481; -. DR PaxDb; Q7DDP5; -. DR EnsemblBacteria; AAF40918; AAF40918; NMB0481. DR GeneID; 902598; -. DR KEGG; nme:NMB0481; -. DR PATRIC; 20356218; VBINeiMen85645_0629. DR HOGENOM; HOG000218810; -. DR OMA; ISFPDNS; -. DR OrthoDB; EOG6H1Q2Q; -. DR BioCyc; NMEN122586:GHGG-506-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009509; DUF1132. DR Pfam; PF06575; DUF1132; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 110 AA; 13017 MW; 3BE8E2B9589B78FB CRC64; MKGRTMNKPF ITQAQLALYK YQPSSKYFGQ SMAVIAQSEF VEFAKINKSE NVIDCFSFFW NRRIKHDIWL ISFSDNSEMV IKESLKDGHK IYKFEFCEIV DNCNFDDVFV // ID Q7DDD7_NEIMB Unreviewed; 315 AA. AC Q7DDD7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Stomatin/Mec-2 family protein {ECO:0000313|EMBL:AAF41602.1}; GN OrderedLocusNames=NMB1220 {ECO:0000313|EMBL:AAF41602.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41602.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41602.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41602.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41602.1; -; Genomic_DNA. DR RefSeq; NP_274245.1; NC_003112.2. DR RefSeq; WP_002222438.1; NC_003112.2. DR ProteinModelPortal; Q7DDD7; -. DR STRING; 122586.NMB1220; -. DR PaxDb; Q7DDD7; -. DR EnsemblBacteria; AAF41602; AAF41602; NMB1220. DR GeneID; 903642; -. DR KEGG; nme:NMB1220; -. DR PATRIC; 20358023; VBINeiMen85645_1524. DR eggNOG; ENOG4107QX8; Bacteria. DR eggNOG; COG0330; LUCA. DR HOGENOM; HOG000217038; -. DR OMA; SRERINM; -. DR OrthoDB; EOG6J48MH; -. DR BioCyc; NMEN122586:GHGG-1257-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR InterPro; IPR001107; Band_7. DR InterPro; IPR032435; Band_7_C. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR Pfam; PF01145; Band_7; 1. DR Pfam; PF16200; Band_7_C; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 175 PHB. {ECO:0000259|SMART:SM00244}. SQ SEQUENCE 315 AA; 34506 MW; 330F361C519F9C7D CRC64; MEFFIILLVA VAVFGFKSFV VIPQQEVHVV ERLGRFHRAL TAGLNILIPF IDRVAYRHSL KEIPLDVPSQ VCITRDNTQL TVDGIIYFQV TDPKLASYGS SNYIMAITQL AQTTLRSVIG RMELDKTFEE RDEINSTVVA ALDEAAGAWG VKVLRYEIKD LVPPQEILRS MQAQITAERE KRARIAESEG RKIEQINLAS GQREAEIQQS EGEAQAAVNA SNAEKIARIN RAKGEAESLR LVAEANAEAI RQIAAALQTQ GGADAVNLKI AEQYVAAFNN LAKESNTLIM PANVADIGSL ISAGMKIIDS SKTAK // ID Q9K0E0_NEIMB Unreviewed; 331 AA. AC Q9K0E0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41087.1}; GN OrderedLocusNames=NMB0669 {ECO:0000313|EMBL:AAF41087.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41087.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41087.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41087.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41087.1; -; Genomic_DNA. DR PIR; A81173; A81173. DR RefSeq; NP_273711.1; NC_003112.2. DR RefSeq; WP_002225508.1; NC_003112.2. DR ProteinModelPortal; Q9K0E0; -. DR STRING; 122586.NMB0669; -. DR PaxDb; Q9K0E0; -. DR EnsemblBacteria; AAF41087; AAF41087; NMB0669. DR GeneID; 902780; -. DR KEGG; nme:NMB0669; -. DR PATRIC; 20356639; VBINeiMen85645_0838. DR eggNOG; ENOG4105HHA; Bacteria. DR eggNOG; COG1559; LUCA. DR HOGENOM; HOG000050562; -. DR KO; K07082; -. DR OMA; LRIYQTA; -. DR OrthoDB; EOG67T5RG; -. DR BioCyc; NMEN122586:GHGG-696-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.160.60; -; 1. DR InterPro; IPR003770; UPF0755_YceG-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Pfam; PF02618; YceG; 1. DR TIGRFAMs; TIGR00247; TIGR00247; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 331 AA; 36875 MW; B5273F58B217A73C CRC64; MLRKLLKWSA VFLTVSAAVF AALLFVPKDN GRAYRIKIAK NQGISSVGRK LAEDRIVFSR HVLTAAAYVL GVHNRLHTGT YRLPSEVSAW DILQKMRGGR PDSVTVQIIE GSRFSHMRKV IDATPDIGHD TKGWSNEKLM AEVAPDAFSG NPEGQFFPDS YEIDAGGSDL QIYQTAYKAM QRRLNEAWES RQDGLPYKNP YEMLIMASLV EKETGHEADR DHVASVFVNR LKIGMRLQTD PSVIYGMGAA YKGKIRKADL RRDTPYNTYT RGGLPPTPIA LPGKAALDAA AHPSGEKYLY FVSKMDGTGL SQFSHDLTEH NAAVRKYILK K // ID Q7DDI7_NEIMB Unreviewed; 258 AA. AC Q7DDI7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Ferredoxin--NADP reductase {ECO:0000313|EMBL:AAF41442.1}; DE EC=1.18.1.2 {ECO:0000313|EMBL:AAF41442.1}; GN Name=fpr-1 {ECO:0000313|EMBL:AAF41442.1}; GN OrderedLocusNames=NMB1044 {ECO:0000313|EMBL:AAF41442.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41442.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41442.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41442.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41442.1; -; Genomic_DNA. DR PIR; D81127; D81127. DR RefSeq; NP_274078.1; NC_003112.2. DR RefSeq; WP_002213456.1; NC_003112.2. DR ProteinModelPortal; Q7DDI7; -. DR SMR; Q7DDI7; 4-258. DR STRING; 122586.NMB1044; -. DR PaxDb; Q7DDI7; -. DR EnsemblBacteria; AAF41442; AAF41442; NMB1044. DR GeneID; 903181; -. DR KEGG; nme:NMB1044; -. DR PATRIC; 20357625; VBINeiMen85645_1329. DR eggNOG; ENOG4105DP0; Bacteria. DR eggNOG; COG1018; LUCA. DR HOGENOM; HOG000265759; -. DR KO; K00528; -. DR OMA; DELAYHD; -. DR OrthoDB; EOG6FZ49Q; -. DR BioCyc; NMEN122586:GHGG-1081-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41442.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 102 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. SQ SEQUENCE 258 AA; 29314 MW; 2FB1843CC5AD6DE2 CRC64; MAAFNTQKVL SVHHWTDAYF TFTCTRDESL RFENGQFVMV GLMVDGKPLM RAYSVASANW EEHLEFFSIK VQDGPLTSRL QHLKVGDDVL ISKKPTGTLV AGDLNPGKHL YLLSTGTGIA PFLSITKDPE IYEQFEKIIL VHGVRYKKDL AYYDRFTKEL PEHEYLGDLV KEKLIYYPIV SREEFEHHGR LTDLMVSGKL FEDIGLPKIN PQDDRAMLCG SPAMLKDTCK VLDDFGLTVS PKTGVRGDYL IERAFVDQ // ID Q9JYS7_NEIMB Unreviewed; 259 AA. AC Q9JYS7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Ferredoxin--NADP reductase {ECO:0000313|EMBL:AAF41809.1}; DE EC=1.18.1.2 {ECO:0000313|EMBL:AAF41809.1}; GN Name=fpr-2 {ECO:0000313|EMBL:AAF41809.1}; GN OrderedLocusNames=NMB1450 {ECO:0000313|EMBL:AAF41809.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41809.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41809.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41809.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41809.1; -; Genomic_DNA. DR PIR; C81081; C81081. DR RefSeq; NP_274461.1; NC_003112.2. DR RefSeq; WP_002225108.1; NC_003112.2. DR ProteinModelPortal; Q9JYS7; -. DR STRING; 122586.NMB1450; -. DR PaxDb; Q9JYS7; -. DR EnsemblBacteria; AAF41809; AAF41809; NMB1450. DR GeneID; 903870; -. DR KEGG; nme:NMB1450; -. DR PATRIC; 20358635; VBINeiMen85645_1829. DR eggNOG; ENOG4105DP0; Bacteria. DR eggNOG; COG1018; LUCA. DR HOGENOM; HOG000265758; -. DR KO; K00528; -. DR OMA; PFIAGQF; -. DR OrthoDB; EOG66F050; -. DR BioCyc; NMEN122586:GHGG-1488-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00175; NAD_binding_1; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF41809.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 106 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. SQ SEQUENCE 259 AA; 29321 MW; 61B51D841C0B7C41 CRC64; MAASPEAKFT EEKILWVKHH TPKLITFAIS RPESYRFKAG QFSRLGFYEG EGFIWRAYSI VSAEYADTLE YFAVLIQDGP MSARFAKMQQ GNTILLDKNA TGFLLPERFP DGKDLVMLCT GSGIAPFLSI LEQPEIRQRF DTVNLIHSVS FPEELIFNDR LAALTEHPLV GEYGHSFRFV PVTTRAANPS GLSGKRIPEL LKNNSIEQAL HTKFTPESTR FMICGNPEMV KDTFQTLLDM GYAMHRNRIP GQIMMENGF // ID Q9K0U8_NEIMB Unreviewed; 459 AA. AC Q9K0U8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Spermidine/putrescine ABC transporter, periplasmic spermidine/putrescine-binding protein {ECO:0000313|EMBL:AAF40899.1}; GN Name=potD-1 {ECO:0000313|EMBL:AAF40899.1}; GN OrderedLocusNames=NMB0462 {ECO:0000313|EMBL:AAF40899.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40899.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40899.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40899.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40899.1; -; Genomic_DNA. DR PIR; C81195; C81195. DR RefSeq; NP_273509.1; NC_003112.2. DR RefSeq; WP_010980798.1; NC_003112.2. DR ProteinModelPortal; Q9K0U8; -. DR STRING; 122586.NMB0462; -. DR PaxDb; Q9K0U8; -. DR PRIDE; Q9K0U8; -. DR EnsemblBacteria; AAF40899; AAF40899; NMB0462. DR GeneID; 902578; -. DR KEGG; nme:NMB0462; -. DR PATRIC; 20356166; VBINeiMen85645_0604. DR eggNOG; COG0687; LUCA. DR HOGENOM; HOG000263815; -. DR KO; K02055; -. DR OMA; TNFIHYA; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NMEN122586:GHGG-486-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:InterPro. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PRINTS; PR00909; SPERMDNBNDNG. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 459 AA; 50556 MW; F2A5A8488416F585 CRC64; MQAFSLYPPV GHPDSAKKRQ NRADVFLPFW KQDNFLGKSV QYRFEFAQIY FTMPKPCAGV TMGRGDFFFS NLFHQESARM KKSVLAVLAA LSLAACGGSE KNAVQPQADA ASAANAEAAA TDTLNIYNWS NYVDESTVED FKKANNLKLT YDLYENNETL EAKMLTGKSG YDLVVPGIAF LPRQIEAGAY QKVNKDLIPN YKNIDPELLK MLETADPGNQ YAVPYFSGVN TIAITAKGKE LLGGKLPENG WDLLFKPEYT HKLKSCGIAL WDTPSEMFPI LLNYLGKDPK GSNPEDLKAA AEVLKSIRPD VKRFSPSIID ELARGDICLA AGNGGDLNLA KARSEEVKNN VGIEVLTPKG MGFWIESWLI PADAKNVANA HKYINYTLDP EIAAKNGIAV TFAPASKPAR EKMPAELVNT RSIFPNEQDM KDGFVMPQMS TDAKKLSVSL WQKIKVGTN // ID Q9K1M9_NEIMB Unreviewed; 118 AA. AC Q9K1M9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40526.1}; GN OrderedLocusNames=NMB0057 {ECO:0000313|EMBL:AAF40526.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40526.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40526.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40526.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40526.1; -; Genomic_DNA. DR PIR; B81242; B81242. DR STRING; 122586.NMB0057; -. DR PaxDb; Q9K1M9; -. DR EnsemblBacteria; AAF40526; AAF40526; NMB0057. DR PATRIC; 20355119; VBINeiMen85645_0093. DR eggNOG; COG1555; LUCA. DR HOGENOM; HOG000257817; -. DR BioCyc; NMEN122586:GHGG-63-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010994; RuvA_2-like. DR SUPFAM; SSF47781; SSF47781; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 74 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 118 AA; 12742 MW; 7E5B1AB772EADB96 CRC64; MSVMAGRHPY GVRSGLRRNG LKLWDIHFRM TRFIVARCGL LFATLKGKTM KKMFVLFCML FSCAFSLAAV NINAASQQEL EALPGIGPAV LAKLKDQASV GAPAPKGPAK PVLPADKK // ID Q9JX96_NEIMB Unreviewed; 226 AA. AC Q9JX96; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42466.1}; GN OrderedLocusNames=NMB2158 {ECO:0000313|EMBL:AAF42466.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42466.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42466.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42466.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42466.1; -; Genomic_DNA. DR PIR; D81001; D81001. DR RefSeq; NP_275143.1; NC_003112.2. DR RefSeq; WP_002223230.1; NC_003112.2. DR ProteinModelPortal; Q9JX96; -. DR STRING; 122586.NMB2158; -. DR PaxDb; Q9JX96; -. DR EnsemblBacteria; AAF42466; AAF42466; NMB2158. DR GeneID; 903214; -. DR KEGG; nme:NMB2158; -. DR PATRIC; 20360512; VBINeiMen85645_2752. DR eggNOG; ENOG4108R96; Bacteria. DR eggNOG; COG1720; LUCA. DR HOGENOM; HOG000225518; -. DR OMA; YVPYADI; -. DR OrthoDB; EOG60SCKQ; -. DR BioCyc; NMEN122586:GHGG-2223-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.40.30.70; -; 1. DR InterPro; IPR023370; TsaA-like. DR InterPro; IPR023368; UPF0066_cons_site. DR Pfam; PF01980; UPF0066; 1. DR SUPFAM; SSF118196; SSF118196; 1. DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1. DR PROSITE; PS01318; TSAA_1; 1. DR PROSITE; PS51668; TSAA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 144 TsaA-like. {ECO:0000259|PROSITE:PS51668}. SQ SEQUENCE 226 AA; 25129 MW; 035A4D7C4E983069 CRC64; MTYTITPIGT ARSPYKQKFG IARQPGLVSA AKACIELNPK FTADSVRGLE DFDYVWISFI FHGVLDEGWA QMVRPPRLGG KQKMGVFATR SPHRPNHLGL SLLKLERIET GKPVRLYCSG ADLLDGTPIV DIKPYIPFVE SKPDAASGFV SGKPVELEVV WQENIGAENL SANTKNLISQ SIAQDPRPAY QNIPERIYVM NIADYEVRFQ IEENRATVID LSPTPL // ID Q9JZ34_NEIMB Unreviewed; 146 AA. AC Q9JZ34; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41691.1}; GN OrderedLocusNames=NMB1316 {ECO:0000313|EMBL:AAF41691.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41691.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41691.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41691.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41691.1; -; Genomic_DNA. DR PIR; C81096; C81096. DR STRING; 122586.NMB1316; -. DR PaxDb; Q9JZ34; -. DR EnsemblBacteria; AAF41691; AAF41691; NMB1316. DR BioCyc; NMEN122586:GHGG-1354-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 146 AA; 16664 MW; B477075643061581 CRC64; MNQRAHSSAV IRRRCAIHCF QAALSLYAVF FDALVECDLM NARKTRRSNH DGVVDTQRAQ GFRVCQRDTG IVQRHDRPAS GRLVFSNARK RVLTFAEGFQ LGKRFAFRRI FFCGFNLQNI VRILRILPNG EIAVSIGSPC RRSHQA // ID Q9JYY6_NEIMB Unreviewed; 184 AA. AC Q9JYY6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41743.1}; GN OrderedLocusNames=NMB1369 {ECO:0000313|EMBL:AAF41743.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41743.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41743.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41743.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41743.1; -; Genomic_DNA. DR PIR; F81090; F81090. DR RefSeq; NP_274387.1; NC_003112.2. DR RefSeq; WP_002222329.1; NC_003112.2. DR PaxDb; Q9JYY6; -. DR EnsemblBacteria; AAF41743; AAF41743; NMB1369. DR GeneID; 903791; -. DR KEGG; nme:NMB1369; -. DR PATRIC; 20358407; VBINeiMen85645_1715. DR HOGENOM; HOG000219000; -. DR OMA; RTHMKKI; -. DR OrthoDB; EOG6DNT9S; -. DR BioCyc; NMEN122586:GHGG-1407-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 184 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332264. FT COILED 19 46 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 184 AA; 20197 MW; 245C4402567E63A0 CRC64; MKKIIASALI ATFALAACQD DTQARLEQQQ KQIEALQQQL AQQADDTVYQ LTPEAVKDTI PAEAQANGNN GQPVTGKDGQ QYIYDQSTGS WLLQSLVGAA AGAFIGNALA NKFTRAGNQD SPVARRARAA YHQSARPNAR TSRDLNTRSL RAKQQAAQAQ RYRPTTRPPA NYRRPAMRGF GRRR // ID Q9JY61_NEIMB Unreviewed; 469 AA. AC Q9JY61; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42067.1}; GN OrderedLocusNames=NMB1721 {ECO:0000313|EMBL:AAF42067.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42067.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42067.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42067.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42067.1; -; Genomic_DNA. DR PIR; B81050; B81050. DR RefSeq; NP_274724.1; NC_003112.2. DR RefSeq; WP_002224963.1; NC_003112.2. DR STRING; 122586.NMB1721; -. DR PaxDb; Q9JY61; -. DR EnsemblBacteria; AAF42067; AAF42067; NMB1721. DR GeneID; 903380; -. DR KEGG; nme:NMB1721; -. DR PATRIC; 20359403; VBINeiMen85645_2207. DR eggNOG; ENOG4105CBB; Bacteria. DR eggNOG; COG3182; LUCA. DR HOGENOM; HOG000129765; -. DR OMA; RRLHFYI; -. DR OrthoDB; EOG6MPWQV; -. DR BioCyc; NMEN122586:GHGG-1776-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005625; PepSY-ass_TM. DR Pfam; PF03929; PepSY_TM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 23 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 173 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 223 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 382 404 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 424 453 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 469 AA; 52362 MW; 740213560A83DB88 CRC64; MDTQIKTEAD NQSNRRYLTV WRWHFYAGLL VMPFLTLLAV TGLGMLLFAN ITGKEGERIH VVPQATVQPL SVQAEAARSA VNPETSSVVQ YIAPRADDMV AVFRVNNEGK ATMVAVDPYT AKVVSTMPRN QGWYYTMDEI HSDMMLGAAG DYLLETAASL TIIMVVSGLY LWWVKRRGIK AMLLPSKGRA RSWWRNLHGT FGTWVSLILL LFCLSGIAWA GIWGGKFVQA WSQFPAGKWG VEPNPVSVVP THGEVLNDGK VKEVPWVLEL TPMPVSGTTV GKDGINPDEP MTLETVDRFA REIGFKGRYQ LNLPKGEDGV WTLSQDSMSY DMISPFADRT VHIDQYSGKI LADIRFDDYN PFGKFMAASI ALHMGTLGWW SVLANVLFCL AVIFIGISGC VMWWKRRPTG AVGIVPPAQK VKLPVWWMMA LPLLAIALLF PTSLLAIAVI WLLDTLLLSR IPVLRRWFK // ID Q9JZK5_NEIMB Unreviewed; 315 AA. AC Q9JZK5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41412.1}; GN OrderedLocusNames=NMB1011 {ECO:0000313|EMBL:AAF41412.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41412.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41412.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41412.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41412.1; -; Genomic_DNA. DR PIR; D81131; D81131. DR RefSeq; NP_274046.1; NC_003112.2. DR RefSeq; WP_002225287.1; NC_003112.2. DR STRING; 122586.NMB1011; -. DR PaxDb; Q9JZK5; -. DR EnsemblBacteria; AAF41412; AAF41412; NMB1011. DR GeneID; 903149; -. DR KEGG; nme:NMB1011; -. DR PATRIC; 20357551; VBINeiMen85645_1292. DR eggNOG; ENOG4105SAT; Bacteria. DR eggNOG; ENOG41120MJ; LUCA. DR OMA; HFEANNN; -. DR OrthoDB; EOG6J1DH0; -. DR BioCyc; NMEN122586:GHGG-1048-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 315 AA; 35079 MW; 6B02F7BFACC50C40 CRC64; MMIEKSISIV DGKEYSVFAV SHEFRYTFDE PILVADLISS LKAYETLTSS YLPAILNQLF DVKIQKIKVA VSEIERGSFL EKLIFNLFFK DEDAYNEFCL KIRKFLGTEN QDGSINMSKI IMFAMTTLLG VGAGYLLFKN PPQEKQAITN NIVTVINADS SVALDGEHLV SVVKEVTGSS KQKTAENVAK VYAPASKNNG SITLGTDDVR IEPVAQQTVA TLPKDVDLRD TPLTEDYTDI DVQIRATDRD KNSGWYAVID QIVPSRVRLE LPEDIDLNRL ANNATIRANV TVEFDLKQNG SRKPKKIILT SLSTD // ID Q9JZ91_NEIMB Unreviewed; 512 AA. AC Q9JZ91; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 68. DE SubName: Full=Peptidyl-prolyl cis-trans isomerase-related protein {ECO:0000313|EMBL:AAF41619.1}; GN OrderedLocusNames=NMB1238 {ECO:0000313|EMBL:AAF41619.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41619.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41619.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41619.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41619.1; -; Genomic_DNA. DR PIR; C81105; C81105. DR RefSeq; NP_274262.1; NC_003112.2. DR RefSeq; WP_002225194.1; NC_003112.2. DR ProteinModelPortal; Q9JZ91; -. DR STRING; 122586.NMB1238; -. DR PaxDb; Q9JZ91; -. DR EnsemblBacteria; AAF41619; AAF41619; NMB1238. DR GeneID; 903660; -. DR KEGG; nme:NMB1238; -. DR PATRIC; 20358073; VBINeiMen85645_1549. DR eggNOG; ENOG41084MA; Bacteria. DR eggNOG; ENOG410ZKQQ; LUCA. DR HOGENOM; HOG000218965; -. DR KO; K03770; -. DR OMA; PEMEKQM; -. DR OrthoDB; EOG6M9DS4; -. DR BioCyc; NMEN122586:GHGG-1275-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF13145; Rotamase_2; 1. DR SUPFAM; SSF109998; SSF109998; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF41619.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 230 372 PpiC. {ECO:0000259|Pfam:PF13145}. SQ SEQUENCE 512 AA; 56591 MW; E06BD7589F79DF42 CRC64; MFHSIEKYRT PAQVLLGLIA LTFVGFGVST VSHPGADYIV QVGDEKISDH SINNAIQNEQ ADGGGPSRDA VFQSLLQRAY LKQGAKLMGI SVSSEQIKQI IVDDPNFHDA NGKFDHALLN RYLSQRHMSE DQFVEEIRDQ FALQNLVNLV QNGVLVGDAQ AEQLIRLTQV NRTIRSHTFN PDEFIAQVKV SEADLQKFYN ANKKDYLLPQ AVKLEYVALN LKDFADKQTV SETEVKNAFE ERVARLPANE AKPSFEQEKA AVENELKMKK AVADFNKAKE KLGDDAFNHP SSLAEAAKNS GLKVETQETW LSRQDAQMSG MPENLINAVF SDDVLKKKHN SEVLTINSET AWVVRAKEVR EEKTLPFAEA KDAVRQAYIR TEAAKLAENK AKDVLTQLNG GKAVDVKWSE VSVLGAQQAR QSMPPEAYAE LLKAKPANGK PAYVRLIGLP APVIVEVQAV TPPDDIAAQL PLAKQALAQQ QSANTFDLLI RYFNGKIKQT KGAQSVDNGD GQ // ID Q9K0B4_NEIMB Unreviewed; 1815 AA. AC Q9K0B4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=IgA-specific serine endopeptidase {ECO:0000313|EMBL:AAF41117.1}; DE EC=3.4.21.72 {ECO:0000313|EMBL:AAF41117.1}; GN Name=iga {ECO:0000313|EMBL:AAF41117.1}; GN OrderedLocusNames=NMB0700 {ECO:0000313|EMBL:AAF41117.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41117.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41117.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41117.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41117.1; -; Genomic_DNA. DR PIR; C81169; C81169. DR RefSeq; NP_273742.1; NC_003112.2. DR RefSeq; WP_002225480.1; NC_003112.2. DR ProteinModelPortal; Q9K0B4; -. DR STRING; 122586.NMB0700; -. DR MEROPS; S06.001; -. DR PaxDb; Q9K0B4; -. DR EnsemblBacteria; AAF41117; AAF41117; NMB0700. DR GeneID; 902812; -. DR KEGG; nme:NMB0700; -. DR PATRIC; 20356735; VBINeiMen85645_0889. DR eggNOG; ENOG41063FY; Bacteria. DR eggNOG; COG3468; LUCA. DR HOGENOM; HOG000218846; -. DR KO; K01347; -. DR OMA; AAPQDYM; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NMEN122586:GHGG-728-MONOMER; -. DR BRENDA; 3.4.21.72; 3593. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.160.20.20; -; 1. DR Gene3D; 2.40.128.130; -; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR000710; Peptidase_S6. DR InterPro; IPR030396; Peptidase_S6_dom. DR InterPro; IPR004899; Pertactin_central. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF02395; Peptidase_S6; 1. DR Pfam; PF03212; Pertactin; 1. DR PRINTS; PR00921; IGASERPTASE. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF51126; SSF51126; 2. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS51691; PEPTIDASE_S6; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41117.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 1815 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332289. FT DOMAIN 28 311 Peptidase S6. FT {ECO:0000259|PROSITE:PS51691}. FT DOMAIN 1563 1815 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. FT COILED 1010 1078 {ECO:0000256|SAM:Coils}. FT COILED 1088 1130 {ECO:0000256|SAM:Coils}. FT COILED 1174 1363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1815 AA; 201078 MW; 2259D4D71762C57F CRC64; MKTKRFKINA ISLSIFLAYA LTPYSEAALV RDDVDYQIFR DFAENKGKFF VGATDLSVKN KQGQNIGNAL SNVPMIDFSV ADVNRRTLTV IDPQYAVSVK HVKGDEISYY GHHNGHLDVS NDENEYRSVA QNDYEPNKNW HHGNQGRLED YNMARLNKFV TEVAPIAPTS AGGGVETYKD KNRFSEFVRV GAGTQFEYNS RYNMTELSRA YRYAIAGTPY QDVNVTSNLN QEGLIGFGDN SKHHSPEKLK EVLSQNALTN YAVLGDSGSP LFAYDKQEKR WVFLGAYDYW AGYQKNSWQE WNIYKKEFAD EIKQRDNAGT IKGNGEHHWK TTGTNSHIGS TAVRLANNER DANNGQNVTF ENNGTLVLDQ NINQGAGGLF FKGDYTVKGI NNDITWLGAG IDVADGKKVV WQVKNPNGDR LAKIGKGTLE INGTGVNQGQ LKVGDGTVIL NQQADADKKV QAFSQVGIVS GRGTLVLNSS NQINPDNLYF GFRGGRLDAN GNDLTFEHIR NVDEGARIVN HNTGHASTIT LTGKSLITDP KTISIHYIQN NDDDDAGYYY YRPRKPIPQG KDLYFKNYRY YALKSGGSVN APMPENGQTE NNDWILMGST QEEAKKNAMN HKNNQRISGF SGFFGEENGK GHNGALNLNF NGKSAQNRFL LTGGTNLNGK ISVTQGNVLL SGRPTPHARD FVNKSSARKD AHFSKNNEVV FEDDWINRTF KATEIAVNQS ASFSSGRNVS DITANITATD NAKVNLGYKN GDEVCVRSDY TGYVTCNTGN LSDKALNSFG ATQINGNVNL NQNAALVLGK AALWGQIQGQ GNSRVSLNQH SKWHLTGDSQ VHNLSLADSH IHLNNASDAQ SANKYHTLKI NHLSGNGHFH YLTHLAKNLG DKVLVKESAS GHYQLHVQDK TGEPNQEGLN LFDASSVQDR SRLSVSLANN HVDLGALRYT IKTENGITRL YNPYAENRRR VKPAPSPATN TASQAQKATQ TDGAQIAKPQ NIVVAPPSPQ ANQAEEAKRQ QAKAEQVKRQ QAEAERKSAE LAKQKAEAER EARELATRQK AEQERSSAEL ARRHEKEREA AELSAKQKVE AEREAQALAV RRKAEAEEAK RQAAELARRH EKEREAAELS AKQRVGEEER RQTAQSQPQR RKRRAAPQDY MAASQDRPKR RGHRSVQQNN VEIAQAQAEL ARRQQEERKA AELLAKQRAE AEREAQALAA RRKAEAEEAK RQAAELAHRQ EAERKAAELS ANQKAAAEAQ ALAARQQKAL ARQQEEARKA AELAVKQKAE TERKTAELAK QRAAAEAAKR QQEARQTAEL ARRQEAERQA AELSAKQKAE TDREAAESAK RKAEEEEHRQ AAQSQPQRRK RRAAPQDYMA ASQNRPKRRG RRSTLPAPPS PSFDSSAYAA PRALHNPDWY ENDYEEIPLD ALEDENVSES VDTSDKQPQD NTELHEKYEN DYEEIPLDAL EDEDVSESVD TSDKQPQDNT ELHEKVETVS LQPRAAQPRA QAATQLQAQA AAQADAVSTN TNSALSDAMA STQSILLDTG ASLTRHIAQK SRADAEKNSV WMSNTGYGRD YASAQYRRFS SKRTQTQIGI DRSLSENMQI GGVLTYSDSQ HTFDQASGKN TFVQANLYGK YYLNDAWYVA GDIGAGSLRS RLQTQQKANF NRASIQTGLT LGNTLKINQF EIVPSAGIRY SRLSSADYKL GNDSVKVSSM SVKTLTAGLD FAYRFKVGNL TVKPLLSAAY FANYGKGGVN VGGNSFVYKA DNQQQYSAGA ALLYRNVTLN VNGSITKGKQ LEKQKSGQIK IQIRF // ID Q9JXV2_NEIMB Unreviewed; 146 AA. AC Q9JXV2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Putative ribosomal-protein-alanine acetyltransferase {ECO:0000313|EMBL:AAF42206.1}; GN OrderedLocusNames=NMB1872 {ECO:0000313|EMBL:AAF42206.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42206.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42206.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42206.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42206.1; -; Genomic_DNA. DR PIR; F81032; F81032. DR RefSeq; NP_274868.1; NC_003112.2. DR RefSeq; WP_002225787.1; NC_003112.2. DR ProteinModelPortal; Q9JXV2; -. DR STRING; 122586.NMB1872; -. DR PaxDb; Q9JXV2; -. DR EnsemblBacteria; AAF42206; AAF42206; NMB1872. DR GeneID; 904316; -. DR KEGG; nme:NMB1872; -. DR PATRIC; 20359775; VBINeiMen85645_2393. DR eggNOG; ENOG41080T4; Bacteria. DR eggNOG; COG0456; LUCA. DR HOGENOM; HOG000078523; -. DR KO; K03789; -. DR OMA; LEYWYAH; -. DR OrthoDB; EOG6NKR5W; -. DR BioCyc; NMEN122586:GHGG-1928-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR006464; Rbsml_AcTrfase. DR Pfam; PF13673; Acetyltransf_10; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR01575; rimI; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42206.1}. FT DOMAIN 1 146 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 146 AA; 16261 MW; 8E816E729B748E45 CRC64; MNIRRAVCAD CEELAALDAV CNPSAWTQRQ FESALVSPSE QVFLAEKDGG IAAFIVWQNL PDESELHLIA TAPECRRQGI ASALLEYWFT HLPEDTQRLL LEVRAGNTAA QALYTAHGFS ITGRRKNYYR TADGKTEDAV LMEKIC // ID Q7DDL4_NEIMB Unreviewed; 103 AA. AC Q7DDL4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894}; GN OrderedLocusNames=NMB0773 {ECO:0000313|EMBL:AAF41186.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41186.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41186.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41186.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol CC subfamily. {ECO:0000256|PIRNR:PIRNR005894}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41186.1; -; Genomic_DNA. DR PIR; B81160; B81160. DR RefSeq; NP_273815.1; NC_003112.2. DR RefSeq; WP_002214004.1; NC_003112.2. DR ProteinModelPortal; Q7DDL4; -. DR STRING; 122586.NMB0773; -. DR PaxDb; Q7DDL4; -. DR EnsemblBacteria; AAF41186; AAF41186; NMB0773. DR GeneID; 902888; -. DR KEGG; nme:NMB0773; -. DR PATRIC; 20356919; VBINeiMen85645_0978. DR eggNOG; ENOG4105M2J; Bacteria. DR eggNOG; COG0278; LUCA. DR HOGENOM; HOG000095211; -. DR KO; K07390; -. DR OMA; VPAAPQC; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-804-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014434; Monothiol_GRX. DR InterPro; IPR004480; Monothiol_GRX-rel. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR10293; PTHR10293; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR PIRSF; PIRSF005894; Monothiol_GRX; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00365; TIGR00365; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR005894-2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|PIRSR:PIRSR005894-2}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR005894-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR005894-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 103 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. FT METAL 30 30 Iron-sulfur (2Fe-2S); shared with dimeric FT partner. {ECO:0000256|PIRSR:PIRSR005894- FT 2}. SQ SEQUENCE 103 AA; 11524 MW; 599B954E95F9D6DF CRC64; MASIHDQIKE VVTTHRVVLF MKGTKQFPQC GFSSRAVQIL NAAGCTDYVT VNVLENPEVR QGIKEYSDWP TIPQLYVNGE FVGGSDILME MYEAGELQEL LKA // ID Q9K047_NEIMB Unreviewed; 106 AA. AC Q9K047; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41188.1}; GN OrderedLocusNames=NMB0775 {ECO:0000313|EMBL:AAF41188.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41188.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41188.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41188.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41188.1; -; Genomic_DNA. DR PIR; D81160; D81160. DR RefSeq; NP_273817.1; NC_003112.2. DR RefSeq; WP_002222730.1; NC_003112.2. DR STRING; 122586.NMB0775; -. DR PaxDb; Q9K047; -. DR EnsemblBacteria; AAF41188; AAF41188; NMB0775. DR GeneID; 902890; -. DR KEGG; nme:NMB0775; -. DR PATRIC; 20356925; VBINeiMen85645_0981. DR eggNOG; ENOG4106U8J; Bacteria. DR eggNOG; COG4390; LUCA. DR HOGENOM; HOG000123173; -. DR OMA; FAEHVED; -. DR OrthoDB; EOG6D8BG7; -. DR BioCyc; NMEN122586:GHGG-806-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR016755; UCP019302. DR Pfam; PF10084; DUF2322; 1. DR PIRSF; PIRSF019302; UCP019302; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 106 AA; 11582 MW; D2EA5C892C1CC77A CRC64; MNFQDYLATF PSIDHLGGLD VQDADGKTVH HIPAVQGKLG SLKLYNALAE RFDGKLGKEA AEQGLIWFAE HVADARAHPG KHPNIDLLEN VVQSGETWLL KPLSAQ // ID Q9K1I9_NEIMB Unreviewed; 49 AA. AC Q9K1I9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40594.1}; GN OrderedLocusNames=NMB0135 {ECO:0000313|EMBL:AAF40594.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40594.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40594.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40594.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40594.1; -; Genomic_DNA. DR PIR; H81233; H81233. DR RefSeq; NP_273193.1; NC_003112.2. DR RefSeq; WP_002215381.1; NC_003112.2. DR STRING; 122586.NMB0135; -. DR PaxDb; Q9K1I9; -. DR EnsemblBacteria; AAF40594; AAF40594; NMB0135. DR GeneID; 902243; -. DR KEGG; nme:NMB0135; -. DR PATRIC; 20355291; VBINeiMen85645_0175. DR HOGENOM; HOG000218662; -. DR KO; K07280; -. DR OrthoDB; EOG61047R; -. DR BioCyc; NMEN122586:GHGG-145-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 49 AA; 5860 MW; 8B7B27264DB66E04 CRC64; MSAALWHKKL SWKGFTPQIN FRYNKINSNM PAFYSRSGKE RFVSIEKTY // ID Q9JXD4_NEIMB Unreviewed; 193 AA. AC Q9JXD4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279}; DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279}; GN OrderedLocusNames=NMB2099 {ECO:0000313|EMBL:AAF42416.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42416.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42416.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42416.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + 5-formyltetrahydrofolate = ADP + CC phosphate + 5,10-methenyltetrahydrofolate. CC {ECO:0000256|RuleBase:RU361279}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361279}; CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase CC family. {ECO:0000256|RuleBase:RU361279}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42416.1; -; Genomic_DNA. DR PIR; D81006; D81006. DR RefSeq; NP_275087.1; NC_003112.2. DR RefSeq; WP_002244352.1; NC_003112.2. DR ProteinModelPortal; Q9JXD4; -. DR STRING; 122586.NMB2099; -. DR PaxDb; Q9JXD4; -. DR EnsemblBacteria; AAF42416; AAF42416; NMB2099. DR GeneID; 903943; -. DR KEGG; nme:NMB2099; -. DR PATRIC; 20360368; VBINeiMen85645_2681. DR eggNOG; ENOG4107YJP; Bacteria. DR eggNOG; COG0212; LUCA. DR HOGENOM; HOG000007299; -. DR OMA; PERPSEM; -. DR OrthoDB; EOG6RVG1P; -. DR BioCyc; NMEN122586:GHGG-2164-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10420; -; 1. DR InterPro; IPR002698; FTHF_cligase. DR InterPro; IPR024185; FTHF_cligase-like. DR PANTHER; PTHR23407:SF1; PTHR23407:SF1; 1. DR Pfam; PF01812; 5-FTHF_cyc-lig; 1. DR PIRSF; PIRSF006806; FTHF_cligase; 1. DR TIGRFAMs; TIGR02727; MTHFS_bact; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU361279}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|RuleBase:RU361279}; KW Metal-binding {ECO:0000256|RuleBase:RU361279}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU361279}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 193 AA; 22199 MW; B35B938673EC4334 CRC64; MRNEEKRALR RELRGRRSQM GRDVRAAATV KINHLLKRYI KKGRKIGVYW PMGKELRLDG FVRAAQKRGA ELYLPYIEPR SRRMWFTPYP ADGVKQERKR GRAKLHVPQF AGRKKRVHDL NLLLVPVVGM DRLGYRLGQA GGYYDATLSA MKYRLQAKTV GVGFACQLVD RLPVEAHDRS LDGFVSEAGI LCF // ID Q9K0R9_NEIMB Unreviewed; 640 AA. AC Q9K0R9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40943.1}; GN OrderedLocusNames=NMB0511 {ECO:0000313|EMBL:AAF40943.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40943.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40943.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40943.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40943.1; -; Genomic_DNA. DR PIR; F81191; F81191. DR RefSeq; NP_273557.1; NC_003112.2. DR RefSeq; WP_002225600.1; NC_003112.2. DR STRING; 122586.NMB0511; -. DR PaxDb; Q9K0R9; -. DR EnsemblBacteria; AAF40943; AAF40943; NMB0511. DR GeneID; 902627; -. DR KEGG; nme:NMB0511; -. DR PATRIC; 20356268; VBINeiMen85645_0654. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000027880; -. DR OrthoDB; EOG6FRD4R; -. DR BioCyc; NMEN122586:GHGG-536-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 230 381 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 398 445 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 640 AA; 66849 MW; F9B07B242BB53912 CRC64; MQLLAAEGIH QHQLNVQKST RFIGIKVGKS NYSKNELNET KLPVRVIAQT AKTRSGWDTV LEGTEFKTTL SGADIQAGVG EKARADAKII LKGIVNRIQT EEKLESNSTV WQKQAGSGST VETLKLPSFE GPALPKLTAP GGYIADIPKG NLKTEIEKLA KQPEYAYLKQ LQTVKDVNWN QVQLAYDKWD YKQEGLTGAG AAIIALAVTV VTSGAGTGAV LGLNGAAAAA TDAAFASLAS QASVSFINNK GNIGNTLKEL GRSSTVKNLM VAVATAGVAD KIGASALNNV SDKQWINNLT VNLANAGSAA LINTAVNGGS LKDNLEANIL AALVNTAHGE AASKIKQLDQ HYIAHKIAHA IAGCAAAAAN KGKCQDGAIG AAVGEILGET LLDGRDPGSL NVKDRAKIIA KAKLAAGAVA ALSKGDVSTA ANAAAVAVEN NSLNDIQDRL LSGNYALCMS AGGAESFCES YRPLGLPHFV SVSGEMKLPN KFGNRMVNGK LIINTRNGNV YFSVGKIWST VKSTKSNISG VSVGWVLNVS PNDYLKEASM NDFRNSNQNK AYAEMISQTL VGESVGGSLC LTRACFSVSS TISKSKSPFK DSKIIGEIGL GSGVAAGVEK TIYIGNIKDI DKFISANIKK // ID Q7DDB8_NEIMB Unreviewed; 69 AA. AC Q7DDB8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Tautomerase {ECO:0000256|RuleBase:RU362032}; DE EC=5.3.2.- {ECO:0000256|RuleBase:RU362032}; GN OrderedLocusNames=NMB1474 {ECO:0000313|EMBL:AAF41831.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41831.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41831.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41831.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family. CC {ECO:0000256|RuleBase:RU362032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41831.1; -; Genomic_DNA. DR PIR; H81078; H81078. DR RefSeq; NP_274483.1; NC_003112.2. DR RefSeq; WP_002212949.1; NC_003112.2. DR ProteinModelPortal; Q7DDB8; -. DR PaxDb; Q7DDB8; -. DR EnsemblBacteria; AAF41831; AAF41831; NMB1474. DR GeneID; 903896; -. DR KEGG; nme:NMB1474; -. DR PATRIC; 20358713; VBINeiMen85645_1866. DR eggNOG; ENOG4105VSH; Bacteria. DR eggNOG; COG1942; LUCA. DR HOGENOM; HOG000077848; -. DR KO; K01821; -. DR OMA; WGIGGET; -. DR OrthoDB; EOG62ZHW8; -. DR BioCyc; NMEN122586:GHGG-1514-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. DR InterPro; IPR004370; 4-oxalocrotonate_tautomerase. DR InterPro; IPR014347; Tautomerase/MIF_sf. DR InterPro; IPR018191; Tautomerase_Pseudo-typ. DR Pfam; PF01361; Tautomerase; 1. DR SUPFAM; SSF55331; SSF55331; 1. DR TIGRFAMs; TIGR00013; taut; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU362032}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 64 4-oxalocrotonate_tautomerase. FT {ECO:0000259|Pfam:PF01361}. SQ SEQUENCE 69 AA; 7350 MW; 5C27AE656573792C CRC64; MPYVNIKVTG GKEAPTAAQK AELIGGVTEL LARVLGKNPE TTVVVIDEVD TDNWGIGGKS VSERRKEGR // ID Q9K120_NEIMB Unreviewed; 467 AA. AC Q9K120; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=MafB-related protein {ECO:0000313|EMBL:AAF62308.1}; GN OrderedLocusNames=NMB0374 {ECO:0000313|EMBL:AAF62308.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62308.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62308.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62308.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62308.1; -; Genomic_DNA. DR RefSeq; NP_273423.1; NC_003112.2. DR RefSeq; WP_002221999.1; NC_003112.2. DR STRING; 122586.NMB0374; -. DR PaxDb; Q9K120; -. DR EnsemblBacteria; AAF62308; AAF62308; NMB0374. DR GeneID; 902489; -. DR KEGG; nme:NMB0374; -. DR PATRIC; 20355907; VBINeiMen85645_0471. DR eggNOG; ENOG41068QY; Bacteria. DR eggNOG; ENOG410XWQY; LUCA. DR HOGENOM; HOG000219102; -. DR OrthoDB; EOG66F037; -. DR BioCyc; NMEN122586:GHGG-396-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR028905; Tox-REase-3_dom. DR Pfam; PF06255; DUF1020; 1. DR Pfam; PF15647; Tox-REase-3; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 467 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327885. FT DOMAIN 359 464 Tox-REase-3. {ECO:0000259|Pfam:PF15647}. SQ SEQUENCE 467 AA; 51145 MW; 9DF25C16B1C317C9 CRC64; MKPLRRLTNL LAACAVAAAA LIQPALAADL AQDPFITDNA QRQHYEPGGK YHLFGDPRGS VSDRTGKINV IQDYTHQMGN LLIQQANING TIGYHTRFSG HGHEEHAPFD NHAADSASEE KGNVDEGFTV YRLNWEGHEH HPADAYDGPK GGNYPKPTGA RDEYTYHVNG TARSIKLNPT DTRSIRQRIS DNYSNLGSNF SDRADEANRK MFEHNAKLDR WGNSMEFING VAAGALNPFI SAGEALGIGD ILYGTRYAID KAAMRNIAPL PAEGKFAVIG GLGSVAGFEK NTREAVDRWI QENPNAAETV EAVFNVAAAA KVAKLAKAAK PGKAAVSGDF ADSYKKKLAL SDSARQLYQN AKYREALDIH YEDLIRRKTD GSSKFINGRE IDAVTNDALI QAKRTISAID KPKNFLNQKN RKQIKATIEA ANQQGKRAEF WFKYGVHSQV KSYIESKGGI VKTGLGD // ID Q9K1L7_NEIMB Unreviewed; 62 AA. AC Q9K1L7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40556.1}; GN OrderedLocusNames=NMB0094 {ECO:0000313|EMBL:AAF40556.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40556.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40556.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40556.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40556.1; -; Genomic_DNA. DR PIR; F81239; F81239. DR STRING; 122586.NMB0094; -. DR PaxDb; Q9K1L7; -. DR EnsemblBacteria; AAF40556; AAF40556; NMB0094. DR OrthoDB; EOG63NMTK; -. DR BioCyc; NMEN122586:GHGG-100-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 55 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 62 AA; 7311 MW; E640B7264545F762 CRC64; MKKYSDYFKY LIFFLILLPT NYLVSHYVVQ TSMSMLSILS SSIITTCLFF VFTNLSQSKK HK // ID Q7DDA1_NEIMB Unreviewed; 223 AA. AC Q7DDA1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41919.1}; GN OrderedLocusNames=NMB1565 {ECO:0000313|EMBL:AAF41919.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41919.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41919.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41919.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41919.1; -; Genomic_DNA. DR PIR; A81068; A81068. DR RefSeq; NP_274572.1; NC_003112.2. DR RefSeq; WP_002222212.1; NC_003112.2. DR STRING; 122586.NMB1565; -. DR PaxDb; Q7DDA1; -. DR EnsemblBacteria; AAF41919; AAF41919; NMB1565. DR GeneID; 904140; -. DR KEGG; nme:NMB1565; -. DR PATRIC; 20358992; VBINeiMen85645_2015. DR eggNOG; ENOG4106T62; Bacteria. DR eggNOG; ENOG410YIYG; LUCA. DR HOGENOM; HOG000219031; -. DR OMA; YNIKYSS; -. DR OrthoDB; EOG62NX3T; -. DR BioCyc; NMEN122586:GHGG-1606-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR021457; DUF3108. DR Pfam; PF11306; DUF3108; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 223 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287537. SQ SEQUENCE 223 AA; 24062 MW; 5D8C787F6EA3F4D1 CRC64; MMKTFKNIFS AAILSAALPC AYAAGLPQSA VLHYSGSYGI PATMTFERSG NAYKIVSTIK VPLYNIRFES GGTVVGNTLH PTYYRDIRRG KLYAEAKFAD GSVTYGKAGE SKTEQSPKAM DLFTLAWQLA ANDAKLPPGL KITNGKKLYS VGGLNKAGTG KYSIGGVETE VVKYRVRRGD DAVMYFFAPS LNNIPAQIGY TDDGKTYTLK LKSVQINGQA AKP // ID Q9K193_NEIMB Unreviewed; 766 AA. AC Q9K193; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 105. DE SubName: Full=ATP-dependent DNA helicase RecQ {ECO:0000313|EMBL:AAF40728.1}; DE EC=3.6.1.- {ECO:0000313|EMBL:AAF40728.1}; GN Name=recQ {ECO:0000313|EMBL:AAF40728.1}; GN OrderedLocusNames=NMB0274 {ECO:0000313|EMBL:AAF40728.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40728.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40728.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40728.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40728.1; -; Genomic_DNA. DR PIR; G81216; G81216. DR RefSeq; NP_273330.1; NC_003112.2. DR RefSeq; WP_002221929.1; NC_003112.2. DR ProteinModelPortal; Q9K193; -. DR SMR; Q9K193; 3-506. DR STRING; 122586.NMB0274; -. DR PaxDb; Q9K193; -. DR EnsemblBacteria; AAF40728; AAF40728; NMB0274. DR GeneID; 902385; -. DR KEGG; nme:NMB0274; -. DR PATRIC; 20355634; VBINeiMen85645_0341. DR eggNOG; ENOG4105C9U; Bacteria. DR eggNOG; COG0514; LUCA. DR HOGENOM; HOG000044388; -. DR KO; K03654; -. DR OMA; WDATEPA; -. DR OrthoDB; EOG6ZSPDC; -. DR BioCyc; NMEN122586:GHGG-289-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.150.80; -; 3. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ. DR InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR010997; HRDC-like. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032284; RecQ_Zn-bd. DR InterPro; IPR018982; RQC_domain. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00570; HRDC; 3. DR Pfam; PF16124; RecQ_Zn_bind; 1. DR Pfam; PF09382; RQC; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00341; HRDC; 3. DR SMART; SM00956; RQC; 1. DR SUPFAM; SSF47819; SSF47819; 3. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01389; recQ; 1. DR TIGRFAMs; TIGR00614; recQ_fam; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50967; HRDC; 3. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAF40728.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|RuleBase:RU000452, ECO:0000313|EMBL:AAF40728.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAF40728.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAF40728.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 27 195 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 216 366 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 524 604 HRDC. {ECO:0000259|PROSITE:PS50967}. FT DOMAIN 610 690 HRDC. {ECO:0000259|PROSITE:PS50967}. FT DOMAIN 691 766 HRDC. {ECO:0000259|PROSITE:PS50967}. SQ SEQUENCE 766 AA; 85960 MW; 01726F0D2C14D09F CRC64; MHRPTAKQIL HEVFGYPEFR GRQEAVINTL AGGGSLTVLM PTGGGKSLCY QIPALMREGV AVVVSPLIAL MNDQVANLHA AGIEAAAVNS GTSADEAREI ADRLAQGRLK LLYVAPERLV TDRFLRFLDQ QTVSLFAIDE AHCVSQWGHD FRPEYQQLGM LAERYPNVPR IALTATADAA TRADIKHYLH LDDAPEFVSS FDRPNIYYQV IEKNNGKKQL LDFIRKEMTG QSGIVYCLSR KKVEDVAQFL RENGLNAIPY HAGLSMDVRE ENQRRFTHED NIIVVATVAF GMGIDKPDVR FVAHLDMPQS VEHFYQESGR AGRDGLPAAS WLCYGLNDWV LLRERIAEGN SDEVQKQIEM QKLDAMLAVC ETAACRRVLL LKHFGEASEP CGHCDNCLHP PVRFDGTVLV QKLLSCVYRA GQRFAAGYIT NILRGKSDDW IRGNRHEQLS TFGIGTELSD KEWRSVIRQC ISLGYLTVNI TRYQALQLTE AAKKVLKGET EVMLRPLKRD KPAARTLKDN WLRTEREERL WQALRVWRMK QAEAEGIPAY MIFGDKTLRD LVEKMPQDLN GLHDIYGLGE AKIDRFGHGI LEVCRNAAGF SRDAVIRPQT EREQQLRQKL EAWRYEQARA ENCALHAVLS DESLADMLAD TPETETDLEG VYGLGSVRAA KYGRDILAVC RPFSDGIDET AKRKRRLMRA LIQWCGETAK HEQSEPYRIL SKAALRAIAA KQPEGLAELA AVYGVGEEKA ARYGAAVLAV LERNAV // ID Q9JXI3_NEIMB Unreviewed; 230 AA. AC Q9JXI3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42356.1}; GN OrderedLocusNames=NMB2035 {ECO:0000313|EMBL:AAF42356.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42356.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42356.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42356.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42356.1; -; Genomic_DNA. DR PIR; H81013; H81013. DR RefSeq; NP_275026.1; NC_003112.2. DR RefSeq; WP_002225684.1; NC_003112.2. DR STRING; 122586.NMB2035; -. DR PaxDb; Q9JXI3; -. DR EnsemblBacteria; AAF42356; AAF42356; NMB2035. DR GeneID; 904063; -. DR KEGG; nme:NMB2035; -. DR PATRIC; 20360190; VBINeiMen85645_2594. DR eggNOG; ENOG4105MD7; Bacteria. DR eggNOG; COG1451; LUCA. DR HOGENOM; HOG000218649; -. DR KO; K07043; -. DR OMA; CHLAHAD; -. DR OrthoDB; EOG6WHNTR; -. DR BioCyc; NMEN122586:GHGG-2097-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002725; DUF45. DR Pfam; PF01863; DUF45; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 230 AA; 26289 MW; 0E9D797A7B33E323 CRC64; MTAFVHTLSD GMELTVEIKR RAKKNLIIRP AGTHTVRISV PPCFSVSALN RWLYENEAVL RQTLAKTPPP QTAENRLPES ILFHGRQLAL TAHQDTQILL MPSEIRVPEG APEKQLALLR DFLERQAHSY LIPRLERHAR TTQLFPASSS LTSAKTFWGV CRKTTGIRFN WRLVGAPEYV ADYVCIHELC HLAHPDHSPA FWELTRRFAP YTPKAKQWLK IHGRELFALG // ID Q9JZA6_NEIMB Unreviewed; 52 AA. AC Q9JZA6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41597.1}; GN OrderedLocusNames=NMB1215 {ECO:0000313|EMBL:AAF41597.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41597.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41597.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41597.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41597.1; -; Genomic_DNA. DR PIR; C81109; C81109. DR RefSeq; NP_274240.1; NC_003112.2. DR RefSeq; WP_010980908.1; NC_003112.2. DR STRING; 122586.NMB1215; -. DR PaxDb; Q9JZA6; -. DR EnsemblBacteria; AAF41597; AAF41597; NMB1215. DR GeneID; 903637; -. DR KEGG; nme:NMB1215; -. DR BioCyc; NMEN122586:GHGG-1252-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 52 AA; 6144 MW; FADBB65C18D2E1CA CRC64; MDQQPLLKLP NSHIIIWRMD GLGKIFSQLK NNDNLFIEAY LRPVNFHSNS FE // ID Q9K100_NEIMB Unreviewed; 256 AA. AC Q9K100; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 92. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AAF40839.1}; DE EC=3.1.11.2 {ECO:0000313|EMBL:AAF40839.1}; GN Name=xthA {ECO:0000313|EMBL:AAF40839.1}; GN OrderedLocusNames=NMB0399 {ECO:0000313|EMBL:AAF40839.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40839.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40839.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40839.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2JC4} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=17318183; DOI=10.1038/sj.emboj.7601593; RA Carpenter E.P., Corbett A., Thomson H., Adacha J., Jensen K., RA Bergeron J., Kasampalidis I., Exley R., Winterbotham M., Tang C., RA Baldwin G.S., Freemont P.; RT "AP endonuclease paralogues with distinct activities in DNA repair and RT bacterial pathogenesis."; RL EMBO J. 26:1363-1372(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40839.1; -; Genomic_DNA. DR PIR; G81204; G81204. DR RefSeq; NP_273448.1; NC_003112.2. DR RefSeq; WP_002222015.1; NC_003112.2. DR PDB; 2JC4; X-ray; 1.90 A; A=1-256. DR PDBsum; 2JC4; -. DR ProteinModelPortal; Q9K100; -. DR SMR; Q9K100; 1-256. DR STRING; 122586.NMB0399; -. DR PaxDb; Q9K100; -. DR EnsemblBacteria; AAF40839; AAF40839; NMB0399. DR GeneID; 902514; -. DR KEGG; nme:NMB0399; -. DR PATRIC; 20355961; VBINeiMen85645_0498. DR eggNOG; ENOG4105CGK; Bacteria. DR eggNOG; COG0708; LUCA. DR HOGENOM; HOG000034587; -. DR KO; K01142; -. DR OMA; CTSCEVD; -. DR OrthoDB; EOG60SCPF; -. DR BioCyc; NMEN122586:GHGG-421-MONOMER; -. DR EvolutionaryTrace; Q9K100; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.60.10.10; -; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR PANTHER; PTHR22748; PTHR22748; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; SSF56219; 1. DR TIGRFAMs; TIGR00633; xth; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2JC4}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF40839.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 247 Endo/exonuclease/phosphatase. FT {ECO:0000259|Pfam:PF03372}. FT DISULFID 156 168 {ECO:0000213|PDB:2JC4}. SQ SEQUENCE 256 AA; 29155 MW; D8B1AB6E2A675ACE CRC64; MKITTWNVNS LNVRLPQVQN LLADNPPDIL VLQELKLDQD KFPAAALQMM GWHCVWSGQK TYNGVAIVSR SVPQDVHFGL PALPDDPQRR VIAATVSGVR VINVYCVNGE ALDSPKFKYK EQWFAALTEF VRDEMTRHGK LVLLGDFNIA PADADCYDPE KWHEKIHCSS VERQWFQNLL DLGLTDSLRQ VHPEGAFYTW FDYRGAMFQR KLGLRIDHIL VSPAMAAALK DVRVDLETRA LERPSDHAPV TAEFDW // ID Q9JYS3_NEIMB Unreviewed; 498 AA. AC Q9JYS3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Ferredoxin, 4Fe-4S bacterial type {ECO:0000313|EMBL:AAF41813.1}; GN OrderedLocusNames=NMB1454 {ECO:0000313|EMBL:AAF41813.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41813.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41813.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41813.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41813.1; -; Genomic_DNA. DR PIR; G81081; G81081. DR RefSeq; NP_274465.1; NC_003112.2. DR RefSeq; WP_002219062.1; NC_003112.2. DR ProteinModelPortal; Q9JYS3; -. DR STRING; 122586.NMB1454; -. DR PaxDb; Q9JYS3; -. DR EnsemblBacteria; AAF41813; AAF41813; NMB1454. DR GeneID; 903876; -. DR KEGG; nme:NMB1454; -. DR PATRIC; 20358651; VBINeiMen85645_1835. DR eggNOG; ENOG4105C58; Bacteria. DR eggNOG; COG0348; LUCA. DR HOGENOM; HOG000284963; -. DR OMA; DKNTYIV; -. DR OrthoDB; EOG6WDSCH; -. DR BioCyc; NMEN122586:GHGG-1494-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR014116; Cyt_c_oxidase_cbb3_FixG. DR InterPro; IPR032879; FixG_C. DR InterPro; IPR013783; Ig-like_fold. DR Pfam; PF13746; Fer4_18; 1. DR Pfam; PF12801; Fer4_5; 1. DR Pfam; PF11614; FixG_C; 1. DR TIGRFAMs; TIGR02745; ccoG_rdxA_fixG; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 230 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 360 378 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 277 305 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 309 332 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 498 AA; 55596 MW; F81D32A3DD05353D CRC64; MTTENQAGSP ASGIGTSEQT KAAPKAKKTF DPRASVIQIH PEGERIHPKK AEGRFAKLRI AAVLATQFVF YVIPWFNWSG RQAVVFNIPE RHFFIFGLSL GVGDLIYLAL LLMICAFGLF WWTTIAGRLW CGYSCPQTVY TEIMLWIDNL VEGDRNKRLK LEKSPWNFTK IRIKATKYLL IFLVCAWTGI TFAGWFVPIR QFVPDLFTGA AGGGAMFAAA FYGFMTFFFA HIMREKVCLH MCPYARFQSA MFDKDTLIVS YDAERGEPRG ARKKTVNKEE AGLGDCINCA MCVQVCPVGI DIRNGLQYQC IGCAACIDAC DEIMDKMGYP RGLIRYTTES ALEHEYSEKD IKKRLLRPRV AGYGAVLALV IIAFLAGLST RKMVEVDILK DRGVLVRENA KGWLENAYSL RIINKSEKEQ LITASVKGFD EIALTGLPEG GIKVAPRETV TLPVQVSTIP EYADKGSHPI EFTFQYRESG APDGKPVVLE EDATFIGE // ID Q9K0H8_NEIMB Unreviewed; 379 AA. AC Q9K0H8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574}; GN Name=potD-2 {ECO:0000313|EMBL:AAF41049.1}; GN OrderedLocusNames=NMB0623 {ECO:0000313|EMBL:AAF41049.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41049.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41049.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41049.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine. {ECO:0000256|PIRNR:PIRNR019574}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR019574}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein CC PotD/PotF family. {ECO:0000256|PIRNR:PIRNR019574}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41049.1; -; Genomic_DNA. DR PIR; D81176; D81176. DR RefSeq; NP_273667.1; NC_003112.2. DR RefSeq; WP_002244039.1; NC_003112.2. DR ProteinModelPortal; Q9K0H8; -. DR STRING; 122586.NMB0623; -. DR PaxDb; Q9K0H8; -. DR EnsemblBacteria; AAF41049; AAF41049; NMB0623. DR GeneID; 902736; -. DR KEGG; nme:NMB0623; -. DR PATRIC; 20356539; VBINeiMen85645_0789. DR eggNOG; ENOG4107RUE; Bacteria. DR eggNOG; COG0687; LUCA. DR HOGENOM; HOG000263815; -. DR KO; K02055; -. DR OMA; SVYPPQA; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NMEN122586:GHGG-649-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1. DR PRINTS; PR00909; SPERMDNBNDNG. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Periplasm {ECO:0000256|PIRNR:PIRNR019574}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|PIRNR:PIRNR019574}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 379 Putrescine-binding periplasmic protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327878. SQ SEQUENCE 379 AA; 41208 MW; BC1B87F6CE3A858B CRC64; MKKTLVAAAI LSLALTACGG GSDTAAQTPS AKPEAEQSGK LNIYNWSDYV DPETVAAFEK ETGIKTRSDY YDSNETLEAK VLTGKSGYDL TAPSIANVGR QIKAGAYQKI DKAQIPHYGN IDKDLLKMME AVDPGNEYAV PYFWGINTLA INTQQVKKAL GTDKLPENEW DLVFKPEYTA KLKSCGISYF DSAIEQIPLA LHYLGKDPNS ENPEDIKAAV DMMKAVRGDV KRFSSSGYID DMAAGNLCAA IGYGGDLNIA KTRAEEAANG VEIKVLTPKT GVGVWVDSFM IPRDAQNVAN AHRYIDYTLR PEVAAKNGSF VTYAPASRPA RELMDEKYTS DASIFPNKEL MEKSFIVSPK SAESVKLGVK LWQGLKAGK // ID Q9JXF9_NEIMB Unreviewed; 407 AA. AC Q9JXF9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Probable hydroxymethylpyrimidine transporter CytX {ECO:0000313|EMBL:AAF42386.1}; GN Name=cytX {ECO:0000313|EMBL:AAF42386.1}; GN OrderedLocusNames=NMB2067 {ECO:0000313|EMBL:AAF42386.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42386.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42386.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42386.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42386.1; -; Genomic_DNA. DR PIR; G81010; G81010. DR RefSeq; NP_275057.1; NC_003112.2. DR RefSeq; WP_002225706.1; NC_003112.2. DR STRING; 122586.NMB2067; -. DR PaxDb; Q9JXF9; -. DR EnsemblBacteria; AAF42386; AAF42386; NMB2067. DR GeneID; 904005; -. DR KEGG; nme:NMB2067; -. DR PATRIC; 20360294; VBINeiMen85645_2647. DR eggNOG; ENOG4107UPT; Bacteria. DR eggNOG; COG1457; LUCA. DR HOGENOM; HOG000218719; -. DR OMA; FGLKGSW; -. DR OrthoDB; EOG6SFPCB; -. DR BioCyc; NMEN122586:GHGG-2130-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015209; F:cytosine transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR030191; CodB. DR InterPro; IPR001248; Pur-cyt_permease. DR InterPro; IPR012732; Thia_CytX. DR PANTHER; PTHR30569; PTHR30569; 1. DR Pfam; PF02133; Transp_cyt_pur; 1. DR TIGRFAMs; TIGR02358; thia_cytX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 237 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 311 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 317 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 350 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 373 396 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 407 AA; 42415 MW; 2417689969DEA6B5 CRC64; MSGNASSPSS SSAIGLIWFG AAVSIAEIST GTLLAPLGWQ RGLAALLLGH AVGGALFFAA AYIGALTGRS SMESVRLSFG KRGSVLFSVA NMLQLAGWTA VMIYAGATVS SALGKVLWDG ESFVWWALAN GALIVLWLVF GARKTGGLKT VSMLLMLLAV LWLSAEVFST AGSTAAQVSD GMSFGTAVEL SAVMPLSWLP LAADYTRHAR RPFAATLTAT LAYTLTGCWM YALGLAAALF TGETDVAKIL LGAGLGAAGI LAVVLSTVTT TFLDAYSAGA SANNISARFA ETPVAVGVTL IGTVLAVMLP VTEYENFLLL IGSVFAPMAA VLIADFFVLK RREEIEGFDF AGLVLWLAGF ILYRFLLSSG WESSIGLTAP VMSAVAIATV SVRLFFKKTQ SLQRNPS // ID Q9JZ46_NEIMB Unreviewed; 221 AA. AC Q9JZ46; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41672.1}; GN OrderedLocusNames=NMB1296 {ECO:0000313|EMBL:AAF41672.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41672.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41672.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41672.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41672.1; -; Genomic_DNA. DR PIR; C81099; C81099. DR RefSeq; NP_274316.1; NC_003112.2. DR RefSeq; WP_002222378.1; NC_003112.2. DR ProteinModelPortal; Q9JZ46; -. DR STRING; 122586.NMB1296; -. DR PaxDb; Q9JZ46; -. DR DNASU; 903718; -. DR EnsemblBacteria; AAF41672; AAF41672; NMB1296. DR GeneID; 903718; -. DR KEGG; nme:NMB1296; -. DR PATRIC; 20358221; VBINeiMen85645_1622. DR eggNOG; COG0500; LUCA. DR HOGENOM; HOG000258627; -. DR OMA; IGQIRFW; -. DR OrthoDB; EOG67X1R0; -. DR BioCyc; NMEN122586:GHGG-1334-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 221 AA; 24763 MW; 32D4A0BFB1D20A9B CRC64; MDAWFEDTAM GRYVAKLEQD FFGRYLDSYR FSGMCAVQVG GPWLSLSEDV VCVPRDMSMS AENMALADVS ADMLLFPHTL EGGVPSQILS EAHRILKPCG RLMLTGFNPY SLWGFSRWFD GERLPEKRFC LPLPELKRRL ADVGFDIEFG KFMVYLPPVS SLGQIRFWRF MEKAGDRWWP QCAAVYGLVL VKRAAGVTPL PAWDGYLGGK ALAAGAARVA D // ID Q9K1F3_NEIMB Unreviewed; 136 AA. AC Q9K1F3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40658.1}; GN OrderedLocusNames=NMB0201 {ECO:0000313|EMBL:AAF40658.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40658.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40658.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40658.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40658.1; -; Genomic_DNA. DR PIR; C81226; C81226. DR RefSeq; NP_273259.1; NC_003112.2. DR RefSeq; WP_002220211.1; NC_003112.2. DR STRING; 122586.NMB0201; -. DR PaxDb; Q9K1F3; -. DR EnsemblBacteria; AAF40658; AAF40658; NMB0201. DR GeneID; 902309; -. DR KEGG; nme:NMB0201; -. DR PATRIC; 20355445; VBINeiMen85645_0251. DR HOGENOM; HOG000218656; -. DR OrthoDB; EOG6RVFXB; -. DR BioCyc; NMEN122586:GHGG-212-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 136 AA; 16111 MW; FE72D0637086682C CRC64; MTTYTIPKKD YQFLYIYEGT LLNYTLKNDE FHIIVQNVDY PDFPQEIPTP NYTDWVKIKF KQFSYLKFIY GYATKNQDKN IKNVLELGEL KQDDEILDYG GALEVIGSRY DLPTGFSIDI VCREIELEFL DQESFN // ID Q9JZX3_NEIMB Unreviewed; 85 AA. AC Q9JZX3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41271.1}; GN OrderedLocusNames=NMB0860 {ECO:0000313|EMBL:AAF41271.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41271.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41271.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41271.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41271.1; -; Genomic_DNA. DR PIR; G81150; G81150. DR STRING; 122586.NMB0860; -. DR PaxDb; Q9JZX3; -. DR EnsemblBacteria; AAF41271; AAF41271; NMB0860. DR PATRIC; 20357113; VBINeiMen85645_1075. DR HOGENOM; HOG000218879; -. DR OMA; DSADMPS; -. DR OrthoDB; EOG6WHNSD; -. DR BioCyc; NMEN122586:GHGG-891-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 85 AA; 9777 MW; 12F66DC21A3EE813 CRC64; MDDVYRAFDS VGNILNFRIV EKEQKGFWVS TKIKTVVFDS ADMSSDDLFL KCLQSSYKAY FETEPAGLDK RQLMKTLIQK CGFSC // ID Q9JZD3_NEIMB Unreviewed; 125 AA. AC Q9JZD3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41496.1}; GN OrderedLocusNames=NMB1105 {ECO:0000313|EMBL:AAF41496.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41496.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41496.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41496.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41496.1; -; Genomic_DNA. DR PIR; F81121; F81121. DR RefSeq; NP_274136.1; NC_003112.2. DR RefSeq; WP_002222505.1; NC_003112.2. DR STRING; 122586.NMB1105; -. DR PaxDb; Q9JZD3; -. DR EnsemblBacteria; AAF41496; AAF41496; NMB1105. DR GeneID; 903527; -. DR KEGG; nme:NMB1105; -. DR PATRIC; 20357774; VBINeiMen85645_1403. DR eggNOG; ENOG41061M6; Bacteria. DR eggNOG; ENOG411274G; LUCA. DR HOGENOM; HOG000219051; -. DR OMA; GEKYTVD; -. DR OrthoDB; EOG64V2G3; -. DR BioCyc; NMEN122586:GHGG-1141-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 125 AA; 14114 MW; 42B1E3419E63E13E CRC64; MSDATYADAV IMEMNGRDIE IVSIKPQTTT GRKPVKTMNR NGRVNGYCDG VTEHKLSVTA AIPIDGTEID WDNITKAKIT IYPINDEDRR TSYLDCFTVD TGEQYEVDNE ARIDIEMIAL HKIKE // ID Q9K066_NEIMB Unreviewed; 36 AA. AC Q9K066; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41167.1}; GN OrderedLocusNames=NMB0754 {ECO:0000313|EMBL:AAF41167.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41167.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41167.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41167.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41167.1; -; Genomic_DNA. DR PIR; A81164; A81164. DR RefSeq; NP_273796.1; NC_003112.2. DR RefSeq; WP_010980835.1; NC_003112.2. DR STRING; 122586.NMB0754; -. DR PaxDb; Q9K066; -. DR EnsemblBacteria; AAF41167; AAF41167; NMB0754. DR GeneID; 902869; -. DR KEGG; nme:NMB0754; -. DR BioCyc; NMEN122586:GHGG-785-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 36 AA; 3999 MW; 15198754452B93A2 CRC64; MPSEAGLQAA FFSNQRSLRF CGADDLPVKE ARLDAW // ID Q9JXC2_NEIMB Unreviewed; 266 AA. AC Q9JXC2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=CinA-related protein {ECO:0000313|EMBL:AAF42436.1}; GN OrderedLocusNames=NMB2128 {ECO:0000313|EMBL:AAF42436.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42436.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42436.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42436.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42436.1; -; Genomic_DNA. DR PIR; G81005; G81005. DR RefSeq; NP_275113.1; NC_003112.2. DR RefSeq; WP_002225729.1; NC_003112.2. DR ProteinModelPortal; Q9JXC2; -. DR STRING; 122586.NMB2128; -. DR PaxDb; Q9JXC2; -. DR EnsemblBacteria; AAF42436; AAF42436; NMB2128. DR GeneID; 903407; -. DR KEGG; nme:NMB2128; -. DR PATRIC; 20360432; VBINeiMen85645_2712. DR eggNOG; ENOG4107S37; Bacteria. DR eggNOG; COG1058; LUCA. DR HOGENOM; HOG000262180; -. DR OMA; RHFQTAS; -. DR OrthoDB; EOG6130BR; -. DR BioCyc; NMEN122586:GHGG-2193-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR001453; MoaB/Mog_dom. DR Pfam; PF00994; MoCF_biosynth; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 172 MoCF_biosynth. FT {ECO:0000259|SMART:SM00852}. SQ SEQUENCE 266 AA; 29729 MW; A8E436F853E1D8F0 CRC64; MNAFNLIIIG DEILHGSSQD KHFAFFKSLL ESKGLKLNQV QYLPDEPDLL VRQLRRSFSD GMPTFVTGGI GATPDDHTRQ AAAAALDLPV VRHSEAAKFI EGITQKRGEP LDSPEHAQRL KMADFPEGAE LVPNPFNNIA GFSIREHYFF PGFPVMAHPM AEWVLETYYA DRFNQTERGS RSVYVFEQPE SRITPLMEHI EQTYPGVRSY SLPSVGWTHS DGTQVKPHIE FGIKAEGEAV NLLDAAWAEV LHSLDGLGAE LKNRVN // ID Q9JZA2_NEIMB Unreviewed; 135 AA. AC Q9JZA2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41603.1}; GN OrderedLocusNames=NMB1221 {ECO:0000313|EMBL:AAF41603.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41603.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41603.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41603.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41603.1; -; Genomic_DNA. DR PIR; G81107; G81107. DR RefSeq; NP_274246.1; NC_003112.2. DR RefSeq; WP_002222437.1; NC_003112.2. DR STRING; 122586.NMB1221; -. DR PaxDb; Q9JZA2; -. DR EnsemblBacteria; AAF41603; AAF41603; NMB1221. DR GeneID; 903643; -. DR KEGG; nme:NMB1221; -. DR PATRIC; 20358025; VBINeiMen85645_1525. DR eggNOG; ENOG4106DNB; Bacteria. DR eggNOG; ENOG410Y1MY; LUCA. DR HOGENOM; HOG000261744; -. DR OMA; GHARIHY; -. DR OrthoDB; EOG6W7227; -. DR BioCyc; NMEN122586:GHGG-1258-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002810; NfeD-like_C. DR Pfam; PF01957; NfeD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 61 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 3 133 NfeD. {ECO:0000259|Pfam:PF01957}. SQ SEQUENCE 135 AA; 14568 MW; 7D2CA4B92A505A31 CRC64; MTVWFVAAVA VLIIELLTGT VYLLVVSAAL AGSGIAYGLT GSTPAAVLTA ALLSALGIWF VHAKTAVRKV ETDSYQDLDA GQYVEILRHT GGNRYEVFYR GTHWQAQNTG QEELEPGTRA LIVRKEGNLL IITHP // ID Q9K0U2_NEIMB Unreviewed; 488 AA. AC Q9K0U2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=C4-dicarboxylate transporter {ECO:0000313|EMBL:AAF40907.1}; GN OrderedLocusNames=NMB0470 {ECO:0000313|EMBL:AAF40907.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40907.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40907.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40907.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40907.1; -; Genomic_DNA. DR PIR; A81194; A81194. DR RefSeq; NP_273517.1; NC_003112.2. DR RefSeq; WP_002218844.1; NC_003112.2. DR STRING; 122586.NMB0470; -. DR PaxDb; Q9K0U2; -. DR EnsemblBacteria; AAF40907; AAF40907; NMB0470. DR GeneID; 902586; -. DR KEGG; nme:NMB0470; -. DR PATRIC; 20356188; VBINeiMen85645_0615. DR eggNOG; ENOG4107QPK; Bacteria. DR eggNOG; COG0471; LUCA. DR HOGENOM; HOG000117912; -. DR KO; K03319; -. DR OMA; TSAMFVT; -. DR OrthoDB; EOG6WT8FN; -. DR BioCyc; NMEN122586:GHGG-494-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030676; CitT-rel. DR InterPro; IPR001898; Na/sul_symport. DR PANTHER; PTHR10283:SF13; PTHR10283:SF13; 1. DR Pfam; PF00939; Na_sulph_symp; 1. DR PIRSF; PIRSF002457; DASS; 1. DR TIGRFAMs; TIGR00785; dass; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 278 298 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 304 327 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 358 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 391 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 398 418 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 462 482 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 488 AA; 51693 MW; 0634BEC2EB07EA3B CRC64; MMKLGFKPIP LAIAAVLCAL VLALPVPDGV KPQAWTLLAM FVGVIAAIIG KAMPLGALSI IAVGLVAVTG VTADKPGAAM SDALSAFANP LIWLIAIAVM ISRGLLKTGL GMRIGYLFIA VFGRKTLGIG YSLALSELLL APVTPSNTAR GGGIIHPIMQ SIAGSYGSNP AKGTEGKMGK YLALVNYHSN PISSAMFITA TAPNPLIVNL IAENLGSSFR LSWGAWAWAM AVPGVIAFFV MPLILYFLYP PEIKETPNAV QFAKDRLREM GKMSADEIIM AVIFGILLLL WADVPALITG NHAFSINATA TAFIGLSLLL LSGVLTWDDV LKEKSAWDTI IWFGALIMMA AFLNKLGLIK WFSGVLAESV GGLGVSGTAA GVILVLAYMY AHYMFASTTA HITAMFGAFF AAAVSLNAPA MPTALMMAAA SNIMMTLTHY ATGTSPVIFG SGYTTMGEWW KAGFIMSVVN FLIFFVIGSI WWKVLGYW // ID Q9K170_NEIMB Unreviewed; 64 AA. AC Q9K170; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40752.1}; GN OrderedLocusNames=NMB0306 {ECO:0000313|EMBL:AAF40752.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40752.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40752.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40752.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40752.1; -; Genomic_DNA. DR PIR; E81214; E81214. DR STRING; 122586.NMB0306; -. DR PaxDb; Q9K170; -. DR EnsemblBacteria; AAF40752; AAF40752; NMB0306. DR BioCyc; NMEN122586:GHGG-326-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7418 MW; 5DAC8C8FF2448700 CRC64; MLLQRSLLVY EILPDVKAES AAGVFCTGLS WKWENGCSVQ VCPNEWRVLF LSICFFLFEI KFLK // ID Q9K1A8_NEIMB Unreviewed; 480 AA. AC Q9K1A8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; DE EC=1.6.5.11 {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; DE AltName: Full=NDH-1 subunit N {ECO:0000256|HAMAP-Rule:MF_00445}; GN Name=nuoN {ECO:0000256|HAMAP-Rule:MF_00445, GN ECO:0000313|EMBL:AAF40713.1}; GN OrderedLocusNames=NMB0259 {ECO:0000313|EMBL:AAF40713.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40713.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40713.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40713.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC NuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. {ECO:0000256|HAMAP-Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000256|HAMAP-Rule:MF_00445}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40713.1; -; Genomic_DNA. DR PIR; F81220; F81220. DR RefSeq; NP_273315.1; NC_003112.2. DR RefSeq; WP_002224835.1; NC_003112.2. DR STRING; 122586.NMB0259; -. DR PaxDb; Q9K1A8; -. DR EnsemblBacteria; AAF40713; AAF40713; NMB0259. DR GeneID; 902370; -. DR KEGG; nme:NMB0259; -. DR PATRIC; 20355596; VBINeiMen85645_0322. DR eggNOG; ENOG4105CNR; Bacteria. DR eggNOG; COG1007; LUCA. DR HOGENOM; HOG000100795; -. DR KO; K00343; -. DR OMA; MLAIAWK; -. DR OrthoDB; EOG64JFNZ; -. DR BioCyc; NMEN122586:GHGG-274-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_00445; NDH1_NuoN_1; 1. DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. DR TIGRFAMs; TIGR01770; NDH_I_N; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00445}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00445, KW ECO:0000313|EMBL:AAF40713.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_00445}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00445}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00445}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00445}. FT TRANSMEM 11 31 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 38 58 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 74 94 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 103 123 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 128 148 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 163 183 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 210 230 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 241 261 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 272 292 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 311 331 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 332 352 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 368 388 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 404 424 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 449 469 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00445}. FT DOMAIN 125 418 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 480 AA; 52126 MW; D05A272BAB24EB15 CRC64; MNWSDLNLMP AMPEIVLLSL LVLLLLADLW VSDDKRPWTH YGALATVAVT AVVQLAVWEQ GSTSSFNGMY IADGMSRLAK MVLYALTFAL FVYAKPYNQV RGIFKGEFYT LSLFALLGMS VMVSAGHFLT AYIGLELLSL ALYALIALRR DSGFAAEAAL KYFVLGALAS GLLLYGISMV YGATGSLEFA GVLASSFNEE ANEWLLKLGL VFIVVAVAFK LGAVPFHMWV PDVYHGAPTS VTALVGTAPK IAAVVFTFRI LVTGLGTVHH DWSLMFALLA AASLLVGNLA AIMQTNIKRM FAYSTVSHMG FILLAFMAGA VGFAAGLYYA ITYALMAAAG FGVLMVLSDG DNECENISDL AGLNQHRVWL AFLMLLVMFS MAGIPPLMGF YAKFGVIMAL LKQGHVWLSV FAVIMSLIGA FYYLRVVKVI YFDVPDHDQP VGSNYAAKFV LTVNAFLLLL WGIMPQTVID WCAKALENTL // ID Q9JXT1_NEIMB Unreviewed; 171 AA. AC Q9JXT1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAF42229.1}; GN Name=mlp {ECO:0000313|EMBL:AAF42229.1}; GN OrderedLocusNames=NMB1898 {ECO:0000313|EMBL:AAF42229.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42229.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42229.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42229.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42229.1; -; Genomic_DNA. DR PIR; H81029; H81029. DR RefSeq; NP_274893.1; NC_003112.2. DR RefSeq; WP_002225802.1; NC_003112.2. DR ProteinModelPortal; Q9JXT1; -. DR STRING; 122586.NMB1898; -. DR PaxDb; Q9JXT1; -. DR EnsemblBacteria; AAF42229; AAF42229; NMB1898. DR GeneID; 904273; -. DR KEGG; nme:NMB1898; -. DR PATRIC; 20359835; VBINeiMen85645_2422. DR eggNOG; ENOG41072QX; Bacteria. DR eggNOG; COG2913; LUCA. DR HOGENOM; HOG000218755; -. DR OMA; VEGVTTC; -. DR OrthoDB; EOG6PP9QB; -. DR BioCyc; NMEN122586:GHGG-1955-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR InterPro; IPR007450; Lipoprotein_SmpA/OmlA. DR Pfam; PF04355; SmpA_OmlA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000313|EMBL:AAF42229.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 171 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332231. FT DOMAIN 52 132 SmpA_OmlA. {ECO:0000259|Pfam:PF04355}. SQ SEQUENCE 171 AA; 19245 MW; 6131C33C6C04BCEF CRC64; MKIKQIVKPG LAVLAAGVLS ACATKSNVKA DGTTDNPVFP KPYSVTLDNK RGTFPTYDEL DQMRPGLTKD DIYKILGRPH YDESMYGVRE WDYLFHFHTP GVGIDPENTS GVEDVTTCQY KVIFDKDKFA RSFYWNPVFP KDAACPPPAP KAEPQVIIRE IVPAKPKRIR Q // ID Q9K0F5_NEIMB Unreviewed; 129 AA. AC Q9K0F5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41072.1}; GN OrderedLocusNames=NMB0651 {ECO:0000313|EMBL:AAF41072.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41072.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41072.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41072.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41072.1; -; Genomic_DNA. DR PIR; F81173; F81173. DR RefSeq; NP_273693.1; NC_003112.2. DR RefSeq; WP_002225515.1; NC_003112.2. DR STRING; 122586.NMB0651; -. DR PaxDb; Q9K0F5; -. DR EnsemblBacteria; AAF41072; AAF41072; NMB0651. DR GeneID; 902763; -. DR KEGG; nme:NMB0651; -. DR PATRIC; 20356601; VBINeiMen85645_0819. DR eggNOG; ENOG4106FJ1; Bacteria. DR eggNOG; ENOG410XUYE; LUCA. DR HOGENOM; HOG000218830; -. DR OMA; MPIDNIP; -. DR OrthoDB; EOG62ZHWC; -. DR BioCyc; NMEN122586:GHGG-678-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 14858 MW; 3640BA22E832D4BF CRC64; MWKIIKEDSD DLGFAIKCLF SQSIDLNEFK LWIEQVIRDM PIEDIPFYIF DLADFDGGIA DIDNIVGFVS SCRLSKSKKN ALTGIAFLRG IDVYDPPISK EKALKALEKH PEIYQKFQHF FPFVELPPL // ID Q9JZK7_NEIMB Unreviewed; 64 AA. AC Q9JZK7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41410.1}; GN OrderedLocusNames=NMB1009 {ECO:0000313|EMBL:AAF41410.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41410.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41410.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41410.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41410.1; -; Genomic_DNA. DR PIR; B81131; B81131. DR RefSeq; NP_274044.1; NC_003112.2. DR RefSeq; WP_002233797.1; NC_003112.2. DR ProteinModelPortal; Q9JZK7; -. DR STRING; 122586.NMB1009; -. DR PaxDb; Q9JZK7; -. DR EnsemblBacteria; AAF41410; AAF41410; NMB1009. DR GeneID; 903147; -. DR KEGG; nme:NMB1009; -. DR PATRIC; 20357547; VBINeiMen85645_1290. DR OrthoDB; EOG6TBHDR; -. DR BioCyc; NMEN122586:GHGG-1046-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR SUPFAM; SSF51306; SSF51306; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7348 MW; 68A0620ABF74D1B9 CRC64; MNNYYLYRNC SSDVLWVKRI QRQIDGSLLL ISDNSTYPPM PLALAEHPDI QIIGQVVQVS KDLN // ID Q9JXG1_NEIMB Unreviewed; 423 AA. AC Q9JXG1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126}; DE Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126}; DE EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; GN Name=hemK {ECO:0000313|EMBL:AAF42384.1}; GN Synonyms=prmC {ECO:0000256|HAMAP-Rule:MF_02126}; GN OrderedLocusNames=NMB2065 {ECO:0000313|EMBL:AAF42384.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42384.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42384.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42384.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Methylates the class 1 translation termination release CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the CC universally conserved GGQ motif. {ECO:0000256|HAMAP- CC Rule:MF_02126}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [peptide chain CC release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + CC [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine. CC {ECO:0000256|HAMAP-Rule:MF_02126}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42384.1; -; Genomic_DNA. DR PIR; E81010; E81010. DR RefSeq; NP_275055.1; NC_003112.2. DR RefSeq; WP_010981023.1; NC_003112.2. DR ProteinModelPortal; Q9JXG1; -. DR STRING; 122586.NMB2065; -. DR PaxDb; Q9JXG1; -. DR EnsemblBacteria; AAF42384; AAF42384; NMB2065. DR GeneID; 904010; -. DR KEGG; nme:NMB2065; -. DR PATRIC; 20360290; VBINeiMen85645_2645. DR eggNOG; ENOG4105EQY; Bacteria. DR eggNOG; COG2890; LUCA. DR HOGENOM; HOG000076274; -. DR KO; K02493; -. DR OMA; HGWTQGE; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; NMEN122586:GHGG-2128-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02126; RF_methyltr_PrmC; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004556; Modification_methylase_HemK. DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126, KW ECO:0000256|SAAS:SAAS00461685}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02126, KW ECO:0000256|SAAS:SAAS00461716}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02126, KW ECO:0000256|SAAS:SAAS00461685}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 134 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 241 334 MTS. {ECO:0000259|Pfam:PF05175}. FT REGION 259 263 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_02126}. FT REGION 326 329 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_02126}. FT BINDING 282 282 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_02126}. FT BINDING 309 309 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_02126}. FT BINDING 326 326 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_02126}. SQ SEQUENCE 423 AA; 46355 MW; 0F0B07BA6C0BAEEB CRC64; MQEQNRKPSF PIVMLLVSVA LWIASLSNVA FYLGNHGSME GLTVLILGSI FASLDIRYCA VYANYVWLAA IVLLALRKKV VPVHAALWGL ALVAFSVKAV YVDEAGNTSD IVRYGAGFYL WYAAFAVATI GTFAGKNKER KAASAADGIK MTFDKWLGLS KLPKNEARML LQYVSEYTRV QLLTRGGEEM PDEVRQRADR LAQRRLNGEP VAYILGVREF YGRRFTVNPS VLIPRPETEH LVEAVLARLP ENGRVWDLGT GSGAVAVTVA LERPDAFVRA SDISPPALET ARKNAADLGA RVEFAHGSWF DTDMPSEGKW DIIVSNPPYI ENGDKHLLQG DLRFEPQIAL TDFSDGLSCI RTLAQGAPDR LAEGGFLLLE HGFDQGAAVR GVLAENGFSG VETLPDLAGL DRVTLGKYMK HLK // ID Q9JXM3_NEIMB Unreviewed; 511 AA. AC Q9JXM3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Transporter {ECO:0000256|RuleBase:RU003732}; GN OrderedLocusNames=NMB1975 {ECO:0000313|EMBL:AAF42303.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42303.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42303.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42303.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) family. {ECO:0000256|RuleBase:RU003732}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42303.1; -; Genomic_DNA. DR PIR; H81019; H81019. DR RefSeq; NP_274968.1; NC_003112.2. DR RefSeq; WP_002221654.1; NC_003112.2. DR ProteinModelPortal; Q9JXM3; -. DR PaxDb; Q9JXM3; -. DR EnsemblBacteria; AAF42303; AAF42303; NMB1975. DR GeneID; 904164; -. DR KEGG; nme:NMB1975; -. DR PATRIC; 20360025; VBINeiMen85645_2517. DR eggNOG; ENOG4105C8J; Bacteria. DR eggNOG; COG0733; LUCA. DR HOGENOM; HOG000033130; -. DR KO; K03308; -. DR OMA; KREWQIF; -. DR OrthoDB; EOG6WT8F5; -. DR BioCyc; NMEN122586:GHGG-2032-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro. DR InterPro; IPR000175; Na/ntran_symport. DR PANTHER; PTHR11616; PTHR11616; 1. DR Pfam; PF00209; SNF; 2. DR PRINTS; PR00176; NANEUSMPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Symport {ECO:0000256|RuleBase:RU003732}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003732}. FT TRANSMEM 17 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 320 349 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 361 385 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 391 410 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 431 449 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 469 491 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 511 AA; 54906 MW; 270B4E731EE7A1DD CRC64; MSDSKTKERA TFGTRRAFMI AAIGSAVGLG NIWRFPYIAF ENGGGAFILP YLVALLTAGI PLLLLDYAIG HRYRGSAPLA FRRLGRWFEP VGWWNVMTNI VICIYYAVII GWAASYTYYS VNAAWGADPQ GFFFKDFLQM AGPEALGLDF VGKVAGPLAG VWVFTAAIMA LGVQKGVARA SSFFMPLLLV MFLIMVGISL TLPGAAKGLD ALFTPDWSKL ADSKVWVAAY GQIFFSLSIC FGIMVTYSSY LKKKTDLGGT GLVVGFANSS FELLAGIGVF AALGFMAQAG GKAVNEVASG GIGLAFIAFP TIINQAPMGW LIGILFFGSL VFAGVTSMIS ILEVIVAAIQ DKLNIGRVNA TLLVCIPMGI VSTLLFGTAT GLPVLDVMDK FVNTYGIVAA GFVYVAAIII SGRLPELRKH LNALSSIRIG GLWTVCVVVT VVMLGYMLFK DTSGLMEKNY EGYPDGFLSI FGWGMSAALV VFGLLLSLLP WKHGQDFNVK DEHEHEQGEE K // ID Q7DD45_NEIMB Unreviewed; 99 AA. AC Q7DD45; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42411.1}; GN OrderedLocusNames=NMB2094 {ECO:0000313|EMBL:AAF42411.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42411.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42411.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42411.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42411.1; -; Genomic_DNA. DR PIR; D81008; D81008. DR RefSeq; NP_275082.1; NC_003112.2. DR RefSeq; WP_002215072.1; NC_003112.2. DR ProteinModelPortal; Q7DD45; -. DR STRING; 122586.NMB2094; -. DR PaxDb; Q7DD45; -. DR EnsemblBacteria; AAF42411; AAF42411; NMB2094. DR GeneID; 903952; -. DR KEGG; nme:NMB2094; -. DR PATRIC; 20360358; VBINeiMen85645_2676. DR HOGENOM; HOG000218711; -. DR OMA; QIDINKV; -. DR OrthoDB; EOG6FV87D; -. DR BioCyc; NMEN122586:GHGG-2159-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR SUPFAM; SSF47413; SSF47413; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 99 AA; 11418 MW; 1A69231B216FA7BE CRC64; MKIFENIEDV KAIRKKTGLN QIDFWGKVGV TQSGGSRYET GRKMPKPVRE LLRLVHIECI DLAKVNKKDM EIAALLKKHH PDLYAELSKQ TKSERKKQS // ID Q9JY10_NEIMB Unreviewed; 469 AA. AC Q9JY10; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Penicillin-binding protein 3 {ECO:0000313|EMBL:AAF42135.1}; GN OrderedLocusNames=NMB1797 {ECO:0000313|EMBL:AAF42135.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42135.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42135.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42135.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42135.1; -; Genomic_DNA. DR PIR; C81042; C81042. DR RefSeq; NP_274795.1; NC_003112.2. DR RefSeq; WP_002225643.1; NC_003112.2. DR ProteinModelPortal; Q9JY10; -. DR STRING; 122586.NMB1797; -. DR MEROPS; S13.003; -. DR PaxDb; Q9JY10; -. DR EnsemblBacteria; AAF42135; AAF42135; NMB1797. DR GeneID; 903302; -. DR KEGG; nme:NMB1797; -. DR PATRIC; 20359561; VBINeiMen85645_2286. DR eggNOG; ENOG4106HRJ; Bacteria. DR eggNOG; COG2027; LUCA. DR HOGENOM; HOG000263952; -. DR KO; K07259; -. DR OMA; AHSKPMK; -. DR OrthoDB; EOG6NGVQ4; -. DR BioCyc; NMEN122586:GHGG-1852-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro. DR Gene3D; 3.40.710.10; -; 2. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR000667; Peptidase_S13. DR Pfam; PF02113; Peptidase_S13; 1. DR PRINTS; PR00922; DADACBPTASE3. DR SUPFAM; SSF56601; SSF56601; 1. DR TIGRFAMs; TIGR00666; PBP4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 469 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327695. SQ SEQUENCE 469 AA; 50521 MW; 17AC64FE857BED0B CRC64; MNFPKTAASL LLLLASLAAH ALDTGRIPQN EIAVYVQELD SGKVIIDHRS DVPVNPASTM KLVTAFAAFK TFGSNYRWAT EFKSNGTVND GTLDGNLYWA GSGDPVFNQE NLLDAQKQLR EQGILNITGH LMLDHSLWGE VGSPDDFEAD SGSPFMTPPN PTMLSAGMVM VRAERNAAGS TDILTDPPLP HIFAQNNLKI TASQAACPSI KKLMRASFSD NTLKLRGNIP ESCLGKPVGV RMFALDELIR QSFTNHWLLG GGRISDGIGI ADTPEGAQTL AVAHAKPMKE ILTDMNKRSD NLIARSVFLK LGGDGKLPAV SEQAASAVRR ELAVSGIDVA DLVLENGSGL SRKERVTARM MAQMLETAYF SPFAQDFIDT LPIAGTDGTL RNRFKQSGGL LRLKTGTLNN VRALAGYWLG DKPMAVVVII NSGRAVSLLP DLDNFVANNI ISGGDGWLDA KLMCKERRA // ID Q7DDB1_NEIMB Unreviewed; 99 AA. AC Q7DDB1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41873.1}; GN OrderedLocusNames=NMB1517 {ECO:0000313|EMBL:AAF41873.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41873.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41873.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41873.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41873.1; -; Genomic_DNA. DR PIR; D81074; D81074. DR RefSeq; NP_274525.1; NC_003112.2. DR RefSeq; WP_002222238.1; NC_003112.2. DR STRING; 122586.NMB1517; -. DR PaxDb; Q7DDB1; -. DR EnsemblBacteria; AAF41873; AAF41873; NMB1517. DR GeneID; 903991; -. DR KEGG; nme:NMB1517; -. DR PATRIC; 20358822; VBINeiMen85645_1921. DR HOGENOM; HOG000219022; -. DR OMA; QWGRHIG; -. DR OrthoDB; EOG6CVVFD; -. DR BioCyc; NMEN122586:GHGG-1557-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 99 AA; 11320 MW; 4A0FE5042EDAF293 CRC64; MHYFSIHDQS GRHIGFFILL ADDESEARPQ SGRFAVKLEG GMENHVLSPF GQTEIPQYWR VVKDRIELFF DEAPVGTLRN EYLTVSGQTF VLNDLTGNM // ID Q7DDN8_NEIMB Unreviewed; 143 AA. AC Q7DDN8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40935.1}; GN OrderedLocusNames=NMB0503 {ECO:0000313|EMBL:AAF40935.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40935.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40935.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40935.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:4Q7O} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX PubMed=26057799; DOI=10.1107/S2053230X15006585; RA Tan K., Johnson P.M., Stols L., Boubion B., Eschenfeldt W., RA Babnigg G., Hayes C.S., Joachimiak A., Goulding C.W.; RT "The structure of a contact-dependent growth-inhibition (CDI) immunity RT protein from Neisseria meningitidis MC58."; RL Acta Crystallogr F Struct Biol Commun 71:702-709(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40935.1; -; Genomic_DNA. DR RefSeq; NP_273549.1; NC_003112.2. DR RefSeq; WP_002214437.1; NC_003112.2. DR PDB; 4Q7O; X-ray; 1.45 A; A/B=1-143. DR PDBsum; 4Q7O; -. DR STRING; 122586.NMB0503; -. DR PaxDb; Q7DDN8; -. DR EnsemblBacteria; AAF40935; AAF40935; NMB0503. DR GeneID; 902619; -. DR KEGG; nme:NMB0503; -. DR OMA; SCSLHET; -. DR OrthoDB; EOG6P5ZP9; -. DR BioCyc; NMEN122586:GHGG-528-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4Q7O}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 143 AA; 16727 MW; 11F9C9266F8BA47E CRC64; MKNNIFLNLN KKSINNNHFV ISIFFETIYQ FETKDTLLEC FKNITTTGHF GVIGAQYEKI DATRWIGDYE EVNGFEYIDK APSIYFSVGD DFNPEELIIP INLAYHYFNI AISDFLIAHP EYQKKCKEIQ KTYSQTNCSL HET // ID Q9JZ06_NEIMB Unreviewed; 271 AA. AC Q9JZ06; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Putative RNA methylase {ECO:0000313|EMBL:AAF41722.1}; GN OrderedLocusNames=NMB1348 {ECO:0000313|EMBL:AAF41722.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41722.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41722.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41722.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41722.1; -; Genomic_DNA. DR PIR; G81092; G81092. DR RefSeq; NP_274366.1; NC_003112.2. DR RefSeq; WP_002217017.1; NC_003112.2. DR ProteinModelPortal; Q9JZ06; -. DR STRING; 122586.NMB1348; -. DR PaxDb; Q9JZ06; -. DR EnsemblBacteria; AAF41722; AAF41722; NMB1348. DR GeneID; 903770; -. DR KEGG; nme:NMB1348; -. DR PATRIC; 20358353; VBINeiMen85645_1688. DR eggNOG; ENOG4105CVS; Bacteria. DR eggNOG; COG0565; LUCA. DR HOGENOM; HOG000229628; -. DR KO; K02533; -. DR OMA; ELQRCHF; -. DR OrthoDB; EOG6XSZTC; -. DR BioCyc; NMEN122586:GHGG-1386-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR004384; rRNA_MeTrfase_TrmH_1. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 2. DR PIRSF; PIRSF004808; LasT; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAF41722.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAF41722.1}. FT DOMAIN 15 50 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. FT DOMAIN 72 185 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. SQ SEQUENCE 271 AA; 30018 MW; 299F33E4B4B49014 CRC64; MTTLKPALPA YLDNIRIILT RTSHPANIGS AARAMKTMGL HKLTIVAPNL MATPMTENPP VFDPEHPQSF KLPEESFILA SGAADVLENA TIAASLDEAL ADTTIACALT SRRREITAPL QTPRDLVSEL LQTANRGEKV ALVFGNETFG LSIEEVQACN RLMTINGNPD YFSLNLAQAV QVVCYEIFSQ TGSPMTHLQQ EDHAATHEQI KGMVAHMESV MNDIGFFNRR NGERLMRRMQ SLFGRANTQT EDIDILRGFF NTVSHRIHKK D // ID Q9K198_NEIMB Unreviewed; 241 AA. AC Q9K198; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Competence protein {ECO:0000313|EMBL:AAF40723.1}; GN OrderedLocusNames=NMB0269 {ECO:0000313|EMBL:AAF40723.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40723.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40723.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40723.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40723.1; -; Genomic_DNA. DR PIR; F81218; F81218. DR RefSeq; NP_273325.1; NC_003112.2. DR RefSeq; WP_002224838.1; NC_003112.2. DR ProteinModelPortal; Q9K198; -. DR STRING; 122586.NMB0269; -. DR PaxDb; Q9K198; -. DR EnsemblBacteria; AAF40723; AAF40723; NMB0269. DR GeneID; 902380; -. DR KEGG; nme:NMB0269; -. DR PATRIC; 20355622; VBINeiMen85645_0335. DR eggNOG; ENOG4105MJ2; Bacteria. DR eggNOG; COG1040; LUCA. DR HOGENOM; HOG000075040; -. DR OMA; LARWLGC; -. DR OrthoDB; EOG6716R8; -. DR BioCyc; NMEN122586:GHGG-284-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR029057; PRTase-like. DR SUPFAM; SSF53271; SSF53271; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 241 AA; 27123 MW; 42FEA754CD429BA1 CRC64; MDFLSRWRRI ADAPTIRRCV LCHGSSGVSD GICAGCRDDL AAYRTDAANS CPLCFRHIQG GSVCGGCQKK PPAFDRMWAS LHYEPPVSNM IHALKHLADL SMVQPLADLM MQNPPDRLAD ECFDFVLPVP LSRERLLQRG FNQSESIVGL LAQRYGWQIL PRHTVFRHHR PPQSTLKGGE RRRNIKNAFE IRTPIPENCN ILLIDDVFTT GATLDELAKT LKKSGANRIC CWTLARTPMK K // ID Q9K0R3_NEIMB Unreviewed; 51 AA. AC Q9K0R3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40949.1}; GN OrderedLocusNames=NMB0517 {ECO:0000313|EMBL:AAF40949.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40949.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40949.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40949.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40949.1; -; Genomic_DNA. DR PIR; G81188; G81188. DR STRING; 122586.NMB0517; -. DR PaxDb; Q9K0R3; -. DR EnsemblBacteria; AAF40949; AAF40949; NMB0517. DR OMA; YYGRASI; -. DR BioCyc; NMEN122586:GHGG-542-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 51 AA; 5982 MW; 8157D2FF2F745440 CRC64; MLLQRSHALF CQQVEFFSGN QRGKASPQHR SMYYGRASIY SFRKSFSFKT A // ID Q9JXT0_NEIMB Unreviewed; 147 AA. AC Q9JXT0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42230.1}; GN OrderedLocusNames=NMB1899 {ECO:0000313|EMBL:AAF42230.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42230.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42230.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42230.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42230.1; -; Genomic_DNA. DR PIR; A81030; A81030. DR RefSeq; NP_274894.1; NC_003112.2. DR RefSeq; WP_002225803.1; NC_003112.2. DR STRING; 122586.NMB1899; -. DR PaxDb; Q9JXT0; -. DR EnsemblBacteria; AAF42230; AAF42230; NMB1899. DR GeneID; 904272; -. DR KEGG; nme:NMB1899; -. DR PATRIC; 20359837; VBINeiMen85645_2423. DR HOGENOM; HOG000218754; -. DR OMA; PIFAPAH; -. DR OrthoDB; EOG6J74V5; -. DR BioCyc; NMEN122586:GHGG-1956-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 147 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329322. SQ SEQUENCE 147 AA; 16322 MW; 4076D629FB9DE859 CRC64; MPFRLFLGIL CGLSMVAPVY AQGQPDTVGD FIQKKKVIVD TSKAELCFAD DRQCHPVLIG VATPKGTFGL TLNSTDKPGY GGEVIGFKQE GDFLFALHRV WNQIPSERRN ERIASPSVSD RIMTNGCINV SDAVYEKLRH YFVLEVI // ID Q9JYQ5_NEIMB Unreviewed; 421 AA. AC Q9JYQ5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185}; GN Name=gluD {ECO:0000313|EMBL:AAF41833.1}; GN OrderedLocusNames=NMB1476 {ECO:0000313|EMBL:AAF41833.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41833.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41833.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41833.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000256|PIRNR:PIRNR000185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41833.1; -; Genomic_DNA. DR PIR; B81079; B81079. DR RefSeq; NP_274485.1; NC_003112.2. DR RefSeq; WP_002225092.1; NC_003112.2. DR ProteinModelPortal; Q9JYQ5; -. DR SMR; Q9JYQ5; 12-419. DR STRING; 122586.NMB1476; -. DR PaxDb; Q9JYQ5; -. DR EnsemblBacteria; AAF41833; AAF41833; NMB1476. DR GeneID; 903898; -. DR KEGG; nme:NMB1476; -. DR PATRIC; 20358717; VBINeiMen85645_1868. DR eggNOG; ENOG4105D82; Bacteria. DR eggNOG; COG0334; LUCA. DR HOGENOM; HOG000243801; -. DR KO; K00260; -. DR OMA; NEMIMGW; -. DR OrthoDB; EOG65XN4D; -. DR BioCyc; NMEN122586:GHGG-1516-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185, KW ECO:0000313|EMBL:AAF41833.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 188 419 ELFV_dehydrog. FT {ECO:0000259|SMART:SM00839}. SQ SEQUENCE 421 AA; 46258 MW; BD128F0B6CE417BF CRC64; MSEALAKETL NPFEIARKQV KTACDRLKTD PAVYEILKSP TRVLEVNFPV KLDDDTVKTF TGYRSQHNNA VGPYKGGVRF HPSVNLDEVK ALSIWMTIKC CVAGIPYGGG KGGITLDPRD YSEAELERIA RAYAEAIAPL IGEKIDIPAP DVNTNGKIMS WMVDAYENVV KHSAPGVFTG KPVEFGGSLA RTEATGYGVN LAAVQALEKL GKDVKGATYA IQGFGNVGYH TGYYAHQSGA KVVAVSTVDV AIYNENGLDM EALFKEFQEK GFITNEAGYG KEITNAELLA LDVDVLAPCA LENQLTSENA GKVRAKIVVE GANGPTTPEA DVILRQNGVL VVPDILANCG GVVVSYFEWV QNLQGYYWEF DEVQEKETVV LRRAFRDIWN LAQEYDVDLR TASYMMSIRR VEKAMKLRGW Y // ID Q9K0F1_NEIMB Unreviewed; 109 AA. AC Q9K0F1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41076.1}; GN OrderedLocusNames=NMB0656 {ECO:0000313|EMBL:AAF41076.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41076.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41076.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41076.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41076.1; -; Genomic_DNA. DR PIR; B81174; B81174. DR RefSeq; NP_273698.1; NC_003112.2. DR RefSeq; WP_002222807.1; NC_003112.2. DR STRING; 122586.NMB0656; -. DR PaxDb; Q9K0F1; -. DR EnsemblBacteria; AAF41076; AAF41076; NMB0656. DR GeneID; 902768; -. DR KEGG; nme:NMB0656; -. DR PATRIC; 20356611; VBINeiMen85645_0824. DR HOGENOM; HOG000218650; -. DR OMA; FFIFKKH; -. DR OrthoDB; EOG6K13VJ; -. DR BioCyc; NMEN122586:GHGG-683-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 109 AA; 12261 MW; 3E1F3C1B6AC6A79F CRC64; MTDKSKTEKL ISSDDKQSVI DGILDMVFNS KAYEVPWISE KLMELSKNKD LDIAGLSLTC FGHLARLHSN IGDYDKVIPL LHSKQDDPEL QGRAEDALED ISLFLSENH // ID Q9JYA3_NEIMB Unreviewed; 102 AA. AC Q9JYA3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42024.1}; GN OrderedLocusNames=NMB1675 {ECO:0000313|EMBL:AAF42024.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42024.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42024.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42024.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42024.1; -; Genomic_DNA. DR PIR; F81054; F81054. DR RefSeq; NP_274680.1; NC_003112.2. DR RefSeq; WP_002230789.1; NC_003112.2. DR STRING; 122586.NMB1675; -. DR PaxDb; Q9JYA3; -. DR EnsemblBacteria; AAF42024; AAF42024; NMB1675. DR GeneID; 903435; -. DR KEGG; nme:NMB1675; -. DR PATRIC; 20359294; VBINeiMen85645_2155. DR HOGENOM; HOG000219071; -. DR OMA; YRRASLM; -. DR OrthoDB; EOG6SV5CZ; -. DR BioCyc; NMEN122586:GHGG-1729-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 81 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 102 AA; 11074 MW; 54ED1E43D768D106 CRC64; MEYCEPEEAS DPYATYRRAN LMAGLPLFVV ILVLLNIVFP LPAHPLAWLV PAGFMVLGGG FPLSLPLVAL LVLTCCILAH CPPLSRLLCY PCPNHPMSKN SA // ID Q9JZF0_NEIMB Unreviewed; 173 AA. AC Q9JZF0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41476.1}; GN OrderedLocusNames=NMB1084 {ECO:0000313|EMBL:AAF41476.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41476.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41476.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41476.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41476.1; -; Genomic_DNA. DR PIR; F81122; F81122. DR RefSeq; NP_274116.1; NC_003112.2. DR RefSeq; WP_002219320.1; NC_003112.2. DR STRING; 122586.NMB1084; -. DR PaxDb; Q9JZF0; -. DR EnsemblBacteria; AAF41476; AAF41476; NMB1084. DR GeneID; 903501; -. DR KEGG; nme:NMB1084; -. DR PATRIC; 20357723; VBINeiMen85645_1378. DR BioCyc; NMEN122586:GHGG-1120-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 173 AA; 19881 MW; 221FBB7EC46014BC CRC64; MECHADVWHF ILEKNMKKFY FVLLALGLAA CGQEQSQKAD AEQYFFANKY QFADEKQAFY FERAARFRVL QQGLGGDFER FLKGEIPNQE NLAKYRENIT QAVAYYADTN GDDDPYRVCK QAAQDAEILM KSMVTSGGGG TTDLDKESYQ NYRKSMQECR KTITEAEANL PKK // ID Q9K1R7_NEIMB Unreviewed; 131 AA. AC Q9K1R7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40481.1}; GN OrderedLocusNames=NMB0002 {ECO:0000313|EMBL:AAF40481.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40481.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40481.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40481.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40481.1; -; Genomic_DNA. DR PIR; H81246; H81246. DR RefSeq; NP_273068.1; NC_003112.2. DR RefSeq; WP_002225748.1; NC_003112.2. DR STRING; 122586.NMB0002; -. DR PaxDb; Q9K1R7; -. DR EnsemblBacteria; AAF40481; AAF40481; NMB0002. DR GeneID; 902104; -. DR KEGG; nme:NMB0002; -. DR PATRIC; 20354931; VBINeiMen85645_0002. DR HOGENOM; HOG000218688; -. DR OMA; ILYFLMV; -. DR OrthoDB; EOG6PGK70; -. DR BioCyc; NMEN122586:GHGG-2-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 36 {ECO:0000256|SAM:SignalP}. FT CHAIN 37 131 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327898. FT COILED 64 105 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 131 AA; 14570 MW; AFF910477A857F5F CRC64; MPSDVGIRLQ TAFKWKLKMK KIFYFLMVVF STSVWAGDAE DNLLSIQSGY RALLQKQNNL DGKIIGMQSD LEDARRRLQT AQADIARLEA EIPAAMAQKA RQAEDLRQIG VRLDHAWNAV YGAGGTKASG N // ID Q7DD35_NEIMB Unreviewed; 140 AA. AC Q7DD35; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42455.1}; GN OrderedLocusNames=NMB2147 {ECO:0000313|EMBL:AAF42455.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42455.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42455.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42455.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42455.1; -; Genomic_DNA. DR PIR; A81003; A81003. DR RefSeq; NP_275132.1; NC_003112.2. DR RefSeq; WP_002218252.1; NC_003112.2. DR STRING; 122586.NMB2147; -. DR PaxDb; Q7DD35; -. DR EnsemblBacteria; AAF42455; AAF42455; NMB2147. DR GeneID; 903225; -. DR KEGG; nme:NMB2147; -. DR PATRIC; 20360486; VBINeiMen85645_2739. DR HOGENOM; HOG000218685; -. DR OMA; MIKETLM; -. DR OrthoDB; EOG6C0178; -. DR BioCyc; NMEN122586:GHGG-2212-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15957 MW; 17DE8A162507AA4C CRC64; MRPIFLSFVL FPILITACST PDKSARWENI GTISNGNIHT YINKDSVRKN GNLMIFQDKK VVTNLKQERF ANTPAYKTAI AEWEIHCNNK TYRLSSLQLF DTKNTEISTQ NYTASSLRPM SILSGTLTEK QYETVCGKKL // ID Q7DDS8_NEIMB Unreviewed; 436 AA. AC Q7DDS8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}; GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465, GN ECO:0000313|EMBL:AAF40620.1}; GN OrderedLocusNames=NMB0162 {ECO:0000313|EMBL:AAF40620.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40620.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40620.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40620.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The central subunit of the protein translocation channel CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These CC two domains form a lateral gate at the front which open onto the CC bilayer between TMs 2 and 7, and are clamped together by SecE at CC the back. The channel is closed by both a pore ring composed of CC hydrophobic SecY resides and a short helix (helix 2A) on the CC extracellular side of the membrane which forms a plug. The plug CC probably moves laterally to allow the channel to open. The ring CC and the pore may move independently. {ECO:0000256|HAMAP- CC Rule:MF_01465, ECO:0000256|RuleBase:RU000537}. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of SecY, SecE and SecG subunits. The CC heterotrimers can form oligomers, although 1 heterotrimer is CC thought to be able to translocate proteins. Interacts with the CC ribosome. Interacts with SecDF, and other proteins may be CC involved. Interacts with SecA. {ECO:0000256|HAMAP-Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01465}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003484}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003484}. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. CC {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU004349}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40620.1; -; Genomic_DNA. DR PIR; D81233; D81233. DR RefSeq; NP_273220.1; NC_003112.2. DR RefSeq; WP_002215450.1; NC_003112.2. DR ProteinModelPortal; Q7DDS8; -. DR STRING; 122586.NMB0162; -. DR PaxDb; Q7DDS8; -. DR EnsemblBacteria; AAF40620; AAF40620; NMB0162. DR GeneID; 902269; -. DR KEGG; nme:NMB0162; -. DR PATRIC; 20355347; VBINeiMen85645_0203. DR eggNOG; ENOG4105CGG; Bacteria. DR eggNOG; COG0201; LUCA. DR HOGENOM; HOG000080585; -. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR BioCyc; NMEN122586:GHGG-172-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3370.10; -; 1. DR HAMAP; MF_01465; SecY; 1. DR InterPro; IPR026593; SecY. DR InterPro; IPR002208; SecY/SEC61-alpha. DR InterPro; IPR030659; SecY_CS. DR InterPro; IPR023201; SecY_su_dom. DR PANTHER; PTHR10906; PTHR10906; 1. DR Pfam; PF00344; SecY; 1. DR PIRSF; PIRSF004557; SecY; 1. DR SUPFAM; SSF103491; SSF103491; 1. DR TIGRFAMs; TIGR00967; 3a0501s007; 1. DR PROSITE; PS00755; SECY_1; 1. DR PROSITE; PS00756; SECY_2; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01465}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01465}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01465, KW ECO:0000256|RuleBase:RU003484}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01465, KW ECO:0000256|RuleBase:RU003484}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01465}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01465}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01465, KW ECO:0000256|RuleBase:RU003484}. FT TRANSMEM 21 41 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 72 92 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 122 142 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 147 167 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 176 196 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 210 230 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 266 286 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 309 329 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 365 385 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 386 406 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01465}. SQ SEQUENCE 436 AA; 47539 MW; 5DF3B1EE1FF86724 CRC64; MANQQTSSGS SKFGDLKKRL LFLFGALIVF RIGAHIPVPG VDAVALAKLY ESAGNGILGI LNMFSGGSLE RFSIFAIGIM PYISASIIVQ LASEILPSLK ALKKEGEAGR KVITKYTRYG TVLLAILQSL GVASFVFQQG IVVTSSFEFH VSTVVSLVTG TMFLMWLGEQ ITERGIGNGI SLIITAGIAS GIPSGIAKLV TLTNQGSMSM LTALFIVFGA LLLIYLVVYF ESAQRKIPIH YAKRQFNGRA GSQNTHMPFK LNMAGVIPPI FASSIILFPS TLLGWFGSAD TNSVLHKIAG LLQHGQLLYM ALFAATVIFF CYFYTALVFS PKEMAENLKK SGAFVPGIRP GEQTSRYLEK VVLRLTLFGA LYITTICLIP EFLTTVLNVP FYLGGTSLLI LVVVTMDFST QINSYRLTQQ YDKLMTRSEM KSFSRK // ID Q9JYW8_NEIMB Unreviewed; 324 AA. AC Q9JYW8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=IS1106 transposase {ECO:0000313|EMBL:AAF41763.1}; GN OrderedLocusNames=NMB1399 {ECO:0000313|EMBL:AAF41763.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41763.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41763.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41763.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41763.1; -; Genomic_DNA. DR PIR; G81088; G81088. DR RefSeq; NP_274413.1; NC_003112.2. DR RefSeq; WP_009348598.1; NC_003112.2. DR PaxDb; Q9JYW8; -. DR EnsemblBacteria; AAF41763; AAF41763; NMB1399. DR GeneID; 903821; -. DR KEGG; nme:NMB1399; -. DR PATRIC; 20358485; VBINeiMen85645_1754. DR eggNOG; ENOG4105F2I; Bacteria. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000218682; -. DR KO; K07481; -. DR OMA; FRERMAQ; -. DR OrthoDB; EOG6RZB5B; -. DR BioCyc; NMEN122586:GHGG-1437-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR002559; Transposase_11. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF01609; DDE_Tnp_1; 1. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 40 111 DUF772. {ECO:0000259|Pfam:PF05598}. FT DOMAIN 127 311 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 324 AA; 37294 MW; 7530FD65ED8AD74B CRC64; MIAKHIDRFP LLKLDRVIDW QLIEQYLNRQ KTRYLRDHRG RPAYPLLSMF KAVLLGQWHS LSDPELEHSL ITRIDFNLFC RFDELSIPDY STLCRYRNRL AQDNTLSELL ELINRQLTEK GLKIEKASAA VVDATIIQTA GSKQRQAIEV DEEGQISGQT TPSKDSDARW IKKNGLYKLG YKQHTRTDAE GYIEKLHITP ANAHECKHLS PLLEGLPKGT TVYADKGYDS AENRQHLEEH QLLDGIMRKA HRNRPLTEVQ TKRNRYLSKT RYVVEQSFGT LHRKFRYARA AYFGLVKVSA QSHLKAMCLN LLKAANRLSA PAAA // ID Q7DDK6_NEIMB Unreviewed; 169 AA. AC Q7DDK6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41294.1}; GN OrderedLocusNames=NMB0883 {ECO:0000313|EMBL:AAF41294.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41294.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41294.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41294.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41294.1; -; Genomic_DNA. DR PIR; F81147; F81147. DR RefSeq; NP_273924.1; NC_003112.2. DR RefSeq; WP_002213852.1; NC_003112.2. DR PaxDb; Q7DDK6; -. DR EnsemblBacteria; AAF41294; AAF41294; NMB0883. DR GeneID; 903002; -. DR KEGG; nme:NMB0883; -. DR PATRIC; 20357171; VBINeiMen85645_1099. DR eggNOG; ENOG4108WWS; Bacteria. DR eggNOG; COG1755; LUCA. DR HOGENOM; HOG000044222; -. DR OMA; WIAMIAE; -. DR OrthoDB; EOG6Z6FZS; -. DR BioCyc; NMEN122586:GHGG-919-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:InterPro. DR InterPro; IPR007269; ICMT_MeTrfase. DR Pfam; PF04140; ICMT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 155 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 169 AA; 19422 MW; 0CFE53CF87A5782D CRC64; MTMILSILSL FFIIRLLFLA VSIKHEKALI AKGAKQYGKT NSTLLAAVHT LYYLACFVWV WLSDTAFNGI SLIGTLTVMA SFVILSLIIK QLGEIWTVKI YILPNHQINR SWLFKTFRHP NYFLNIIPEL IGIALLCQAW YVLLIGLPIY LLVLFKRIRQ EEQAMATLF // ID Q9JXH4_NEIMB Unreviewed; 274 AA. AC Q9JXH4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=DNA ligase {ECO:0000313|EMBL:AAF42368.1}; DE EC=6.5.1.1 {ECO:0000313|EMBL:AAF42368.1}; GN Name=ligA-2 {ECO:0000313|EMBL:AAF42368.1}; GN OrderedLocusNames=NMB2048 {ECO:0000313|EMBL:AAF42368.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42368.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42368.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42368.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42368.1; -; Genomic_DNA. DR PIR; D81013; D81013. DR RefSeq; NP_275038.1; NC_003112.2. DR RefSeq; WP_002225694.1; NC_003112.2. DR ProteinModelPortal; Q9JXH4; -. DR STRING; 122586.NMB2048; -. DR PaxDb; Q9JXH4; -. DR DNASU; 904041; -. DR EnsemblBacteria; AAF42368; AAF42368; NMB2048. DR GeneID; 904041; -. DR KEGG; nme:NMB2048; -. DR PATRIC; 20360250; VBINeiMen85645_2625. DR eggNOG; ENOG4105E1T; Bacteria. DR eggNOG; COG1793; LUCA. DR KO; K10747; -. DR OMA; VRGYWDG; -. DR OrthoDB; EOG60919Q; -. DR BioCyc; NMEN122586:GHGG-2111-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR029319; DNA_ligase_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF14743; DNA_ligase_OB_2; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF42368.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 274 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327670. FT DOMAIN 124 202 DNA_LIGASE_A3. FT {ECO:0000259|PROSITE:PS50160}. SQ SEQUENCE 274 AA; 30713 MW; 43BA457AD6AA602D CRC64; MIKKTIGGII PIFTAVFIPA SAGAADLMLA QEYKGQDIAG WAMSEKLDGV RAYWDGKHLM SRQGYAFAPP KGFTAQFPPY PLDGELYSGR GQFEQISATV RSVSSDWRGI RLHVFDVPKA QGNLYQRLAV ATQWLKTHPN APITIIPQIK VRDRQHAMDF LKQIEAQGGE GVMLRQPESR YSGGRSSQLL KLKSQYDDEC TVTRHYEGKG RNAGRLGAVG CKNRHGEFRI GSGFKDKDRD NPPKIGTLIT YRYRGFTRKG TPKFATFVRV RTDR // ID Q9K0E7_NEIMB Unreviewed; 129 AA. AC Q9K0E7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41079.1}; GN OrderedLocusNames=NMB0660 {ECO:0000313|EMBL:AAF41079.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41079.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41079.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41079.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41079.1; -; Genomic_DNA. DR PIR; E81174; E81174. DR RefSeq; NP_273702.1; NC_003112.2. DR RefSeq; WP_002219615.1; NC_003112.2. DR STRING; 122586.NMB0660; -. DR PaxDb; Q9K0E7; -. DR EnsemblBacteria; AAF41079; AAF41079; NMB0660. DR GeneID; 902772; -. DR KEGG; nme:NMB0660; -. DR PATRIC; 20356617; VBINeiMen85645_0827. DR eggNOG; ENOG4106FJ1; Bacteria. DR eggNOG; ENOG410XUYE; LUCA. DR HOGENOM; HOG000218830; -. DR OrthoDB; EOG62ZHWC; -. DR BioCyc; NMEN122586:GHGG-687-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 15073 MW; 0F4AB5F2F0D505FF CRC64; MWKISKENCE DLGFAIVCMF YDAINLSEFK LWLDIVVRDI PIDTIPLYIF DLIDFDKSIG EIYDVIGVVN YGYISNDQKN ALTGIAFLRG IDVYDPPISK EKALKALEKY PEIYQRFQHF FPFVELPLF // ID Q9JZB0_NEIMB Unreviewed; 155 AA. AC Q9JZB0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Putative toxin-activating protein {ECO:0000313|EMBL:AAF41592.1}; GN OrderedLocusNames=NMB1210 {ECO:0000313|EMBL:AAF41592.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41592.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41592.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41592.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41592.1; -; Genomic_DNA. DR PIR; F81108; F81108. DR RefSeq; NP_274235.1; NC_003112.2. DR RefSeq; WP_002222442.1; NC_003112.2. DR STRING; 122586.NMB1210; -. DR PaxDb; Q9JZB0; -. DR EnsemblBacteria; AAF41592; AAF41592; NMB1210. DR GeneID; 903632; -. DR KEGG; nme:NMB1210; -. DR PATRIC; 20358007; VBINeiMen85645_1516. DR eggNOG; ENOG41090Q8; Bacteria. DR eggNOG; COG2994; LUCA. DR HOGENOM; HOG000249645; -. DR KO; K07389; -. DR OMA; WLWMHSP; -. DR OrthoDB; EOG647TZC; -. DR BioCyc; NMEN122586:GHGG-1247-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:InterPro. DR GO; GO:0009404; P:toxin metabolic process; IEA:InterPro. DR InterPro; IPR003996; RTX_toxin-activating_protC_bac. DR Pfam; PF02794; HlyC; 1. DR PRINTS; PR01489; RTXTOXINC. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 155 AA; 18266 MW; 1CC562734C34FA2B CRC64; MKIENIDIIS PELFPQETFN ETEAFGALVW LWAVSPIYQH AGVQEAAVNI LPVLKNGQFA LFSSNGHPVA YCTWAYFDEE TEWQYLQSND VLRHSENWCS GNRMWLINWF APFGDSRMMK RILVHLFPKR EIRWLYHRGS EKGKRIMRFP ALSKQ // ID Q9JXC9_NEIMB Unreviewed; 114 AA. AC Q9JXC9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42427.1}; GN OrderedLocusNames=NMB2115 {ECO:0000313|EMBL:AAF42427.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42427.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42427.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42427.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42427.1; -; Genomic_DNA. DR PIR; F81004; F81004. DR RefSeq; NP_275102.1; NC_003112.2. DR RefSeq; WP_002219989.1; NC_003112.2. DR PaxDb; Q9JXC9; -. DR EnsemblBacteria; AAF42427; AAF42427; NMB2115. DR GeneID; 903512; -. DR KEGG; nme:NMB2115; -. DR PATRIC; 20360404; VBINeiMen85645_2698. DR HOGENOM; HOG000218653; -. DR OMA; FEFSSHI; -. DR OrthoDB; EOG6W19MX; -. DR BioCyc; NMEN122586:GHGG-2180-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 114 AA; 13949 MW; 76454ED3C2D009BC CRC64; MFLDDVNVFL DDLNVFLDDL NTNPITDEWY MSNFADKHIK ILESYEAFDI LKQFVDYMIE EYDEKSEYEI MEILRQLKYQ ADTNEKFYTN TQKQKIVELY KQEISQDILN EIFR // ID Q9JXJ6_NEIMB Unreviewed; 363 AA. AC Q9JXJ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Transcriptional regulator, HTH_3 family {ECO:0000313|EMBL:AAF42336.1}; GN OrderedLocusNames=NMB2012 {ECO:0000313|EMBL:AAF42336.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42336.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42336.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42336.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42336.1; -; Genomic_DNA. DR PIR; A81016; A81016. DR RefSeq; NP_275004.1; NC_003112.2. DR RefSeq; WP_002225876.1; NC_003112.2. DR STRING; 122586.NMB2012; -. DR PaxDb; Q9JXJ6; -. DR EnsemblBacteria; AAF42336; AAF42336; NMB2012. DR GeneID; 904110; -. DR KEGG; nme:NMB2012; -. DR PATRIC; 20360127; VBINeiMen85645_2568. DR eggNOG; ENOG4106EI2; Bacteria. DR eggNOG; COG1396; LUCA. DR eggNOG; COG2856; LUCA. DR HOGENOM; HOG000006406; -. DR OMA; ISANPMY; -. DR OrthoDB; EOG6ZWJK0; -. DR BioCyc; NMEN122586:GHGG-2069-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010359; HTH_IrrE. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF06114; DUF955; 1. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 9 60 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 363 AA; 42095 MW; 3642F898F451DD8A CRC64; MQTFNRERLE FALDKRGCTQ TKLAELLGIT ARQVRNYVKD EQIPDLNELA NLLEFPVHFF TNDERLPELK SQAVSFRARS RTSKRLEKQA LNHSITAFLL NDWLETEFTL SQAVLPDFSD ISPEEAAQEL RLEWGLGNEP IPNMITLLEV KGVRVFSLSL DTKDIDAFCT WYENHPFVFL NTQKSAERSR FDAAHELGHL IRDKYSMEHS KNSEITEDEP RDIIEKEANA FASAFLMPEA ALRLYRHVPI TIENLLKIKR RFGVSLVALA YRMHKLGMIT DRMYIHNLCP LFAKKKYRTI EPEPMEREIS SALRKMLTIL KNDGIGIEQI AENLNVSPKD VADLTFGLVE RDLNRYRKLR LVK // ID Q7DDD5_NEIMB Unreviewed; 92 AA. AC Q7DDD5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41617.1}; GN OrderedLocusNames=NMB1236 {ECO:0000313|EMBL:AAF41617.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41617.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41617.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41617.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41617.1; -; Genomic_DNA. DR PIR; A81105; A81105. DR RefSeq; NP_274260.1; NC_003112.2. DR RefSeq; WP_002213502.1; NC_003112.2. DR STRING; 122586.NMB1236; -. DR PaxDb; Q7DDD5; -. DR EnsemblBacteria; AAF41617; AAF41617; NMB1236. DR GeneID; 903658; -. DR KEGG; nme:NMB1236; -. DR PATRIC; 20358069; VBINeiMen85645_1547. DR HOGENOM; HOG000218964; -. DR OMA; MNIRKIS; -. DR OrthoDB; EOG67HK0Z; -. DR BioCyc; NMEN122586:GHGG-1273-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 92 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004288457. SQ SEQUENCE 92 AA; 9163 MW; 49217884D0AD15B5 CRC64; MNIRTAFALC AIALSAAAAA YAKEIKIDAN NTPYSEADAQ KLAATAVGMG VKEPISLNGG SGSITVSGSS ATQCVFKVGN GGALQIQGLN CK // ID Q9JZU2_NEIMB Unreviewed; 118 AA. AC Q9JZU2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41307.1}; GN OrderedLocusNames=NMB0899 {ECO:0000313|EMBL:AAF41307.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41307.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41307.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41307.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41307.1; -; Genomic_DNA. DR PIR; H81143; H81143. DR PaxDb; Q9JZU2; -. DR EnsemblBacteria; AAF41307; AAF41307; NMB0899. DR PATRIC; 20357229; VBINeiMen85645_1128. DR HOGENOM; HOG000220713; -. DR OMA; MTVIGVF; -. DR OrthoDB; EOG686NHT; -. DR BioCyc; NMEN122586:GHGG-937-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR031876; DUF4760. DR Pfam; PF15956; DUF4760; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 118 AA; 13488 MW; 0A87FCEC9D1E0D21 CRC64; MAERNNAALQ EAITIVNGLA KTDGCILATY TSDTPDKKKD REAILTVLNQ REFVCAGVLG GALHEKMYKD FEYSMLLRDW DNLSSFIFEI RRIRSAPTAF QEFEAVARKW KKKPLKTK // ID Q9JZW8_NEIMB Unreviewed; 307 AA. AC Q9JZW8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=YabO/YceC/SfhB family protein {ECO:0000313|EMBL:AAF41278.1}; GN OrderedLocusNames=NMB0867 {ECO:0000313|EMBL:AAF41278.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41278.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41278.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41278.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41278.1; -; Genomic_DNA. DR PIR; C81148; C81148. DR RefSeq; NP_273908.1; NC_003112.2. DR RefSeq; WP_010980864.1; NC_003112.2. DR ProteinModelPortal; Q9JZW8; -. DR STRING; 122586.NMB0867; -. DR PaxDb; Q9JZW8; -. DR EnsemblBacteria; AAF41278; AAF41278; NMB0867. DR GeneID; 902981; -. DR KEGG; nme:NMB0867; -. DR PATRIC; 20357123; VBINeiMen85645_1080. DR eggNOG; ENOG4105WH7; Bacteria. DR eggNOG; COG0564; LUCA. DR HOGENOM; HOG000275916; -. DR KO; K06177; -. DR OMA; GEYVEQT; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NMEN122586:GHGG-898-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR PROSITE; PS01129; PSI_RLU; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 103 253 PseudoU_synth_2. FT {ECO:0000259|Pfam:PF00849}. SQ SEQUENCE 307 AA; 35205 MW; FFA633B53C991489 CRC64; MKKRNNPLPL LNGVKPSYLV LPHEKQFYGL PLLHFLCIRF PFVGADDWRR RLNSGFVVGS DGAALDEHSL FEPGKVVFYY RETSRESEPR IPFEEKILHI DEHLIVVDKP HFLPVIPSGR FLRETLLTRL RLRPELQHLN VEDITPLHRL DKDTAGVMLL SHNPATRGAY QTMFQNKTVW KTYEALAPTR TDLPYPLDVV SRLVRGEKFF TTQEAEGEPN AHTTVELIEN RGEFSLYRLT PHTGKKHQLR VHMMGLGMPL LNDALYPVPS EAGSEDYRKP LKLLAKKIAF ADPLSGRERV FCSGFCL // ID Q9JXE1_NEIMB Unreviewed; 202 AA. AC Q9JXE1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative hemolysin {ECO:0000313|EMBL:AAF42408.1}; GN OrderedLocusNames=NMB2091 {ECO:0000313|EMBL:AAF42408.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42408.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42408.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42408.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42408.1; -; Genomic_DNA. DR PIR; A81008; A81008. DR RefSeq; NP_275079.1; NC_003112.2. DR RefSeq; WP_002215066.1; NC_003112.2. DR STRING; 122586.NMB2091; -. DR PaxDb; Q9JXE1; -. DR EnsemblBacteria; AAF42408; AAF42408; NMB2091. DR GeneID; 903958; -. DR KEGG; nme:NMB2091; -. DR PATRIC; 20360352; VBINeiMen85645_2673. DR eggNOG; ENOG4105W4M; Bacteria. DR eggNOG; COG2823; LUCA. DR HOGENOM; HOG000254779; -. DR OMA; MLQGCIG; -. DR OrthoDB; EOG6C5RQ0; -. DR BioCyc; NMEN122586:GHGG-2156-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007055; BON_dom. DR Pfam; PF04972; BON; 2. DR PROSITE; PS50914; BON; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 202 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327666. FT DOMAIN 53 123 BON. {ECO:0000259|PROSITE:PS50914}. FT DOMAIN 133 202 BON. {ECO:0000259|PROSITE:PS50914}. SQ SEQUENCE 202 AA; 21746 MW; 6715D110C53E1359 CRC64; MKPKPHTVRT LIAAIFSLAL SGCVSAVIGS AAVGAKSAVD RRTTGAQTDD NVMALRIETT ARSYLRQNNQ TKGYTPQISV VGYNRHLLLL GQVATEGEKQ FVGQIARSEQ AAEGVYNYIT VASLPRTAGD IAGDTWNTSK VRATLLGISP ATQARVKIVT YGNVTYVMGI LTPEEQAQIT QKVSTTVGVQ KVITLYQNYV QR // ID Q9K1M8_NEIMB Unreviewed; 52 AA. AC Q9K1M8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40527.1}; GN OrderedLocusNames=NMB0058 {ECO:0000313|EMBL:AAF40527.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40527.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40527.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40527.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40527.1; -; Genomic_DNA. DR PIR; C81242; C81242. DR STRING; 122586.NMB0058; -. DR PaxDb; Q9K1M8; -. DR EnsemblBacteria; AAF40527; AAF40527; NMB0058. DR PATRIC; 20355121; VBINeiMen85645_0094. DR OrthoDB; EOG6MH5NH; -. DR BioCyc; NMEN122586:GHGG-64-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 52 AA; 6077 MW; 27B596339EC39938 CRC64; MPSEHAFGRR FYNKNTSWRL VLCLSKFLCR AYLKISDGIG LCCLKSVFRF SL // ID Q9JXN6_NEIMB Unreviewed; 208 AA. AC Q9JXN6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Cadmium resistance protein {ECO:0000313|EMBL:AAF42284.1}; GN OrderedLocusNames=NMB1955 {ECO:0000313|EMBL:AAF42284.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42284.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42284.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42284.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42284.1; -; Genomic_DNA. DR PIR; D81021; D81021. DR RefSeq; NP_274949.1; NC_003112.2. DR RefSeq; WP_002225839.1; NC_003112.2. DR STRING; 122586.NMB1955; -. DR PaxDb; Q9JXN6; -. DR EnsemblBacteria; AAF42284; AAF42284; NMB1955. DR GeneID; 904195; -. DR KEGG; nme:NMB1955; -. DR PATRIC; 20359969; VBINeiMen85645_2489. DR eggNOG; ENOG4105MVG; Bacteria. DR eggNOG; COG4300; LUCA. DR HOGENOM; HOG000099674; -. DR OMA; VIIYCIV; -. DR OrthoDB; EOG6RG02S; -. DR BioCyc; NMEN122586:GHGG-2012-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004676; Cd-R_transporter. DR Pfam; PF03596; Cad; 1. DR TIGRFAMs; TIGR00779; cad; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 13 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 195 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 208 AA; 23056 MW; 73E619FA74CF419E CRC64; MRCFMIQNVV TSIILYSGTA VDLLIILMLF FAKRKSRKDI INIYLGQFLG SVSLILLSLL FAFVLDYIPS KEILGLLGLI PILLGIKVLL LGDSDGEAIA KEGLRKDNKN LIFLVAMITF ASCGADNIGV FVPYFTTLNL ANLIVALLTF LVMIYLLVFS AQKLAQVPSV GETLEKYSRW FVAVVYLGLG IYILVENNSF DMLWTVLG // ID Q9JZ54_NEIMB Unreviewed; 146 AA. AC Q9JZ54; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41660.1}; GN OrderedLocusNames=NMB1284 {ECO:0000313|EMBL:AAF41660.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41660.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41660.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41660.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41660.1; -; Genomic_DNA. DR PIR; C81100; C81100. DR RefSeq; NP_274304.1; NC_003112.2. DR RefSeq; WP_002222384.1; NC_003112.2. DR STRING; 122586.NMB1284; -. DR PaxDb; Q9JZ54; -. DR EnsemblBacteria; AAF41660; AAF41660; NMB1284. DR GeneID; 903706; -. DR KEGG; nme:NMB1284; -. DR PATRIC; 20358195; VBINeiMen85645_1609. DR HOGENOM; HOG000258661; -. DR OMA; FHAEAWI; -. DR OrthoDB; EOG6MD96X; -. DR BioCyc; NMEN122586:GHGG-1322-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR025423; DUF4149. DR Pfam; PF13664; DUF4149; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 138 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 13 103 DUF4149. {ECO:0000259|Pfam:PF13664}. SQ SEQUENCE 146 AA; 15926 MW; E0E21892562E129A CRC64; MMQTFRKISR YVATLWLGMQ IMAGYIAAPV LFKMLPKMQA GEIAGVLFDI LSWSGLAVWG AVLAAAFAAL TRRQTALLLF LLSALAANRF LITPVIEALK YGHENWLLSF VGGSFGMWHG ISSIVFMATA LLSAVLSWRL SGKDAV // ID Q9K0R4_NEIMB Unreviewed; 311 AA. AC Q9K0R4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40948.1}; GN OrderedLocusNames=NMB0516 {ECO:0000313|EMBL:AAF40948.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40948.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40948.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40948.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40948.1; -; Genomic_DNA. DR PIR; F81188; F81188. DR RefSeq; NP_273562.1; NC_003112.2. DR RefSeq; WP_002246836.1; NC_003112.2. DR STRING; 122586.NMB0516; -. DR PaxDb; Q9K0R4; -. DR EnsemblBacteria; AAF40948; AAF40948; NMB0516. DR GeneID; 902632; -. DR KEGG; nme:NMB0516; -. DR PATRIC; 20356276; VBINeiMen85645_0658. DR eggNOG; ENOG4105RU2; Bacteria. DR eggNOG; ENOG4111YYF; LUCA. DR HOGENOM; HOG000218793; -. DR OMA; ETCPISI; -. DR OrthoDB; EOG6TTVKC; -. DR BioCyc; NMEN122586:GHGG-541-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR029074; Imm49. DR Pfam; PF15575; Imm49; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 311 AA; 36516 MW; 62844E9820A1E5C8 CRC64; MGHNMMTTQK WYEHITNVII GNTANFNSGC PESIDYVDEK KGVPLAAMKY ILMYTEAAAS HAYLFEHDLK KFKQYAYVAG KLGILQSVDD EDPEPFFFPC DMLNIQDPMF LMLMSDSPQL REFLVRNIDN IANDTEAFVN RYDLNRHMIY NTLLMVEGKQ LDRLKQRSEK VLAHPTPSKW LQKRLYDYRF FLAFAEQDAE AMKAALEPLF DKKTARMAAK ETLSYFDFYL QPQIVTYAKI ASMHGFDLGI DHEIAPRDLT VYDPLPADEY QDIFDFMKQY DLSYPYEYLQ DWIDYYTFKT DKLVFGNAKR E // ID Q9K0F2_NEIMB Unreviewed; 235 AA. AC Q9K0F2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41075.1}; GN OrderedLocusNames=NMB0655 {ECO:0000313|EMBL:AAF41075.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41075.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41075.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41075.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41075.1; -; Genomic_DNA. DR PIR; A81174; A81174. DR RefSeq; NP_273697.1; NC_003112.2. DR RefSeq; WP_002222808.1; NC_003112.2. DR ProteinModelPortal; Q9K0F2; -. DR STRING; 122586.NMB0655; -. DR PaxDb; Q9K0F2; -. DR EnsemblBacteria; AAF41075; AAF41075; NMB0655. DR GeneID; 902767; -. DR KEGG; nme:NMB0655; -. DR PATRIC; 20356609; VBINeiMen85645_0823. DR eggNOG; ENOG4105YIQ; Bacteria. DR eggNOG; ENOG41126JQ; LUCA. DR HOGENOM; HOG000219103; -. DR OMA; QTRIFND; -. DR OrthoDB; EOG6P5ZDG; -. DR BioCyc; NMEN122586:GHGG-682-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR SUPFAM; SSF51294; SSF51294; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 235 AA; 26154 MW; 6EDA50CE12CE68A9 CRC64; MVKTADGYKA IARIRTGDRV FAKDEASGKT GYKPVTARYG NPYQETVYIE ISDGIGNNQT LISNKIHPFY SQGKWIQAGR LKKGDTLLSE SGAKQTVQNI TFKQQPLKAY NLTVADWHTY FVKGSQAETE GVWVHNDCPY DKGNQRYKDA SYHGKNDNSV KSRAPTNGQA ALDNSVQVKS TSPRRVGVDK ANNEIVVLNK TQTFNNGSAE YHGHVRSWQD LHTDQKNALK KAGLD // ID Q7DDN6_NEIMB Unreviewed; 87 AA. AC Q7DDN6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40942.1}; GN OrderedLocusNames=NMB0510 {ECO:0000313|EMBL:AAF40942.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40942.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40942.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40942.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40942.1; -; Genomic_DNA. DR RefSeq; NP_273556.1; NC_003112.2. DR RefSeq; WP_002234239.1; NC_003112.2. DR STRING; 122586.NMB0510; -. DR PaxDb; Q7DDN6; -. DR EnsemblBacteria; AAF40942; AAF40942; NMB0510. DR GeneID; 902626; -. DR KEGG; nme:NMB0510; -. DR PATRIC; 20356266; VBINeiMen85645_0653. DR HOGENOM; HOG000218791; -. DR OrthoDB; EOG60PHFF; -. DR BioCyc; NMEN122586:GHGG-535-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 87 AA; 10685 MW; 7809E9BD020A4D61 CRC64; MDKEIKICPR CEQGYLYHAK PKYFSGEVIL CDECYAMWLG DMKIFYGQYG KDFYDYHEFM KDKGIEEINM WEGELFDHPY YEDEKFK // ID Q9JZS4_NEIMB Unreviewed; 122 AA. AC Q9JZS4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Death-on-curing protein {ECO:0000313|EMBL:AAF41325.1}; GN OrderedLocusNames=NMB0917 {ECO:0000313|EMBL:AAF41325.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41325.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41325.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41325.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41325.1; -; Genomic_DNA. DR PIR; G81142; G81142. DR RefSeq; NP_273957.1; NC_003112.2. DR RefSeq; WP_002217436.1; NC_003112.2. DR ProteinModelPortal; Q9JZS4; -. DR STRING; 122586.NMB0917; -. DR PaxDb; Q9JZS4; -. DR EnsemblBacteria; AAF41325; AAF41325; NMB0917. DR GeneID; 903038; -. DR KEGG; nme:NMB0917; -. DR PATRIC; 20357271; VBINeiMen85645_1149. DR eggNOG; ENOG4107ZD0; Bacteria. DR eggNOG; COG3654; LUCA. DR HOGENOM; HOG000072185; -. DR KO; K07341; -. DR OMA; FHDRILQ; -. DR OrthoDB; EOG64BQCR; -. DR BioCyc; NMEN122586:GHGG-955-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:InterPro. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR006440; Doc. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR PIRSF; PIRSF018297; Doc; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR TIGRFAMs; TIGR01550; DOC_P1; 1. DR PROSITE; PS51459; FIDO; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 118 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 122 AA; 13387 MW; 452A954661DEA271 CRC64; MIDGELVALI HQTVLADEAG LKGRADMARL DGALSRIANW RQYENLEDIY EIAALYAQAI AKAHAFPDGN KRTALLTMLT YLDLQGISIA ADQGLDDLIV SLAAGETDFK QLAETLRRLD KE // ID Q9JZX5_NEIMB Unreviewed; 66 AA. AC Q9JZX5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41269.1}; GN OrderedLocusNames=NMB0858 {ECO:0000313|EMBL:AAF41269.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41269.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41269.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41269.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41269.1; -; Genomic_DNA. DR PIR; E81150; E81150. DR RefSeq; NP_273899.1; NC_003112.2. DR RefSeq; WP_002217509.1; NC_003112.2. DR STRING; 122586.NMB0858; -. DR PaxDb; Q9JZX5; -. DR EnsemblBacteria; AAF41269; AAF41269; NMB0858. DR GeneID; 902972; -. DR KEGG; nme:NMB0858; -. DR PATRIC; 20357109; VBINeiMen85645_1073. DR HOGENOM; HOG000218877; -. DR OMA; MEISVRI; -. DR OrthoDB; EOG6H4K9K; -. DR BioCyc; NMEN122586:GHGG-889-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 66 AA; 7795 MW; D30CB2F7516226EE CRC64; MQLICADWTG IGNFMKTFEK TWSAQYRDME ISVRNFWNLE RTGAEVYING RRVYHNEAEM ASASLR // ID Q9JZD4_NEIMB Unreviewed; 469 AA. AC Q9JZD4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Phage sheath protein {ECO:0000313|EMBL:AAF41495.1}; GN OrderedLocusNames=NMB1104 {ECO:0000313|EMBL:AAF41495.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41495.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41495.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41495.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41495.1; -; Genomic_DNA. DR PIR; E81121; E81121. DR RefSeq; NP_274135.1; NC_003112.2. DR RefSeq; WP_002225237.1; NC_003112.2. DR STRING; 122586.NMB1104; -. DR PaxDb; Q9JZD4; -. DR EnsemblBacteria; AAF41495; AAF41495; NMB1104. DR GeneID; 903526; -. DR KEGG; nme:NMB1104; -. DR PATRIC; 20357772; VBINeiMen85645_1402. DR eggNOG; ENOG4105TKZ; Bacteria. DR eggNOG; COG4386; LUCA. DR HOGENOM; HOG000123724; -. DR OMA; TYTKDAQ; -. DR OrthoDB; EOG6TJ7X1; -. DR BioCyc; NMEN122586:GHGG-1140-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007067; Tail_sheath. DR Pfam; PF04984; Phage_sheath_1; 1. DR PIRSF; PIRSF007349; Tsp_L; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 469 AA; 49269 MW; 493C6B1C8C2737A1 CRC64; MPHIDFDTIP GSIRVPGQYI EFNTRNAVQG LPQNPQKVLM VAPMLTAGIQ PALEPVQLFS DAEAADLFGQ GSLAHLMVRQ AFANNPYLDL TVIGIADHSA GVQATATVTL SGTATAPGVV EITIGGKQVS TAVNTGETAA TVADRLKTAI TAADVTVTAS GSGAAVTLTA KHKGEIGNES GLTVSTGNTG LTYQANAFTG GAKNADIATA LSKVAGKHYH IICSPFSDDA NAKALSNHIT NVSNAIEQRG CIGVLGMSAA LSTATTATGE INDGRMTCAW YKGAVEPNGI IAAGYAAVLA FEEDPAKPLN TLEIKGLAVT PDAQWPLFAE CNNALYNGLT PLTVVNNRVQ IMRAVSTYTK SANNTDDPAL LDITTIRTLD YVRRSVKERI ALRFPRDKLS DRLLPKVKSE ILDVLIKLDQ AEIIENAEAN KGKLVVARAQ NDPNRVNAII PADVVNGLHV FAGRIDLIL // ID Q9K1M7_NEIMB Unreviewed; 672 AA. AC Q9K1M7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40529.1}; GN OrderedLocusNames=NMB0060 {ECO:0000313|EMBL:AAF40529.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40529.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40529.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40529.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40529.1; -; Genomic_DNA. DR PIR; E81242; E81242. DR RefSeq; NP_273125.1; NC_003112.2. DR RefSeq; WP_002224746.1; NC_003112.2. DR PaxDb; Q9K1M7; -. DR EnsemblBacteria; AAF40529; AAF40529; NMB0060. DR GeneID; 902167; -. DR KEGG; nme:NMB0060; -. DR PATRIC; 20355125; VBINeiMen85645_0096. DR eggNOG; ENOG4105EPD; Bacteria. DR eggNOG; COG1297; LUCA. DR HOGENOM; HOG000060682; -. DR OMA; FMTANLY; -. DR OrthoDB; EOG67DPKN; -. DR BioCyc; NMEN122586:GHGG-66-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004814; Oligopep_transpt. DR InterPro; IPR004813; OPT. DR Pfam; PF03169; OPT; 1. DR TIGRFAMs; TIGR00728; OPT_sfam; 1. DR TIGRFAMs; TIGR00733; TIGR00733; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 286 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 350 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 402 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 417 437 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 458 475 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 522 541 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 561 580 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 601 626 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 646 664 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 672 AA; 70300 MW; 79E13C5CA16D7774 CRC64; MNKSLSSSVE EYRELTLRGM ILGALITVIF TASNVYLGLK VGLTFASSIP AAVISMAVLK FFKGSNILEN NMVQTQASAA GTLSTIIFVL PGLLMAGYWS GFPFWQTTLL CIAGGILGVI FTIPLRYAMV VKSDLPYPEG VAAAEILKVG GHEEGDNRQG GSGIKELAAG GALAGLMSFC AGGLRVIADS ASYWFKSGTA IFQLPMGFSL ALLGAGYLVG LTGGIAILLG ISIAWGIAVP YFSSHIPQPS DMEMAAFAMK LWKEKVRFIG AGTIGIAAVW TLLMLLKPMV EGMKMSFKSF GGGAPAAERA EQDLSPKAMI FWVLAMMFVL GVSFYHFIGD SHITGGMAWL LVVVCTLLAS VIGFLVAAAC GYMAGLVGSS SSPISGVGIV SVVVISLVLL LVGESGGLLA DEANRKFLLA LTLFCGSAVI CVASISNDNL QDLKTGYLLK ATPWRQQVAL IIGCIVGALV ISPVLELLYE AYGFTGAMPR EGMDAAQALA APQATLMTTI ASGIFAHNLE WVYIFTGIVI GAVLIVVDLV LKKSSGGKLA LPVLAVGMGI YLPPSVNMPI VAGAVLAAVL KHIIGKKAEN REGRLKNAER IGTLFSAGLI VGESLIGVIM AFIIAFSVTN GGSDAPLALN LQNWDAAASW LGLAFFVTGM FFFAQRVLKA GK // ID Q9JZU8_NEIMB Unreviewed; 140 AA. AC Q9JZU8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=AzlC-related protein {ECO:0000313|EMBL:AAF41301.1}; GN OrderedLocusNames=NMB0892 {ECO:0000313|EMBL:AAF41301.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41301.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41301.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41301.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41301.1; -; Genomic_DNA. DR PIR; B81146; B81146. DR RefSeq; NP_273933.1; NC_003112.2. DR RefSeq; WP_002225355.1; NC_003112.2. DR STRING; 122586.NMB0892; -. DR PaxDb; Q9JZU8; -. DR EnsemblBacteria; AAF41301; AAF41301; NMB0892. DR GeneID; 903011; -. DR KEGG; nme:NMB0892; -. DR PATRIC; 20357205; VBINeiMen85645_1118. DR eggNOG; COG1296; LUCA. DR HOGENOM; HOG000218898; -. DR OMA; YNMTHIS; -. DR OrthoDB; EOG6K9QNJ; -. DR BioCyc; NMEN122586:GHGG-928-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011606; Brnchd-chn_aa_trnsp_permease. DR Pfam; PF03591; AzlC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15271 MW; 430C1451B18C9AAB CRC64; MLIGLLPWAL ILGMQGGQKG MSWLEMLLMT SMNFAGGSEF ATVNLWAEPL PILLIATVTF MINSRHILMG AALAPHLKGI PLKKAVPALF FMCDESWAMA FSEIQKRKAA GLPAFNMPFY SGLTKTSTAL PRLSSKKTIL // ID Q7DD96_NEIMB Unreviewed; 470 AA. AC Q7DD96; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Trk system potassium uptake protein TrkA {ECO:0000313|EMBL:AAF41966.1}; GN Name=trkA {ECO:0000313|EMBL:AAF41966.1}; GN OrderedLocusNames=NMB1614 {ECO:0000313|EMBL:AAF41966.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41966.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41966.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41966.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41966.1; -; Genomic_DNA. DR PIR; D81063; D81063. DR RefSeq; NP_274620.1; NC_003112.2. DR RefSeq; WP_002212772.1; NC_003112.2. DR ProteinModelPortal; Q7DD96; -. DR STRING; 122586.NMB1614; -. DR PaxDb; Q7DD96; -. DR EnsemblBacteria; AAF41966; AAF41966; NMB1614. DR GeneID; 904179; -. DR KEGG; nme:NMB1614; -. DR PATRIC; 20359120; VBINeiMen85645_2072. DR eggNOG; ENOG4105C1A; Bacteria. DR eggNOG; COG0569; LUCA. DR HOGENOM; HOG000227130; -. DR KO; K03499; -. DR OMA; IACQVAY; -. DR OrthoDB; EOG6ZH2G8; -. DR BioCyc; NMEN122586:GHGG-1662-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006036; K_uptake_TrkA. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF02080; TrkA_C; 2. DR Pfam; PF02254; TrkA_N; 2. DR PRINTS; PR00335; KUPTAKETRKA. DR SUPFAM; SSF116726; SSF116726; 2. DR SUPFAM; SSF51735; SSF51735; 2. DR PROSITE; PS51202; RCK_C; 2. DR PROSITE; PS51201; RCK_N; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ion transport {ECO:0000256|SAAS:SAAS00513537}; KW Potassium {ECO:0000256|SAAS:SAAS00513537}; KW Potassium transport {ECO:0000256|SAAS:SAAS00513537}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|SAAS:SAAS00513537}. FT DOMAIN 2 138 RCK N-terminal. FT {ECO:0000259|PROSITE:PS51201}. FT DOMAIN 150 235 RCK C-terminal. FT {ECO:0000259|PROSITE:PS51202}. FT DOMAIN 242 362 RCK N-terminal. FT {ECO:0000259|PROSITE:PS51201}. FT DOMAIN 376 464 RCK C-terminal. FT {ECO:0000259|PROSITE:PS51202}. SQ SEQUENCE 470 AA; 51070 MW; 98F41B4CAE8CF0FC CRC64; MKILILGNGQ VGSTVAQNLA AIPNNDVTVI DIDEKALQET GSRLDVQTVF GNGASPFTLE RAGAEDADLL LALSRSDETN IVACKVAADL FNIPGRIARV RSSEYLEYLS PKLENNENGS LSIFGITETI SPEQLVTEQL AGLIDCPGAL QVLRFADDRV RMVIIQARRG GLLVGRSIAD IAQDLPDGAD CQICAVYRNN RLIVPAPQTV IIEGDEILFA AAAENIGAVI PELRPKETST RRIMIAGGGN IGYRLAKQLE HAYNVKIIEC RPRRAEWIAE NLDNTLVLQG SATDETLLDN EYIDEIDVFC ALTNDDESNI MSALLAKNLG AKRVIGIVNR SSYVDLLEGN KIDIVVSPHL ITIGSILAHI RRGDIVAVHP IRRGTAEAIE VVAHGDKKTS AIIGRRISGI KWPEGCHIAA VVRAGTGETI MGHHTETVIQ DGDHIIFFVS RRRILNELEK LIQVKMGFFG // ID Q9JXD3_NEIMB Unreviewed; 77 AA. AC Q9JXD3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42417.1}; GN OrderedLocusNames=NMB2100 {ECO:0000313|EMBL:AAF42417.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42417.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42417.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42417.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42417.1; -; Genomic_DNA. DR PIR; E81006; E81006. DR RefSeq; NP_275088.1; NC_003112.2. DR RefSeq; WP_002225724.1; NC_003112.2. DR STRING; 122586.NMB2100; -. DR PaxDb; Q9JXD3; -. DR EnsemblBacteria; AAF42417; AAF42417; NMB2100. DR GeneID; 903941; -. DR KEGG; nme:NMB2100; -. DR PATRIC; 20360370; VBINeiMen85645_2682. DR HOGENOM; HOG000218709; -. DR OrthoDB; EOG6JDWJK; -. DR BioCyc; NMEN122586:GHGG-2165-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 47 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 50 73 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 77 AA; 8951 MW; B023622AF2265248 CRC64; MWHIVAIGYL FVAVMYSAAQ PSIARALIYL VFWAVLPTVF TVFTITVRRR NHLMRQQEQA ESEQQRAQRQ KDSGTKP // ID Q9JXM5_NEIMB Unreviewed; 505 AA. AC Q9JXM5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42300.1}; GN OrderedLocusNames=NMB1971 {ECO:0000313|EMBL:AAF42300.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42300.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42300.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42300.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42300.1; -; Genomic_DNA. DR PIR; B81021; B81021. DR RefSeq; NP_274965.1; NC_003112.2. DR RefSeq; WP_002244327.1; NC_003112.2. DR ProteinModelPortal; Q9JXM5; -. DR STRING; 122586.NMB1971; -. DR PaxDb; Q9JXM5; -. DR EnsemblBacteria; AAF42300; AAF42300; NMB1971. DR GeneID; 904170; -. DR KEGG; nme:NMB1971; -. DR PATRIC; 20360011; VBINeiMen85645_2510. DR HOGENOM; HOG000218740; -. DR KO; K07280; -. DR OMA; YAIEGHH; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NMEN122586:GHGG-2028-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 505 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327679. SQ SEQUENCE 505 AA; 56756 MW; A631E22A120B52B8 CRC64; MLYFRYGFLV VWCAAGVSAA YGADAPAILD DKALLQVQRS VSDKWAESDW KVENDAPRVV DGDFLLAHPK MLEHSLRDAL NGNQADLIAS LADLYAKLPD YDAVLYGRAR ALLAKLAGRP AEAVARYREL HGENAADERI LLDLAAAEFD DFRLKSAERH FAEAAKLDLP APVLENVGRF RKKTEGLTGW RFSGGISPAV NRNANNAAPQ YCRQNGGRQI CSVSRAERAA GLNYEIEAEK LTPLADNHYL LFRSNIGGTS YYFSKKSAYD DGFGRAYLGW QYKNARQTAG ILPFYQVQLS GSDGFDAKTK RVNNRRLPPY MLAHGVGVQL SHTYRPNPGW QFSVALEHYR QRYREQDRAE YNNGRQDGFY VSSAKRLGES ATVFGGWQFV RFVPKRETVG GAVNNAAYRR NGVYAGWAQE WRQLGGLNSR VSASYARRNY KGIAAFSTEA QRNREWNVSL ALSHDKLSYK GIVPALNYRF GRTESNVPYA KRRNSEVFVS ADWRF // ID Q9JY68_NEIMB Unreviewed; 467 AA. AC Q9JY68; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Multidrug efflux pump channel protein {ECO:0000313|EMBL:AAF42061.1}; GN Name=mtrE {ECO:0000313|EMBL:AAF42061.1}; GN OrderedLocusNames=NMB1714 {ECO:0000313|EMBL:AAF42061.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42061.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42061.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42061.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362097}; Lipid-anchor CC {ECO:0000256|RuleBase:RU362097}. CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) CC family. {ECO:0000256|RuleBase:RU362097}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42061.1; -; Genomic_DNA. DR PIR; D81051; D81051. DR RefSeq; NP_274717.1; NC_003112.2. DR RefSeq; WP_002244265.1; NC_003112.2. DR ProteinModelPortal; Q9JY68; -. DR STRING; 122586.NMB1714; -. DR PaxDb; Q9JY68; -. DR EnsemblBacteria; AAF42061; AAF42061; NMB1714. DR GeneID; 903388; -. DR KEGG; nme:NMB1714; -. DR PATRIC; 20359389; VBINeiMen85645_2200. DR eggNOG; ENOG4105ENJ; Bacteria. DR eggNOG; COG1538; LUCA. DR HOGENOM; HOG000111955; -. DR KO; K18139; -. DR OMA; TITKARY; -. DR OrthoDB; EOG6MWN87; -. DR BioCyc; NMEN122586:GHGG-1769-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT. DR Pfam; PF02321; OEP; 2. DR TIGRFAMs; TIGR01845; outer_NodT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000256|RuleBase:RU362097}; KW Membrane {ECO:0000256|RuleBase:RU362097}; KW Palmitate {ECO:0000256|RuleBase:RU362097}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362097}; KW Transmembrane beta strand {ECO:0000256|RuleBase:RU362097}. SQ SEQUENCE 467 AA; 50477 MW; C76032302F34F939 CRC64; MDTTLKTTLT SVAAAFALSA CTMIPQYEQP KVEVAETFKN DTADSGIRAV DLGWHDYFAD PRLQKLIDIA LERNTSLRTA VLNSEIYRKQ YMIERNNLLP TLAANANDSR QGSLSGGNVS SSYKVGLGAA SYELDLFGRV RSSSEAALQG YFASTANRDA AHLSLIATVA KAYFNERYAE EAMSLAQRVL KTREETYKLS ELRYKAGVIS AVALRQQEAL IESAKADYAH AARSREQARN ALATLINQPI PEDLPAGLPL DKQFFVEKLP AGLSSEVLLD RPDIRAAEHA LKQANANIGA ARAAFFPSIR LTGTVGTGSA ELGGLFKSGT GVWSFAPSIT LPIFTWGTNK ANLDVAKLRQ QVQIVAYESA VQSAFQDVAN ALAAREQLDK AYDALSKQSR ASKEALRLVG LRYKHGVSGA LDLLDAERSS YAAEGAALSA QLTRAENLAD LYKALGGGLK RDTQTDK // ID Q9JYP6_NEIMB Unreviewed; 46 AA. AC Q9JYP6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41842.1}; GN OrderedLocusNames=NMB1486 {ECO:0000313|EMBL:AAF41842.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41842.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41842.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41842.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41842.1; -; Genomic_DNA. DR PIR; D81077; D81077. DR RefSeq; NP_274494.1; NC_003112.2. DR RefSeq; WP_010980945.1; NC_003112.2. DR STRING; 122586.NMB1486; -. DR PaxDb; Q9JYP6; -. DR EnsemblBacteria; AAF41842; AAF41842; NMB1486. DR GeneID; 903908; -. DR KEGG; nme:NMB1486; -. DR PATRIC; 20358738; VBINeiMen85645_1878. DR HOGENOM; HOG000027853; -. DR OrthoDB; EOG6KQ6MF; -. DR BioCyc; NMEN122586:GHGG-1526-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 46 AA; 5449 MW; 404E1ABB66D2A50A CRC64; MAFCHCPDKL LNYLNYFDRR YTHMQDPEQS SKPARRFLCV PSVQAA // ID Q9K129_NEIMB Unreviewed; 257 AA. AC Q9K129; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=FrpC operon protein {ECO:0000313|EMBL:AAF40807.1}; GN OrderedLocusNames=NMB0364 {ECO:0000313|EMBL:AAF40807.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40807.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40807.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40807.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40807.1; -; Genomic_DNA. DR PIR; C81206; C81206. DR RefSeq; NP_273413.1; NC_003112.2. DR RefSeq; WP_010980785.1; NC_003112.2. DR STRING; 122586.NMB0364; -. DR PaxDb; Q9K129; -. DR EnsemblBacteria; AAF40807; AAF40807; NMB0364. DR GeneID; 902480; -. DR KEGG; nme:NMB0364; -. DR PATRIC; 20355885; VBINeiMen85645_0460. DR HOGENOM; HOG000219111; -. DR OMA; NNATKWL; -. DR BioCyc; NMEN122586:GHGG-386-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010692; FrpC. DR Pfam; PF06901; FrpC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 257 AA; 29955 MW; 8193A2129BC55F5C CRC64; MRPYATTIYQ LFILFIGSVF TMTSCEPVNE QTSFNNPEPM TGFEHTVTFD FQGTKMVIPY GYLARYTQNN ATKWLSDTPG QDAYSINLIE ISVYYKKTDQ GWVLEPYNQQ NKAHFIQFLR DGLDSVDDIV IRKDACSLST TMGERLLTYG VKKMPSAYPE YEAYEDKRHI PENPYFHEFY YIKKGENPAI ITHRNNRINQ TEEDSYSTSV GSCINGFTVR YYPFIREKQQ LTQQELVGYH QQVEQLVQSF VNNSSKK // ID Q9JYQ1_NEIMB Unreviewed; 44 AA. AC Q9JYQ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41837.1}; GN OrderedLocusNames=NMB1481 {ECO:0000313|EMBL:AAF41837.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41837.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41837.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41837.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41837.1; -; Genomic_DNA. DR PIR; F81079; F81079. DR RefSeq; NP_274489.1; NC_003112.2. DR RefSeq; WP_010980944.1; NC_003112.2. DR STRING; 122586.NMB1481; -. DR PaxDb; Q9JYQ1; -. DR EnsemblBacteria; AAF41837; AAF41837; NMB1481. DR GeneID; 903903; -. DR KEGG; nme:NMB1481; -. DR BioCyc; NMEN122586:GHGG-1521-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 44 AA; 5124 MW; 80BA28FC0A348946 CRC64; MPSETFRRHR QPISAGYPII AFFSLNSTFP FPKIFPHPFQ NTLS // ID Q9K022_NEIMB Unreviewed; 221 AA. AC Q9K022; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Putative NAD(P)H nitroreductase {ECO:0000313|EMBL:AAF41217.1}; GN OrderedLocusNames=NMB0804 {ECO:0000313|EMBL:AAF41217.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41217.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41217.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41217.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41217.1; -; Genomic_DNA. DR PIR; C81155; C81155. DR RefSeq; NP_273846.1; NC_003112.2. DR RefSeq; WP_002225416.1; NC_003112.2. DR ProteinModelPortal; Q9K022; -. DR STRING; 122586.NMB0804; -. DR PaxDb; Q9K022; -. DR EnsemblBacteria; AAF41217; AAF41217; NMB0804. DR GeneID; 902919; -. DR KEGG; nme:NMB0804; -. DR PATRIC; 20356995; VBINeiMen85645_1016. DR eggNOG; ENOG4108RCM; Bacteria. DR eggNOG; COG0778; LUCA. DR HOGENOM; HOG000146738; -. DR OMA; CLAEEGL; -. DR OrthoDB; EOG65QWJJ; -. DR BioCyc; NMEN122586:GHGG-835-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 14 181 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. SQ SEQUENCE 221 AA; 24703 MW; A1B9E6C21F0F4C3D CRC64; MTVLSKEQVL SAFKNRKSCR HYDAARKISA EDFQFILELG RLSPSSVGSE PWQFIVVQNP EIRQAIKPFS WGMADALDTA SHLVVFLAKK NARSDSPFML ESLKRRGVTE PDAVAKSLAR YQAFQADDIK ILDDSRALFD WCCRQTYIAL ANMMTGAAMA GIDSCPVEGF NYAEMERILS GQFGLFDAAE WGVSVAATFG YRVQEIATKA RRPLEETVIW A // ID Q9JYT8_NEIMB Unreviewed; 259 AA. AC Q9JYT8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41797.1}; GN OrderedLocusNames=NMB1436 {ECO:0000313|EMBL:AAF41797.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41797.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41797.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41797.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41797.1; -; Genomic_DNA. DR PIR; D81083; D81083. DR RefSeq; NP_274448.1; NC_003112.2. DR RefSeq; WP_002222289.1; NC_003112.2. DR STRING; 122586.NMB1436; -. DR PaxDb; Q9JYT8; -. DR EnsemblBacteria; AAF41797; AAF41797; NMB1436. DR GeneID; 903857; -. DR KEGG; nme:NMB1436; -. DR PATRIC; 20358585; VBINeiMen85645_1804. DR eggNOG; ENOG4105CHG; Bacteria. DR eggNOG; COG0247; LUCA. DR HOGENOM; HOG000262113; -. DR KO; K18928; -. DR OMA; NSCLMHI; -. DR OrthoDB; EOG6GTZM6; -. DR BioCyc; NMEN122586:GHGG-1474-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR004017; Cys_rich_dom. DR Pfam; PF02754; CCG; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 100 CCG. {ECO:0000259|Pfam:PF02754}. FT DOMAIN 146 230 CCG. {ECO:0000259|Pfam:PF02754}. SQ SEQUENCE 259 AA; 28253 MW; 49FE5B8B348AE18C CRC64; MSATIPPKII RYDSNPTDVY FFGTCVLDLF MPEAGMDAIT LIEQQGIRVH FPMAQSCCGQ PAYSSGHPTE AFDVAKAQLD LFPENWPIVV PSGSCGGMMK HHWPTLFKGS EYEERAVDCA GRIIEFTHFL LAIGFKPEDK GEPLKVAVHT SCAARREMNV HLSGWQLIDG MENVERIVHD HESECCGFGG TFSVKQADIS GAMVTDKVAA LKETGATEII SADCGCMMNI GGKIAKDEPD MPRPKHIASF LLERTGGKA // ID Q9JZE0_NEIMB Unreviewed; 353 AA. AC Q9JZE0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Putative I protein {ECO:0000313|EMBL:AAF41489.1}; GN OrderedLocusNames=NMB1098 {ECO:0000313|EMBL:AAF41489.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41489.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41489.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41489.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41489.1; -; Genomic_DNA. DR PIR; G81120; G81120. DR RefSeq; NP_274129.1; NC_003112.2. DR RefSeq; WP_002232421.1; NC_003112.2. DR STRING; 122586.NMB1098; -. DR PaxDb; Q9JZE0; -. DR EnsemblBacteria; AAF41489; AAF41489; NMB1098. DR GeneID; 903520; -. DR KEGG; nme:NMB1098; -. DR PATRIC; 20357760; VBINeiMen85645_1396. DR eggNOG; ENOG4108TVE; Bacteria. DR eggNOG; COG4388; LUCA. DR HOGENOM; HOG000219055; -. DR OMA; KAVEPWA; -. DR OrthoDB; EOG6K6VCN; -. DR BioCyc; NMEN122586:GHGG-1134-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR012106; Phage_Mu_Gp1. DR Pfam; PF10123; Mu-like_Pro; 1. DR PIRSF; PIRSF016624; Mu_prophg_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 353 AA; 38029 MW; B4AC1EA7753487FA CRC64; MSKNAQKTLL AVCSFEVQPK DGRIQLLPYG EFRAVDGRPT DVPAWYLTEE NGHDVALLAN SSRNQLVVDY EHQTLYKEKN GQPAPAAGWM RWLEFTPKGM FAEVEWTDKA AAAIAAKEYR YISAVFSYDT KGYVSKIFHA ALTNFPALDG MDEVLAAASA QILKPETEQN PMKELLQQLF DLPDAGEEEL KAALSALVEA KPKDVALSAD VFAQLAEKDS RIAALTAQTA KPDLTKYAPI SVVQELQSKV AALTAKQEAD KGNELITAAL TSGKLLPAQK EWAKGVLKQP GGLAFLTGFI ENAQPVAALA GSQTGGKAPD ERVAALTAEE AAAAKMLGMS GEEFVKIKES EGK // ID Q9K0P5_NEIMB Unreviewed; 397 AA. AC Q9K0P5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:AAF40969.1}; DE EC=2.6.1.1 {ECO:0000313|EMBL:AAF40969.1}; GN Name=aspC {ECO:0000313|EMBL:AAF40969.1}; GN OrderedLocusNames=NMB0540 {ECO:0000313|EMBL:AAF40969.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40969.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40969.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40969.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000479}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU000479}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40969.1; -; Genomic_DNA. DR PIR; C81188; C81188. DR RefSeq; NP_273585.1; NC_003112.2. DR RefSeq; WP_002217853.1; NC_003112.2. DR ProteinModelPortal; Q9K0P5; -. DR SMR; Q9K0P5; 3-397. DR STRING; 122586.NMB0540; -. DR PaxDb; Q9K0P5; -. DR EnsemblBacteria; AAF40969; AAF40969; NMB0540. DR GeneID; 902655; -. DR KEGG; nme:NMB0540; -. DR PATRIC; 20356339; VBINeiMen85645_0688. DR eggNOG; ENOG4105CGF; Bacteria. DR eggNOG; COG1448; LUCA. DR HOGENOM; HOG000185899; -. DR KO; K00813; -. DR OMA; RVGACTI; -. DR OrthoDB; EOG6C2WBK; -. DR BioCyc; NMEN122586:GHGG-566-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR000796; Asp_trans. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11879; PTHR11879; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00799; TRANSAMINASE. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAF40969.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAF40969.1}. FT DOMAIN 28 393 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 397 AA; 43928 MW; 7ACCB5C043C6AF58 CRC64; MFFKHIEAAP ADPILGLGEA FKAETRPEKV NLGIGVYKDA SGATPLVKAV KEAEKRLLES ETTKNYLTID GVADYNAQTQ ILLFGKDHEI IASRRAKTAQ SLGGTGALRI AAEFAKRQLN AQTIWISNPT WPNHNAIAKA VGIQDKPYRY YDAAKHGLDW DGMIEDLSQA QKGDIVLLHG CCHNPTGIDP TPEQWETLAK LSAEKGWLPL FDFAYQGFGN GLEEDAYGLR VFLKHNTELL IASSYSKNFG MYNERVGAFT LVAEDEETAA RAHSQVKTII RTLYSNPASH GANTIALVLK NDDLKAQWIA ELDEMRGRIK AMRQKFVGLL KAKGASQNFD FIIKQNGMFS FSGLTPEQVD RLKNEFAIYA VRSGRINVAG ITDNNIDYLC ESIVKVL // ID Q7DDD8_NEIMB Unreviewed; 2273 AA. AC Q7DDD8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Hemagglutinin/hemolysin-related protein {ECO:0000313|EMBL:AAF41596.1}; GN OrderedLocusNames=NMB1214 {ECO:0000313|EMBL:AAF41596.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41596.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41596.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41596.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41596.1; -; Genomic_DNA. DR RefSeq; NP_274239.1; NC_003112.2. DR RefSeq; WP_002222440.1; NC_003112.2. DR ProteinModelPortal; Q7DDD8; -. DR STRING; 122586.NMB1214; -. DR PaxDb; Q7DDD8; -. DR EnsemblBacteria; AAF41596; AAF41596; NMB1214. DR GeneID; 903636; -. DR KEGG; nme:NMB1214; -. DR PATRIC; 20358011; VBINeiMen85645_1518. DR eggNOG; ENOG4105CKT; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000254529; -. DR OMA; VIPPDDS; -. DR OrthoDB; EOG6K3ZW8; -. DR BioCyc; NMEN122586:GHGG-1251-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; -; 2. DR InterPro; IPR024973; ESPR. DR InterPro; IPR010069; Fil_hemagglutn_20-aa_x2_rpt. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR025157; Haemagluttinin_rpt. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF13018; ESPR; 1. DR Pfam; PF13332; Fil_haemagg_2; 3. DR Pfam; PF05860; Haemagg_act; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. DR TIGRFAMs; TIGR01731; fil_hemag_20aa; 7. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 75 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 98 218 Haemagg_act. {ECO:0000259|SMART:SM00912}. SQ SEQUENCE 2273 AA; 242989 MW; 51F30A5A1941A0EB CRC64; MNKRCYKVIF NKKRSCMMAV AENVHRDGKS MQDSEAASVR VTGAASVSSA RAAFGFRMAA FSVMLALGVA AFSPAPASGI IADKSAPKNQ QAVILQTANG LPQVNIQTPS SQGVSVNRFK QFDVDEKGVI LNNSRSNTQT QLGGWIQGNP HLARGEARVI VNQIDSSNPS LLNGYIEVGG KRAEVVVANP SGIRVNGGGL INAASVTLTS GVPVLNNGNL TGFDVSSGKV VIGGKGLDTS DADYTRILSR AAEINAGVWG KDVKVVSGKN KLDFDGSLAK TASAPSSSDS VTPTVAIDTA TLGGMYADKI TLISTDNGAV IRNKGRIFAA TGGVTLSADG KLSNSGSIDA AEITISAQTV DNRQGFIRSG KGSVLKVSDG INNQAGLIGS AGLLDIRDTG KSSLHINNTD GTIIAGKDVS LQAKSLDNDG ILTAARDVSV SLHDDFAGKR DIEAGRTLTF STQGRLKNTR IIQAGDTVSL TAAQIDNTVS GKIQSGNRTG LNGKNGITNR GLINSNGITL LQTEAKSDNA GTGRIYGSRV AVEADTLLNR EETVNGETKA AVIAARERLD IGAREIENRE AALLSSSGDL HIGSALNGSR QVQGANTSLH NRSAAIESSG NIRIATKDLQ NTNEHLRFHT EETHREHRIE YQAEGRTERY PEGSQKELGW EIFEDESLHM RTPDGSPHSV WYKYDYERIT AESKITESKP GQIISGGNLV LDAAKLKNHN SRIIAGGRLI VGTPESALDN DETLGTKTIT DKGDLHRYHR HHKKGRDSTG YSRSPYEPAP EVSSIRMGIS AYKGYAPQQA SDIPGTVVPV VAENGIHPTF TLPNSSLFAI APNNKGYLIE TDPAFTDYRK WLGSGYMLAA LQQDPNHIHK RLGDGYYEQK LVNEQIAKLT GYRRLDGYTN DEEQFKALMD NGITIAKELQ LTPGIALSAE QVARLTSDIV WLENETVTLP DGTTQTVLKP KVYVRARPKD MNGQGALLSG SVVDIGSGAI ENRGGLIAGR EALILNAQNI KNLQGDLQGK NIFAAAGSDI TNTGSIGAEN ALLLKASNNI ESRSETRSNQ NEQGSVRNIG RVAGIYLTGR QNGSVLLDAG NNIVLTASEL TNQSEDGQTV LNAGGDIRSD TTGISRNQNT IFDSDNYVIR KEQNEVGSTI RTRGNLSLNA KGDIRIRAAE VGSEQGRLKL AAGRDIKVEA GKAHTETEDA LKYTGRSGGG IKQKMTRHLK NQNGQAVSGT LDGKEIILVS GRDITVTGSN IIADNHTILS AKNNIVLKAA ETRSRSAEMN KKEKSGLMGS GGIGFTAGSK KDTQTNRSET VSHTESVVGS LNGNTLISAG KHYTQTGSTI SSPQGDVGIS SGKISIDAAQ NRYSQESKQV YEQKGVTVAI SVPVVNTVMG AVDAVKAVQT VGKSKNSRVN AMAAANALNK GVDSGVALYN AARNPKKAAG QGISVSVTYG EQKNTSESRI KGTQVQEGKI TGGGKVSLTA SGAGKDSRIT ITGSDVYGGK GTRLKAENAV QIEAARQTHQ ERSENKSAGF NAGVAIAINK GISFGFTAGA NYGKGYGNGD ETAYRNSHIG SKDSQTAIES GGDTVIKGGQ LKGKGVGVTA ESLHIESLQD TAVFKGKQEN VSAQVTVGYG FSVGGSYNRS KSSSDYASVN EQSGIFAGGD GYRIRVNGKT GLVGAAVVSD ADKSKNLLKT SEIWHKDIQN HASAAASALG LSGGFSYSPK PTSGQYSTKK EAEIGKIGGK PVSLMRFDQV SAKDDELNEK YRSERIEKGE TFKEANLNQN NAGGLKFGLK QNDIHSNDKY ALAKMGLGNL LGNAKESESR QSITRSVISE GDWQIASAQG RKNIAGIEKG TSSAHKALAK ADREGLLKEV ELNRDVAKEF INETLIGGIA DEAYRSQFIA EHRLMTFKMD ENGEPIEDKQ LEEDINKQFD NSVKLKKEFA SFKDYWEAYK AIGGNIYELR EVSDQERKNL KTARYTDPET GKTVEKIVVG VNGIFNNIQA AAKFAAQQYV GRFNPEKNRY ERTYENVYFL HNPETNGRGF SKLPEIAVAA FHKMLEGAKI GNKTVIGLSN SGLALGNIME DYGKDKNGLF VGSHSRGTLV VDNVLNTLNT QANRDKKILS NTELKMVGPA ANVVRADKRL FQLQQGVTTP RTADFARQSI QIENHELDLI GMLIGRNPAT VGTNTRQKSQ WQAIRDIIGD YTSPHNCYGM ANKQCVTDGY RDPENKQTQS PTGVFERGVS NEIEIMYRPV RIYDLQHPKG KTK // ID Q9JXQ8_NEIMB Unreviewed; 241 AA. AC Q9JXQ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Ribosomal RNA small subunit methyltransferase E {ECO:0000256|PIRNR:PIRNR015601}; DE EC=2.1.1.193 {ECO:0000256|PIRNR:PIRNR015601}; GN OrderedLocusNames=NMB1925 {ECO:0000313|EMBL:AAF42254.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42254.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42254.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42254.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Specifically methylates the N3 position of the uracil CC ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully CC assembled 30S ribosomal subunit. {ECO:0000256|PIRNR:PIRNR015601}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(1498) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S CC rRNA. {ECO:0000256|PIRNR:PIRNR015601}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015601}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family. CC {ECO:0000256|PIRNR:PIRNR015601}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42254.1; -; Genomic_DNA. DR PIR; H81026; H81026. DR RefSeq; NP_274919.1; NC_003112.2. DR RefSeq; WP_002223081.1; NC_003112.2. DR ProteinModelPortal; Q9JXQ8; -. DR STRING; 122586.NMB1925; -. DR PaxDb; Q9JXQ8; -. DR EnsemblBacteria; AAF42254; AAF42254; NMB1925. DR GeneID; 904230; -. DR KEGG; nme:NMB1925; -. DR PATRIC; 20359897; VBINeiMen85645_2453. DR eggNOG; ENOG4105QF0; Bacteria. DR eggNOG; COG1385; LUCA. DR HOGENOM; HOG000015265; -. DR KO; K09761; -. DR OMA; ERMEFTI; -. DR OrthoDB; EOG6FJNHQ; -. DR BioCyc; NMEN122586:GHGG-1982-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR006700; rRNA_ssu_MeTrfase-E. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF04452; Methyltrans_RNA; 1. DR PIRSF; PIRSF015601; MTase_slr0722; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00046; TIGR00046; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR015601}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR015601}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW rRNA processing {ECO:0000256|PIRNR:PIRNR015601}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR015601}; KW Transferase {ECO:0000256|PIRNR:PIRNR015601}. SQ SEQUENCE 241 AA; 26685 MW; 4920775D8294F0A8 CRC64; MPRFHLPENL SVGQTVALPD NIVRHLNVLR VRPNENITLF DGKGKAHAAR LTVLEKRRAE AEILHEDTTD NESPLNITLI QSISSGDRMD FTLQKSVELG VTAIQPVISE RCIVRLDGER AAKRLARWQE IVISACEQSG RNTVPPVLPI IGYREALDKM PSESTKLIMS INRARKLGDI RQPSGAIVFM VGPEGGWTEQ EEQQAFEAGF QAVTLGKRIL RTETAPLAAL AAMQTLWGDF A // ID Q9JYT9_NEIMB Unreviewed; 468 AA. AC Q9JYT9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Drug resistance translocase family protein {ECO:0000313|EMBL:AAF41796.1}; GN OrderedLocusNames=NMB1435 {ECO:0000313|EMBL:AAF41796.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41796.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41796.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41796.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41796.1; -; Genomic_DNA. DR PIR; C81083; C81083. DR RefSeq; NP_274447.1; NC_003112.2. DR RefSeq; WP_002244170.1; NC_003112.2. DR ProteinModelPortal; Q9JYT9; -. DR STRING; 122586.NMB1435; -. DR PaxDb; Q9JYT9; -. DR EnsemblBacteria; AAF41796; AAF41796; NMB1435. DR GeneID; 903856; -. DR KEGG; nme:NMB1435; -. DR PATRIC; 20358583; VBINeiMen85645_1803. DR eggNOG; ENOG4105C0R; Bacteria. DR eggNOG; ENOG410XNN3; LUCA. DR HOGENOM; HOG000193484; -. DR OMA; MTERESY; -. DR OrthoDB; EOG651SWK; -. DR BioCyc; NMEN122586:GHGG-1473-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 189 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 293 315 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 350 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 356 382 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 403 425 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 431 451 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 15 459 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 468 AA; 50499 MW; 0E40C5CE2B299948 CRC64; MEKNTLSARA PSPWLPLLLA IAIFMQMLDA TILNTALPEI AADLNESPLD MQLAVISYTL TVALLIPLSG YLADRFGTKK VFFGSIAVFM LGSALCAASG SLFELTLSRV VQGIGGSMLV PIPRLTILRV YDKSKLLNAI NYAVMPALIG PVLGPLAGGY LVEYASWHWI FLLNLPIGLL GFILGRNIMP DIKGSNISLD FKGYLIFSAA ACLLLLSAES LSHALPPYFA LLPLCGGLLF ARRYFRHMKT ASKPIYSADL FLIRTFRLGL AGNLFSRLGI SSIPFLMPLM FQIAFGFGAS LSGWLVAPVA LSSLLVKPLI APLMKRFGYR TVLLWNTKLL AAFIMLLALP DGNSPLWIWV FLSLAIGACN SLQFSAMNTL TLADLRPQQT GSGNSLMAVN QQLAISMGIV AGALILKNWT FLIPASSGLH SAFRMTLLSI GGITLASSLV FKRLHVSDGT NLTRNTPS // ID Q7DD51_NEIMB Unreviewed; 79 AA. AC Q7DD51; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42358.1}; GN OrderedLocusNames=NMB2037 {ECO:0000313|EMBL:AAF42358.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42358.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42358.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42358.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42358.1; -; Genomic_DNA. DR PIR; B81014; B81014. DR RefSeq; NP_275028.1; NC_003112.2. DR RefSeq; WP_002218169.1; NC_003112.2. DR ProteinModelPortal; Q7DD51; -. DR STRING; 122586.NMB2037; -. DR PaxDb; Q7DD51; -. DR EnsemblBacteria; AAF42358; AAF42358; NMB2037. DR GeneID; 904059; -. DR KEGG; nme:NMB2037; -. DR PATRIC; 20360204; VBINeiMen85645_2603. DR eggNOG; ENOG41084RF; Bacteria. DR eggNOG; ENOG410ZY18; LUCA. DR HOGENOM; HOG000133721; -. DR KO; K07172; -. DR OMA; RRMGNSQ; -. DR OrthoDB; EOG6TN49K; -. DR BioCyc; NMEN122586:GHGG-2099-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 79 AA; 8784 MW; 397EC519BAC353E9 CRC64; MILNIRKMGN SQGVILPKSL LGQIGAVDSL AVTVEKGNII LSCPTVRRGW AEAAAMLVET EQEHFFSEIE NEADKEWIW // ID Q9K1Q8_NEIMB Unreviewed; 323 AA. AC Q9K1Q8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40491.1}; GN OrderedLocusNames=NMB0012 {ECO:0000313|EMBL:AAF40491.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40491.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40491.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40491.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40491.1; -; Genomic_DNA. DR PIR; B81248; B81248. DR RefSeq; NP_273078.1; NC_003112.2. DR RefSeq; WP_002225756.1; NC_003112.2. DR STRING; 122586.NMB0012; -. DR PaxDb; Q9K1Q8; -. DR EnsemblBacteria; AAF40491; AAF40491; NMB0012. DR GeneID; 902115; -. DR KEGG; nme:NMB0012; -. DR PATRIC; 20354955; VBINeiMen85645_0013. DR eggNOG; ENOG4105DU1; Bacteria. DR eggNOG; COG0861; LUCA. DR HOGENOM; HOG000230189; -. DR KO; K05794; -. DR OMA; HLRMTDS; -. DR OrthoDB; EOG6RC3R0; -. DR BioCyc; NMEN122586:GHGG-13-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005496; Integral_membrane_TerC. DR InterPro; IPR022369; Integral_membrane_TerC_rswitch. DR PANTHER; PTHR30238:SF0; PTHR30238:SF0; 1. DR Pfam; PF03741; TerC; 1. DR TIGRFAMs; TIGR03718; R_switched_Alx; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 241 261 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298 317 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 323 AA; 35699 MW; 8500891EE4CC054E CRC64; MTEYPGIGSP LFYGVFFAAV LVMIALDMFS LKKNGSHKVG VKEALAWSGL WVAVSCLFAG WLYFELAGNP GYGAAVAKEK VLEFFTGYIL EKSLAVDNIF VFLMIFGYFK VAPQFQHRVL LYGVLGALVL RTVMIFVGAA LVQQFEWILY LFGAFLLYTG IHMMKPEGDE KEDLANSRLL NTVKKVVPVG TEFHGEKFFT VENGKKIATP LFLVLVMIEL SDVVFAVDSI PAVFAVTTDP FIVLTSNIFA ILGLRAMYFL LADVAERFIF LKYGLAFVLG FIGVKMLVMH WVHIPISVSL SVVFGALGAS VLTSLVYTKK TGR // ID Q9JYM2_NEIMB Unreviewed; 436 AA. AC Q9JYM2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative transporter {ECO:0000313|EMBL:AAF41871.1}; GN OrderedLocusNames=NMB1515 {ECO:0000313|EMBL:AAF41871.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41871.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41871.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41871.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41871.1; -; Genomic_DNA. DR PIR; B81074; B81074. DR RefSeq; NP_274523.1; NC_003112.2. DR RefSeq; WP_002219025.1; NC_003112.2. DR ProteinModelPortal; Q9JYM2; -. DR STRING; 122586.NMB1515; -. DR PaxDb; Q9JYM2; -. DR EnsemblBacteria; AAF41871; AAF41871; NMB1515. DR GeneID; 903986; -. DR KEGG; nme:NMB1515; -. DR PATRIC; 20358818; VBINeiMen85645_1919. DR eggNOG; ENOG4105CEY; Bacteria. DR eggNOG; COG0318; LUCA. DR HOGENOM; HOG000259439; -. DR OMA; PLYALMQ; -. DR OrthoDB; EOG628F2J; -. DR BioCyc; NMEN122586:GHGG-1555-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 248 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 268 285 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 292 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 334 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 397 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 403 420 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 436 AA; 47450 MW; 031ED6E97DFB6264 CRC64; MYAKKGGLGL VKSRRFAPLF ATQFLGAFND NVFKTALFVM IGFYGLGQNG FLPAGQMLNL GALLFILPYF LFSSLSGQLG NKFDKAVLAR WVKVLEMIIM AVAAYGFYIR SAPLLLACLF CMGAQSTLFG PLKYAILPDY LDDKELMMGN SLIESGTFVA ILFGQILGTA VAGVPPYIVG ILVLLVAVGG TVGSLFMPSV PAKAADTQIE WNIVRGTKSL LRETVRHKPV FTAIIGISWF WFVGAVYTTQ LPTFTQIHLG GNDNVFNLML ALFSIGIAAG SVLCAKFSRE RLMLAWVTVG ALGLTVCGLV LVWLTHGHRF EGLNGIFWFL SQGWAYPVMA VMTLIGFFGG FFSVPLYTWL QTASSETFRA RAVAANNIVN GIFMVSAAVL SAVLLFLFDS ISLLYLIVAL GNIPLSVFLI KRERRFLGAA AIRKKP // ID Q9K0C9_NEIMB Unreviewed; 107 AA. AC Q9K0C9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41103.1}; GN OrderedLocusNames=NMB0685 {ECO:0000313|EMBL:AAF41103.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41103.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41103.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41103.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41103.1; -; Genomic_DNA. DR PIR; C81172; C81172. DR RefSeq; NP_273727.1; NC_003112.2. DR RefSeq; WP_002219594.1; NC_003112.2. DR STRING; 122586.NMB0685; -. DR PaxDb; Q9K0C9; -. DR EnsemblBacteria; AAF41103; AAF41103; NMB0685. DR GeneID; 902797; -. DR KEGG; nme:NMB0685; -. DR PATRIC; 20356683; VBINeiMen85645_0859. DR eggNOG; ENOG4105VHZ; Bacteria. DR eggNOG; COG4859; LUCA. DR HOGENOM; HOG000218842; -. DR OMA; EYMEDSD; -. DR OrthoDB; EOG6K4009; -. DR BioCyc; NMEN122586:GHGG-713-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018689; DUF2185. DR Pfam; PF09951; DUF2185; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 98 DUF2185. {ECO:0000259|Pfam:PF09951}. SQ SEQUENCE 107 AA; 11797 MW; 54F6D701E3610A9F CRC64; MNAFAQALSS ALDRCIATNT VAKQNRPVGF LYREAPVFEN DSGWRFFSGD ETDEYTDDPD NFSIVSLADI AKTNPETAAL LSQPEGSAWE LAEDGTFQTV ADWQPQD // ID Q9JZK3_NEIMB Unreviewed; 197 AA. AC Q9JZK3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41415.1}; GN OrderedLocusNames=NMB1014 {ECO:0000313|EMBL:AAF41415.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41415.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41415.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41415.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41415.1; -; Genomic_DNA. DR PIR; G81131; G81131. DR STRING; 122586.NMB1014; -. DR PaxDb; Q9JZK3; -. DR EnsemblBacteria; AAF41415; AAF41415; NMB1014. DR PATRIC; 20357557; VBINeiMen85645_1295. DR HOGENOM; HOG000218925; -. DR OMA; RRVCINQ; -. DR OrthoDB; EOG676Z61; -. DR BioCyc; NMEN122586:GHGG-1051-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 89 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 197 AA; 22607 MW; FDE7A87DA3178E7C CRC64; MGKRRRSRHD LEVRAGGGRA RMALVGLWRI GRRVCINQTR HRGDSAVGRN QKIRKSGRGA AMIEFVRAKK RLLWAFVLLL VWTCGYRYAA DKAEAKQTAL IATYRHSSMV AAEQYALQLK KAQDERQRWY DFSQKQGRKP VKKQYPPQTK KAGYLKTKEE LLAELACLKA EMVALKKPDA LIHGKEVRQK ERNSSQG // ID Q9K0F3_NEIMB Unreviewed; 105 AA. AC Q9K0F3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41074.1}; GN OrderedLocusNames=NMB0654 {ECO:0000313|EMBL:AAF41074.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41074.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41074.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41074.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41074.1; -; Genomic_DNA. DR PIR; H81173; H81173. DR RefSeq; NP_273696.1; NC_003112.2. DR RefSeq; WP_002222809.1; NC_003112.2. DR STRING; 122586.NMB0654; -. DR PaxDb; Q9K0F3; -. DR EnsemblBacteria; AAF41074; AAF41074; NMB0654. DR GeneID; 902766; -. DR KEGG; nme:NMB0654; -. DR HOGENOM; HOG000220703; -. DR OMA; HADMEYL; -. DR OrthoDB; EOG6ZKXZ2; -. DR BioCyc; NMEN122586:GHGG-681-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 105 AA; 12401 MW; 99519FFF0362587A CRC64; MNILPSWLRV GMNIAMLGMI HSDIRLITVD YEEGRRFLKI KNYLSREAIT EDHEDMEYLI TELWSMCGEY FDEADFECIY SNHSSMELNQ INGAVFRRKE LISQA // ID Q9K166_NEIMB Unreviewed; 142 AA. AC Q9K166; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40756.1}; GN OrderedLocusNames=NMB0310 {ECO:0000313|EMBL:AAF40756.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40756.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40756.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40756.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40756.1; -; Genomic_DNA. DR PIR; E81213; E81213. DR RefSeq; NP_273360.1; NC_003112.2. DR RefSeq; WP_002212270.1; NC_003112.2. DR STRING; 122586.NMB0310; -. DR PaxDb; Q9K166; -. DR EnsemblBacteria; AAF40756; AAF40756; NMB0310. DR GeneID; 902426; -. DR KEGG; nme:NMB0310; -. DR PATRIC; 20355733; VBINeiMen85645_0386. DR eggNOG; ENOG4108YXA; Bacteria. DR eggNOG; COG1981; LUCA. DR HOGENOM; HOG000219492; -. DR KO; K08973; -. DR OMA; QGWMHAK; -. DR OrthoDB; EOG67DPNK; -. DR BioCyc; NMEN122586:GHGG-330-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005265; UPF0093. DR Pfam; PF03653; UPF0093; 1. DR PIRSF; PIRSF004638; UCP004638; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 100 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 139 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 142 AA; 16574 MW; 156CA82A4A7F0990 CRC64; MMFSWFKLFH LFFVISWFAG LFYLPRIFVN MAMIDVPRGN PEYVRLSGMA VRLYRFMSPL GFGAVVFGAA IPFAAGWWGS GWVHVKLCLG LMLLAYQLYC GVLLRRFQDY SNAFSHRWYR VFNEIPVLLM VAALYLVVFK PF // ID Q7DDC9_NEIMB Unreviewed; 135 AA. AC Q7DDC9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transcriptional regulator, MerR family {ECO:0000313|EMBL:AAF41678.1}; GN OrderedLocusNames=NMB1303 {ECO:0000313|EMBL:AAF41678.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41678.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41678.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41678.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH merR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41678.1; -; Genomic_DNA. DR PIR; E81097; E81097. DR RefSeq; NP_274322.1; NC_003112.2. DR RefSeq; WP_002213348.1; NC_003112.2. DR ProteinModelPortal; Q7DDC9; -. DR STRING; 122586.NMB1303; -. DR PaxDb; Q7DDC9; -. DR EnsemblBacteria; AAF41678; AAF41678; NMB1303. DR GeneID; 903725; -. DR KEGG; nme:NMB1303; -. DR PATRIC; 20358247; VBINeiMen85645_1635. DR eggNOG; ENOG4105VUF; Bacteria. DR eggNOG; COG0789; LUCA. DR HOGENOM; HOG000266077; -. DR OMA; CLKNSGM; -. DR OrthoDB; EOG6Z0QGQ; -. DR BioCyc; NMEN122586:GHGG-1341-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR000551; MerR-type_HTH_dom. DR Pfam; PF13411; MerR_1; 1. DR PRINTS; PR00040; HTHMERR. DR SMART; SM00422; HTH_MERR; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR PROSITE; PS00552; HTH_MERR_1; 1. DR PROSITE; PS50937; HTH_MERR_2; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000703}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 71 HTH merR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50937}. FT COILED 83 110 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 135 AA; 15355 MW; 5B7BEF8EE6BA7449 CRC64; MTYTTAKAAE KIGISAHTLR FYDKEGLLPN IGRDEYGNRC FTDNDLQWLG LLQCLKNTGM SLKDIKRFAE CTVIGDDTIE ERLSLFENQI ENVKCQIAEL KRYLDLLEYK LAFYQKAKAL GSVKAVNLPQ IPETA // ID Q9K0Y8_NEIMB Unreviewed; 455 AA. AC Q9K0Y8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 104. DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019}; GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019, GN ECO:0000313|EMBL:AAF40854.1}; GN OrderedLocusNames=NMB0416 {ECO:0000313|EMBL:AAF40854.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40854.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40854.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40854.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final CC step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the CC precursor of murein. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- CC glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N- CC acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- CC alanine. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40854.1; -; Genomic_DNA. DR PIR; D81202; D81202. DR RefSeq; NP_273464.1; NC_003112.2. DR RefSeq; WP_002243999.1; NC_003112.2. DR ProteinModelPortal; Q9K0Y8; -. DR STRING; 122586.NMB0416; -. DR PaxDb; Q9K0Y8; -. DR EnsemblBacteria; AAF40854; AAF40854; NMB0416. DR GeneID; 902532; -. DR KEGG; nme:NMB0416; -. DR PATRIC; 20356026; VBINeiMen85645_0528. DR eggNOG; ENOG4107EES; Bacteria. DR eggNOG; COG0770; LUCA. DR HOGENOM; HOG000268120; -. DR KO; K01929; -. DR OMA; YTALHMP; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NMEN122586:GHGG-440-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02019; MurF; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. DR PANTHER; PTHR23135:SF3; PTHR23135:SF3; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01143; murF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AAF40854.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 24 96 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 106 296 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 316 382 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 108 114 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}. SQ SEQUENCE 455 AA; 48429 MW; E08BF767A558F7BB CRC64; MKPLDLNFIC QALKLPMPSE SKPVSRIVTD SRDIRAGDVF FALAGERFDA HDFVEDVLAA GAAAVVVSRE DCAAMDGALK VDDTLAALQT LAKAWRENVN PFVFGITGSG GKTTVKEMLA AVLRRRFGDD AVLATAGNFN NHIGLPLTLL KLNEKHRYAV IEMGMNHFGE LAVLTQIAKP NAALVNNAMR AHVGCGFDGV GDIAKAKSEI YQGLCSDGIA LIPQEDANMA VFKTATLNLN TRTFGIDSGD VHAENIVLKP LSCEFDLVCG DERAAVVLPV PGRHNVHNAA AAAALALAAG LSLNDVAEGL KGFSNIKGRL NVKSGIKGAT LIDDTYNANP DSMKAAIDVL ARMPAPRIFV MGDMGELGEL GEDEAAAMHA EVGAYARDQG IEAAYFVGDN SVEAAEKFGA DGLWFAAKDP LIQVLRHDLP ERATVLVKGS RFMQMEEVVE ALEDK // ID Q9K0F8_NEIMB Unreviewed; 140 AA. AC Q9K0F8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41069.1}; GN OrderedLocusNames=NMB0648 {ECO:0000313|EMBL:AAF41069.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41069.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41069.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41069.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41069.1; -; Genomic_DNA. DR PIR; C81176; C81176. DR RefSeq; NP_273690.1; NC_003112.2. DR RefSeq; WP_002261379.1; NC_003112.2. DR STRING; 122586.NMB0648; -. DR PaxDb; Q9K0F8; -. DR EnsemblBacteria; AAF41069; AAF41069; NMB0648. DR GeneID; 902760; -. DR KEGG; nme:NMB0648; -. DR PATRIC; 20356595; VBINeiMen85645_0816. DR HOGENOM; HOG000220702; -. DR OrthoDB; EOG67MF3J; -. DR BioCyc; NMEN122586:GHGG-675-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 16552 MW; FF9CCF76ACA4B614 CRC64; MMKRIKCFCD KFPSGDTFRM CIILDDYDNR VDYYVGIYDY ITSTLMSDIY YRSTIDEHFK IIELIENNPN EIYDDGGGQQ FCLEFHHDKV IFYHNEFDEE DGYPVLSCSL HTFKTALIAW NAFLQLPKSI HSVVETVIEE // ID Q9JYH5_NEIMB Unreviewed; 143 AA. AC Q9JYH5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Transcriptional regulator, MarR family {ECO:0000313|EMBL:AAF41938.1}; GN OrderedLocusNames=NMB1585 {ECO:0000313|EMBL:AAF41938.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41938.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41938.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41938.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3G3Z} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RX PubMed=19255465; DOI=10.1107/S174430910900414X; RA Nichols C.E., Sainsbury S., Ren J., Walter T.S., Verma A., RA Stammers D.K., Saunders N.J., Owens R.J.; RT "The structure of NMB1585, a MarR-family regulator from Neisseria RT meningitidis."; RL Acta Crystallogr. F 65:204-209(2009). CC -!- SIMILARITY: Contains 1 HTH marR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41938.1; -; Genomic_DNA. DR PIR; C81065; C81065. DR RefSeq; NP_274591.1; NC_003112.2. DR RefSeq; WP_002222199.1; NC_003112.2. DR PDB; 3G3Z; X-ray; 2.10 A; A/B=1-143. DR PDBsum; 3G3Z; -. DR ProteinModelPortal; Q9JYH5; -. DR STRING; 122586.NMB1585; -. DR PaxDb; Q9JYH5; -. DR EnsemblBacteria; AAF41938; AAF41938; NMB1585. DR GeneID; 904237; -. DR KEGG; nme:NMB1585; -. DR PATRIC; 20359036; VBINeiMen85645_2036. DR eggNOG; ENOG4105RFN; Bacteria. DR eggNOG; COG1846; LUCA. DR HOGENOM; HOG000219033; -. DR OMA; KQICDEW; -. DR OrthoDB; EOG6NGVRR; -. DR BioCyc; NMEN122586:GHGG-1627-MONOMER; -. DR EvolutionaryTrace; Q9JYH5; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000835; HTH_MarR-typ. DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01047; MarR; 1. DR SMART; SM00347; HTH_MARR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS01117; HTH_MARR_1; 1. DR PROSITE; PS50995; HTH_MARR_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3G3Z}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}; KW Transcription regulation {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}. FT DOMAIN 1 139 HTH marR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50995}. SQ SEQUENCE 143 AA; 16161 MW; D8242D037917C4B0 CRC64; MNQLDQLGTR INLICNVFDK WIGQQDLNYN LFAVLYTLAT EGSRTQKHIG EKWSLPKQTV SGVCKTLAGQ GLIEWQEGEQ DRRKRLLSLT ETGKAYAAPL TESAQEFSDK VFATFGDKRT TRLFADLDAL AEVMEKTISE NKK // ID Q9K0E6_NEIMB Unreviewed; 129 AA. AC Q9K0E6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Putative ribonuclease {ECO:0000313|EMBL:AAF41080.1}; GN OrderedLocusNames=NMB0662 {ECO:0000313|EMBL:AAF41080.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41080.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41080.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41080.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41080.1; -; Genomic_DNA. DR PIR; F81174; F81174. DR RefSeq; NP_273704.1; NC_003112.2. DR RefSeq; WP_002217718.1; NC_003112.2. DR ProteinModelPortal; Q9K0E6; -. DR STRING; 122586.NMB0662; -. DR PaxDb; Q9K0E6; -. DR EnsemblBacteria; AAF41080; AAF41080; NMB0662. DR GeneID; 902773; -. DR KEGG; nme:NMB0662; -. DR PATRIC; 20356623; VBINeiMen85645_0830. DR eggNOG; ENOG4105KME; Bacteria. DR eggNOG; COG0251; LUCA. DR HOGENOM; HOG000267215; -. DR OMA; AGMDFNN; -. DR OrthoDB; EOG6QVRPF; -. DR BioCyc; NMEN122586:GHGG-689-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.1330.40; -; 1. DR InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like. DR InterPro; IPR006056; RidA. DR InterPro; IPR006175; YjgF/YER057c/UK114. DR PANTHER; PTHR11803; PTHR11803; 1. DR Pfam; PF01042; Ribonuc_L-PSP; 1. DR SUPFAM; SSF55298; SSF55298; 1. DR TIGRFAMs; TIGR00004; TIGR00004; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 13408 MW; 1B4AC84AD0364470 CRC64; MSKTIIHTDK APAAIGAYSQ AVRAGDTVYM SGQIPLDPAT MTVVGNGDFR AEARQVFQNL QAVAEAAGGT LADIVKLNAY LTDLGNFAVF NEVMAEFIAE PFPARAAVGV ASLPKGVQVE AEAVLVLNA // ID Q9JZE5_NEIMB Unreviewed; 65 AA. AC Q9JZE5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41483.1}; GN OrderedLocusNames=NMB1091 {ECO:0000313|EMBL:AAF41483.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41483.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41483.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41483.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41483.1; -; Genomic_DNA. DR PIR; E81123; E81123. DR RefSeq; NP_274123.1; NC_003112.2. DR RefSeq; WP_002213716.1; NC_003112.2. DR STRING; 122586.NMB1091; -. DR PaxDb; Q9JZE5; -. DR EnsemblBacteria; AAF41483; AAF41483; NMB1091. DR GeneID; 903509; -. DR KEGG; nme:NMB1091; -. DR PATRIC; 20357745; VBINeiMen85645_1389. DR HOGENOM; HOG000218914; -. DR OrthoDB; EOG68H8CW; -. DR BioCyc; NMEN122586:GHGG-1127-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7128 MW; 25D87EDA017826FD CRC64; MSDPILDALA RIENKTDQTL KNQKEMQAEI AQIRQDTKRT AITFGALGGG VITVGWELLK AKMGL // ID Q9JYP5_NEIMB Unreviewed; 262 AA. AC Q9JYP5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Fimbrial assembly protein {ECO:0000313|EMBL:AAF41843.1}; GN Name=fimB {ECO:0000313|EMBL:AAF41843.1}; GN OrderedLocusNames=NMB1487 {ECO:0000313|EMBL:AAF41843.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41843.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41843.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41843.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41843.1; -; Genomic_DNA. DR PIR; E81077; E81077. DR RefSeq; NP_274495.1; NC_003112.2. DR RefSeq; WP_002224433.1; NC_003112.2. DR STRING; 122586.NMB1487; -. DR PaxDb; Q9JYP5; -. DR EnsemblBacteria; AAF41843; AAF41843; NMB1487. DR GeneID; 903909; -. DR KEGG; nme:NMB1487; -. DR PATRIC; 20358740; VBINeiMen85645_1879. DR eggNOG; ENOG4105TWP; Bacteria. DR eggNOG; ENOG41120N0; LUCA. DR HOGENOM; HOG000219018; -. DR OMA; YPYREIS; -. DR OrthoDB; EOG6Q8J3F; -. DR BioCyc; NMEN122586:GHGG-1527-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 103 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 262 AA; 29178 MW; FAC6AF0A130EA65D CRC64; MMENGKTVPR WRFALKSAGW HLLISLSVAG LAALLVFKVW YPYPYAELTG GLSLYQLVVA VDIVCGPLLT LILASPKKKT KARMVDFSMV GIIQLAALVY GLHSVSLARP VVEAFEQDRM TIVTAAEVVV EDLHKAPEGL QSLSWFGIRR IALKEPEDAD EKNKTLDLSL KGIEPSMRPD QWLPYSDKEA EEIRKHLKPL KVLADARKTT VADILKQAGL AEGEELYYLP FTSSRQKEWI VITDKEGNTK GYAPIDGFII TP // ID Q9JXX7_NEIMB Unreviewed; 169 AA. AC Q9JXX7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:AAF42180.1}; GN OrderedLocusNames=NMB1845 {ECO:0000313|EMBL:AAF42180.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42180.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42180.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42180.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42180.1; -; Genomic_DNA. DR PIR; E81036; E81036. DR RefSeq; NP_274842.1; NC_003112.2. DR RefSeq; WP_002223011.1; NC_003112.2. DR ProteinModelPortal; Q9JXX7; -. DR STRING; 122586.NMB1845; -. DR PaxDb; Q9JXX7; -. DR EnsemblBacteria; AAF42180; AAF42180; NMB1845. DR GeneID; 903254; -. DR KEGG; nme:NMB1845; -. DR PATRIC; 20359695; VBINeiMen85645_2353. DR eggNOG; ENOG4105N2G; Bacteria. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000283395; -. DR OMA; WLTRKKM; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NMEN122586:GHGG-1900-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 30 167 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 169 AA; 18308 MW; 9366CF2FD0DFC833 CRC64; MKKKLLSGIK FAVQTALVFL LVSLFLDWIR KPEEPAGAAG RPLTLLSGQR LTLGQFSRDK AVLVYFWGSW CGVCRYQSPI IDDLAADGVP VVGVAVRSGS SAEVAAYMAK RGLGFPTVND EDGGLARSWR IVATPAVVLV KNGKMVHYTT GISSYWGLRA RIFQADVFG // ID Q9JXY6_NEIMB Unreviewed; 306 AA. AC Q9JXY6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=Riboflavin biosynthesis protein {ECO:0000256|PIRNR:PIRNR004491}; DE EC=2.7.1.26 {ECO:0000256|PIRNR:PIRNR004491}; DE EC=2.7.7.2 {ECO:0000256|PIRNR:PIRNR004491}; GN Name=ribF {ECO:0000313|EMBL:AAF42169.1}; GN OrderedLocusNames=NMB1834 {ECO:0000313|EMBL:AAF42169.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42169.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42169.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42169.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD. CC {ECO:0000256|PIRNR:PIRNR004491}. CC -!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN. CC {ECO:0000256|PIRNR:PIRNR004491}. CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: CC step 1/1. {ECO:0000256|PIRNR:PIRNR004491}. CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from CC riboflavin (ATP route): step 1/1. {ECO:0000256|PIRNR:PIRNR004491}. CC -!- SIMILARITY: Belongs to the ribF family. CC {ECO:0000256|PIRNR:PIRNR004491}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42169.1; -; Genomic_DNA. DR PIR; H81036; H81036. DR RefSeq; NP_274831.1; NC_003112.2. DR RefSeq; WP_002244299.1; NC_003112.2. DR ProteinModelPortal; Q9JXY6; -. DR STRING; 122586.NMB1834; -. DR PaxDb; Q9JXY6; -. DR DNASU; 903266; -. DR EnsemblBacteria; AAF42169; AAF42169; NMB1834. DR GeneID; 903266; -. DR KEGG; nme:NMB1834; -. DR PATRIC; 20359669; VBINeiMen85645_2340. DR eggNOG; ENOG4105DTN; Bacteria. DR eggNOG; COG0196; LUCA. DR HOGENOM; HOG000006845; -. DR KO; K11753; -. DR OMA; IHITHPH; -. DR OrthoDB; EOG6QP0ZV; -. DR BioCyc; NMEN122586:GHGG-1889-MONOMER; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.30; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR015864; FAD_synthase. DR InterPro; IPR023468; Riboflavin_kinase. DR InterPro; IPR002606; Riboflavin_kinase_bac. DR InterPro; IPR015865; Riboflavin_kinase_bac/euk. DR InterPro; IPR023465; Riboflavin_kinase_domain. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR22749; PTHR22749; 1. DR Pfam; PF06574; FAD_syn; 1. DR Pfam; PF01687; Flavokinase; 1. DR PIRSF; PIRSF004491; FAD_Synth; 1. DR SMART; SM00904; Flavokinase; 1. DR SUPFAM; SSF82114; SSF82114; 1. DR TIGRFAMs; TIGR00083; ribF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR004491}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|PIRNR:PIRNR004491}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR004491}; KW FMN {ECO:0000256|PIRNR:PIRNR004491}; KW Kinase {ECO:0000256|PIRNR:PIRNR004491, ECO:0000313|EMBL:AAF42169.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004491}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491, KW ECO:0000313|EMBL:AAF42169.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR004491, KW ECO:0000313|EMBL:AAF42169.1}. FT DOMAIN 184 306 Flavokinase. {ECO:0000259|SMART:SM00904}. SQ SEQUENCE 306 AA; 34344 MW; 91B272027698F6DF CRC64; MRIRLGRHNA PDFPQGAAVT IGNFDGVHLG HKHILQKLRL EADARGLPVV TVVFEPQPKE FFALRTGRMP PCRISPLRTK LELLEGTGCV DAVWVLRFDQ NFSEISAQGF IDRLLRQTLN TRYLLVGDDF RFGAGREGCF ELLAQQPDMQ TERTPSVIVE DIRTSSTAVR QALSDGNLAY AKKLLGHDYV LSGRVVHGRK LGRTLNAPTA NIRLPRHRYA LGGVFVVEAD GAFGTRRGVA SFGFNPTVDS GCSQKLEVHL FDFQGDLYGQ GLNVRFLHKL RDEEKFDGME ELKRQIEADM EAARRW // ID Q9K0U1_NEIMB Unreviewed; 358 AA. AC Q9K0U1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40908.1}; GN OrderedLocusNames=NMB0471 {ECO:0000313|EMBL:AAF40908.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40908.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40908.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40908.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40908.1; -; Genomic_DNA. DR PIR; B81194; B81194. DR RefSeq; NP_273518.1; NC_003112.2. DR RefSeq; WP_002224950.1; NC_003112.2. DR ProteinModelPortal; Q9K0U1; -. DR STRING; 122586.NMB0471; -. DR PaxDb; Q9K0U1; -. DR EnsemblBacteria; AAF40908; AAF40908; NMB0471. DR GeneID; 902587; -. DR KEGG; nme:NMB0471; -. DR PATRIC; 20356192; VBINeiMen85645_0617. DR eggNOG; ENOG4108QQZ; Bacteria. DR eggNOG; COG1376; LUCA. DR HOGENOM; HOG000219087; -. DR OMA; AMRARSQ; -. DR OrthoDB; EOG64V2GW; -. DR BioCyc; NMEN122586:GHGG-495-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR InterPro; IPR005490; LD_TPept_cat_dom. DR Pfam; PF03734; YkuD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 47 176 YkuD. {ECO:0000259|Pfam:PF03734}. SQ SEQUENCE 358 AA; 38564 MW; 272F903694F1E4B9 CRC64; MICRKPIGHT PYFDMNKTIC RTAALLISGF SYANTIIPDV SPVAQGQHVF INIPQQRLFL YTDGKLTKVY PVAVGRAMTQ TNLGEHKIGA KAYNPVWYIP KSIQKERGDG VKTIAAGPDN PLGPVFVRLG DPKLGLGIHG TNAPASVPGV RSHGCVRMKS PDALEFAKTI ASGSPASVIY QMAGLNEDAD RNLWLAAFRD PYGKNNLDIA SLKKSIAQWA KTQGKTIAPE KVDAVLKDRT GSAVCLTCGK NGKMKMPLKS LAWIQGSSSY SQAEVIEQTE ETNSAEISET RTPEVPDVHT PEAQPHLNTQ SDGTPTAYTE PAADSSPQVE TPDQAASEPV DVLFSIDVIR QGNLRLGN // ID Q9JZC8_NEIMB Unreviewed; 381 AA. AC Q9JZC8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Tail protein, 43 kDa {ECO:0000313|EMBL:AAF41501.1}; GN OrderedLocusNames=NMB1110 {ECO:0000313|EMBL:AAF41501.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41501.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41501.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41501.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3D37} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND DISULFIDE BONDS. RA Zhang R., Li H., Bargassa M., Joachimiak A.; RT "The crystal structure of the tail protein from Neisseria meningitidis RT MC58."; RL Submitted (MAY-2008) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41501.1; -; Genomic_DNA. DR PIR; C81122; C81122. DR RefSeq; NP_274141.1; NC_003112.2. DR RefSeq; WP_002225233.1; NC_003112.2. DR PDB; 3D37; X-ray; 2.10 A; A/B=1-381. DR PDBsum; 3D37; -. DR ProteinModelPortal; Q9JZC8; -. DR STRING; 122586.NMB1110; -. DR PaxDb; Q9JZC8; -. DR EnsemblBacteria; AAF41501; AAF41501; NMB1110. DR GeneID; 903532; -. DR KEGG; nme:NMB1110; -. DR PATRIC; 20357786; VBINeiMen85645_1409. DR eggNOG; ENOG4106P9E; Bacteria. DR eggNOG; COG4379; LUCA. DR HOGENOM; HOG000218946; -. DR OMA; IFFLMGR; -. DR OrthoDB; EOG6X9MJB; -. DR BioCyc; NMEN122586:GHGG-1146-MONOMER; -. DR EvolutionaryTrace; Q9JZC8; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.1920.10; -; 1. DR InterPro; IPR023399; Baseplate-like_2-layer_sand. DR InterPro; IPR026276; Baseplate_GpP. DR PIRSF; PIRSF004440; GpP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3D37}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DISULFID 190 198 {ECO:0000213|PDB:3D37}. SQ SEQUENCE 381 AA; 42063 MW; AAE09EA78DC99262 CRC64; MQNNSYGYAV SVRVGGKEHR HWERYDIDSD FLIPADSFDF VIGRLGPEAA IPDLSGESCE VVIDGQIVMT GIIGSQRHGK SKGSRELSLS GRDLAGFLVD CSAPQLNVKG MTVLDAAKKL AAPWPQIKAV VLKAENNPAL GKIDIEPGET VWQALTHIAN SVGLHPWLEP DGTLVVGGAD YSSPPVATLC WSRTDSRCNI ERMDIEWDTD NRFSEVTFLA QSHGRSGDSA KHDLKWVYKD PTMTLHRPKT VVVSDADNLA ALQKQAKKQL ADWRLEGFTL TITVGGHKTR DGVLWQPGLR VHVIDDEHGI DAVFFLMGRR FMLSRMDGTQ TELRLKEDGI WTPDAYPKKA EAARKRKGKR KGVSHKGKKG GKKQAETAVF E // ID Q9JZC5_NEIMB Unreviewed; 657 AA. AC Q9JZC5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative tail fibre protein {ECO:0000313|EMBL:AAF41505.1}; GN OrderedLocusNames=NMB1115 {ECO:0000313|EMBL:AAF41505.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41505.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41505.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41505.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41505.1; -; Genomic_DNA. DR PIR; E81119; E81119. DR RefSeq; NP_274145.1; NC_003112.2. DR RefSeq; WP_002225231.1; NC_003112.2. DR ProteinModelPortal; Q9JZC5; -. DR STRING; 122586.NMB1115; -. DR PaxDb; Q9JZC5; -. DR EnsemblBacteria; AAF41505; AAF41505; NMB1115. DR GeneID; 903537; -. DR KEGG; nme:NMB1115; -. DR PATRIC; 20357799; VBINeiMen85645_1415. DR HOGENOM; HOG000218947; -. DR OMA; NQEIGGQ; -. DR OrthoDB; EOG65F8PP; -. DR BioCyc; NMEN122586:GHGG-1151-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.1340.10; -; 1. DR InterPro; IPR011083; Phage_tail_collar_dom. DR Pfam; PF07484; Collar; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 253 297 Collar. {ECO:0000259|Pfam:PF07484}. SQ SEQUENCE 657 AA; 72083 MW; ED5ABE74133CE314 CRC64; MHPIETPDKT FHDGDGVSEL GTILPAWWLN QVQSELLAVL TAAGIQPDKS QPNQLLAALN RLAVVITGDQ TVNGQKTFTA QTQFQSGIHL SANQTNWNGG HKAYIGADAD NAHIVFGDDT LRLHGANNRI SYNNHDIFHK ANKPRFAEDI QGKPNTLSGY GIGNFKVETF RGDLNTLKTD GIYSLPTAVG SSNLPVENTA CHIQVIAGTK HGWCRQLGYP AYTSDVYERH QTSSANDNWS AWKKLNSDGI PVGAIVSFPK AVQNPAGYLK ANGTTFAQNT FPDLYRALGN SNRLPDLSRT DIGITAWFPS DQIPTGWLAF DDIRTRVTET AYPELYRLLT GKYGSIQNVP QAEDRFIRNA GNSLAVGTKQ EDEIKRHVHK VFSHWTNHTD AAALGYEDRN ERQRSALVST WTDENLNDNG FLTPRSDSKM ATGGDENRPK ALVLKLCIKA ADTLGEAVFW IKSHGETINA GALDAGTLAQ GLQDKADRDH THTAAQIQGL DEKISTAVAA QFTRQTIGGV DIVRFPDGTM IQTGSYRFTR SGGPIENEVV FPVAFADGNV KCFVSERHSE RVTGDRRQHN WLFIRAKNHA AAIITNWYEG SCDWMAIGKA ASGNAASSPI GPEIPETNEE PQRESGRTST GPRNRRRRDG LLEALQD // ID Q9K030_NEIMB Unreviewed; 120 AA. AC Q9K030; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41207.1}; GN OrderedLocusNames=NMB0794 {ECO:0000313|EMBL:AAF41207.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41207.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41207.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41207.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41207.1; -; Genomic_DNA. DR PIR; A81157; A81157. DR RefSeq; NP_273836.1; NC_003112.2. DR RefSeq; WP_002226480.1; NC_003112.2. DR STRING; 122586.NMB0794; -. DR PaxDb; Q9K030; -. DR EnsemblBacteria; AAF41207; AAF41207; NMB0794. DR GeneID; 902909; -. DR KEGG; nme:NMB0794; -. DR PATRIC; 20356973; VBINeiMen85645_1005. DR HOGENOM; HOG000218865; -. DR OMA; FAQIXLL; -. DR OrthoDB; EOG6HXJ5Z; -. DR BioCyc; NMEN122586:GHGG-825-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR006976; VanZ-like. DR Pfam; PF04892; VanZ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 88 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 35 113 VanZ. {ECO:0000259|Pfam:PF04892}. SQ SEQUENCE 120 AA; 13345 MW; 422EF2FB8A317DD5 CRC64; MNLPRNRFIL LSALWFAGSI YSLLFKAAET APPPFPHFDK VAHLALFFAQ IWLLTKAFRT DNRPIPYRSL MVFALCFALF SECAQAWFTA TRTGSLGDVL ADLTGAALAL FTARAACRPD // ID Q9JYG2_NEIMB Unreviewed; 95 AA. AC Q9JYG2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41952.1}; GN OrderedLocusNames=NMB1599 {ECO:0000313|EMBL:AAF41952.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41952.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41952.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41952.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41952.1; -; Genomic_DNA. DR PIR; B81064; B81064. DR STRING; 122586.NMB1599; -. DR PaxDb; Q9JYG2; -. DR EnsemblBacteria; AAF41952; AAF41952; NMB1599. DR OrthoDB; EOG66B3XP; -. DR BioCyc; NMEN122586:GHGG-1647-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 95 AA; 11075 MW; D5264DB7D572368E CRC64; MQVTSAEYLS NEESIKKGGN ILMEKYNEKY NESIDGNKTL YKSYYESRRE SIKNYNPDAK YINEIESIYM MLGEIYPNAP DFMSPHFEGD CSEGE // ID Q9K0T7_NEIMB Unreviewed; 463 AA. AC Q9K0T7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40912.1}; GN OrderedLocusNames=NMB0475 {ECO:0000313|EMBL:AAF40912.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40912.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40912.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40912.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40912.1; -; Genomic_DNA. DR PIR; F81194; F81194. DR RefSeq; NP_273522.1; NC_003112.2. DR RefSeq; WP_010980800.1; NC_003112.2. DR STRING; 122586.NMB0475; -. DR PaxDb; Q9K0T7; -. DR EnsemblBacteria; AAF40912; AAF40912; NMB0475. DR GeneID; 902591; -. DR KEGG; nme:NMB0475; -. DR PATRIC; 20356202; VBINeiMen85645_0622. DR eggNOG; ENOG4106ZG3; Bacteria. DR eggNOG; ENOG410XZ3B; LUCA. DR HOGENOM; HOG000219086; -. DR OMA; YQYADID; -. DR OrthoDB; EOG6X3W1Z; -. DR BioCyc; NMEN122586:GHGG-499-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 463 AA; 51774 MW; FC616538CFE4C6EB CRC64; MLLVMRAKQG KKTPKRKSQG VGNTQGQTPG SNDSDWVDQI GQSVSDGTQP DWSWNESAET ASAAVSAQEV DPLTEYQVYK QFGYQGKAAE SLAAYLDGIP DGEAKPENLI RELLDINLEV GDVDVLADNL QKYGKLILSE LLAKYIEQAL QRDSNHLRIR VLAEEGLGWG TQEIEKRAEG GSATAASASP PPDAGGKAYE AEEIKRIPIV RGKKDVSGIS QEEIGAIAGL VRADQGAKIL KDKVSYETAS KQYDRAIQTS EKPANLIIDA LKLDYQHADI DRFAGHLWKL YQTLGNYGRQ VKERMLGWGY SLGYHEVFDD LEKGPNDRQI KDIGMGHGYL PKNIQKFKSQ HRDLVLQDSS LINTGSSPAD DAVKEVESLL MYGQIEAAMD VLEQAVLKYP DESQLYITLI DIYERTEDWD RLGQFLRVLR ERADRLPEEV VMLMSRLLQR MNQNIKKIKR YGK // ID Q9JYE7_NEIMB Unreviewed; 268 AA. AC Q9JYE7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AAF41968.1}; DE EC=2.7.4.7 {ECO:0000313|EMBL:AAF41968.1}; GN Name=thiD {ECO:0000313|EMBL:AAF41968.1}; GN OrderedLocusNames=NMB1616 {ECO:0000313|EMBL:AAF41968.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41968.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41968.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41968.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41968.1; -; Genomic_DNA. DR PIR; F81061; F81061. DR RefSeq; NP_274622.1; NC_003112.2. DR RefSeq; WP_002222176.1; NC_003112.2. DR ProteinModelPortal; Q9JYE7; -. DR STRING; 122586.NMB1616; -. DR PaxDb; Q9JYE7; -. DR EnsemblBacteria; AAF41968; AAF41968; NMB1616. DR GeneID; 904166; -. DR KEGG; nme:NMB1616; -. DR PATRIC; 20359132; VBINeiMen85645_2077. DR eggNOG; ENOG4105DWF; Bacteria. DR eggNOG; COG0351; LUCA. DR HOGENOM; HOG000225273; -. DR KO; K00941; -. DR OMA; FAFHCVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NMEN122586:GHGG-1665-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR004399; HMP/HMP-P_kinase. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF08543; Phos_pyr_kin; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00440402}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|SAAS:SAAS00440394, ECO:0000313|EMBL:AAF41968.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00440402}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00440394, KW ECO:0000313|EMBL:AAF41968.1}. FT DOMAIN 15 262 Phos_pyr_kin. {ECO:0000259|Pfam:PF08543}. SQ SEQUENCE 268 AA; 28394 MW; 84F967D8377D2330 CRC64; MKSSFVQTLT IAGSDSGGGA GIQADLKTFQ MRGVFGTCVI TAVTAQNTLG VSAVHLVPTE TITAQIQAIR EDFDIRAYKI GMLGTAEIIE CVADKLKHCS FGRRVLDPVM IAKGGAPLLQ DSAVAALTRL LLPDTDVLTP NLPEAEALTG VHIENRKDAE RAAKILLDYG VKNVVIKGGH LNGSTSGRCT DWLFTQNETL EFDSPRFPTA HTHGTGCTFS ACITAELAKG SDVCEAVQTA KAYITAAISN PLEIGAGHGP VNHWAYRD // ID Q9JYI5_NEIMB Unreviewed; 356 AA. AC Q9JYI5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41924.1}; GN OrderedLocusNames=NMB1571 {ECO:0000313|EMBL:AAF41924.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41924.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41924.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41924.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41924.1; -; Genomic_DNA. DR PIR; F81068; F81068. DR RefSeq; NP_274577.1; NC_003112.2. DR RefSeq; WP_002212823.1; NC_003112.2. DR STRING; 122586.NMB1571; -. DR PaxDb; Q9JYI5; -. DR DNASU; 904157; -. DR EnsemblBacteria; AAF41924; AAF41924; NMB1571. DR GeneID; 904157; -. DR KEGG; nme:NMB1571; -. DR PATRIC; 20359006; VBINeiMen85645_2022. DR eggNOG; ENOG4108K5H; Bacteria. DR eggNOG; COG0795; LUCA. DR HOGENOM; HOG000263593; -. DR KO; K11720; -. DR OMA; FAYLHAR; -. DR OrthoDB; EOG6J1D9D; -. DR BioCyc; NMEN122586:GHGG-1612-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030923; LptG. DR InterPro; IPR005495; LptG/LptF_permease. DR Pfam; PF03739; YjgP_YjgQ; 1. DR TIGRFAMs; TIGR04408; LptG_lptG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 320 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 332 350 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 356 AA; 39309 MW; E362552137A7C74F CRC64; MNLISRYIIR QMAVMAVYAL LAFLALYSFF EILYETGNLG KGSYGIWEML GYTALKMPAR AYELIPLAVL IGGLVSLSQL AAGSELTVIK ASGMSTKKLL LILSQFGFIF AIATVALGEW VAPTLSQKAE NIKAAAINGK ISTGNTGLWL KEKNSIINVR EMLPDHTLLG IKIWARNDKN ELAEAVEADS AVLNSDGSWQ LKNIRRSTLG EDKVEVSIAA EENWPISVKR NLMDVLLVKP DQMSVGELTT YIRHLQNNSQ NTRIYAIAWW RKLVYPAAAW VMALVAFAFT PQTTRHGNMG LKLFGGICLG LLFHLAGRLF GFTSQLYGIP PFLAGALPTI AFALLAVWLI RKQEKR // ID Q9K1F4_NEIMB Unreviewed; 129 AA. AC Q9K1F4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40657.1}; GN OrderedLocusNames=NMB0200 {ECO:0000313|EMBL:AAF40657.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40657.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40657.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40657.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40657.1; -; Genomic_DNA. DR PIR; B81226; B81226. DR RefSeq; NP_273258.1; NC_003112.2. DR RefSeq; WP_002216284.1; NC_003112.2. DR ProteinModelPortal; Q9K1F4; -. DR STRING; 122586.NMB0200; -. DR PaxDb; Q9K1F4; -. DR EnsemblBacteria; AAF40657; AAF40657; NMB0200. DR GeneID; 902308; -. DR KEGG; nme:NMB0200; -. DR PATRIC; 20355443; VBINeiMen85645_0250. DR eggNOG; COG3792; LUCA. DR HOGENOM; HOG000220684; -. DR OrthoDB; EOG6FNHPP; -. DR BioCyc; NMEN122586:GHGG-211-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3510.10; -; 1. DR InterPro; IPR023138; NMB0513-like_domain. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 15558 MW; 79FDEBE198D10AE8 CRC64; MNVKIKYNLL EYCEYLGGIF GVYKNYLNMD IKDPNLKIRF FDFLEELLSD GVIELCDYRE NPPKILTGSP KTQVDELRRI WPDMEEMLLY FPDNPWFYVE HFWWGATCPI ELTQLPKIEI YEEQMKQGK // ID Q9JZ23_NEIMB Unreviewed; 64 AA. AC Q9JZ23; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41704.1}; GN OrderedLocusNames=NMB1329 {ECO:0000313|EMBL:AAF41704.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41704.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41704.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41704.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41704.1; -; Genomic_DNA. DR PIR; D81095; D81095. DR PaxDb; Q9JZ23; -. DR EnsemblBacteria; AAF41704; AAF41704; NMB1329. DR BioCyc; NMEN122586:GHGG-1367-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7391 MW; DE639A1A2AA591C4 CRC64; MDCNDGNVEG FVGYKYPTYA CCYISFDLMT KYDKVKVQIT ASMICFFRLL SFHDIDISSF SFSL // ID Q9JY04_NEIMB Unreviewed; 671 AA. AC Q9JY04; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Putative cytochrome c-type biogenesis protein {ECO:0000313|EMBL:AAF42141.1}; GN OrderedLocusNames=NMB1804 {ECO:0000313|EMBL:AAF42141.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42141.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42141.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42141.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42141.1; -; Genomic_DNA. DR PIR; E81040; E81040. DR RefSeq; NP_274801.1; NC_003112.2. DR RefSeq; WP_002225648.1; NC_003112.2. DR STRING; 122586.NMB1804; -. DR PaxDb; Q9JY04; -. DR EnsemblBacteria; AAF42141; AAF42141; NMB1804. DR GeneID; 903294; -. DR KEGG; nme:NMB1804; -. DR PATRIC; 20359577; VBINeiMen85645_2294. DR eggNOG; ENOG4105EBH; Bacteria. DR eggNOG; COG1333; LUCA. DR HOGENOM; HOG000254993; -. DR KO; K07399; -. DR OMA; YSAWWFL; -. DR OrthoDB; EOG67T5FM; -. DR BioCyc; NMEN122586:GHGG-1859-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007816; ResB-like_domain. DR Pfam; PF05140; ResB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 604 623 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 22 654 ResB. {ECO:0000259|Pfam:PF05140}. SQ SEQUENCE 671 AA; 76075 MW; 44EDD7B019FB1DB8 CRC64; MSKSRRSPPL LSRPWFAFFS SMRFAVALLS LLGIASVIGT VLQQNQPQTD YLVKFGSFWA QIFGFLGLYD VYASAWFVVI MMFLVVSTSL CLIRNVPPFW REMKSFREKV KEKSLAAMRH SSLLDVKIAP EVAKRYLEVQ GFQGKTINRE DGSVLIAAKK GTMNKWGYIF AHVALIVICL GGLIDSNLLL KLGMLTGRIV PDNQAVYAKD FKPESILGAS NLSFRGNVNI SEGQSADVVF LNADNGILVQ DLPFEVKLKK FHIDFYNTGM PRDFASDIEV TDKATGEKLE RTIRVNHPLT LHGITIYQAS FADGGSDLTF KAWNLGDASR EPVVLKATSI HQFPLEIGKH KYRLEFDQFT SMNVEDMSEG AEREKSLKST LNDVRAVTQE GKKYTNIGPS IVYRIRDAAG QAVEYKNYML PVLQEQDYFW ITGTRSGLQQ QYRWLRIPLD KQLKADTFMA LREFLKDGEG RKRLVADATK GAPAEIREQF MLAAENTLNI FAQKGYLGLD EFITSNIPKE QQDKMQGYFY EMLYGVMNAA LDETIRRYGL PEWQQDEARN RFLLHSMDAY TGLTEYPAPM LLQLDGFSEV RSSGLQMTRS PGALLVYLGS VLLVLGTVLM FYVREKRAWV LFSDGKIRFA MSSARSERDL QKEFPKHVES LQRLGKDLNH D // ID Q9K0V5_NEIMB Unreviewed; 269 AA. AC Q9K0V5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=MutT protein {ECO:0000313|EMBL:AAF40890.1}; GN Name=mutT {ECO:0000313|EMBL:AAF40890.1}; GN OrderedLocusNames=NMB0453 {ECO:0000313|EMBL:AAF40890.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40890.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40890.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40890.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC {ECO:0000256|RuleBase:RU003476}. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC {ECO:0000256|SAAS:SAAS00499431}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40890.1; -; Genomic_DNA. DR PIR; G81197; G81197. DR RefSeq; NP_273500.1; NC_003112.2. DR RefSeq; WP_002216566.1; NC_003112.2. DR ProteinModelPortal; Q9K0V5; -. DR STRING; 122586.NMB0453; -. DR PaxDb; Q9K0V5; -. DR EnsemblBacteria; AAF40890; AAF40890; NMB0453. DR GeneID; 902569; -. DR KEGG; nme:NMB0453; -. DR PATRIC; 20356120; VBINeiMen85645_0576. DR eggNOG; ENOG4107ZZ3; Bacteria. DR eggNOG; COG0494; LUCA. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; REGQAWS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NMEN122586:GHGG-477-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU003476, KW ECO:0000256|SAAS:SAAS00499465}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 137 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 269 AA; 29888 MW; 8FE009B5E358F61F CRC64; MIQDTRPLIR VVAGILLDSD GNYLLSSRPE GKPYAGYWEF AGGKVEAGET DFQALQREFE EELGIRILAA TPWLTKIHSY EHARVCLKFL WVNPDQWTGK PQSREGQEWS WQKAGDFTVA PMLPANGALL RSLSVPRRLY GSLKTGLHGE NSMGAYRVLP LGSAEGSGAN VLMEAAQWQD RPEHADSVWM VVQTREQWRR AQEKGADAVV WRVCDDVQAQ EAAEALRQGV SVPLVLAANG QTVARYGKLW LGLGAHVVVR DETIGKNHE // ID Q9K011_NEIMB Unreviewed; 104 AA. AC Q9K011; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41229.1}; GN OrderedLocusNames=NMB0816 {ECO:0000313|EMBL:AAF41229.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41229.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41229.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41229.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41229.1; -; Genomic_DNA. DR PIR; G81153; G81153. DR STRING; 122586.NMB0816; -. DR PaxDb; Q9K011; -. DR EnsemblBacteria; AAF41229; AAF41229; NMB0816. DR HOGENOM; HOG000218868; -. DR OMA; CKYLVRT; -. DR OrthoDB; EOG69WFV8; -. DR BioCyc; NMEN122586:GHGG-847-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 104 AA; 12121 MW; D85516566E8175F3 CRC64; MCVLLHRRLS HAGDESVYVA QSPLAASEGR GARERGGQVL SHWLSPYYLS NYGCIMRLCL FFVKHYTVKM CKYLVRTYTL FFTFSSIGYQ CVQRKFENFY ILVV // ID Q9JY05_NEIMB Unreviewed; 395 AA. AC Q9JY05; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Putative cytochrome c-type biogenesis protein {ECO:0000313|EMBL:AAF42140.1}; GN OrderedLocusNames=NMB1803 {ECO:0000313|EMBL:AAF42140.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42140.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42140.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42140.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42140.1; -; Genomic_DNA. DR PIR; D81040; D81040. DR RefSeq; NP_274800.1; NC_003112.2. DR RefSeq; WP_002225647.1; NC_003112.2. DR STRING; 122586.NMB1803; -. DR PaxDb; Q9JY05; -. DR EnsemblBacteria; AAF42140; AAF42140; NMB1803. DR GeneID; 903295; -. DR KEGG; nme:NMB1803; -. DR PATRIC; 20359575; VBINeiMen85645_2293. DR eggNOG; ENOG4105CRE; Bacteria. DR eggNOG; COG0755; LUCA. DR HOGENOM; HOG000099341; -. DR OMA; MWYSVAR; -. DR OrthoDB; EOG6Z9B0Z; -. DR BioCyc; NMEN122586:GHGG-1858-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro. DR InterPro; IPR002541; Cyt_c_assembly. DR InterPro; IPR017562; Cyt_c_biogenesis_CcsA. DR Pfam; PF01578; Cytochrom_C_asm; 1. DR TIGRFAMs; TIGR03144; cytochr_II_ccsB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 260 280 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 386 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 183 390 Cytochrom_C_asm. FT {ECO:0000259|Pfam:PF01578}. SQ SEQUENCE 395 AA; 44458 MW; 2706705815674343 CRC64; MTEHYKTLPE HELLIQKSLI SNLNLWDWVF AVLVFAATVF VQTRSGMHMD IYETVMLWAS AGIAVFLGWF FKPMRWFVPL SVLLAYAAVG LYGGDIKSAE IFLLRYFLSS QSAIMWQCAF VFFALFAYIS GAVLASVKNV PTNTLLGMGT VFAWVSAVAG FTGLLVRWHE SYLLRPDAGH IPVSNLYEVF ILFLVITALM YLYYEGKFAI QKLGGFVFGF MAVVVGFVLW YSVSREAHTI QPLIPALQSW WMKIHVPANF IGYGAFCISA MLGIAELVSL RAEGKGGKLW LPPSALIDEV MYKAIAVGFL FFTIATILGA LWAADAWGRY WSWDPKETWA FIVWLNYAVW LHLRLVAGWR GKVLAWWAII GLFVTAFAFI GVNMFLSGLH SYGTL // ID Q9K053_NEIMB Unreviewed; 370 AA. AC Q9K053; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AAF41181.1}; GN Name=pilT-2 {ECO:0000313|EMBL:AAF41181.1}; GN OrderedLocusNames=NMB0768 {ECO:0000313|EMBL:AAF41181.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41181.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41181.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41181.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41181.1; -; Genomic_DNA. DR PIR; E81159; E81159. DR RefSeq; NP_273810.1; NC_003112.2. DR RefSeq; WP_010980842.1; NC_003112.2. DR ProteinModelPortal; Q9K053; -. DR STRING; 122586.NMB0768; -. DR PaxDb; Q9K053; -. DR EnsemblBacteria; AAF41181; AAF41181; NMB0768. DR GeneID; 902883; -. DR KEGG; nme:NMB0768; -. DR PATRIC; 20356909; VBINeiMen85645_0973. DR eggNOG; ENOG4108J2M; Bacteria. DR eggNOG; COG5008; LUCA. DR HOGENOM; HOG000008425; -. DR KO; K02670; -. DR OMA; TIRDMIK; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NMEN122586:GHGG-799-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006321; PilT. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01420; pilT_fam; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 197 211 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 370 AA; 41508 MW; 02FA857EA4FF250D CRC64; MTAKEELFAW LRHMNQNKGS DLFVTTHFPP AMKLDGKITR ITDEPLTAEK CMEIAFSIMS AKQAEEFSST NECNFAISLP DTSRFRVNAM IQRGATALVF RTITSKIPKF ESLNLPPVLK DVALKKRGLV IFVGGTGSGK STSLASLIDY RNENSFGHII TIEDPIEFVH EHKNCIITQR EVGVDTENWM AALKNTLRQA PDVILIGEIR DRETMDYAIA FAETGHLCMA TLHANSTNQA LDRIINFFPE ERREQLLTDL SLNLQAFISQ RLVPRDGGKG RVAAVEVLLN SPLISELIHN GNIHEIKEVM KKSTTLGMQT FDQHLYQLYE KGDISLQEAL KNADSAHDLR LAVQLRSRRA QSSSPDLELL // ID Q9JZY8_NEIMB Unreviewed; 107 AA. AC Q9JZY8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41255.1}; GN OrderedLocusNames=NMB0844 {ECO:0000313|EMBL:AAF41255.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41255.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41255.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41255.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41255.1; -; Genomic_DNA. DR PIR; A81152; A81152. DR RefSeq; NP_273885.1; NC_003112.2. DR RefSeq; WP_002236499.1; NC_003112.2. DR PaxDb; Q9JZY8; -. DR EnsemblBacteria; AAF41255; AAF41255; NMB0844. DR GeneID; 902958; -. DR KEGG; nme:NMB0844; -. DR PATRIC; 20357077; VBINeiMen85645_1057. DR HOGENOM; HOG000218872; -. DR OrthoDB; EOG6KT2S0; -. DR BioCyc; NMEN122586:GHGG-875-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 107 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329359. SQ SEQUENCE 107 AA; 11854 MW; 337A4B31680A1E26 CRC64; MKKCILGILT ACAAMPAFAD RIGDLEARLA QLEHRVAVLE SGGNTVKIDL FGSNSTMYVC SVTPFQKTFE ASDRNEGVAR QKVRQACNRE TSAMFCEDEA IRCRKFD // ID Q9JYS4_NEIMB Unreviewed; 163 AA. AC Q9JYS4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41812.1}; GN OrderedLocusNames=NMB1453 {ECO:0000313|EMBL:AAF41812.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41812.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41812.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41812.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41812.1; -; Genomic_DNA. DR PIR; F81081; F81081. DR RefSeq; NP_274464.1; NC_003112.2. DR RefSeq; WP_002224580.1; NC_003112.2. DR STRING; 122586.NMB1453; -. DR PaxDb; Q9JYS4; -. DR EnsemblBacteria; AAF41812; AAF41812; NMB1453. DR GeneID; 903875; -. DR KEGG; nme:NMB1453; -. DR PATRIC; 20358649; VBINeiMen85645_1834. DR eggNOG; COG3198; LUCA. DR HOGENOM; HOG000277953; -. DR KO; K09926; -. DR OMA; HEYLLHR; -. DR OrthoDB; EOG6NKR09; -. DR BioCyc; NMEN122586:GHGG-1493-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008620; FixH. DR Pfam; PF05751; FixH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 163 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328330. SQ SEQUENCE 163 AA; 18222 MW; 323348D16BAE99CF CRC64; MAGPIFVVIA SVAMFFVAQQ HATDLVTDDY YKDGKHIDIQ LHRDEEAVRR HIGVQVLISP DMNAAKVFVG GEFDGKQPLN LLLMHPTRKA DDQTVALKPV GSAQNGRAEY EAVFKTLSPT NHWYVRVEDA AGVWRVENKW ITSQGNAVDL TPMDKLFNNT ESK // ID Q9JZL3_NEIMB Unreviewed; 98 AA. AC Q9JZL3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41404.1}; GN OrderedLocusNames=NMB1003 {ECO:0000313|EMBL:AAF41404.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41404.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41404.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41404.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41404.1; -; Genomic_DNA. DR PIR; A81133; A81133. DR RefSeq; NP_274038.1; NC_003112.2. DR RefSeq; WP_002213688.1; NC_003112.2. DR ProteinModelPortal; Q9JZL3; -. DR STRING; 122586.NMB1003; -. DR PaxDb; Q9JZL3; -. DR EnsemblBacteria; AAF41404; AAF41404; NMB1003. DR GeneID; 903139; -. DR KEGG; nme:NMB1003; -. DR PATRIC; 20357539; VBINeiMen85645_1286. DR eggNOG; ENOG41062VS; Bacteria. DR eggNOG; ENOG41129YN; LUCA. DR HOGENOM; HOG000218922; -. DR OMA; PANINRA; -. DR OrthoDB; EOG62RSH8; -. DR BioCyc; NMEN122586:GHGG-1040-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 98 AA; 11043 MW; FA31D9A2CD494919 CRC64; MRMAESKRVQ RLLRVFIALD EHPIIGLSNK DLSVGLGLTP SQVSRDIDDL VASGLVIKLE NGNYAYGIKT LQIAERFRQQ HERLQSKIAE IGKRVDVD // ID Q9K119_NEIMB Unreviewed; 38 AA. AC Q9K119; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40816.1}; GN OrderedLocusNames=NMB0376 {ECO:0000313|EMBL:AAF40816.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40816.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40816.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40816.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40816.1; -; Genomic_DNA. DR PIR; D81207; D81207. DR RefSeq; NP_273425.1; NC_003112.2. DR RefSeq; WP_002243989.1; NC_003112.2. DR PaxDb; Q9K119; -. DR EnsemblBacteria; AAF40816; AAF40816; NMB0376. DR GeneID; 902491; -. DR KEGG; nme:NMB0376; -. DR PATRIC; 20355911; VBINeiMen85645_0473. DR BioCyc; NMEN122586:GHGG-398-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 38 AA; 4456 MW; FF6D5D5B5E087DEE CRC64; MPSESHFRRS DGIFAPFVYK PLKSLYTQNP FNIKQTPL // ID Q9JY20_NEIMB Unreviewed; 79 AA. AC Q9JY20; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42124.1}; GN OrderedLocusNames=NMB1785 {ECO:0000313|EMBL:AAF42124.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42124.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42124.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42124.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42124.1; -; Genomic_DNA. DR PIR; B81043; B81043. DR RefSeq; NP_274784.1; NC_003112.2. DR RefSeq; WP_010980990.1; NC_003112.2. DR STRING; 122586.NMB1785; -. DR PaxDb; Q9JY20; -. DR EnsemblBacteria; AAF42124; AAF42124; NMB1785. DR GeneID; 903314; -. DR KEGG; nme:NMB1785; -. DR HOGENOM; HOG000218784; -. DR OMA; ACYQLLY; -. DR OrthoDB; EOG6K6VCP; -. DR BioCyc; NMEN122586:GHGG-1840-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 67 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 79 AA; 9798 MW; 879CDC72E79487AF CRC64; MRDSMKNWKQ FTFFVILVIA CYQVLYFLSD MFLLDYINKY SWNLNFIQGT LNFFSIYLPY VFVSRIFRNT NQEKEYKND // ID Q9JYT3_NEIMB Unreviewed; 222 AA. AC Q9JYT3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Putative O-methyltransferase {ECO:0000313|EMBL:AAF41802.1}; GN OrderedLocusNames=NMB1441 {ECO:0000313|EMBL:AAF41802.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41802.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41802.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41802.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41802.1; -; Genomic_DNA. DR PIR; A81084; A81084. DR RefSeq; NP_274453.1; NC_003112.2. DR RefSeq; WP_002222286.1; NC_003112.2. DR ProteinModelPortal; Q9JYT3; -. DR STRING; 122586.NMB1441; -. DR PaxDb; Q9JYT3; -. DR EnsemblBacteria; AAF41802; AAF41802; NMB1441. DR GeneID; 903862; -. DR KEGG; nme:NMB1441; -. DR PATRIC; 20358595; VBINeiMen85645_1809. DR eggNOG; ENOG4108VQJ; Bacteria. DR eggNOG; COG4122; LUCA. DR HOGENOM; HOG000016839; -. DR OMA; MVPIADG; -. DR OrthoDB; EOG6ZPT3K; -. DR BioCyc; NMEN122586:GHGG-1479-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002935; O-MeTrfase_3. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01596; Methyltransf_3; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51682; SAM_OMT_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF41802.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41802.1}. SQ SEQUENCE 222 AA; 24278 MW; E8368A184F4D5443 CRC64; MTTHLSNVAP DLQNYLNAIG EPEHPVLTRL REKTGHHRMG KMAIAREQAA VLVWLAKLIR AEKYLEIGVF TGYSSTALAL ALPEHGRITA CDINVTFTDT ARQVWNEAGV AHKISLHLQP ALLTLDDLIA QGEAGSYDLA LIDADKPPTP QYFERCLKLV RQGGIIAIDN ILLNGRVMRE AASDAPPSVG ILKDFNQNLP NDPRIVPITL PVGDGLTLLL KK // ID Q7DDI3_NEIMB Unreviewed; 272 AA. AC Q7DDI3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Class 5 outer membrane protein {ECO:0000313|EMBL:AAF41451.1}; GN Name=opc {ECO:0000313|EMBL:AAF41451.1}; GN OrderedLocusNames=NMB1053 {ECO:0000313|EMBL:AAF41451.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41451.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41451.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41451.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41451.1; -; Genomic_DNA. DR RefSeq; NP_274087.1; NC_003112.2. DR RefSeq; WP_002222545.1; NC_003112.2. DR ProteinModelPortal; Q7DDI3; -. DR SMR; Q7DDI3; 24-272. DR STRING; 122586.NMB1053; -. DR PaxDb; Q7DDI3; -. DR EnsemblBacteria; AAF41451; AAF41451; NMB1053. DR GeneID; 903235; -. DR KEGG; nme:NMB1053; -. DR PATRIC; 20357645; VBINeiMen85645_1339. DR HOGENOM; HOG000218928; -. DR OMA; TKINEYG; -. DR OrthoDB; EOG64V2B4; -. DR BioCyc; NMEN122586:GHGG-1090-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.40.128.100; -; 1. DR InterPro; IPR020080; OM_adhesin/peptidase_omptin. DR InterPro; IPR009876; OM_adhesin_OpcA. DR Pfam; PF07239; OpcA; 1. DR SUPFAM; SSF69917; SSF69917; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287261. SQ SEQUENCE 272 AA; 29991 MW; B1D17829426CCB77 CRC64; MKKTVFTCAM IALTGTAAAA QELQTANEFT VHTDLSSISS TRAFLKEKHK AAKHISVRAD IPFDANQGIR LEAGFGRSKK NIINLETDEN KLGKTKNVKL PTGVPENRID LYTGYTYTQT LSDSLNFRVG AGLGFESSKD SIKTTKHTLH SSRQSWLAKV HADLLSQLGN GWYINPWSEV KFDLNSRYKL NTGVTNLKKD INQKTNGWGF GLGANIGKKL GESASIEAGP FYKQRTYKES GEFSVTTKSG DVSLTIPKTS IREYGLRVGI KF // ID Q9K0I0_NEIMB Unreviewed; 220 AA. AC Q9K0I0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 82. DE SubName: Full=Phosphoglycolate phosphatase {ECO:0000313|EMBL:AAF41046.1}; DE EC=3.1.3.18 {ECO:0000313|EMBL:AAF41046.1}; GN Name=pgp {ECO:0000313|EMBL:AAF41046.1}; GN OrderedLocusNames=NMB0620 {ECO:0000313|EMBL:AAF41046.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41046.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41046.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41046.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41046.1; -; Genomic_DNA. DR PIR; A81178; A81178. DR RefSeq; NP_273664.1; NC_003112.2. DR RefSeq; WP_002222833.1; NC_003112.2. DR ProteinModelPortal; Q9K0I0; -. DR STRING; 122586.NMB0620; -. DR PaxDb; Q9K0I0; -. DR DNASU; 902733; -. DR EnsemblBacteria; AAF41046; AAF41046; NMB0620. DR GeneID; 902733; -. DR KEGG; nme:NMB0620; -. DR PATRIC; 20356529; VBINeiMen85645_0784. DR eggNOG; ENOG4108VXP; Bacteria. DR eggNOG; COG0546; LUCA. DR HOGENOM; HOG000248344; -. DR KO; K01091; -. DR OMA; YIHPDDN; -. DR OrthoDB; EOG6HB9PJ; -. DR BioCyc; NMEN122586:GHGG-646-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41046.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 184 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 220 AA; 24029 MW; 48C58231A1A48830 CRC64; MIQAVLFDLD GTLADTALDL GGALNTLLAR HGLPAKSMDE IRTQASHGAA GLIKLGAGIT PDHPDYARWR TEYLDEYDSR YAQDTTLFDG VNELIAELGK RGIKWGIITN KPMRFTDKLV PKLGFIIPPA VVVSGDTCGE PKPSVKPMLY ACGQIHADPQ HTLYVGDAER DIQAGRNAGM TTVLAEWGYI APEDDTGSWQ ADFHIRTPLD LLECLDKIQP // ID Q9JYD9_NEIMB Unreviewed; 517 AA. AC Q9JYD9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Putative tspB protein {ECO:0000313|EMBL:AAF41979.1}; GN OrderedLocusNames=NMB1628 {ECO:0000313|EMBL:AAF41979.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41979.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41979.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41979.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41979.1; -; Genomic_DNA. DR PIR; G81060; G81060. DR RefSeq; NP_274634.1; NC_003112.2. DR RefSeq; WP_010980967.1; NC_003112.2. DR STRING; 122586.NMB1628; -. DR PaxDb; Q9JYD9; -. DR EnsemblBacteria; AAF41979; AAF41979; NMB1628. DR GeneID; 904007; -. DR KEGG; nme:NMB1628; -. DR PATRIC; 20359160; VBINeiMen85645_2091. DR eggNOG; ENOG41067SK; Bacteria. DR eggNOG; ENOG410Y4J8; LUCA. DR HOGENOM; HOG000218809; -. DR OMA; GIFQNSA; -. DR OrthoDB; EOG62NX16; -. DR BioCyc; NMEN122586:GHGG-1677-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008708; Neisseria_TspB. DR Pfam; PF05616; Neisseria_TspB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 517 AA; 57361 MW; B35B0AF6EC21D883 CRC64; MLGMFSVNSY AERFKYPIGN SDVRLDIDHK KSVVTDFRVD GQRFSGRIIE PSIIEHVPTG ARSLEKVPVK FTASVSRAAV LSGVGKLARL GAKLSTRAVP YVGTALLAHD VYETFKEDIQ AQGYQYDPET DKFVKGYEYS NCLWYEDKRR INRTYGCYGV DSSIMRLMSD DSRFPEVKEL MESQMYRLAR PFWNWHKEEL NKLSSLDWNN FVLNRCTFNW NGGDCLVNKG DDFRNGADFS LIRNSKYKEE MDAKKLEEIL SLKVDANPDK YIKATGYPGY SEKVEVAPGT KVNMGPVTDR NGNPVQVVAT FGRDSQGNTT VDVQVIPRPD LTPGSAEAPN AQPLPEVSPA ENPANNPNPN ENPGTSPNPE PDPDLNPDAN PDTDGQPGTR PDSPAVPGRT NGRDGKDGKD GKDGGLLCKF FPDILACDRL PESNPAEDLN LPSETVNVEF QKSGIFQDSA QCPAPVTFTV TVLDSSRQFA FSFENACTIA ERLRYMLLAL AWAVAAFFCI RTVSREV // ID Q9K0I5_NEIMB Unreviewed; 431 AA. AC Q9K0I5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:AAF41041.1}; GN OrderedLocusNames=NMB0614 {ECO:0000313|EMBL:AAF41041.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41041.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41041.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41041.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41041.1; -; Genomic_DNA. DR PIR; G81179; G81179. DR RefSeq; NP_273658.1; NC_003112.2. DR RefSeq; WP_002225537.1; NC_003112.2. DR ProteinModelPortal; Q9K0I5; -. DR STRING; 122586.NMB0614; -. DR PaxDb; Q9K0I5; -. DR EnsemblBacteria; AAF41041; AAF41041; NMB0614. DR GeneID; 902728; -. DR KEGG; nme:NMB0614; -. DR PATRIC; 20356515; VBINeiMen85645_0777. DR eggNOG; ENOG4105CJP; Bacteria. DR eggNOG; ENOG410XWBT; LUCA. DR HOGENOM; HOG000185563; -. DR KO; K09471; -. DR OMA; AKVPHIT; -. DR OrthoDB; EOG67DPGV; -. DR BioCyc; NMEN122586:GHGG-640-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 34 387 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 431 AA; 48414 MW; 35D2FD1C22FAC6BD CRC64; MIRPDFQEYL PSYYFSSVNP HTVYPKLQCR LKTDTCIIGG GLGGLCTALP LAEQGHETVV LEAARIGFGA SGRSGGQVIS DYACGMGEIE KQVGLEQAQW FWQQSLQAVE LVDERVRKHA VDCDWQRGYA TVAVRPQHWE ELQQWHEHAQ RHYGASHYQL WDKAELKQQL DSDMYQGAQF DPLSGHLHPL TYTLGIARAA AEAGAQIFEQ SPMTCIEPHQ NGWLVYTPEG SVECKNVVYA VNTYAGLNPI FRPLERKAIA VSTFIIATEP LGARAKGLIR NNMAVCDNRH ILDYYRLSAD GRLLFGGKDN EFIDNPERMT ELVRQDMLKV FPQLADVKIE YSWGGECDIT ANLVPHFGRL APNVFYAQGY SGHGMAITGI AGLAVAEAIL GDECRLKPFE RLRQPNIILQ PFLRKLGSFL GSKYYQWKDS R // ID Q9JXK6_NEIMB Unreviewed; 112 AA. AC Q9JXK6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Nitrogen regulatory protein P-II {ECO:0000313|EMBL:AAF42322.1}; GN Name=glnB {ECO:0000313|EMBL:AAF42322.1}; GN OrderedLocusNames=NMB1995 {ECO:0000313|EMBL:AAF42322.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42322.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42322.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42322.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2GW8} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX PubMed=16754965; DOI=10.1107/S1744309106015430; RA Nichols C.E., Sainsbury S., Berrow N.S., Alderton D., Saunders N.J., RA Stammers D.K., Owens R.J.; RT "Structure of the PII signal transduction protein of Neisseria RT meningitidis at 1.85 A resolution."; RL Acta Crystallogr. F 62:494-497(2006). CC -!- SIMILARITY: Belongs to the P(II) protein family. CC {ECO:0000256|RuleBase:RU003936}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42322.1; -; Genomic_DNA. DR PIR; B81019; B81019. DR RefSeq; NP_274987.1; NC_003112.2. DR RefSeq; WP_002225869.1; NC_003112.2. DR PDB; 2GW8; X-ray; 1.85 A; A=1-112. DR PDBsum; 2GW8; -. DR ProteinModelPortal; Q9JXK6; -. DR SMR; Q9JXK6; 1-112. DR STRING; 122586.NMB1995; -. DR PaxDb; Q9JXK6; -. DR EnsemblBacteria; AAF42322; AAF42322; NMB1995. DR GeneID; 904133; -. DR KEGG; nme:NMB1995; -. DR PATRIC; 20360087; VBINeiMen85645_2548. DR eggNOG; ENOG4108YZA; Bacteria. DR eggNOG; COG0347; LUCA. DR HOGENOM; HOG000017847; -. DR KO; K04751; -. DR OMA; AIEVKGF; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NMEN122586:GHGG-2052-MONOMER; -. DR EvolutionaryTrace; Q9JXK6; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR002187; N-reg_PII. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR InterPro; IPR017918; N-reg_PII_CS. DR InterPro; IPR002332; N-reg_PII_urydylation_site. DR Pfam; PF00543; P-II; 1. DR PIRSF; PIRSF039144; GlnB; 1. DR PRINTS; PR00340; PIIGLNB. DR SMART; SM00938; P-II; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR PROSITE; PS00638; PII_GLNB_CTER; 1. DR PROSITE; PS51343; PII_GLNB_DOM; 1. DR PROSITE; PS00496; PII_GLNB_UMP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GW8}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR602187-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU003936}; KW Transcription regulation {ECO:0000256|RuleBase:RU003936}. FT MOD_RES 51 51 O-UMP-tyrosine. FT {ECO:0000256|PIRSR:PIRSR039144-50}. SQ SEQUENCE 112 AA; 12311 MW; 22963CF2526D4332 CRC64; MKKIEAIVKP FKLDDVREAL TEIGITGMTV SEVKGFGRQK GHTEIYRGAE YAVDFLPKIK IELVLADDAV ERAIDVIVEV ARSGKIGDGK IFVLPVEEAI RIRTGERSDA AV // ID Q9JXV3_NEIMB Unreviewed; 225 AA. AC Q9JXV3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42205.1}; GN OrderedLocusNames=NMB1871 {ECO:0000313|EMBL:AAF42205.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42205.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42205.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42205.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42205.1; -; Genomic_DNA. DR PIR; E81032; E81032. DR RefSeq; NP_274867.1; NC_003112.2. DR RefSeq; WP_002225786.1; NC_003112.2. DR ProteinModelPortal; Q9JXV3; -. DR STRING; 122586.NMB1871; -. DR PaxDb; Q9JXV3; -. DR EnsemblBacteria; AAF42205; AAF42205; NMB1871. DR GeneID; 904317; -. DR KEGG; nme:NMB1871; -. DR PATRIC; 20359773; VBINeiMen85645_2392. DR eggNOG; ENOG41072GX; Bacteria. DR eggNOG; COG1214; LUCA. DR HOGENOM; HOG000052125; -. DR KO; K14742; -. DR OMA; LFHQEAG; -. DR OrthoDB; EOG6D8B8B; -. DR BioCyc; NMEN122586:GHGG-1927-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022496; T6A_YeaZ. DR Pfam; PF00814; Peptidase_M22; 1. DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 40 128 Peptidase_M22. FT {ECO:0000259|Pfam:PF00814}. SQ SEQUENCE 225 AA; 23762 MW; A49379983DAE9D23 CRC64; MQADFNRPVL AVDTGTSRLS LALRADGETR LFHQEVGSRQ SELILPEIRT LFRDAGITAA DLGAVVYAQG PGAFTGLRIG IGVAQGLATP FDTPLIGVPS LDAAASLPPP QSCILAATDA RMGEVFYAWF DTLNCHRLSD YQVGRAADIR LPEGCAFSDG IGSAFALEEA PPFSGRPDMP TAADFLALAA KGGYPAVHAA HAGLLYVRNK IALTAKEQAE RRARP // ID Q7DD94_NEIMB Unreviewed; 544 AA. AC Q7DD94; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=YhbX/YhjW/YijP/YjdB family protein {ECO:0000313|EMBL:AAF41987.1}; GN OrderedLocusNames=NMB1638 {ECO:0000313|EMBL:AAF41987.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41987.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41987.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41987.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:4KAV, ECO:0000213|PDB:4KAY} RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 210-544 IN COMPLEX WITH RP COPPER; MAGNESIUM AND ZINC, AND DISULFIDE BONDS. RX PubMed=23810904; DOI=10.1016/j.jmb.2013.06.029; RA Wanty C., Anandan A., Piek S., Walshe J., Ganguly J., Carlson R.W., RA Stubbs K.A., Kahler C.M., Vrielink A.; RT "The structure of the neisserial lipooligosaccharide RT phosphoethanolamine transferase A (LptA) required for resistance to RT polymyxin."; RL J. Mol. Biol. 425:3389-3402(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41987.1; -; Genomic_DNA. DR RefSeq; NP_274643.1; NC_003112.2. DR RefSeq; WP_002216735.1; NC_003112.2. DR PDB; 4KAV; X-ray; 1.43 A; A=210-544. DR PDB; 4KAY; X-ray; 1.78 A; A/B=210-544. DR PDBsum; 4KAV; -. DR PDBsum; 4KAY; -. DR ProteinModelPortal; Q7DD94; -. DR STRING; 122586.NMB1638; -. DR PaxDb; Q7DD94; -. DR DNASU; 903951; -. DR EnsemblBacteria; AAF41987; AAF41987; NMB1638. DR GeneID; 903951; -. DR KEGG; nme:NMB1638; -. DR PATRIC; 20359194; VBINeiMen85645_2109. DR eggNOG; ENOG4105DIJ; Bacteria. DR eggNOG; COG2194; LUCA. DR HOGENOM; HOG000275171; -. DR KO; K03760; -. DR OMA; FKNNAYE; -. DR OrthoDB; EOG62ZHS6; -. DR BioCyc; NMEN122586:GHGG-1687-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR012549; DUF1705. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF08019; DUF1705; 1. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4KAV, ECO:0000213|PDB:4KAY}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Copper {ECO:0000213|PDB:4KAV}; Magnesium {ECO:0000213|PDB:4KAV}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000213|PDB:4KAV, ECO:0000213|PDB:4KAY}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0000213|PDB:4KAV, ECO:0000213|PDB:4KAY}. FT TRANSMEM 48 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 174 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 57 205 DUF1705. {ECO:0000259|Pfam:PF08019}. FT DOMAIN 233 524 Sulfatase. {ECO:0000259|Pfam:PF00884}. FT METAL 210 210 Copper. {ECO:0000213|PDB:4KAV}. FT METAL 211 211 Copper. {ECO:0000213|PDB:4KAV}. FT METAL 240 240 Zinc 1. {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT METAL 280 280 Zinc 1. {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT METAL 280 280 Zinc 2. {ECO:0000213|PDB:4KAY}. FT METAL 286 286 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:4KAV}. FT METAL 289 289 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:4KAV}. FT METAL 291 291 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:4KAV}. FT METAL 303 303 Copper; via tele nitrogen. FT {ECO:0000213|PDB:4KAV}. FT METAL 383 383 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:4KAY}. FT METAL 452 452 Zinc 1. {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT METAL 453 453 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT METAL 465 465 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:4KAY}. FT DISULFID 276 286 {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT DISULFID 327 331 {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT DISULFID 348 353 {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT DISULFID 402 410 {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. FT DISULFID 499 540 {ECO:0000213|PDB:4KAV, FT ECO:0000213|PDB:4KAY}. SQ SEQUENCE 544 AA; 61363 MW; 78D9DB56FB8C6927 CRC64; MIKPNLRPKL GSSALIAFLS LYSSLVLNYA FFAKVVELHP FNGTGADIFL YTMPVVLFFL SNFVFHVIAL PFVHKVLIPL ILVISAAVSY QEIFFNIYFN KSMLNNVLQT TAAESARLIT PGYVLWIVCL GVLPALAYIA VKVKYRVWYK ELLTRLVLAA VSFLCALGIA MLQYQDYASF FRNNKSVTHL IVPSNFIGAG VSKYKDWKRS NIPYTQLDMA VVQNRPAGSL RRFVVLVVGE TTRAANWGLN GYSRQTTPLL AARGDEIVNF PQVRSCGTST AHSLPCMFST FDRTDYDEIK AEHQDNLLDI VQRAGVEVTW LENDSGCKGV CGKVPNTDVT SLNLPEYCRN GECLDNILLT KFDEVLNKND KDAVLILHTI GSHGPTYYER YTEAERKFTP TCDTNEINKC TRATLVNTYD NTVLYVDQFI DKVIRKLENR DDLESVVHYV SDHGESLGEN GMYLHAAPYA IAPSGQTHIP MVMWFSKAFR QHGGIDFQCL KQKAAENEYS HDHYFSTVLG LMDISNSQTY RKEMDILAAC RRPR // ID Q9JYK3_NEIMB Unreviewed; 73 AA. AC Q9JYK3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41897.1}; GN OrderedLocusNames=NMB1542 {ECO:0000313|EMBL:AAF41897.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41897.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41897.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41897.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41897.1; -; Genomic_DNA. DR PIR; A81071; A81071. DR STRING; 122586.NMB1542; -. DR PaxDb; Q9JYK3; -. DR EnsemblBacteria; AAF41897; AAF41897; NMB1542. DR PATRIC; 20358918; VBINeiMen85645_1973. DR HOGENOM; HOG000152756; -. DR OrthoDB; EOG6K13WK; -. DR BioCyc; NMEN122586:GHGG-1583-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 73 AA; 8431 MW; C7A52E7ECE09401A CRC64; MSAVNVIFSC SYWRIFKKSD SCVLCFYQFR HGEPHKLINQ ENFSKLYQAF DYIDSVGSNF PVIITTDGCG LFC // ID Q9K174_NEIMB Unreviewed; 61 AA. AC Q9K174; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40749.1}; GN OrderedLocusNames=NMB0298 {ECO:0000313|EMBL:AAF40749.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40749.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40749.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40749.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40749.1; -; Genomic_DNA. DR PIR; A81216; A81216. DR STRING; 122586.NMB0298; -. DR PaxDb; Q9K174; -. DR EnsemblBacteria; AAF40749; AAF40749; NMB0298. DR BioCyc; NMEN122586:GHGG-313-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 61 AA; 7058 MW; EEA2218B248AEC00 CRC64; MTNFPKKIPL KALTVFPCGR IVRFFAAAEV ADELKSIAQN VGDIERYLDR RKEYFIIRNA L // ID Q9K148_NEIMB Unreviewed; 389 AA. AC Q9K148; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994}; GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994}; GN OrderedLocusNames=NMB0339 {ECO:0000313|EMBL:AAF40782.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40782.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40782.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40782.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Modulates cellular lipopolysaccharide (LPS) levels by CC regulating LpxC, which is involved in lipid A biosynthesis. May CC act by modulating the proteolytic activity of FtsH towards LpxC. CC May also coordinate assembly of proteins involved in LPS synthesis CC at the plasma membrane. {ECO:0000256|HAMAP-Rule:MF_00994}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00994}; Single-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00994}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_00994}. CC -!- SIMILARITY: Belongs to the LapB family. {ECO:0000256|HAMAP- CC Rule:MF_00994}. CC -!- SIMILARITY: Contains 2 TPR repeats. {ECO:0000256|HAMAP- CC Rule:MF_00994}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40782.1; -; Genomic_DNA. DR PIR; F81211; F81211. DR RefSeq; NP_273388.1; NC_003112.2. DR RefSeq; WP_002220285.1; NC_003112.2. DR ProteinModelPortal; Q9K148; -. DR STRING; 122586.NMB0339; -. DR PaxDb; Q9K148; -. DR DNASU; 902454; -. DR EnsemblBacteria; AAF40782; AAF40782; NMB0339. DR GeneID; 902454; -. DR KEGG; nme:NMB0339; -. DR PATRIC; 20355823; VBINeiMen85645_0430. DR eggNOG; ENOG4105CFV; Bacteria. DR eggNOG; COG2956; LUCA. DR HOGENOM; HOG000257805; -. DR KO; K19804; -. DR OMA; RYRCAAC; -. DR OrthoDB; EOG68SVV7; -. DR BioCyc; NMEN122586:GHGG-360-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:InterPro. DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.25.40.10; -; 1. DR HAMAP; MF_00994; LPS_assembly_LapB; 1. DR InterPro; IPR030865; LapB. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13176; TPR_7; 1. DR SUPFAM; SSF48452; SSF48452; 2. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00994}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00994}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00994}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00994}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00994}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00994}; KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}. FT TRANSMEM 7 26 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00994}. FT TOPO_DOM 27 389 Cytoplasmic. {ECO:0000256|HAMAP- FT Rule:MF_00994}. FT REPEAT 74 107 TPR 1. {ECO:0000256|HAMAP-Rule:MF_00994}. FT REPEAT 217 250 TPR 2. {ECO:0000256|HAMAP-Rule:MF_00994}. FT METAL 359 359 Iron. {ECO:0000256|HAMAP-Rule:MF_00994}. FT METAL 362 362 Iron. {ECO:0000256|HAMAP-Rule:MF_00994}. FT METAL 373 373 Iron. {ECO:0000256|HAMAP-Rule:MF_00994}. FT METAL 376 376 Iron. {ECO:0000256|HAMAP-Rule:MF_00994}. SQ SEQUENCE 389 AA; 44577 MW; DBA8F3BA22DEA517 CRC64; MDNELWIILL PIILLPVFFA MGWFAARVDM KTVLKQAKSI PSGFYKSLDA LVDRNSGRAA RELAEVVDGR PQSYDLNLTL GKLYRQRGEN DKAINIHRTM LDSPDTVGEK RARVLFELAQ NYQSAGLVDR AEQIFLGLQD GKMAREARQH LLNIYQQDRD WEKAVETARL LSHDDQTYQF EIAQFYCELA QAALFKSNFD VARFNVGKAL EANKKCTRAN MILGDIEHRQ GNFPAAVEAY AAIEQQNHAY LSMVGEKLYE AYAAQGKPEE GLNRLTGYMQ TFPELDLINV VYEKSLLLKC EKEAAQTAVE LVRRKPDLNG VYRLLGLKLS DMNPAWKADA DMMRSVIGRQ LQRSVMYRCR NCHFKSQVFF WHCPACNKWQ TFTPNKIEV // ID Q7DDQ9_NEIMB Unreviewed; 176 AA. AC Q7DDQ9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Lipopolysaccharide export system protein LptA {ECO:0000256|HAMAP-Rule:MF_01914}; DE Flags: Precursor; GN Name=lptA {ECO:0000256|HAMAP-Rule:MF_01914}; GN OrderedLocusNames=NMB0355 {ECO:0000313|EMBL:AAF40798.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40798.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40798.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40798.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). CC Required for the translocation of LPS from the inner membrane to CC the outer membrane. {ECO:0000256|HAMAP-Rule:MF_01914}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. {ECO:0000256|HAMAP-Rule:MF_01914}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01914}. CC -!- SIMILARITY: Belongs to the LptA family. {ECO:0000256|HAMAP- CC Rule:MF_01914}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40798.1; -; Genomic_DNA. DR PIR; B81208; B81208. DR RefSeq; NP_273404.1; NC_003112.2. DR RefSeq; WP_002216438.1; NC_003112.2. DR ProteinModelPortal; Q7DDQ9; -. DR STRING; 122586.NMB0355; -. DR PaxDb; Q7DDQ9; -. DR EnsemblBacteria; AAF40798; AAF40798; NMB0355. DR GeneID; 902470; -. DR KEGG; nme:NMB0355; -. DR PATRIC; 20355859; VBINeiMen85645_0448. DR eggNOG; ENOG4105WI0; Bacteria. DR eggNOG; COG1934; LUCA. DR HOGENOM; HOG000264762; -. DR KO; K09774; -. DR OMA; RADRDKP; -. DR OrthoDB; EOG6KQ6FT; -. DR BioCyc; NMEN122586:GHGG-376-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01914; LPS_assembly_LptA; 1. DR InterPro; IPR014340; LptA. DR InterPro; IPR005653; OstA-like_N. DR Pfam; PF03968; OstA; 1. DR TIGRFAMs; TIGR03002; outer_YhbN_LptA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Periplasm {ECO:0000256|HAMAP-Rule:MF_01914}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|HAMAP-Rule:MF_01914}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01914}. FT SIGNAL 1 22 {ECO:0000256|HAMAP-Rule:MF_01914}. FT CHAIN 23 176 Lipopolysaccharide export system protein FT LptA. {ECO:0000256|HAMAP-Rule:MF_01914}. FT /FTId=PRO_5005078932. FT DOMAIN 32 142 OstA-like_N. {ECO:0000259|Pfam:PF03968}. SQ SEQUENCE 176 AA; 18192 MW; 377BE73CAFA1CF45 CRC64; MIQKICKLFV LIAFFSASPA FALQSDSRQP IQIEADQGSL DQANQSTTFS GNVVIRQGTL NISAARVNVT RGGKGGESVR AEGSPVRFSQ TLDGGKGTVR GQANNVAYSS AGSTVVLTGN AKVQRGGDVA EGAVITYNTK TEVYTISGST KSGAKSASKS GRVSVVIQPS STQKSE // ID Q9K046_NEIMB Unreviewed; 139 AA. AC Q9K046; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41189.1}; GN OrderedLocusNames=NMB0776 {ECO:0000313|EMBL:AAF41189.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41189.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41189.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41189.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41189.1; -; Genomic_DNA. DR PIR; E81160; E81160. DR RefSeq; NP_273818.1; NC_003112.2. DR RefSeq; WP_002222729.1; NC_003112.2. DR STRING; 122586.NMB0776; -. DR PaxDb; Q9K046; -. DR EnsemblBacteria; AAF41189; AAF41189; NMB0776. DR GeneID; 902891; -. DR KEGG; nme:NMB0776; -. DR PATRIC; 20356929; VBINeiMen85645_0983. DR eggNOG; ENOG4106GQ1; Bacteria. DR eggNOG; ENOG410Y3YG; LUCA. DR HOGENOM; HOG000218861; -. DR OrthoDB; EOG66MQQT; -. DR BioCyc; NMEN122586:GHGG-807-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 139 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332286. SQ SEQUENCE 139 AA; 15627 MW; 1BF1C746A430242E CRC64; MKKMFLSAVL LLSAAAQTVW ADTVFSCKTD NNKYIEVQKI NRNLYEYSFG SAAKKEIAIR NSKADLLGRS DRWQGMGSGR WATMKFQNGE FMYTIWTGFD SVTHTESSGV VVERRGKEVA RVGCTPKTAQ ANFNDDDFS // ID Q9K0R1_NEIMB Unreviewed; 67 AA. AC Q9K0R1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40951.1}; GN OrderedLocusNames=NMB0519 {ECO:0000313|EMBL:AAF40951.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40951.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40951.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40951.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40951.1; -; Genomic_DNA. DR PIR; A81189; A81189. DR STRING; 122586.NMB0519; -. DR PaxDb; Q9K0R1; -. DR EnsemblBacteria; AAF40951; AAF40951; NMB0519. DR HOGENOM; HOG000152760; -. DR BioCyc; NMEN122586:GHGG-544-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 6753 MW; 1CB97BE9E618830E CRC64; MLSLEIQQEG FTIGGGLVLG GCAGAHLARK EPLILTGKTG AGASAIANAS IGYQWTVNLS KPKEGAK // ID Q9JY51_NEIMB Unreviewed; 136 AA. AC Q9JY51; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42084.1}; GN OrderedLocusNames=NMB1740 {ECO:0000313|EMBL:AAF42084.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42084.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42084.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42084.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42084.1; -; Genomic_DNA. DR PIR; D81047; D81047. DR PaxDb; Q9JY51; -. DR EnsemblBacteria; AAF42084; AAF42084; NMB1740. DR PATRIC; 20359447; VBINeiMen85645_2229. DR OMA; CNPTIPI; -. DR OrthoDB; EOG6NSGGM; -. DR BioCyc; NMEN122586:GHGG-1795-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 136 AA; 15593 MW; 95793779FA3E01E7 CRC64; MGNTAMWMSC NPTIPILFGI QVKIFPLNQI FNHIHPARYA VTFENNVDSK LRRHWVAGAT IRIIDRQTDE VIAKKTIYVF EKGLDGTGGA RMPWKFAILC NKERLTSSEP LSDFVLSVLK PYILRPLYIA SLRRDD // ID Q9JZJ8_NEIMB Unreviewed; 181 AA. AC Q9JZJ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41420.1}; GN OrderedLocusNames=NMB1020 {ECO:0000313|EMBL:AAF41420.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41420.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41420.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41420.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41420.1; -; Genomic_DNA. DR PIR; D81132; D81132. DR RefSeq; NP_274054.1; NC_003112.2. DR RefSeq; WP_002243498.1; NC_003112.2. DR STRING; 122586.NMB1020; -. DR PaxDb; Q9JZJ8; -. DR EnsemblBacteria; AAF41420; AAF41420; NMB1020. DR GeneID; 903158; -. DR KEGG; nme:NMB1020; -. DR PATRIC; 20357575; VBINeiMen85645_1304. DR HOGENOM; HOG000218927; -. DR OrthoDB; EOG6SNDW1; -. DR BioCyc; NMEN122586:GHGG-1057-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR012441; DUF1643. DR Pfam; PF07799; DUF1643; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 181 AA; 20916 MW; 8CA777AA908C2F8D CRC64; MTYEKLYELR QTLRPTTKDG LYTDNEKNRE ILTVRWSGNT ENPKNFSAVA IGINPSKAND ERSDKTLTQL ARFLDMYGFT NFKMLNIFSS YSTQQTGIRA NTQTDFSKFK GCLEDADMII LAWGTDRGAY KDEKNRILEF LKAEKFMEKV FCISETGNSS DTRHPSRISY SYQLVQFEES A // ID Q9K1L8_NEIMB Unreviewed; 28 AA. AC Q9K1L8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40555.1}; GN OrderedLocusNames=NMB0093 {ECO:0000313|EMBL:AAF40555.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40555.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40555.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40555.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40555.1; -; Genomic_DNA. DR PIR; E81239; E81239. DR RefSeq; NP_273154.1; NC_003112.2. DR RefSeq; WP_010980753.1; NC_003112.2. DR STRING; 122586.NMB0093; -. DR PaxDb; Q9K1L8; -. DR EnsemblBacteria; AAF40555; AAF40555; NMB0093. DR GeneID; 902197; -. DR KEGG; nme:NMB0093; -. DR BioCyc; NMEN122586:GHGG-99-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 28 AA; 3243 MW; 0CA20A25B8E83E1D CRC64; MSNDENLLFS QPHLTKVNIM QVLTLNEI // ID Q9K101_NEIMB Unreviewed; 93 AA. AC Q9K101; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Transcriptional regulator, ArsR family {ECO:0000313|EMBL:AAF40838.1}; GN OrderedLocusNames=NMB0398 {ECO:0000313|EMBL:AAF40838.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40838.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40838.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40838.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40838.1; -; Genomic_DNA. DR PIR; F81204; F81204. DR RefSeq; NP_273447.1; NC_003112.2. DR RefSeq; WP_002222014.1; NC_003112.2. DR ProteinModelPortal; Q9K101; -. DR STRING; 122586.NMB0398; -. DR PaxDb; Q9K101; -. DR EnsemblBacteria; AAF40838; AAF40838; NMB0398. DR GeneID; 902513; -. DR KEGG; nme:NMB0398; -. DR PATRIC; 20355959; VBINeiMen85645_0497. DR eggNOG; COG0640; LUCA. DR HOGENOM; HOG000144506; -. DR OMA; DIFCATA; -. DR OrthoDB; EOG679TGC; -. DR BioCyc; NMEN122586:GHGG-420-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PRINTS; PR00778; HTHARSR. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000711}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000711}; KW Transcription regulation {ECO:0000256|RuleBase:RU000711}. FT DOMAIN 1 92 HTH arsR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50987}. SQ SEQUENCE 93 AA; 10635 MW; A17AC49B967DBF97 CRC64; MNTIPLHTIL KLMAHPERMA ILIQLLDSER NIAELAKSLS LPATAVSNHL NRLRVEGLVD FTRYHRIIEY RLVSEEAAAI LHTVRDLENK RVA // ID Q9JY97_NEIMB Unreviewed; 661 AA. AC Q9JY97; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 105. DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_00938}; DE AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00938}; GN Name=parE {ECO:0000256|HAMAP-Rule:MF_00938, GN ECO:0000313|EMBL:AAF42030.1}; GN OrderedLocusNames=NMB1682 {ECO:0000313|EMBL:AAF42030.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42030.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42030.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42030.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Topoisomerase IV is essential for chromosome CC segregation. It relaxes supercoiled DNA. Performs the decatenation CC events required during the replication of a circular DNA molecule. CC {ECO:0000256|HAMAP-Rule:MF_00938}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_00938, CC ECO:0000256|SAAS:SAAS00470725}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00938}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00938}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00938}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt CC bridges with both the protein and the DNA. Can also accept other CC divalent metal cations, such as Mn(2+) or Ca(2+). CC {ECO:0000256|HAMAP-Rule:MF_00938}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000256|HAMAP-Rule:MF_00938}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type CC 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00938}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP- CC Rule:MF_00938}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42030.1; -; Genomic_DNA. DR PIR; D81055; D81055. DR RefSeq; NP_274686.1; NC_003112.2. DR RefSeq; WP_002224983.1; NC_003112.2. DR ProteinModelPortal; Q9JY97; -. DR STRING; 122586.NMB1682; -. DR PaxDb; Q9JY97; -. DR EnsemblBacteria; AAF42030; AAF42030; NMB1682. DR GeneID; 903425; -. DR KEGG; nme:NMB1682; -. DR PATRIC; 20359315; VBINeiMen85645_2164. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR HOGENOM; HOG000075154; -. DR KO; K02622; -. DR OMA; VEVARFK; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; NMEN122586:GHGG-1737-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR HAMAP; MF_00938; ParE_type1; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR013759; Topo_IIA_cen_dom. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR005737; TopoIV_B_Gneg. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01055; parE_Gneg; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00938, KW ECO:0000256|SAAS:SAAS00528655}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00938, KW ECO:0000256|SAAS:SAAS00528650}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00938}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00938}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938, KW ECO:0000256|SAAS:SAAS00528655}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00938, KW ECO:0000256|SAAS:SAAS00528650}. FT DOMAIN 429 546 Toprim. {ECO:0000256|HAMAP-Rule:MF_00938, FT ECO:0000259|PROSITE:PS50880}. FT NP_BIND 116 122 ATP. {ECO:0000256|HAMAP-Rule:MF_00938}. FT METAL 435 435 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00938}. FT METAL 511 511 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00938}. FT METAL 511 511 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00938}. FT METAL 513 513 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00938}. FT BINDING 7 7 ATP. {ECO:0000256|HAMAP-Rule:MF_00938}. FT BINDING 44 44 ATP. {ECO:0000256|HAMAP-Rule:MF_00938}. FT BINDING 71 71 ATP. {ECO:0000256|HAMAP-Rule:MF_00938}. FT BINDING 351 351 ATP. {ECO:0000256|HAMAP-Rule:MF_00938}. FT SITE 460 460 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00938}. FT SITE 463 463 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00938}. FT SITE 518 518 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00938}. FT SITE 646 646 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00938}. SQ SEQUENCE 661 AA; 72217 MW; E8D814AE8A748C27 CRC64; MAKNNQYSES SITVLKGLEP VKERPGMYTR TDSPTHICQE VIDNASDEAL GGFATAIDVQ IHEDGSLSVH DNGRGIPVGL HPEEGVSVVE LVFTRLHAGG KFNKKDGGSA YAFSGGLHGV GVSVTNALST RLEVTVKREG KIHRIVFAGG DVVEPLAQVG KCAVKDSGTE VRVWPDGKYF ESPNYSIPEL ERLLRAKAVL LPGVRVSLTR PVKGEDEAHT QTWHYPDGLK SYLTDLIADA QEAVPLFSCE NYISDEHNGD FSIGEGAAFA LTWLEEGSCA NESYVNLIPT PLGGTHEAGL KQAVFNAVNN FINLHNLLPR GVKVQSDDVF GKTAFVLSAR VLDPQFQGQT KDKLTNRDAL KLVATVSGDP LELWLNQNVD FGKKIAELAI RQAQARMRSV KKIEKKKGSG VAVLPGKLTD CESEDIRENE LFLVEGDSAG GSAKLARDKA TQAILPLRGK VLNSFEVHPD QLFGNAEIHD ISVAIGVDPH GINDHPDLSG LRYGKIAILS DADVDGSHIQ VLLLTLFYRH FPKLVADGHI YVAQPPLFRV DVNAQGKSKP ARKFYALDQN ELDSILERLQ KEGVKETAYS ISRFKGLGEM NPDQLKDTTM HPDTRRLLQV QIPEGADDET RDIFVKLMGK GEAAARRAWM EREGDTAELD I // ID Q9JXN4_NEIMB Unreviewed; 166 AA. AC Q9JXN4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Putative thioredoxin {ECO:0000313|EMBL:AAF42287.1}; GN OrderedLocusNames=NMB1958 {ECO:0000313|EMBL:AAF42287.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42287.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42287.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42287.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2L5O} RP STRUCTURE BY NMR OF 24-165. RA Harris R., Foti R., Seidel R.D., Bonanno J.B., Freeman J., Bain K.T., RA Sauder J.M., Burley S.K., Girvin M.E., Almo S.C.; RT "Solution Structure of a Putative Thioredoxin from Neisseria RT meningitidis."; RL Submitted (NOV-2010) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42287.1; -; Genomic_DNA. DR PIR; G81021; G81021. DR RefSeq; NP_274952.1; NC_003112.2. DR RefSeq; WP_010981013.1; NC_003112.2. DR PDB; 2L5O; NMR; -; A=24-165. DR PDBsum; 2L5O; -. DR ProteinModelPortal; Q9JXN4; -. DR STRING; 122586.NMB1958; -. DR PaxDb; Q9JXN4; -. DR EnsemblBacteria; AAF42287; AAF42287; NMB1958. DR GeneID; 904192; -. DR KEGG; nme:NMB1958; -. DR PATRIC; 20359977; VBINeiMen85645_2493. DR eggNOG; ENOG4105KJP; Bacteria. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000097217; -. DR OMA; EPEWDAL; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NMEN122586:GHGG-2015-MONOMER; -. DR EvolutionaryTrace; Q9JXN4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2L5O}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 22 161 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 166 AA; 18139 MW; 8AF6E5C4173BDDD3 CRC64; MKKILTAAVV ALIGILLAIV LIPDSKTAPA FSLPDLHGKT VSNADLQGKV TLINFWFPSC PGCVSEMPKI IKTANDYKNK NFQVLAVAQP IDPIESVRQY VKDYGLPFTV MYDADKAVGQ AFGTQVYPTS VLIGKKGEIL KTYVGEPDFG KLYQEIDTAW RNSDAV // ID Q9JY23_NEIMB Unreviewed; 1995 AA. AC Q9JY23; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Hemagglutinin/hemolysin-related protein {ECO:0000313|EMBL:AAF42119.1}; GN OrderedLocusNames=NMB1779 {ECO:0000313|EMBL:AAF42119.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42119.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42119.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42119.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42119.1; -; Genomic_DNA. DR PIR; G81044; G81044. DR RefSeq; NP_274779.1; NC_003112.2. DR RefSeq; WP_010980989.1; NC_003112.2. DR ProteinModelPortal; Q9JY23; -. DR STRING; 122586.NMB1779; -. DR PaxDb; Q9JY23; -. DR EnsemblBacteria; AAF42119; AAF42119; NMB1779. DR GeneID; 903320; -. DR KEGG; nme:NMB1779; -. DR PATRIC; 20359513; VBINeiMen85645_2262. DR eggNOG; ENOG4108XKC; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000218788; -. DR KO; K15125; -. DR OMA; VAITSEN; -. DR OrthoDB; EOG65QWD9; -. DR BioCyc; NMEN122586:GHGG-1834-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR008619; Filamentous_hemagglutn_rpt. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF05594; Fil_haemagg; 2. DR Pfam; PF05860; Haemagg_act; 1. DR Pfam; PF04829; PT-VENN; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 93 201 Haemagg_act. {ECO:0000259|SMART:SM00912}. SQ SEQUENCE 1995 AA; 207212 MW; F40F81F28357285F CRC64; MNKGLHRIIF SKKHSTMVAV AETANSQGKG KQAGSSVSVS LKTSGDLCGK LKTTLKTLVC SLVSLSMVLP AHAQITTDKS APKNQQVVIL KTNTGAPLVN IQTPNGRGLS HNRYTQFDVD NKGAVLNNDR NNNPFVVKGS AQLILNEVRG TASKLNGIVT VGGQKADVII ANPNGITVNG GGFKNVGRGI LTTGAPQIGK DGALTGFDVR QGTLTVGAAG WNDKGGADYT GVLARAVALQ GKLQGKNLAV STGPQKVDYA SGEISAGTAA GTKPTIALDT AALGGMYADS ITLIANEKGV GVKNAGTLEA AKQLIVTSSG RIENSGRIAT TADGTEASPT YLSIETTEKG AAGTFISNGG RIESKGLLVI ETGEDISLRN GAVVQNNGSR PATTVLNAGH NLVIESKTNV NNAKGPATLS ADGRTVIKEA SIQTGTTVYS SSKGNAELGN NTRITGADVT VLSNGTISSS AVIDAKDTAH IEAGKPLSLE ASTVTSDIRL NGGSIKGGKQ LALLADDNIT AKTTNLNTPG NLYVHTGKDL NLNVDKDLSA ASIHLKSDNA AHITGTSKTL TASKDMGVEA GSLNVTNTNL RTNSGNLHIQ AAKGNIQLRN TKLNAAKALE TTALQGNIVS DGLHAVSADG HVSLLANGNA DFTGHNTLTA KADVNAGSVG KGRLKADNTN ITSSSGDITL VAGNGIQLGD GKQRNSINGK HISIKNNGGN ADLKNLNVHA KSGALNIHSD RALSIENTKL ESTHNTHLNA QHERVTLNQV DAYAHRHLSI TGSQIWQNDK LPSANKLVAN GVLALNARYS QIADNTTLRA GAINLTAGTA LVKRGNINWS TVSTKTLEDN AELKPLAGRL NIEAGSGTLT IEPANRISAH TDLSIKTGGK LLLSAKGGNA GAPSAQVSSL EAKGNIRLVT GETDLRGSKI TAGKNLVVAT TKGKLNIEAV NNSFSNYFPT QKAAELNQKS KELEQQIAQL KKSSPKSKLI PTLQEERDRL AFYIQAINKE VKGKKPKGKE YLQAKLSAQN IDLISAQGIE ISGSDITASK KLNLHAAGVL PKAADSEAAA ILIDGITDQY EIGKPTYKSH YDKAALNKPS RLTGRTGVSI HAAAALDDAR IIIGASEIKA PSGSIDIKAH SDIVLEAGQN DAYTFLKTKG KSGKIIRKTK FTSTRDHLIM PAPVELTANG ITLQAGGNIE ANTTRFNAPA GKVTLVAGEE LQLLAEEGIH KHELDVQKSR RFIGIKVGKS NYSKNELNET KLPVRVVAQT AATRSGWDTV LEGTEFKTTL AGADIQAGVG EKARADAKII LKGIVNRIQS EEKLETNSTV WQKQAGRGST IETLKLPSFE SPTPPKLTAP GGYIVDIPKG NLKTEIEKLA KQPEYAYLKQ LQVAKNVNWN QVQLAYDKWD YKQEGLTRAG AAIVTIIVTA LTYGYGATAA GGVAASGSST AAAAGTAATT TAAATTVSTA TAMQTAALAS LYSQAAVSII NNKGDVGKAL KDLGTSDTVK QIVTSALTAG ALNQMGADIA QLNSKVRTEL FSSTGNQTIA NLGGRLATNL SNAGISAGIN TAVNGGSLKD NLGNAALGAL VNSFQGEAAS KIKTTFSDDY VAKQFAHALA GCVSGLVQGK CKDGAIGAAV GEIVADSMLG GRNPATLSDA EKHKVISYSK IIAGSVAALN GGDVNTAANA AEVAVVNNAL NFDSTPTNAK KHQPQKPDKT ALEKIIQGIM PAHAAGAMTN PQDKDAAIWI SNIRNGITGP IVITSYGVYA AGWTAPLIGT AGKLAISTCM ANPSGCTVMV TQAAEAGAGI ATGAVTVGNA WEAPVGALSK AKAAKQAAPK ETINNLANLA KAEQQILFRI AQRDTQLDAW KTGFNNRVRK GAGLLDASNI PITINGKTIK PVQAISLKGA PVYSGVSEQE IFALYRQMTG QNPNFRVLPD GRLANGIIST GEWAGTKIAL RNFSKTENST QARWTLDLQN PPSFIKGTKL ELKFQ // ID Q9JXA7_NEIMB Unreviewed; 59 AA. AC Q9JXA7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42453.1}; GN OrderedLocusNames=NMB2145 {ECO:0000313|EMBL:AAF42453.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42453.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42453.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42453.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42453.1; -; Genomic_DNA. DR PIR; G81002; G81002. DR RefSeq; NP_275130.1; NC_003112.2. DR RefSeq; WP_002215152.1; NC_003112.2. DR STRING; 122586.NMB2145; -. DR PaxDb; Q9JXA7; -. DR EnsemblBacteria; AAF42453; AAF42453; NMB2145. DR GeneID; 903227; -. DR KEGG; nme:NMB2145; -. DR PATRIC; 20360484; VBINeiMen85645_2738. DR HOGENOM; HOG000027918; -. DR OMA; KPEVNVM; -. DR OrthoDB; EOG63VC55; -. DR BioCyc; NMEN122586:GHGG-2210-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR027383; Znf_put. DR Pfam; PF13490; zf-HC2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 38 zf-HC2. {ECO:0000259|Pfam:PF13490}. SQ SEQUENCE 59 AA; 7028 MW; 80BDD3F4D67A6EB8 CRC64; MKKCRDIALL LSKHQDRETT PGEKISIYTH LLFCPYCREY KRQLQTIKRS LAKTTRTSK // ID Q9K0A8_NEIMB Unreviewed; 259 AA. AC Q9K0A8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Laccase domain protein {ECO:0000256|RuleBase:RU361274}; GN OrderedLocusNames=NMB0706 {ECO:0000313|EMBL:AAF41123.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41123.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41123.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41123.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:1RV9} RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS). RA Eswaramoorthy S., Swaminathan S.; RT "Crystal Structure of a hypothetical protein, NMB0706."; RL Submitted (DEC-2003) to the PDB data bank. CC -!- SIMILARITY: Belongs to the LACC1 family. CC {ECO:0000256|RuleBase:RU361274}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41123.1; -; Genomic_DNA. DR PIR; C81168; C81168. DR RefSeq; NP_273748.1; NC_003112.2. DR RefSeq; WP_002244057.1; NC_003112.2. DR PDB; 1RV9; X-ray; 1.53 A; A=1-259. DR PDBsum; 1RV9; -. DR ProteinModelPortal; Q9K0A8; -. DR SMR; Q9K0A8; 15-256. DR STRING; 122586.NMB0706; -. DR PaxDb; Q9K0A8; -. DR EnsemblBacteria; AAF41123; AAF41123; NMB0706. DR GeneID; 902818; -. DR KEGG; nme:NMB0706; -. DR PATRIC; 20356759; VBINeiMen85645_0901. DR eggNOG; ENOG4105DBW; Bacteria. DR eggNOG; COG1496; LUCA. DR HOGENOM; HOG000242994; -. DR KO; K05810; -. DR OMA; VVMTADC; -. DR OrthoDB; EOG60GRZN; -. DR BioCyc; NMEN122586:GHGG-734-MONOMER; -. DR EvolutionaryTrace; Q9K0A8; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.60.140.10; -; 1. DR InterPro; IPR003730; Cu_polyphenol_OxRdtase_Laccase. DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat. DR Pfam; PF02578; Cu-oxidase_4; 1. DR SUPFAM; SSF64438; SSF64438; 1. DR TIGRFAMs; TIGR00726; TIGR00726; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1RV9}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 259 AA; 27130 MW; 398428B38409F201 CRC64; MKTITETLNL APKGKNFLTA DWPAPANVKT LITTRNGGVS QGAYQSLNLG THVGDNPEAV RRNREIVQQQ VGLPVAYLNQ IHSTVVVNAA EALGGTPDAD ASVDDTGKVA CAVMTADCLP VLFCDRAGTA VAAAHAGWRG LAGGVLQNTI AAMKVPPVEM MAYLGPAISA DAFEVGQDVF DAFCTPMPEA ATAFEGIGSG KFLADLYALA RLILKREGVG GVYGGTHCTV LERDTFFSYR RDGATGRMAS LIWLDGNAV // ID Q9K1F7_NEIMB Unreviewed; 95 AA. AC Q9K1F7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40654.1}; GN OrderedLocusNames=NMB0197 {ECO:0000313|EMBL:AAF40654.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40654.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40654.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40654.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40654.1; -; Genomic_DNA. DR PIR; G81225; G81225. DR STRING; 122586.NMB0197; -. DR PaxDb; Q9K1F7; -. DR EnsemblBacteria; AAF40654; AAF40654; NMB0197. DR PATRIC; 20355437; VBINeiMen85645_0247. DR BioCyc; NMEN122586:GHGG-208-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 63 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 95 AA; 10459 MW; 0C08F65E09BFFE0F CRC64; MHVPENRVRK GRIQKAIKID AAVCLPRSER CGRKNGGRLL LVIVMPVFWA VCVWDLGPAA VLLPRRNGKI NSNLITFCAC RLGTGAGKML CGVRF // ID Q9K0S4_NEIMB Unreviewed; 71 AA. AC Q9K0S4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40936.1}; GN OrderedLocusNames=NMB0504 {ECO:0000313|EMBL:AAF40936.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40936.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40936.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40936.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40936.1; -; Genomic_DNA. DR PIR; G81190; G81190. DR STRING; 122586.NMB0504; -. DR PaxDb; Q9K0S4; -. DR EnsemblBacteria; AAF40936; AAF40936; NMB0504. DR BioCyc; NMEN122586:GHGG-529-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 71 AA; 7574 MW; 47683EF44F4A65FF CRC64; MPMRTVASCS APRISVRKTA KSKFNLTVTN ITMRDRANSI PLNAAATKLA NGTTANTLPK SKNTKTPSPT Q // ID Q7DDK9_NEIMB Unreviewed; 181 AA. AC Q7DDK9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41272.1}; GN OrderedLocusNames=NMB0861 {ECO:0000313|EMBL:AAF41272.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41272.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41272.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41272.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41272.1; -; Genomic_DNA. DR PIR; H81150; H81150. DR RefSeq; NP_273902.1; NC_003112.2. DR RefSeq; WP_002213897.1; NC_003112.2. DR STRING; 122586.NMB0861; -. DR PaxDb; Q7DDK9; -. DR EnsemblBacteria; AAF41272; AAF41272; NMB0861. DR GeneID; 902975; -. DR KEGG; nme:NMB0861; -. DR PATRIC; 20357115; VBINeiMen85645_1076. DR eggNOG; ENOG4107AP1; Bacteria. DR eggNOG; ENOG410Z5UK; LUCA. DR HOGENOM; HOG000218880; -. DR OrthoDB; EOG61P6VJ; -. DR BioCyc; NMEN122586:GHGG-892-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 181 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287262. SQ SEQUENCE 181 AA; 19533 MW; 6F785B609924B32C CRC64; MKKQITAAVM MLSMIAPAMA NGLDNQAFED QVFHTRADAP MQLAELSQKE MKETEGAFLP LAILGGAAIG MWTQHGFSYA TTGRPASVRD VAIAGGLGAI PGGVGAAGKV VSFAKYGREI KIGNNMRIAP FGNRTGHPIG KFPHYHRRVT DNTGKTLPGQ GIGRHRPWES KSTDRSWKNR F // ID Q9K0W4_NEIMB Unreviewed; 321 AA. AC Q9K0W4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF40880.1}; GN OrderedLocusNames=NMB0443 {ECO:0000313|EMBL:AAF40880.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40880.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40880.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40880.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40880.1; -; Genomic_DNA. DR PIR; C81199; C81199. DR RefSeq; NP_273490.1; NC_003112.2. DR RefSeq; WP_002224817.1; NC_003112.2. DR ProteinModelPortal; Q9K0W4; -. DR STRING; 122586.NMB0443; -. DR PaxDb; Q9K0W4; -. DR EnsemblBacteria; AAF40880; AAF40880; NMB0443. DR GeneID; 902559; -. DR KEGG; nme:NMB0443; -. DR PATRIC; 20356094; VBINeiMen85645_0562. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; GSCENIN; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-467-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38055 MW; 8B130D0255F04E10 CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS QTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLRK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JZ59_NEIMB Unreviewed; 369 AA. AC Q9JZ59; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Putative membrane-bound lytic murein transglycosylase B {ECO:0000313|EMBL:AAF41655.1}; GN OrderedLocusNames=NMB1279 {ECO:0000313|EMBL:AAF41655.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41655.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41655.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41655.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41655.1; -; Genomic_DNA. DR PIR; G81101; G81101. DR RefSeq; NP_274299.1; NC_003112.2. DR RefSeq; WP_002244148.1; NC_003112.2. DR ProteinModelPortal; Q9JZ59; -. DR STRING; 122586.NMB1279; -. DR PaxDb; Q9JZ59; -. DR EnsemblBacteria; AAF41655; AAF41655; NMB1279. DR GeneID; 903701; -. DR KEGG; nme:NMB1279; -. DR PATRIC; 20358183; VBINeiMen85645_1603. DR eggNOG; ENOG4105CVE; Bacteria. DR eggNOG; COG2951; LUCA. DR HOGENOM; HOG000257828; -. DR KO; K08305; -. DR OMA; NYRVIDA; -. DR OrthoDB; EOG6R87H7; -. DR BioCyc; NMEN122586:GHGG-1317-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR011757; Lytic_transglycosylase_MltB. DR InterPro; IPR031304; SLT_2. DR PANTHER; PTHR30163; PTHR30163; 1. DR Pfam; PF13406; SLT_2; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR TIGRFAMs; TIGR02282; MltB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 369 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332267. FT DOMAIN 69 361 SLT_2. {ECO:0000259|Pfam:PF13406}. SQ SEQUENCE 369 AA; 40422 MW; 3A309E2A9A9ED9D3 CRC64; MKKRKILPLA ICLAALSACT AMEARPPRAN EAQAPRAVEM KKESRPAFDA AAVFDAAAVP VSDSGFAANA NVRRFVDDEV GKGDFSRAEW QDFFDKAAYK ADIVKIMHRP STSRPWYVFR TGNSGKAKFR GARRFYAENR ALIDDVAQKY GVPAELIVAV IGIETNYGKN TGSFRVADAL ATLGFDYPRR AGFFQKELVE LLKLAKEEGG DVFAFKGSYA GAMGMPQFMP SSYRKWAVDY DGDGHRDIWG NVGDVAASVA NYMKQHGWRT GGKMLVSATL APGADVQAII GEKTALTRTV ADLKAYGIIP GEELADDEKA VLFKLETAPG VFEYYLGLNN FYTVWQYNHS RMYVTAVRDI ANSLGGPGL // ID Q9K0W1_NEIMB Unreviewed; 362 AA. AC Q9K0W1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Chorismate mutase/prephenate dehydratase {ECO:0000313|EMBL:AAF40883.1}; DE EC=4.2.1.- {ECO:0000313|EMBL:AAF40883.1}; DE EC=5.4.99.5 {ECO:0000313|EMBL:AAF40883.1}; GN Name=pheA {ECO:0000313|EMBL:AAF40883.1}; GN OrderedLocusNames=NMB0446 {ECO:0000313|EMBL:AAF40883.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40883.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40883.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40883.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40883.1; -; Genomic_DNA. DR PIR; H81196; H81196. DR RefSeq; NP_273493.1; NC_003112.2. DR RefSeq; WP_002222056.1; NC_003112.2. DR ProteinModelPortal; Q9K0W1; -. DR STRING; 122586.NMB0446; -. DR PaxDb; Q9K0W1; -. DR EnsemblBacteria; AAF40883; AAF40883; NMB0446. DR GeneID; 902562; -. DR KEGG; nme:NMB0446; -. DR PATRIC; 20356104; VBINeiMen85645_0568. DR eggNOG; ENOG4105CQC; Bacteria. DR eggNOG; COG0077; LUCA. DR eggNOG; COG1605; LUCA. DR HOGENOM; HOG000018971; -. DR KO; K14170; -. DR OMA; WREVMSA; -. DR OrthoDB; EOG6WHNT1; -. DR BioCyc; NMEN122586:GHGG-470-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.59.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase. DR InterPro; IPR002701; Chorismate_mutase. DR InterPro; IPR020822; Chorismate_mutase_type_II. DR InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase. DR InterPro; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR Pfam; PF01842; ACT; 1. DR Pfam; PF01817; CM_2; 1. DR Pfam; PF00800; PDT; 1. DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR TIGRFAMs; TIGR01807; CM_P2; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1. DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF40883.1}; KW Lyase {ECO:0000313|EMBL:AAF40883.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 91 Chorismate mutase. FT {ECO:0000259|PROSITE:PS51168}. FT DOMAIN 91 269 Prephenate dehydratase. FT {ECO:0000259|PROSITE:PS51171}. FT DOMAIN 281 356 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 362 AA; 39377 MW; B102B8732830D504 CRC64; MSQTIDELLL PHRNAIDTID AEILRLLNER AQHAHAIGEL KGTGAVYRPE REVAVLRRIQ DLNKGPLPDE SVARLFREVM SECLAVERPL TIAYLGPQGT FTQQAAIKHF GHAAHTMACP TIDDCFKQVE TRQADYLVAP VENSTEGSVG RTLDLLAVTA LQACGEIVLR IHHNLLRKNN GSTEGIAKVF SHAQALAQCN DWLGRHLPNA ERIAVSSNAE AARLVAESDD GTVAAIAGRT AAEIYGLDMV AECIEDEPNN TTRFLVMGHH ETGASGSDKT SLAVSAPNRA GAVASLLQPL TESGISMTKF ESRPSKSVLW EYLFFIDIEG HRRDAQIQTA LERLGERASF VKVIGSYPTA VL // ID Q9JY21_NEIMB Unreviewed; 117 AA. AC Q9JY21; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42123.1}; GN OrderedLocusNames=NMB1784 {ECO:0000313|EMBL:AAF42123.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42123.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42123.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42123.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42123.1; -; Genomic_DNA. DR PIR; A81043; A81043. DR RefSeq; NP_274783.1; NC_003112.2. DR RefSeq; WP_002234250.1; NC_003112.2. DR STRING; 122586.NMB1784; -. DR PaxDb; Q9JY21; -. DR EnsemblBacteria; AAF42123; AAF42123; NMB1784. DR GeneID; 903315; -. DR KEGG; nme:NMB1784; -. DR PATRIC; 20359529; VBINeiMen85645_2270. DR HOGENOM; HOG000218785; -. DR OMA; SIKMIEL; -. DR OrthoDB; EOG65TRTR; -. DR BioCyc; NMEN122586:GHGG-1839-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 117 AA; 12049 MW; 774404645A06428C CRC64; MIELQLHELK LVSGGGPVTD NIAGNVANAA TTKGGPTWGD LVAIPAAAAA VYYLPKNAYG AAGANGVYNV TRNWVNDAVN APPYNGRPIF EIEHGLTAPA TKADKSGNGY TDGTDYC // ID Q7DDB5_NEIMB Unreviewed; 119 AA. AC Q7DDB5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41863.1}; GN OrderedLocusNames=NMB1507 {ECO:0000313|EMBL:AAF41863.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41863.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41863.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41863.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41863.1; -; Genomic_DNA. DR STRING; 122586.NMB1507; -. DR PaxDb; Q7DDB5; -. DR EnsemblBacteria; AAF41863; AAF41863; NMB1507. DR HOGENOM; HOG000027855; -. DR OMA; RHACAPP; -. DR OrthoDB; EOG6VMTTV; -. DR BioCyc; NMEN122586:GHGG-1547-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 119 AA; 13100 MW; FE489DB5A0777D89 CRC64; MRNKQTPSKQ ASKQASKQAS KQKIITPFLP THALSARRIP LFPPLKSAFS SGRVSARLFS LFSFPRHACA PPAALCCTFA PGRHRSAIRF SVLHTPVSER NADVSTHRTT HKAPPYVLP // ID Q7DDC1_NEIMB Unreviewed; 60 AA. AC Q7DDC1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41761.1}; GN OrderedLocusNames=NMB1397 {ECO:0000313|EMBL:AAF41761.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41761.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41761.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41761.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41761.1; -; Genomic_DNA. DR PIR; E81088; E81088. DR RefSeq; NP_274411.1; NC_003112.2. DR RefSeq; WP_002232653.1; NC_003112.2. DR STRING; 122586.NMB1397; -. DR PaxDb; Q7DDC1; -. DR EnsemblBacteria; AAF41761; AAF41761; NMB1397. DR GeneID; 903819; -. DR KEGG; nme:NMB1397; -. DR HOGENOM; HOG000219004; -. DR OMA; FLQITIM; -. DR OrthoDB; EOG66MQVF; -. DR BioCyc; NMEN122586:GHGG-1435-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 45 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 60 AA; 6970 MW; 8A1E9C876432E30E CRC64; MNTNLNDKDK AMDTAIRFQK RMRIPKFFFL ILGITMVLAF IQDVITGSNF LQITINVKFS // ID Q4W589_NEIMB Unreviewed; 112 AA. AC Q4W589; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52142.1}; GN OrderedLocusNames=NMB0022 {ECO:0000313|EMBL:AAY52142.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52142.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52142.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52142.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52142.1; -; Genomic_DNA. DR RefSeq; WP_002221781.1; NC_003112.2. DR RefSeq; YP_338287.1; NC_003112.2. DR ProteinModelPortal; Q4W589; -. DR SMR; Q4W589; 5-90. DR STRING; 122586.NMB0022; -. DR PaxDb; Q4W589; -. DR EnsemblBacteria; AAY52142; AAY52142; NMB0022. DR GeneID; 902125; -. DR KEGG; nme:NMB0022; -. DR PATRIC; 20354989; VBINeiMen85645_0031. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000008197; -. DR OMA; ESTAGCI; -. DR BioCyc; NMEN122586:GHGG-23-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 112 AA; 12071 MW; 8CEDA1052AB81B5E CRC64; MTGFNDAAGV ASSSTIKGKY VKEVEVKNGV VTATMLSTGV NNEIKGKKLS LWAKRQAGSV KWFCGQPVTR ADNAKDDVAA ATGTDKIDTK LKKPFYPISF RTDEAGFPLL RE // ID Q9K0R6_NEIMB Unreviewed; 79 AA. AC Q9K0R6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40946.1}; GN OrderedLocusNames=NMB0514 {ECO:0000313|EMBL:AAF40946.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40946.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40946.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40946.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40946.1; -; Genomic_DNA. DR PIR; D81188; D81188. DR STRING; 122586.NMB0514; -. DR PaxDb; Q9K0R6; -. DR EnsemblBacteria; AAF40946; AAF40946; NMB0514. DR PATRIC; 20356272; VBINeiMen85645_0656. DR OrthoDB; EOG686NF5; -. DR BioCyc; NMEN122586:GHGG-539-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 79 AA; 8341 MW; 7CCCCF000A30A27F CRC64; MLGVVPGIGE SIQAYKVAKA AKNLQGMKKA LDKAATVATA QGYVSKTKIK IGQTELRVTA ATDKQLLKAI GEGRTRQVK // ID Q9JY45_NEIMB Unreviewed; 145 AA. AC Q9JY45; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=VapD-related protein {ECO:0000313|EMBL:AAF42094.1}; GN OrderedLocusNames=NMB1753 {ECO:0000313|EMBL:AAF42094.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42094.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42094.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42094.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42094.1; -; Genomic_DNA. DR PIR; H81045; H81045. DR RefSeq; NP_274753.1; NC_003112.2. DR RefSeq; WP_002219746.1; NC_003112.2. DR STRING; 122586.NMB1753; -. DR PaxDb; Q9JY45; -. DR EnsemblBacteria; AAF42094; AAF42094; NMB1753. DR GeneID; 903345; -. DR KEGG; nme:NMB1753; -. DR PATRIC; 20359479; VBINeiMen85645_2245. DR eggNOG; ENOG4105Y8T; Bacteria. DR eggNOG; COG3309; LUCA. DR HOGENOM; HOG000286076; -. DR OMA; ARFEWFY; -. DR OrthoDB; EOG6VB6WH; -. DR BioCyc; NMEN122586:GHGG-1808-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2. DR Pfam; PF09827; CRISPR_Cas2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 145 AA; 16730 MW; ADCEE4309F3DBED6 CRC64; MSRYLITFDM DTNCLKDNYH GNNYTNAYSD IKTILARHGF ENIQGSVYLG REGISEAHGT IAIQELTARF DWFYSCISNI KFYRLESDLN AQFIADGVYQ AKQAFLQRVE QLRISLTEAG LSDEQINQVL EKQKFELESP NLKLN // ID Q9K128_NEIMB Unreviewed; 377 AA. AC Q9K128; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40808.1}; GN OrderedLocusNames=NMB0366 {ECO:0000313|EMBL:AAF40808.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40808.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40808.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40808.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40808.1; -; Genomic_DNA. DR PIR; D81206; D81206. DR RefSeq; NP_273415.1; NC_003112.2. DR RefSeq; WP_010980786.1; NC_003112.2. DR STRING; 122586.NMB0366; -. DR PaxDb; Q9K128; -. DR EnsemblBacteria; AAF40808; AAF40808; NMB0366. DR GeneID; 902481; -. DR KEGG; nme:NMB0366; -. DR PATRIC; 20355889; VBINeiMen85645_0462. DR HOGENOM; HOG000219108; -. DR OMA; SMRTEES; -. DR OrthoDB; EOG6HF5VS; -. DR BioCyc; NMEN122586:GHGG-388-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 377 AA; 43159 MW; 9B1930636F732E3F CRC64; MFKKFKPVLL SFFALVFAFW LGTGIAYEIN PRWFLSDTAT EVPKNPNAFV AKLARLFRNA DRAVVIVKES IRTEENLAGT VDDGPLQSEK DYLALAIRLS RLKEKAKWFH VTEQEHGKEV WLDYHIGEGG LVAVSLSQRS PEAFVNAEYL YRNDRPFSVN VYGGTVHGEN YETTGEYRVV WQPDGSVFDA AGRGKIGEDV YEHCLGCYQM AQVYLAKYRD VANDEQKVWD FRKESNRIAS DSRNSVFYQN MRELMPRGMK ANSLVVGYDA DGLPQKVYWS FDNGKKRQSF EYYLKNGNLF IAQSSTVALK ADGVTADMQT YHAQQTWYLD GGRIVREEKQ GDRLPDFPLN LENLEKEVRR YAEAAARRSG GRRDLSH // ID Q4W581_NEIMB Unreviewed; 121 AA. AC Q4W581; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Transposase, truncation {ECO:0000313|EMBL:AAY52166.1}; GN OrderedLocusNames=NMB0141 {ECO:0000313|EMBL:AAY52166.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52166.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52166.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52166.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52166.1; -; Genomic_DNA. DR STRING; 122586.NMB0141; -. DR PaxDb; Q4W581; -. DR EnsemblBacteria; AAY52166; AAY52166; NMB0141. DR PATRIC; 20355303; VBINeiMen85645_0181. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000220750; -. DR OrthoDB; EOG6R2GWH; -. DR BioCyc; NMEN122586:GHGG-151-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 40 91 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 121 AA; 14449 MW; 3E49ADFCE850E45C CRC64; MIAKHIDRFP LLKLDRVIDW QPIEQYLNRQ RTRYLRDHRG RPAYPLLSMF KAVLLGQWHS LSDPELEHSL ITRIDFNLFC RFDELSIPDY SHQPYSGLSE KDAYAVMTGY RPVKRVRPYA V // ID Q9K072_NEIMB Unreviewed; 124 AA. AC Q9K072; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41159.1}; GN OrderedLocusNames=NMB0746 {ECO:0000313|EMBL:AAF41159.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41159.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41159.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41159.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41159.1; -; Genomic_DNA. DR PIR; A81163; A81163. DR RefSeq; NP_273788.1; NC_003112.2. DR RefSeq; WP_002217625.1; NC_003112.2. DR STRING; 122586.NMB0746; -. DR PaxDb; Q9K072; -. DR EnsemblBacteria; AAF41159; AAF41159; NMB0746. DR GeneID; 902861; -. DR KEGG; nme:NMB0746; -. DR PATRIC; 20356863; VBINeiMen85645_0950. DR eggNOG; COG3094; LUCA. DR HOGENOM; HOG000270268; -. DR OMA; AIAWVVY; -. DR OrthoDB; EOG65F8WK; -. DR BioCyc; NMEN122586:GHGG-777-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007360; SirB. DR Pfam; PF04247; SirB; 1. DR PIRSF; PIRSF005610; SirB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 117 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 124 AA; 14527 MW; 3A805FECE6C81E62 CRC64; MQYLIVKYSH QIFVTITILV FNIRFFLLWK NPEKPLAGFW KALPHLNDTM LLFTGLWLMK ITHFSPFNAP WLGTKILLLL AYIALGMMMM RARPRSTKFY TVYLLAMCCV ACIVYLAKTK VLPF // ID Q9JXV0_NEIMB Unreviewed; 144 AA. AC Q9JXV0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42209.1}; GN OrderedLocusNames=NMB1875 {ECO:0000313|EMBL:AAF42209.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42209.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42209.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42209.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42209.1; -; Genomic_DNA. DR PIR; A81033; A81033. DR RefSeq; NP_274871.1; NC_003112.2. DR RefSeq; WP_002214654.1; NC_003112.2. DR STRING; 122586.NMB1875; -. DR PaxDb; Q9JXV0; -. DR EnsemblBacteria; AAF42209; AAF42209; NMB1875. DR GeneID; 904313; -. DR KEGG; nme:NMB1875; -. DR PATRIC; 20359781; VBINeiMen85645_2396. DR HOGENOM; HOG000218758; -. DR OMA; EGFNWTI; -. DR OrthoDB; EOG6TXQTR; -. DR BioCyc; NMEN122586:GHGG-1931-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR011723; Znf/thioredoxin_put. DR TIGRFAMs; TIGR02098; MJ0042_CXXC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 143 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 144 AA; 15546 MW; FD1294993673E171 CRC64; MPACFCPHCK TRLWVKETQL NVAQGFVVCQ KCEGLFKAKD HLASTKEPIF NDLPEAVSDV KLVHRIGTRA IGKKQISRDE IAGILNGGTT QPDIPPATAA TPAAAPQVTV PPAAPARQDG FNWTIATLFA LIVLIMQLSY LVIL // ID Q9K0A5_NEIMB Unreviewed; 188 AA. AC Q9K0A5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62318.1}; GN OrderedLocusNames=NMB0710 {ECO:0000313|EMBL:AAF62318.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62318.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62318.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62318.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62318.1; -; Genomic_DNA. DR RefSeq; NP_273752.1; NC_003112.2. DR RefSeq; WP_002225471.1; NC_003112.2. DR STRING; 122586.NMB0710; -. DR PaxDb; Q9K0A5; -. DR EnsemblBacteria; AAF62318; AAF62318; NMB0710. DR GeneID; 902822; -. DR KEGG; nme:NMB0710; -. DR PATRIC; 20356767; VBINeiMen85645_0905. DR eggNOG; ENOG4105SZ4; Bacteria. DR eggNOG; COG1714; LUCA. DR HOGENOM; HOG000262647; -. DR OMA; PRRQFLH; -. DR OrthoDB; EOG63VC0G; -. DR BioCyc; NMEN122586:GHGG-738-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010432; RDD. DR Pfam; PF06271; RDD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 82 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 165 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 24 178 RDD. {ECO:0000259|Pfam:PF06271}. SQ SEQUENCE 188 AA; 21037 MW; 93BA59ED2FCE7A90 CRC64; MPSEACWRFR RHILIEKMMT LKTAPLKRRF AAMLYEMLLV GAATCLAALI AGIAAIFLNP VSIAVSALVT SILIMGAWWL YFRANWHGQG QTLAMRTWKI GLCDLNGIQP SLHLLRLRFI WACIFIVFIP MLAYAGLRHF LGIPPKGAAG AALIWLILPW GFALLNPDRQ FLYDFLAGTR LVAVKGKP // ID Q9JY59_NEIMB Unreviewed; 203 AA. AC Q9JY59; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Cytochrome c oxidase, subunit II {ECO:0000313|EMBL:AAF42069.1}; DE EC=1.9.3.1 {ECO:0000313|EMBL:AAF42069.1}; GN Name=fixO {ECO:0000313|EMBL:AAF42069.1}; GN OrderedLocusNames=NMB1724 {ECO:0000313|EMBL:AAF42069.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42069.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42069.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42069.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42069.1; -; Genomic_DNA. DR PIR; D81050; D81050. DR RefSeq; NP_274727.1; NC_003112.2. DR RefSeq; WP_002212596.1; NC_003112.2. DR ProteinModelPortal; Q9JY59; -. DR STRING; 122586.NMB1724; -. DR PaxDb; Q9JY59; -. DR DNASU; 903378; -. DR EnsemblBacteria; AAF42069; AAF42069; NMB1724. DR GeneID; 903378; -. DR KEGG; nme:NMB1724; -. DR PATRIC; 20359411; VBINeiMen85645_2211. DR eggNOG; ENOG4105DUJ; Bacteria. DR eggNOG; COG2993; LUCA. DR HOGENOM; HOG000277919; -. DR KO; K00405; -. DR OMA; YAWLSKT; -. DR OrthoDB; EOG6RZB37; -. DR BioCyc; NMEN122586:GHGG-1779-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR003468; Cyt_c_oxidase_monohaem-su/FixO. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF02433; FixO; 1. DR SUPFAM; SSF46626; SSF46626; 1. DR TIGRFAMs; TIGR00781; ccoO; 1. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42069.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 51 196 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 203 AA; 22529 MW; AC6B7D81D3037C16 CRC64; MKLQQLAEEK IGVLIVFTLL VVSVGLLIEV VPLAFTKAAT QPAPGVKPYN ALQVAGRDIY IREGCYNCHS QMIRPFRAET ERYGHYSVAG ESVYDHPFQW GSKRTGPDLA RVGGRYSDEW HRIHLLNPRD VVPESNMPAF PWLARNKVDV DATVANMKAL RKVGTPYSDE EIAKAPEALA NKSELDAVVA YLQGLGLALK NVR // ID Q9K1C9_NEIMB Unreviewed; 33 AA. AC Q9K1C9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40688.1}; GN OrderedLocusNames=NMB0233 {ECO:0000313|EMBL:AAF40688.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40688.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40688.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40688.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40688.1; -; Genomic_DNA. DR PIR; H81220; H81220. DR RefSeq; NP_273290.1; NC_003112.2. DR RefSeq; WP_010980763.1; NC_003112.2. DR STRING; 122586.NMB0233; -. DR PaxDb; Q9K1C9; -. DR EnsemblBacteria; AAF40688; AAF40688; NMB0233. DR GeneID; 902344; -. DR KEGG; nme:NMB0233; -. DR BioCyc; NMEN122586:GHGG-248-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 33 AA; 3759 MW; 493DB4538D5C1BCE CRC64; MGFFYESSPK FQTAFLAVII VDEAHATMYT QSK // ID Q9K065_NEIMB Unreviewed; 47 AA. AC Q9K065; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41168.1}; GN OrderedLocusNames=NMB0755 {ECO:0000313|EMBL:AAF41168.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41168.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41168.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41168.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41168.1; -; Genomic_DNA. DR PIR; B81164; B81164. DR RefSeq; NP_273797.1; NC_003112.2. DR RefSeq; WP_010980836.1; NC_003112.2. DR STRING; 122586.NMB0755; -. DR PaxDb; Q9K065; -. DR EnsemblBacteria; AAF41168; AAF41168; NMB0755. DR GeneID; 902870; -. DR KEGG; nme:NMB0755; -. DR HOGENOM; HOG000027901; -. DR OrthoDB; EOG6XQ3W5; -. DR BioCyc; NMEN122586:GHGG-786-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5798 MW; 76F7D46FE56D47E1 CRC64; MLHINPFFIL FVGWEDSYLL IFSIKIRKFI VRCYCWQSYH VLLLMEA // ID Q9JYE9_NEIMB Unreviewed; 507 AA. AC Q9JYE9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Fumarate hydratase, class I, anaerobic {ECO:0000313|EMBL:AAF41965.1}; DE EC=4.2.1.2 {ECO:0000313|EMBL:AAF41965.1}; GN Name=fumB {ECO:0000313|EMBL:AAF41965.1}; GN OrderedLocusNames=NMB1613 {ECO:0000313|EMBL:AAF41965.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41965.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41965.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41965.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41965.1; -; Genomic_DNA. DR PIR; C81063; C81063. DR RefSeq; NP_274619.1; NC_003112.2. DR RefSeq; WP_002222179.1; NC_003112.2. DR ProteinModelPortal; Q9JYE9; -. DR STRING; 122586.NMB1613; -. DR PaxDb; Q9JYE9; -. DR EnsemblBacteria; AAF41965; AAF41965; NMB1613. DR GeneID; 904181; -. DR KEGG; nme:NMB1613; -. DR PATRIC; 20359116; VBINeiMen85645_2070. DR eggNOG; ENOG4107GFK; Bacteria. DR eggNOG; COG1838; LUCA. DR eggNOG; COG1951; LUCA. DR HOGENOM; HOG000262369; -. DR KO; K01676; -. DR OMA; GPQNKLE; -. DR OrthoDB; EOG6TXR10; -. DR BioCyc; NMEN122586:GHGG-1661-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro. DR Gene3D; 3.20.130.10; -; 1. DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat. DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat. DR InterPro; IPR011167; Fe_dep_fumarate_hydratase. DR Pfam; PF05681; Fumerase; 1. DR Pfam; PF05683; Fumerase_C; 1. DR PIRSF; PIRSF001394; Fe_dep_fumar_hy; 1. DR SUPFAM; SSF117457; SSF117457; 1. DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1. DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF41965.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 288 Fumerase. {ECO:0000259|Pfam:PF05681}. FT DOMAIN 292 491 Fumerase_C. {ECO:0000259|Pfam:PF05683}. SQ SEQUENCE 507 AA; 54950 MW; 1AA1595C31373665 CRC64; MTVIKQEDFI QSICDAFQFI SYYHPKDYID ALYKAWQKEE NPAAKDAMTQ ILVNSRMCAE NNRPICQDTG IATVFLKVGM NVQWDADMSV EEMVNEGVRR AYTWEGNTLR ASVLADPAGK RQNTKDNTPA VIHMSIVPGG KVEVTCAAKG GGSENKSKLA MLNPSDNIVD WVLKTIPTMG AGWCPPGILG IGIGGTPEKA VLMAKESLMS HIDIQELQEK AASGAELSTT EALRLELFEK VNALGIGAQG LGGLTTVLDV KILDYPTHAA SKPIAMIPNC AATRHVEFEL DGSGPVELTP PRVEDWPDLT YSPDNGKRVD VDKLTKEEVA SWKTGDVLLL NGKILTGRDA AHKRLVDMLN KGEELPVDFT NRLIYYVGPV DPVGDEVVGP AGPTTATRMD KFTRQMLEQT DLLGMIGKSE RGVATCEAIA DNKAVYLMAV GGAAYLVAKA IKSSKVLAFP ELGMEAIYEF EVKDMPVTVA VDSKGESIHA TAPRKWQAKI GIIPVES // ID Q9JY52_NEIMB Unreviewed; 117 AA. AC Q9JY52; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42083.1}; GN OrderedLocusNames=NMB1739 {ECO:0000313|EMBL:AAF42083.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42083.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42083.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42083.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42083.1; -; Genomic_DNA. DR PIR; C81047; C81047. DR RefSeq; NP_274741.1; NC_003112.2. DR RefSeq; WP_002218854.1; NC_003112.2. DR ProteinModelPortal; Q9JY52; -. DR STRING; 122586.NMB1739; -. DR PaxDb; Q9JY52; -. DR EnsemblBacteria; AAF42083; AAF42083; NMB1739. DR GeneID; 903360; -. DR KEGG; nme:NMB1739; -. DR PATRIC; 20359443; VBINeiMen85645_2227. DR OMA; QFCPSKE; -. DR BioCyc; NMEN122586:GHGG-1794-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 14 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 66 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 117 AA; 13753 MW; F0E9E0F38F88E720 CRC64; MFTTNDLRHF LEGLAILFSI GYWGTMLLLL WFLVRFAYKK PKRNPGKILS GSLTAAAILM LFVWIIPKQF GPIKEEIQAQ EEWDRKYKEA EAVFNEQCKT AGERFTRRRT MWKGLCC // ID Q4W586_NEIMB Unreviewed; 225 AA. AC Q4W586; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Large pilS cassette {ECO:0000313|EMBL:AAY52145.1}; GN OrderedLocusNames=NMB0025 {ECO:0000313|EMBL:AAY52145.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52145.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52145.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52145.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52145.1; -; Genomic_DNA. DR RefSeq; WP_002221784.1; NC_003112.2. DR RefSeq; YP_338290.1; NC_003112.2. DR ProteinModelPortal; Q4W586; -. DR SMR; Q4W586; 5-98, 109-216. DR STRING; 122586.NMB0025; -. DR PaxDb; Q4W586; -. DR EnsemblBacteria; AAY52145; AAY52145; NMB0025. DR GeneID; 902128; -. DR KEGG; nme:NMB0025; -. DR PATRIC; 20354999; VBINeiMen85645_0036. DR HOGENOM; HOG000027824; -. DR OMA; PDGNSNA; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-26-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 225 AA; 23777 MW; 39243319F7ECDBD2 CRC64; MTGFNDAAGV ASSSKIKGKY VKEVTVANGV VTATMLSSGV NKEIQGKKLS LWAKRQNGSV KWFCGQPVTR AGTDDTVAAD NTGNKKTNTK HLPSTCRDAA SAVCTKTPEY YPNHGEWPKN NTSAGVASSS TIKGKYVKEV TVANGVITAT MLSSGVNKEI QGKKLSLWAK RQDGSVKWFC GQPVTRNAAN AKAGTDEVTA ATPDTDKINT KHLPSTAPTR KSTPN // ID Q9JZS5_NEIMB Unreviewed; 46 AA. AC Q9JZS5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41324.1}; GN OrderedLocusNames=NMB0916 {ECO:0000313|EMBL:AAF41324.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41324.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41324.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41324.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41324.1; -; Genomic_DNA. DR PIR; F81142; F81142. DR RefSeq; NP_273956.1; NC_003112.2. DR RefSeq; WP_010980870.1; NC_003112.2. DR STRING; 122586.NMB0916; -. DR PaxDb; Q9JZS5; -. DR EnsemblBacteria; AAF41324; AAF41324; NMB0916. DR GeneID; 903037; -. DR KEGG; nme:NMB0916; -. DR BioCyc; NMEN122586:GHGG-954-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 38 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 46 AA; 5331 MW; 4B548FD59840AF91 CRC64; MRVLMAGKVR KQIKQGGWLS VIALTSLFVS VFTLFYIFRH SVQFNL // ID Q9JZD1_NEIMB Unreviewed; 200 AA. AC Q9JZD1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41498.1}; GN OrderedLocusNames=NMB1107 {ECO:0000313|EMBL:AAF41498.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41498.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41498.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41498.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41498.1; -; Genomic_DNA. DR PIR; H81121; H81121. DR RefSeq; NP_274138.1; NC_003112.2. DR RefSeq; WP_002222503.1; NC_003112.2. DR STRING; 122586.NMB1107; -. DR PaxDb; Q9JZD1; -. DR EnsemblBacteria; AAF41498; AAF41498; NMB1107. DR GeneID; 903529; -. DR KEGG; nme:NMB1107; -. DR PATRIC; 20357780; VBINeiMen85645_1406. DR BioCyc; NMEN122586:GHGG-1143-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 200 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329351. SQ SEQUENCE 200 AA; 21660 MW; 3E4FB71A24B6C9ED CRC64; MNMKKLISAI CVSIVLSACN QQSKTAQAEE PVQSIQAADC TAPMDITVEQ YLINLEQAFK TQNVSTKIHN KNIVKTDCGY DLTLVMDFGA IALKLDEQQK IRAISVGYIL KTDGEKGQNL VNNAINGLHS IQAVLSLTTT DKLGESEAGK QLFTALTEVV KESNQTGATA QKDVPADGIL YSVVFEKETN TIAIIGRKQP // ID Q9JXN0_NEIMB Unreviewed; 266 AA. AC Q9JXN0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 102. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF42295.1}; GN OrderedLocusNames=NMB1966 {ECO:0000313|EMBL:AAF42295.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42295.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42295.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42295.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42295.1; -; Genomic_DNA. DR PIR; G81022; G81022. DR RefSeq; NP_274960.1; NC_003112.2. DR RefSeq; WP_002221642.1; NC_003112.2. DR ProteinModelPortal; Q9JXN0; -. DR STRING; 122586.NMB1966; -. DR PaxDb; Q9JXN0; -. DR EnsemblBacteria; AAF42295; AAF42295; NMB1966. DR GeneID; 904178; -. DR KEGG; nme:NMB1966; -. DR PATRIC; 20359993; VBINeiMen85645_2501. DR eggNOG; ENOG4105DHJ; Bacteria. DR eggNOG; COG1127; LUCA. DR KO; K02065; -. DR OMA; IRSIVLM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-2023-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42295.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42295.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 7 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 266 AA; 29286 MW; 09E10BCD5B7DCEAF CRC64; MSPSPFIEMK DVAFAYGDRP ILKNINFSIP QGNFAAVMGG SGSGKTTLMR LITGQIRPQS GQVLIEGRDL AGFSADELYE HRRRMGVLFQ HGALFTDLSV FDNIAFPMRE LTRLPEAVIR DLVLLKLNAV GLRGVENLMP SELSGGMSRR VALARTIALD PEIMLYDEPF TGLDPISLGV IAHLISRVNK ALRSTSIMVT HDIEKSLEIV DQVIFLAHGE IMFSGSPQEM RELDSPWVRQ FVGGLADGPV AYRYPAQTSL QQDLLG // ID Q9JZH5_NEIMB Unreviewed; 489 AA. AC Q9JZH5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41446.1}; GN OrderedLocusNames=NMB1048 {ECO:0000313|EMBL:AAF41446.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41446.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41446.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41446.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41446.1; -; Genomic_DNA. DR PIR; H81127; H81127. DR RefSeq; NP_274082.1; NC_003112.2. DR RefSeq; WP_002217121.1; NC_003112.2. DR STRING; 122586.NMB1048; -. DR PaxDb; Q9JZH5; -. DR EnsemblBacteria; AAF41446; AAF41446; NMB1048. DR GeneID; 903185; -. DR KEGG; nme:NMB1048; -. DR PATRIC; 20357633; VBINeiMen85645_1333. DR eggNOG; ENOG4105ZE7; Bacteria. DR eggNOG; ENOG410XRKA; LUCA. DR HOGENOM; HOG000218127; -. DR OMA; AFVICLA; -. DR OrthoDB; EOG686ND3; -. DR BioCyc; NMEN122586:GHGG-1085-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021794; DUF3360. DR Pfam; PF11840; DUF3360; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 431 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 451 478 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 489 AA; 52589 MW; 23A26859DDE6A742 CRC64; MEKHNGTYRD LHRPASEFAT RDEYLEHELQ IMQPKRWRPN LPFRDYRFEW EDLIPAMAGT IGKVVMVGAV AAAFAAPLGL PDSFVLENVR YELLIAAAFI LLVSGFFLPG ANLPGTHGPL IPMIPIVVSA GGHPLAFGIS IAVLGLLMAL FRGGSIMAKL TSNGVCGGLL LYLGFIGTTG QVKKLFSWAG GFNMPYIAFT VIIVTIVMYA LLEHWKKRWL AVPLGCLIAG VVAFALGAPF EFHTAPGLPP MSPAYWWGEN SGWHLGLPTA ESFLVVFPFA VLAVAMWSPD FLGHQVFQKI SYPEKTDKVL MNIDDTMTSC SVRQAVGSIL GGANFTSSWG TYIVPASIAK RPIPGGAVLT AVLCIIAGLW GYPMDLAIWQ PVLSVALVVG VYLPLLEAGM EMTRKGKTTQ SAAIVVFSSA LVNPVFGWAL TMLLDNLGLI GCKERSAQLG FAGRVLIPAV GFLILCVAMG AVGMLPGIPP FLEHFKSLG // ID Q9JXX3_NEIMB Unreviewed; 91 AA. AC Q9JXX3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42184.1}; GN OrderedLocusNames=NMB1850 {ECO:0000313|EMBL:AAF42184.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42184.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42184.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42184.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42184.1; -; Genomic_DNA. DR PIR; G81034; G81034. DR STRING; 122586.NMB1850; -. DR PaxDb; Q9JXX3; -. DR EnsemblBacteria; AAF42184; AAF42184; NMB1850. DR BioCyc; NMEN122586:GHGG-1906-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 91 AA; 10171 MW; E0123F8AA1E57E30 CRC64; MPADRYATGN GFTGIIRTRH QTFKRHRSAH RRNGQNPIGL PARSRWQPAG NQQLLIFRRL MQNKKQPAQA VFLAASLTPT AAPSSLPVGK R // ID Q9JXM7_NEIMB Unreviewed; 1082 AA. AC Q9JXM7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Putative serotype-1-specific antigen {ECO:0000313|EMBL:AAF42298.1}; GN OrderedLocusNames=NMB1969 {ECO:0000313|EMBL:AAF42298.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42298.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42298.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42298.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42298.1; -; Genomic_DNA. DR PIR; H81020; H81020. DR RefSeq; NP_274963.1; NC_003112.2. DR RefSeq; WP_010981014.1; NC_003112.2. DR ProteinModelPortal; Q9JXM7; -. DR SMR; Q9JXM7; 784-1082. DR STRING; 122586.NMB1969; -. DR MEROPS; S08.160; -. DR PaxDb; Q9JXM7; -. DR EnsemblBacteria; AAF42298; AAF42298; NMB1969. DR GeneID; 904173; -. DR KEGG; nme:NMB1969; -. DR PATRIC; 20360003; VBINeiMen85645_2506. DR eggNOG; ENOG4107ZYM; Bacteria. DR eggNOG; COG1404; LUCA. DR HOGENOM; HOG000218741; -. DR KO; K12688; -. DR OMA; STGADEH; -. DR OrthoDB; EOG632D07; -. DR BioCyc; NMEN122586:GHGG-2026-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.40.128.130; -; 1. DR Gene3D; 3.40.50.200; -; 2. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR013425; Autotrns_rpt. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR023828; Peptidase_S8_Ser-AS. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF52743; SSF52743; 3. DR TIGRFAMs; TIGR02601; autotrns_rpt; 1. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 1082 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328301. FT DOMAIN 808 1082 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. SQ SEQUENCE 1082 AA; 113615 MW; 377E9C7177FAF056 CRC64; MRTTPTFPTK TFKPTAMALA VATTLSACLG GGGGGTSAPD FNAGGTGIGS NSRATTAKSA AVSYAGIKNE MCKDRSMLCA GRDDVAVTDR DAKINAPPPN LHTGDFPNPN DAYKNLINLK PAIEAGYTGR GVEVGIVDTG ESVGSISFPE LYGRKEHGYN ENYKNYTAYM RKEAPEDGGG KDIEASFDDE AVIETEAKPT DIRHVKEIGH IDLVSHIIGG RSVDGRPAGG IAPDATLHIM NTNDETKNEM MVAAIRNAWV KLGERGVRIV NNSFGTTSRA GTADLFQIAN SEEQYRQALL DYSGGDKTDE GIRLMQQSDY GNLSYHIRNK NMLFIFSTGN DAQAQPNTYA LLPFYEKDAQ KGIITVAGVD RSGEKFKREM YGEPGTEPLE YGSNHCGITA MWCLSAPYEA SVRFTRTNPI QIAGTSFSAP IVTGTAALLL QKYPWMSNDN LRTTLLTTAQ DIGAVGVDSK FGWGLLDAGK AMNGPASFPF GDFTADTKGT SDIAYSFRND ISGTGGLIKK GGSQLQLHGN NTYTGKTIIE GGSLVLYGNN KSDMRVETKG ALIYNGAASG GSLNSDGIVY LADTDQSGAN ETVHIKGSLQ LDGKGTLYTR LGKLLKVDGT AIIGGKLYMS ARGKGAGYLN STGRRVPFLS AAKIGQDYSF FTNIETDGGL LASLDSVEKT AGSEGDTLSY YVRRGNAART ASAAAHSAPA GLKHAVEQGG SNLENLMVEL DASESSATPE TVETAAADRT DMPGIRPYGA TFRAAAAVQH ANAADGVRIF NSLAATVYAD STAAHADMQG RRLKAVSDGL DHNGTGLRVI AQTQQDGGTW EQGGVEGKMR GSTQTVGIAA KTGENTTAAA TLGMGRSTWS ENSANAKTDS ISLFAGIRHD AGDIGYLKGL FSYGRYKNSI SRSTGADEHA EGSVNGTLMQ LGALGGVNVP FAATGDLTVE GGLRYDLLKQ DAFAEKGSAL GWSGNSLTEG TLVGLAGLKL SQPLSDKAVL FATAGVERDL NGRDYTVTGG FTGATAATGK TGARNMPHTR LVAGLGADVE FGNGWNGLAR YSYAGSKQYG NHSGRVGVGY RF // ID Q9JZS2_NEIMB Unreviewed; 319 AA. AC Q9JZS2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Putative IS1106 transposase {ECO:0000313|EMBL:AAF41327.1}; GN OrderedLocusNames=NMB0919 {ECO:0000313|EMBL:AAF41327.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41327.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41327.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41327.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41327.1; -; Genomic_DNA. DR PIR; A81143; A81143. DR RefSeq; NP_273959.1; NC_003112.2. DR RefSeq; WP_002225342.1; NC_003112.2. DR STRING; 122586.NMB0919; -. DR PaxDb; Q9JZS2; -. DR EnsemblBacteria; AAF41327; AAF41327; NMB0919. DR GeneID; 903040; -. DR KEGG; nme:NMB0919; -. DR PATRIC; 20357279; VBINeiMen85645_1153. DR eggNOG; ENOG4105F2I; Bacteria. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000218682; -. DR KO; K07481; -. DR OMA; RIQHRRN; -. DR OrthoDB; EOG69SK7X; -. DR BioCyc; NMEN122586:GHGG-957-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR002559; Transposase_11. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF01609; DDE_Tnp_1; 1. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 51 122 DUF772. {ECO:0000259|Pfam:PF05598}. FT DOMAIN 139 311 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 319 AA; 36943 MW; 0D8D065A2AC1F1BC CRC64; MSTFFQQTAQ AMIAKHIDRF PLLKLDQVID WQPIEQYLNR QKTRYLRDHR GRPACPLLSM FKAVLLGQWH NLSDPELEHS LITRIDFNLF CRFDELSIPD YSTLCRYRNR LAQDDTLSEL LELINRQLTE KGLKVEKASA AVVDATIIQT VGSKQRQAIE VDEEGQVSGQ TTLSKDKNAR WTKKNSLYKL GYKQHTRTDA EGYIEKLHIT PANAHECKHL SPLLEGLPEG TTIYADKGYD SAENRQHLEE HQLQDGIMRK ACRNRPLTET QTKRNRYLSK TRYVVEQSFG TLHRKFRYAR AAYFGLICAR CRLKGSPDA // ID Q9K145_NEIMB Unreviewed; 92 AA. AC Q9K145; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=BolA/YrbA family protein {ECO:0000313|EMBL:AAF40787.1}; GN OrderedLocusNames=NMB0344 {ECO:0000313|EMBL:AAF40787.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40787.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40787.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40787.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the BolA/IbaG family. CC {ECO:0000256|RuleBase:RU003860}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40787.1; -; Genomic_DNA. DR PIR; F81209; F81209. DR RefSeq; NP_273393.1; NC_003112.2. DR RefSeq; WP_002216424.1; NC_003112.2. DR ProteinModelPortal; Q9K145; -. DR STRING; 122586.NMB0344; -. DR PaxDb; Q9K145; -. DR EnsemblBacteria; AAF40787; AAF40787; NMB0344. DR GeneID; 902459; -. DR KEGG; nme:NMB0344; -. DR PATRIC; 20355835; VBINeiMen85645_0436. DR eggNOG; ENOG4108ABZ; Bacteria. DR eggNOG; COG0271; LUCA. DR HOGENOM; HOG000255169; -. DR KO; K05527; -. DR OMA; RHAGHKG; -. DR OrthoDB; EOG6VMTQ7; -. DR BioCyc; NMEN122586:GHGG-365-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002634; BolA. DR Pfam; PF01722; BolA; 1. DR PIRSF; PIRSF003113; BolA; 1. DR SUPFAM; SSF82657; SSF82657; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 92 AA; 10003 MW; FEDB6622396D0600 CRC64; MPAVDLIRER LQTLDPLVLE IGDESHLHKG HAGNTGGGHY AVLVVSGRFE GVSRLNRQKT VKSLLKDLFS GGMIHALGIR AATPDEYFHT AD // ID Q9JYU5_NEIMB Unreviewed; 59 AA. AC Q9JYU5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41788.1}; GN OrderedLocusNames=NMB1427 {ECO:0000313|EMBL:AAF41788.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41788.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41788.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41788.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41788.1; -; Genomic_DNA. DR PIR; D81084; D81084. DR RefSeq; NP_274439.1; NC_003112.2. DR RefSeq; WP_010980935.1; NC_003112.2. DR STRING; 122586.NMB1427; -. DR PaxDb; Q9JYU5; -. DR EnsemblBacteria; AAF41788; AAF41788; NMB1427. DR GeneID; 903849; -. DR KEGG; nme:NMB1427; -. DR BioCyc; NMEN122586:GHGG-1465-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 49 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 59 AA; 6844 MW; A163EF5C58406D82 CRC64; MENIVKFEHE VLIVCVGRYL DYVTIRVFIK ISLPGGILFL KTVGFGFVWG QSRPNWSNR // ID Q7DD60_NEIMB Unreviewed; 164 AA. AC Q7DD60; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42293.1}; GN OrderedLocusNames=NMB1964 {ECO:0000313|EMBL:AAF42293.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42293.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42293.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42293.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42293.1; -; Genomic_DNA. DR PIR; E81022; E81022. DR RefSeq; NP_274958.1; NC_003112.2. DR RefSeq; WP_002219881.1; NC_003112.2. DR STRING; 122586.NMB1964; -. DR PaxDb; Q7DD60; -. DR EnsemblBacteria; AAF42293; AAF42293; NMB1964. DR GeneID; 904185; -. DR KEGG; nme:NMB1964; -. DR PATRIC; 20359989; VBINeiMen85645_2499. DR eggNOG; ENOG4107PE3; Bacteria. DR eggNOG; COG1463; LUCA. DR HOGENOM; HOG000255143; -. DR KO; K02067; -. DR OMA; EQYIGLE; -. DR OrthoDB; EOG6F296G; -. DR BioCyc; NMEN122586:GHGG-2021-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro. DR InterPro; IPR030970; ABC_MlaD. DR InterPro; IPR003399; Mce/MlaD. DR Pfam; PF02470; MlaD; 1. DR TIGRFAMs; TIGR04430; OM_asym_MlaD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 40 117 MlaD. {ECO:0000259|Pfam:PF02470}. SQ SEQUENCE 164 AA; 16962 MW; 69E1CEB671874180 CRC64; MKKNILEFWV GLFVLIGAAA VAFLAFRVAG GAAFGGSDKT YAVYADFGDI GGLKVNAPVK SAGVLVGRVG AIGLDPKSYQ ARVRLDLDGK YQFSSDVSAQ ILTSGLLGEQ YIGLQQGGDT ENLAAGDTIS VTSSAMVLEN LIGKFMTSFA EKNADGGNAE KAAE // ID Q9JZT9_NEIMB Unreviewed; 63 AA. AC Q9JZT9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41310.1}; GN OrderedLocusNames=NMB0902 {ECO:0000313|EMBL:AAF41310.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41310.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41310.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41310.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41310.1; -; Genomic_DNA. DR PIR; C81144; C81144. DR RefSeq; NP_273942.1; NC_003112.2. DR RefSeq; WP_002219435.1; NC_003112.2. DR STRING; 122586.NMB0902; -. DR PaxDb; Q9JZT9; -. DR EnsemblBacteria; AAF41310; AAF41310; NMB0902. DR GeneID; 903023; -. DR KEGG; nme:NMB0902; -. DR PATRIC; 20357239; VBINeiMen85645_1133. DR OrthoDB; EOG61CKX9; -. DR BioCyc; NMEN122586:GHGG-940-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 63 AA; 7005 MW; DC638B4FBE9C26B9 CRC64; MNTNQDTIPF GGNLVICCST GNGGDGRFSC LITDQIPDLN LVRSGQAFPM FIYEYETREK RKA // ID Q9JZK9_NEIMB Unreviewed; 123 AA. AC Q9JZK9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAF41408.1}; GN OrderedLocusNames=NMB1007 {ECO:0000313|EMBL:AAF41408.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41408.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41408.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41408.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41408.1; -; Genomic_DNA. DR PIR; H81130; H81130. DR RefSeq; NP_274042.1; NC_003112.2. DR RefSeq; WP_002222575.1; NC_003112.2. DR ProteinModelPortal; Q9JZK9; -. DR STRING; 122586.NMB1007; -. DR PaxDb; Q9JZK9; -. DR EnsemblBacteria; AAF41408; AAF41408; NMB1007. DR GeneID; 903144; -. DR KEGG; nme:NMB1007; -. DR PATRIC; 20357545; VBINeiMen85645_1289. DR eggNOG; ENOG410879R; Bacteria. DR eggNOG; COG1396; LUCA. DR HOGENOM; HOG000218923; -. DR OMA; KWERGEN; -. DR OrthoDB; EOG62G5W2; -. DR BioCyc; NMEN122586:GHGG-1044-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF12844; HTH_19; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 64 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 123 AA; 13917 MW; F4DC18D50F60D6CA CRC64; MNNSSFFGNR LKEERKKLKM TQAEIAEKCG VSGRMWGDYE RGISQPKAEL FFQFEKVGID VQYVMHGRRG ETAVMPSETL NAEEQELLVL FREAAAADRE MILMVARRAE KKAQTALGKV SNG // ID Q9JY38_NEIMB Unreviewed; 168 AA. AC Q9JY38; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42101.1}; GN OrderedLocusNames=NMB1760 {ECO:0000313|EMBL:AAF42101.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42101.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42101.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42101.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42101.1; -; Genomic_DNA. DR PIR; G81046; G81046. DR RefSeq; NP_274760.1; NC_003112.2. DR RefSeq; WP_002222956.1; NC_003112.2. DR STRING; 122586.NMB1760; -. DR PaxDb; Q9JY38; -. DR EnsemblBacteria; AAF42101; AAF42101; NMB1760. DR GeneID; 903338; -. DR KEGG; nme:NMB1760; -. DR eggNOG; ENOG4108ZSQ; Bacteria. DR eggNOG; ENOG4111NRC; LUCA. DR HOGENOM; HOG000077348; -. DR OMA; EVMLDEW; -. DR OrthoDB; EOG6TTVP4; -. DR BioCyc; NMEN122586:GHGG-1815-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 168 AA; 19472 MW; 845094F76ABE7D01 CRC64; METTFALLNF KESLCYIYPP TEPVRYVSSI VALNVHSPNG TGDWHSAKAL SDRAYPEKFY IYGENQERNT NHLFGDNGII DGTDRLNKMG YFPENIPVWL ADHPRACVDY LYTAVLQTGS IGRVILDDWF PSDEDKQSVY DLLNQIEPHL NTQEWENLQL WKRKNPIM // ID Q9K0Q1_NEIMB Unreviewed; 137 AA. AC Q9K0Q1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40963.1}; GN OrderedLocusNames=NMB0534 {ECO:0000313|EMBL:AAF40963.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40963.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40963.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40963.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40963.1; -; Genomic_DNA. DR PIR; E81187; E81187. DR RefSeq; NP_273579.1; NC_003112.2. DR RefSeq; WP_002225588.1; NC_003112.2. DR STRING; 122586.NMB0534; -. DR PaxDb; Q9K0Q1; -. DR EnsemblBacteria; AAF40963; AAF40963; NMB0534. DR GeneID; 902649; -. DR KEGG; nme:NMB0534; -. DR PATRIC; 20356321; VBINeiMen85645_0679. DR eggNOG; ENOG4105W39; Bacteria. DR eggNOG; COG1238; LUCA. DR HOGENOM; HOG000183101; -. DR OMA; RYAAVAW; -. DR OrthoDB; EOG6VF37Q; -. DR BioCyc; NMEN122586:GHGG-560-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032818; DedA. DR PANTHER; PTHR30353; PTHR30353; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 132 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 137 AA; 15115 MW; 46998FFDEB1A4729 CRC64; MIPSYTYAAL AFSAFTSATL LPGTSEAAFA LFVHRFPEHA YGALLCAGLA NGLGSMVSYW MGRLLPSRKM PSEKTLNLMR RFGIWLLAFT WLPVVGDALP LAAGWLRLNP WTSGLMLVIG KTARYAFILW GMQYYAA // ID Q9K156_NEIMB Unreviewed; 34 AA. AC Q9K156; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40772.1}; GN OrderedLocusNames=NMB0328 {ECO:0000313|EMBL:AAF40772.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40772.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40772.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40772.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40772.1; -; Genomic_DNA. DR PIR; B81213; B81213. DR RefSeq; NP_273377.1; NC_003112.2. DR RefSeq; WP_010980779.1; NC_003112.2. DR STRING; 122586.NMB0328; -. DR PaxDb; Q9K156; -. DR EnsemblBacteria; AAF40772; AAF40772; NMB0328. DR GeneID; 902444; -. DR KEGG; nme:NMB0328; -. DR BioCyc; NMEN122586:GHGG-349-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 3866 MW; B7E6D4683ED97471 CRC64; MLREVSDIRP FSVGGLFCHL KTFSSCLKNR PLGR // ID Q7DDR3_NEIMB Unreviewed; 324 AA. AC Q7DDR3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 69. DE SubName: Full=Octaprenyl-diphosphate synthase {ECO:0000313|EMBL:AAF40771.1}; GN Name=ispB {ECO:0000313|EMBL:AAF40771.1}; GN OrderedLocusNames=NMB0326 {ECO:0000313|EMBL:AAF40771.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40771.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40771.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40771.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000256|RuleBase:RU004466}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40771.1; -; Genomic_DNA. DR PIR; A81213; A81213. DR RefSeq; NP_273375.1; NC_003112.2. DR RefSeq; WP_002216396.1; NC_003112.2. DR ProteinModelPortal; Q7DDR3; -. DR STRING; 122586.NMB0326; -. DR PaxDb; Q7DDR3; -. DR EnsemblBacteria; AAF40771; AAF40771; NMB0326. DR GeneID; 902442; -. DR KEGG; nme:NMB0326; -. DR PATRIC; 20355789; VBINeiMen85645_0414. DR eggNOG; ENOG4105EAH; Bacteria. DR eggNOG; COG0142; LUCA. DR HOGENOM; HOG000009102; -. DR KO; K02523; -. DR OMA; NIYITIN; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; NMEN122586:GHGG-346-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU004466}. SQ SEQUENCE 324 AA; 35537 MW; BA21DBCF6DF244CE CRC64; MLENLPYFQR HLPEDLAKVN EVINRAVQSD VALISQIGTY IISAGGKRLR PIMTILAGKA VGYDDEKLYS LAAMVEFIHT STLLHDDVVD ESDLRRGRAT ANNLFGNAAA VLVGDFLYTR AFQLMVASGS MRVLEVMADA TNIIAEGEVM QLMNIGNTDI TEEQYIQVIQ YKTAKLFEAA AQVGAILGKA SPEHERALKD YGMYVGTAFQ IIDDVLDYSG ETEETGKNVG DDLAEGKPTL PLIYLMRQGS EQVANDVRTA LENADRSYFE KIHDYVVRSD ALAYSIGEAR KAVDCAVTAL DALPDSEVKD AMIQLAKESL VRVS // ID Q9JZX1_NEIMB Unreviewed; 96 AA. AC Q9JZX1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41275.1}; GN OrderedLocusNames=NMB0864 {ECO:0000313|EMBL:AAF41275.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41275.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41275.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41275.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41275.1; -; Genomic_DNA. DR PIR; H81147; H81147. DR RefSeq; NP_273905.1; NC_003112.2. DR RefSeq; WP_002220650.1; NC_003112.2. DR STRING; 122586.NMB0864; -. DR PaxDb; Q9JZX1; -. DR EnsemblBacteria; AAF41275; AAF41275; NMB0864. DR GeneID; 902978; -. DR KEGG; nme:NMB0864; -. DR PATRIC; 20357119; VBINeiMen85645_1078. DR HOGENOM; HOG000218882; -. DR OMA; RDIKVPF; -. DR OrthoDB; EOG6JDWFH; -. DR BioCyc; NMEN122586:GHGG-895-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 85 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 96 AA; 11062 MW; 0C5BCBF21226347B CRC64; MDDLILYFLS GIFGNQVAEY IIKNNREIKV PFIVLYAIFF TLIYTVALLF LSLIYWVNGA EIAWKGIGIF SMSVSFCIVF CLYLIDKAGR CKDKKQ // ID Q7DDP8_NEIMB Unreviewed; 214 AA. AC Q7DDP8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40915.1}; GN OrderedLocusNames=NMB0478 {ECO:0000313|EMBL:AAF40915.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40915.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40915.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40915.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40915.1; -; Genomic_DNA. DR PIR; A81195; A81195. DR RefSeq; NP_273525.1; NC_003112.2. DR RefSeq; WP_002212574.1; NC_003112.2. DR STRING; 122586.NMB0478; -. DR PaxDb; Q7DDP8; -. DR EnsemblBacteria; AAF40915; AAF40915; NMB0478. DR GeneID; 902594; -. DR KEGG; nme:NMB0478; -. DR PATRIC; 20356208; VBINeiMen85645_0625. DR eggNOG; ENOG4111T2P; LUCA. DR HOGENOM; HOG000219084; -. DR OMA; LELIFRM; -. DR OrthoDB; EOG6GR381; -. DR BioCyc; NMEN122586:GHGG-502-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 214 AA; 23630 MW; 9B90852D0E350F9C CRC64; MESTLSLQAN LYPRLTPAGA FYAVSSDAPS AGKTLLHSLL KADADEMVSS EKLLTWADTA DIDTALNLLY RLQKLEFLYG DENGHSDGIN LSDEQLPLLM EQLSGSGKAL LVDRNGLYLA NANFHHEAAE ELGLLAAEVA QMEKKYRLLI KNNLYINNNA WGVCDPSGQS ELTFFPLYIG STKFILVIGG IPDLGKEAFV TLVRILYRRY SNRV // ID Q9JZB9_NEIMB Unreviewed; 68 AA. AC Q9JZB9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41517.1}; GN OrderedLocusNames=NMB1129 {ECO:0000313|EMBL:AAF41517.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41517.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41517.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41517.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41517.1; -; Genomic_DNA. DR PIR; H81117; H81117. DR STRING; 122586.NMB1129; -. DR PaxDb; Q9JZB9; -. DR EnsemblBacteria; AAF41517; AAF41517; NMB1129. DR HOGENOM; HOG000220732; -. DR OrthoDB; EOG6C2WK9; -. DR BioCyc; NMEN122586:GHGG-1165-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 64 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 8458 MW; 2EDB73D983208AAC CRC64; MKAVRDIALW LAVTVWINFF PDSYRYDTVP QGRYGYWHAD HPWYPYARFL LPLFLACILF YRHFRKRK // ID Q9JZA7_NEIMB Unreviewed; 120 AA. AC Q9JZA7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Putative lipoprotein {ECO:0000313|EMBL:AAF41595.1}; GN OrderedLocusNames=NMB1213 {ECO:0000313|EMBL:AAF41595.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41595.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41595.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41595.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41595.1; -; Genomic_DNA. DR PIR; A81109; A81109. DR RefSeq; NP_274238.1; NC_003112.2. DR RefSeq; WP_002242618.1; NC_003112.2. DR STRING; 122586.NMB1213; -. DR PaxDb; Q9JZA7; -. DR EnsemblBacteria; AAF41595; AAF41595; NMB1213. DR GeneID; 903635; -. DR KEGG; nme:NMB1213; -. DR eggNOG; ENOG4107CEW; Bacteria. DR eggNOG; ENOG410ZBYK; LUCA. DR HOGENOM; HOG000152757; -. DR OrthoDB; EOG6SFPF4; -. DR BioCyc; NMEN122586:GHGG-1250-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoprotein {ECO:0000313|EMBL:AAF41595.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 120 AA; 13706 MW; E26952F36E5D19F2 CRC64; MKYIVSISLA MGLAACSFGG FKPPPDDSAF WRLTNYAKLY PGLTSATLDQ YPPEERRRQL HDSFAREKKD WKECGYDPIG GGGGSEADAC MRKRGWYRVG NDIYPENKKY EWPREEGKTK // ID Q9JYX9_NEIMB Unreviewed; 128 AA. AC Q9JYX9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU {ECO:0000256|RuleBase:RU362089}; GN OrderedLocusNames=NMB1380 {ECO:0000313|EMBL:AAF62330.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62330.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62330.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62330.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters. It is CC likely that Fe-S cluster coordination is flexible as the role of CC this complex is to build and then hand off Fe-S clusters. CC {ECO:0000256|RuleBase:RU362089}. CC -!- SIMILARITY: Belongs to the NifU family. CC {ECO:0000256|RuleBase:RU362089}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62330.1; -; Genomic_DNA. DR RefSeq; NP_274396.1; NC_003112.2. DR RefSeq; WP_002225139.1; NC_003112.2. DR ProteinModelPortal; Q9JYX9; -. DR SMR; Q9JYX9; 1-125. DR STRING; 122586.NMB1380; -. DR PaxDb; Q9JYX9; -. DR EnsemblBacteria; AAF62330; AAF62330; NMB1380. DR GeneID; 903802; -. DR KEGG; nme:NMB1380; -. DR PATRIC; 20358439; VBINeiMen85645_1731. DR eggNOG; ENOG4107XTC; Bacteria. DR eggNOG; COG0822; LUCA. DR HOGENOM; HOG000069228; -. DR KO; K04488; -. DR OMA; VMDHFTN; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; NMEN122586:GHGG-1418-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU. DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N. DR Pfam; PF01592; NifU_N; 1. DR TIGRFAMs; TIGR01999; iscU; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 126 NifU_N. {ECO:0000259|Pfam:PF01592}. SQ SEQUENCE 128 AA; 13876 MW; 757DBC6FB499F5A1 CRC64; MAYSDKVIDH YENPRNVGTF DKGDDSVGTG MVGAPACGDV MRLQIKVNDE GIIEDAKFKT YGCGSAIASS SLITEWVKGK SLDDALAIKN SEIAEELELP PVKIHCSILA EDAVKAAVAD YRKRQENR // ID Q9JZF2_NEIMB Unreviewed; 66 AA. AC Q9JZF2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41474.1}; GN OrderedLocusNames=NMB1082 {ECO:0000313|EMBL:AAF41474.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41474.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41474.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41474.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41474.1; -; Genomic_DNA. DR PIR; B81125; B81125. DR STRING; 122586.NMB1082; -. DR PaxDb; Q9JZF2; -. DR EnsemblBacteria; AAF41474; AAF41474; NMB1082. DR OMA; LEGNCEP; -. DR OrthoDB; EOG6QZN1P; -. DR BioCyc; NMEN122586:GHGG-1118-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 66 AA; 7195 MW; 8A528FC7D201E50D CRC64; MMDKQQNAAF SAELVEKLKL KRALGRIQRA QAKIQGVPAE RNQAQTFLPA LEGNCEPAQS KSALDG // ID Q9JY63_NEIMB Unreviewed; 522 AA. AC Q9JY63; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Efflux pump component MtrF {ECO:0000313|EMBL:AAF62337.1}; GN Name=mtrF {ECO:0000313|EMBL:AAF62337.1}; GN OrderedLocusNames=NMB1719 {ECO:0000313|EMBL:AAF62337.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62337.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62337.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62337.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62337.1; -; Genomic_DNA. DR RefSeq; NP_274722.1; NC_003112.2. DR RefSeq; WP_002224966.1; NC_003112.2. DR STRING; 122586.NMB1719; -. DR PaxDb; Q9JY63; -. DR EnsemblBacteria; AAF62337; AAF62337; NMB1719. DR GeneID; 903382; -. DR KEGG; nme:NMB1719; -. DR PATRIC; 20359399; VBINeiMen85645_2205. DR eggNOG; ENOG4105CFC; Bacteria. DR eggNOG; COG2978; LUCA. DR HOGENOM; HOG000285565; -. DR KO; K12942; -. DR OMA; KNDRDVI; -. DR OrthoDB; EOG63586P; -. DR BioCyc; NMEN122586:GHGG-1774-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015558; F:p-aminobenzoyl-glutamate uptake transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR004697; AbgT. DR InterPro; IPR011540; AbgT_Proteobac. DR PANTHER; PTHR30282:SF0; PTHR30282:SF0; 1. DR Pfam; PF03806; ABG_transport; 1. DR TIGRFAMs; TIGR00819; ydaH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 237 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 272 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 373 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 413 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 420 438 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 450 470 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 490 512 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 522 AA; 56241 MW; 41CCE4AC20E190D1 CRC64; MSQTDTQRDG RFLRTVEWLG NMLPHPVTLF IIFIVLLLIA SAVGAYFGLS VPDPRPVGAK GRADDGLIYI VSLLNADGFI KILTHTVKNF TGFAPLGTVL VSLLGVGIAE KSGLISALMR LLLTKSPRKL TTFMVVFTGI LSNTASELGY VVLIPLSAII FHSLGRHPLA GLAAAFAGVS GGYSANLFLG TIDPLLAGIT QQAAQIIHPD YVVGPEANWF FMVASTFVIA LIGYFVTEKI VEPQLGPYQS DLSQEEKDIR HSNEITPLEY KGLIWAGVVF VALSALLAWS IVPADGILRH PETGLVSGSP FLKSIVVFIF LLFALPGIVY GRVTRSLRGE QEVVNAMAES MSTLGLYLVI IFFAAQFVAF FNWTNIGQYI AVKGATFLKE VGLGGSVLFI GFILICAFIN LMIGSASAQW AVTAPIFVPM LMLAGYAPEV IQAAYRIGDS VTNIITPMMS YFGLIMATVI KYKKDAGVGT LISMMLPYSA FFLIAWIALF CIWVFVLGLP VGPGAPTFYP AP // ID Q9JZV8_NEIMB Unreviewed; 278 AA. AC Q9JZV8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Sulfate ABC transporter, permease protein {ECO:0000313|EMBL:AAF41292.1}; GN Name=cysT {ECO:0000313|EMBL:AAF41292.1}; GN OrderedLocusNames=NMB0881 {ECO:0000313|EMBL:AAF41292.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41292.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41292.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41292.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41292.1; -; Genomic_DNA. DR PIR; D81147; D81147. DR RefSeq; NP_273922.1; NC_003112.2. DR RefSeq; WP_002225366.1; NC_003112.2. DR ProteinModelPortal; Q9JZV8; -. DR STRING; 122586.NMB0881; -. DR PaxDb; Q9JZV8; -. DR EnsemblBacteria; AAF41292; AAF41292; NMB0881. DR GeneID; 903000; -. DR KEGG; nme:NMB0881; -. DR PATRIC; 20357167; VBINeiMen85645_1097. DR eggNOG; ENOG4108I5D; Bacteria. DR eggNOG; COG0555; LUCA. DR HOGENOM; HOG000263698; -. DR KO; K02046; -. DR OMA; AYCLGAN; -. DR OrthoDB; EOG654P2T; -. DR BioCyc; NMEN122586:GHGG-917-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015419; F:sulfate transmembrane-transporting ATPase activity; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR011865; CysT_permease. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005667; Sulph_transpt2. DR PANTHER; PTHR30406:SF6; PTHR30406:SF6; 1. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR00969; 3a0106s02; 1. DR TIGRFAMs; TIGR02139; permease_CysT; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00524216, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00524216, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00524216, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 270 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 60 263 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 278 AA; 29778 MW; 70C89F5DD8D97981 CRC64; MLALKTPGVL PGFKLSLGLT VLCLSLLVVL PFAMMAAKAA EIGWGGFWNT IAEPNVLAAV WLSLRMSFYA MLTNVVFGTL VAWVLVRYEF PGKGLANALV DLPFALPTAV TGIALATLYA PNGWIGRFFE PLGIKIAFTP VGIWIALVVV SLPFIVRAVQ PVLEELSGEY EEAAATLGAS RWTTFRRVLL PEITPALLTG AGMMFARATG EYGSVIFIAG NIPMVSEILP LIITGKLEQF DVQGASAVAL FMLLVSFVIL FALNVMQWAL GRRSGAKG // ID Q7DDP9_NEIMB Unreviewed; 178 AA. AC Q7DDP9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40914.1}; GN OrderedLocusNames=NMB0477 {ECO:0000313|EMBL:AAF40914.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40914.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40914.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40914.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40914.1; -; Genomic_DNA. DR PIR; H81194; H81194. DR RefSeq; NP_273524.1; NC_003112.2. DR RefSeq; WP_002212573.1; NC_003112.2. DR ProteinModelPortal; Q7DDP9; -. DR STRING; 122586.NMB0477; -. DR PaxDb; Q7DDP9; -. DR EnsemblBacteria; AAF40914; AAF40914; NMB0477. DR GeneID; 902593; -. DR KEGG; nme:NMB0477; -. DR PATRIC; 20356206; VBINeiMen85645_0624. DR eggNOG; ENOG4108RCI; Bacteria. DR eggNOG; COG2229; LUCA. DR HOGENOM; HOG000021469; -. DR KO; K06945; -. DR OMA; KIIARGM; -. DR OrthoDB; EOG6RC3QJ; -. DR BioCyc; NMEN122586:GHGG-501-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004130; Gpn. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03029; ATP_bind_1; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 178 AA; 19771 MW; 7FABA4A1E59915EB CRC64; MRENKIIFTG PVGVGKTTAI AAISDEALVQ TDASASDMTL DRKRNTTVAM DYGAISLDED TKVHLYGTPG QERFNFMWEI LSQGSMGLVL LLDNARTNPL KDLEFFLHSF RGLLEKAPVV VGITKMDIRS QPGIDVYHKY LAKHNLNVPV FEIDARKEDD VKQLVSAMLF SIDPGLEV // ID Q9JYN3_NEIMB Unreviewed; 258 AA. AC Q9JYN3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=HesA/MoeB/ThiF family protein {ECO:0000313|EMBL:AAF41857.1}; GN OrderedLocusNames=NMB1501 {ECO:0000313|EMBL:AAF41857.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41857.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41857.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41857.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41857.1; -; Genomic_DNA. DR PIR; A81077; A81077. DR RefSeq; NP_274509.1; NC_003112.2. DR RefSeq; WP_002225075.1; NC_003112.2. DR ProteinModelPortal; Q9JYN3; -. DR STRING; 122586.NMB1501; -. DR PaxDb; Q9JYN3; -. DR DNASU; 903934; -. DR EnsemblBacteria; AAF41857; AAF41857; NMB1501. DR GeneID; 903934; -. DR KEGG; nme:NMB1501; -. DR PATRIC; 20358786; VBINeiMen85645_1903. DR eggNOG; ENOG4105CUZ; Bacteria. DR eggNOG; COG1179; LUCA. DR HOGENOM; HOG000263839; -. DR OMA; DMDDICV; -. DR OrthoDB; EOG628F8J; -. DR BioCyc; NMEN122586:GHGG-1541-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR Pfam; PF00899; ThiF; 1. DR SUPFAM; SSF69572; SSF69572; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 20 254 ThiF. {ECO:0000259|Pfam:PF00899}. SQ SEQUENCE 258 AA; 27853 MW; D5FA84391CAF8013 CRC64; MSDNALTSSR RFGGIARLYG DSALAHFSQA HVCVVGVGGV GSWAVEALAR TGIGRLTLID LDNVAESNVN RQLHALTGDF GKAKVTALRE RITQINPQCE VFEIEDFVTE DNLPEYFGKG FDFVIDAIDQ VRVKAAMAAY FVERKQPFVL SGGAGGQKNP ALIQTADLSR VTHDPLLANL RYTLRKRYGF SRDTKANMRV PCVYSTENIV PPQSREACSA DAAPQGLSCA GYGASMLVTA SFGLYCAQAA VEHIADKK // ID Q9K042_NEIMB Unreviewed; 146 AA. AC Q9K042; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41193.1}; GN OrderedLocusNames=NMB0780 {ECO:0000313|EMBL:AAF41193.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41193.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41193.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41193.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41193.1; -; Genomic_DNA. DR PIR; A81161; A81161. DR RefSeq; NP_273822.1; NC_003112.2. DR RefSeq; WP_002222725.1; NC_003112.2. DR STRING; 122586.NMB0780; -. DR PaxDb; Q9K042; -. DR EnsemblBacteria; AAF41193; AAF41193; NMB0780. DR GeneID; 902895; -. DR KEGG; nme:NMB0780; -. DR PATRIC; 20356937; VBINeiMen85645_0987. DR eggNOG; ENOG4106C4C; Bacteria. DR eggNOG; ENOG410Y3B1; LUCA. DR HOGENOM; HOG000081604; -. DR OMA; AWRECIR; -. DR OrthoDB; EOG65N1BP; -. DR BioCyc; NMEN122586:GHGG-811-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 146 AA; 16466 MW; B877F2A8B915D4EF CRC64; MGSSDSFKEK KEIFEIGTPA YRQKLIDVWK KSINGNEKSW VLFENGTCVI LLEPEKDLAK QAKEMLSKWG KVQIGTPSAD FGIITLDSGD GYAVSCHHPE IFTLILKEEG LDEDFKIGIE GRSHRDCDAE EPKVIHIEDK RTIETP // ID Q7DD99_NEIMB Unreviewed; 299 AA. AC Q7DD99; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41933.1}; GN OrderedLocusNames=NMB1580 {ECO:0000313|EMBL:AAF41933.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41933.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41933.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41933.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41933.1; -; Genomic_DNA. DR PIR; D81067; D81067. DR RefSeq; NP_274586.1; NC_003112.2. DR RefSeq; WP_002216786.1; NC_003112.2. DR STRING; 122586.NMB1580; -. DR PaxDb; Q7DD99; -. DR EnsemblBacteria; AAF41933; AAF41933; NMB1580. DR GeneID; 904219; -. DR KEGG; nme:NMB1580; -. DR PATRIC; 20359026; VBINeiMen85645_2031. DR eggNOG; ENOG41065WA; Bacteria. DR eggNOG; COG3680; LUCA. DR HOGENOM; HOG000219032; -. DR KO; K09968; -. DR OMA; RINEICS; -. DR OrthoDB; EOG6Z6FTR; -. DR BioCyc; NMEN122586:GHGG-1622-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR000305; GIY-YIG_SF. DR PROSITE; PS50164; GIY_YIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 21 115 GIY-YIG. {ECO:0000259|PROSITE:PS50164}. SQ SEQUENCE 299 AA; 33633 MW; 0160C089FE012BBB CRC64; MVAKIKKFSD STLSVLNNGE RRFYVYCLTD LKKDKILYIG KGCGNRIFEH EWVASRSQDP VSGEIIDRKL KAISKCKKLG RYIISYHLTE VEALAAESAL IHFVKSVLGK KLKNKIAGHG PGGISVEELD RRFGFSSLPL NEINPDGLIL AIKIHNAFDL DTDEELDYLF DNQDDANLKS RTLGNWVIGK DVASKVKYVI GVHTGLQNAV VSAYEVDGFE TMVEETKNGR KQSRYRFRTT SRSEEVLAKL GLQQKCLPEL KFGSGGEKAY IRPKTETETE QENIQTTPNP KIKKEKTKS // ID Q9JZ22_NEIMB Unreviewed; 120 AA. AC Q9JZ22; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41705.1}; GN OrderedLocusNames=NMB1330 {ECO:0000313|EMBL:AAF41705.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41705.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41705.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41705.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41705.1; -; Genomic_DNA. DR PIR; E81095; E81095. DR RefSeq; NP_274349.1; NC_003112.2. DR RefSeq; WP_002222360.1; NC_003112.2. DR PaxDb; Q9JZ22; -. DR EnsemblBacteria; AAF41705; AAF41705; NMB1330. DR GeneID; 903752; -. DR KEGG; nme:NMB1330; -. DR eggNOG; ENOG4106D90; Bacteria. DR eggNOG; ENOG410Y54V; LUCA. DR OrthoDB; EOG60394H; -. DR BioCyc; NMEN122586:GHGG-1368-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 120 AA; 14323 MW; 59A84B7DF048998F CRC64; MSQLDFNLEL FIKNSNFDDY KIFDIVKEAI ETQDEIGSIL RTHLFFERIL EAWIYAKCNK EDFFNDTQIG FRTKLKIARN LGLFSEVYDI GERLNKIRNT IAHHVLREVN QENLTLYMKV // ID Q7DDB7_NEIMB Unreviewed; 64 AA. AC Q7DDB7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41850.1}; GN OrderedLocusNames=NMB1494 {ECO:0000313|EMBL:AAF41850.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41850.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41850.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41850.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41850.1; -; Genomic_DNA. DR PIR; D81078; D81078. DR RefSeq; NP_274502.1; NC_003112.2. DR RefSeq; WP_002212918.1; NC_003112.2. DR STRING; 122586.NMB1494; -. DR PaxDb; Q7DDB7; -. DR EnsemblBacteria; AAF41850; AAF41850; NMB1494. DR GeneID; 903916; -. DR KEGG; nme:NMB1494; -. DR PATRIC; 20358754; VBINeiMen85645_1886. DR eggNOG; COG2879; LUCA. DR HOGENOM; HOG000239011; -. DR OrthoDB; EOG6M9F3Z; -. DR BioCyc; NMEN122586:GHGG-1534-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007423; DUF466. DR Pfam; PF04328; DUF466; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7428 MW; FAE66A7DF7F8BC60 CRC64; MKHKLASWWK TIKLTANLMA GVPDYENYVA QQRKHNPNAP VMTKLQFQDY CRKRRCGANG GRCC // ID Q9JYF5_NEIMB Unreviewed; 505 AA. AC Q9JYF5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAF41958.1}; GN OrderedLocusNames=NMB1606 {ECO:0000313|EMBL:AAF41958.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41958.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41958.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41958.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41958.1; -; Genomic_DNA. DR PIR; H81064; H81064. DR RefSeq; NP_274612.1; NC_003112.2. DR RefSeq; WP_002225015.1; NC_003112.2. DR ProteinModelPortal; Q9JYF5; -. DR STRING; 122586.NMB1606; -. DR PaxDb; Q9JYF5; -. DR EnsemblBacteria; AAF41958; AAF41958; NMB1606. DR GeneID; 904302; -. DR KEGG; nme:NMB1606; -. DR PATRIC; 20359092; VBINeiMen85645_2058. DR eggNOG; ENOG4107TUY; Bacteria. DR eggNOG; ENOG410XSGR; LUCA. DR HOGENOM; HOG000219043; -. DR OMA; FHTTKER; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NMEN122586:GHGG-1654-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR Pfam; PF00512; HisKA; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000313|EMBL:AAF41958.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41958.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 186 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 319 468 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 505 AA; 56085 MW; 97F13DCD75A748B6 CRC64; MVISNPRELE KLKDRIPNLI NIIRVAIVFP LMIMHILGLE TGSRANLHAS WTAWAFYVWL AIACWLIFFS IIHPHWQWQS LKMPRFSAVA DITMIGVLTY LFGGIDSGFG ILILPFVVCS CLLSYGRYPL LYSSYAAILL IFNAIADGDI GKYPLISDAR TASATFILVA ASYLSAIFTS LSVKYIDRAG KLAYDSHIAY HRIKGLSQTV LERVQEAVVV INAEGLAVLF NRKAKDLFPA LEIGRRAGLS DSAAELWDQA SPHTFEYVLG TPGLNAGIRA VPVNKGSDKL LILYIRPQSE IQAEALSVKL AALGQLTANL AHEIRNPMSA IRHANDLLRE NMEAGAADPF NAKLCKIIDG NICRIDKMLE DISSLNKRNK TERETIGLIP FWEEFKQEFL LGHPDAADCI RPDIQGGSPT AYFDPAHLRQ IMWNLANNAW RHSRKQPGSI SVTIRPAQKN TVCILFADRP KCRNTCSNPF TPRRKTAPAS GCMSPANWRT PISAI // ID Q9K103_NEIMB Unreviewed; 293 AA. AC Q9K103; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Nicotinate-nucleotide pyrophosphorylase {ECO:0000313|EMBL:AAF40836.1}; DE EC=2.4.2.19 {ECO:0000313|EMBL:AAF40836.1}; GN Name=nadC {ECO:0000313|EMBL:AAF40836.1}; GN OrderedLocusNames=NMB0396 {ECO:0000313|EMBL:AAF40836.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40836.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40836.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40836.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the NadC/ModD family. CC {ECO:0000256|PIRNR:PIRNR006250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40836.1; -; Genomic_DNA. DR PIR; D81204; D81204. DR RefSeq; NP_273445.1; NC_003112.2. DR RefSeq; WP_002218766.1; NC_003112.2. DR ProteinModelPortal; Q9K103; -. DR STRING; 122586.NMB0396; -. DR PaxDb; Q9K103; -. DR EnsemblBacteria; AAF40836; AAF40836; NMB0396. DR GeneID; 902511; -. DR KEGG; nme:NMB0396; -. DR PATRIC; 20355955; VBINeiMen85645_0495. DR eggNOG; ENOG4105D18; Bacteria. DR eggNOG; COG0157; LUCA. DR HOGENOM; HOG000224022; -. DR KO; K00767; -. DR OMA; LYDMIML; -. DR OrthoDB; EOG6KT2XH; -. DR BioCyc; NMEN122586:GHGG-418-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1170.20; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004393; NadC. DR InterPro; IPR027277; NadC/ModD. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N. DR Pfam; PF01729; QRPTase_C; 1. DR Pfam; PF02749; QRPTase_N; 1. DR PIRSF; PIRSF006250; NadC_ModD; 1. DR SUPFAM; SSF51690; SSF51690; 1. DR TIGRFAMs; TIGR00078; nadC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AAF40836.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AAF40836.1}. FT DOMAIN 29 117 QRPTase_N. {ECO:0000259|Pfam:PF02749}. FT DOMAIN 119 290 QRPTase_C. {ECO:0000259|Pfam:PF01729}. SQ SEQUENCE 293 AA; 31217 MW; 4936AF6372B49B92 CRC64; MPSEKTLFPL PDTLLRPIVE QALSEDLGRR GDITSAAVIA PDKTAKLFLV SREDGVIAGM DLARLAFQTM DPSVRFQAEI RDGQAVRAGQ TLAAVEGNAR ALLAAERTAL NYLTHLSGIA TATARAVAEV AEYGTDIVCS RKTIPLLRVL QKYAVRAGGG VNHRMGLDDA VLIKDNHLAY CGSIAQAVQQ AKQAVGALTC VEIEVDTLAQ LDEAIAAGAE RILLDNMDDE TLKEAANRCH TQTAHPHTIY CEASGGIGFD RLKRVAQTGV DGIALGYLTH SSRSLDIGLD FVA // ID Q9K1E0_NEIMB Unreviewed; 283 AA. AC Q9K1E0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Putative RNA polymerase sigma-54 factor RpoN {ECO:0000313|EMBL:AAF40673.1}; GN OrderedLocusNames=NMB0217 {ECO:0000313|EMBL:AAF40673.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40673.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40673.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40673.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40673.1; -; Genomic_DNA. DR PIR; E81224; E81224. DR RefSeq; NP_273274.1; NC_003112.2. DR RefSeq; WP_002224812.1; NC_003112.2. DR ProteinModelPortal; Q9K1E0; -. DR SMR; Q9K1E0; 240-271. DR STRING; 122586.NMB0217; -. DR PaxDb; Q9K1E0; -. DR EnsemblBacteria; AAF40673; AAF40673; NMB0217. DR GeneID; 902329; -. DR KEGG; nme:NMB0217; -. DR PATRIC; 20355504; VBINeiMen85645_0276. DR eggNOG; COG1508; LUCA. DR HOGENOM; HOG000218654; -. DR KO; K03092; -. DR OMA; DARFSHY; -. DR OrthoDB; EOG60CWN7; -. DR BioCyc; NMEN122586:GHGG-232-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR InterPro; IPR000394; RNA_pol_sigma_54. DR InterPro; IPR007046; RNA_pol_sigma_54_core-bd. DR InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd. DR Pfam; PF00309; Sigma54_AID; 1. DR Pfam; PF04963; Sigma54_CBD; 1. DR Pfam; PF04552; Sigma54_DBD; 1. DR PROSITE; PS00718; SIGMA54_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 79 240 Sigma54_CBD. {ECO:0000259|Pfam:PF04963}. FT DOMAIN 241 280 Sigma54_DBD. {ECO:0000259|Pfam:PF04552}. SQ SEQUENCE 283 AA; 31476 MW; 6083B8E65835A5C7 CRC64; MTLLGIKLKQ TQQLNQRLQQ SLRVLQMSGI ELEREVENWL SDNPLLERKD TDEFSDAEFS HYTAPARQIG GDEGEDMLSN IAGEQDFKQY LHAQVCEHPL SDQEAACVHI LIDFLDEQGY LTDSIEDILD HTPLEWMLDE AMLQHALTAL KKFDPAGVAA ADLNESLILQ IERLGECAAK PAALHIVRNA LDSIDGNRSQ TLARIKKHLP QTDSGTLEAA LDLIASLNPF PAAGFASSTP TPYSDEALAN LLAFRGMEVS RRTIAKYRES FEIPAAHKRK TAE // ID Q9JYR7_NEIMB Unreviewed; 461 AA. AC Q9JYR7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Drug resistance translocase family protein {ECO:0000313|EMBL:AAF41820.1}; GN OrderedLocusNames=NMB1461 {ECO:0000313|EMBL:AAF41820.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41820.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41820.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41820.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41820.1; -; Genomic_DNA. DR PIR; B81080; B81080. DR RefSeq; NP_274472.1; NC_003112.2. DR RefSeq; WP_002226238.1; NC_003112.2. DR ProteinModelPortal; Q9JYR7; -. DR STRING; 122586.NMB1461; -. DR PaxDb; Q9JYR7; -. DR EnsemblBacteria; AAF41820; AAF41820; NMB1461. DR GeneID; 903883; -. DR KEGG; nme:NMB1461; -. DR PATRIC; 20358669; VBINeiMen85645_1844. DR eggNOG; ENOG4107RDB; Bacteria. DR eggNOG; COG0477; LUCA. DR HOGENOM; HOG000264695; -. DR OMA; PPYVTSL; -. DR OrthoDB; EOG6T7N4X; -. DR BioCyc; NMEN122586:GHGG-1501-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 170 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 220 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 301 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 307 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 346 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 373 393 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 399 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 461 AA; 48822 MW; 3093432874688999 CRC64; MMARDNRIQM FPHEWRASTT LSGVYALRML GMFLVLPVLA VYAASLPGAE GNKTLVGLAM GIYGLTQALL QLPLGIASDK FGRKKTIYAG LVVFAAGSFL AAAADTLPML VAARAIQGAG AVSAAVTALL ADLTRDGVRT RAMAMIGLSI GLTFSVSLVV APVIADAVGV RGLFMLTGIL TVISIGVVAW MTPDPEVSKL HEDTQAQPSR IGEVLKNRRL LTLDFGIFAL HAAQMALFTA LPFAMTQLGL EKIQHWKVYL PSTITGLVVM VPLIIVGETR NKLKQVFVLG IVCIAAAQLG LLSGMRSVGL ITAYLVVYFI GFNVLEASLP SMVSKIAPSD LKGTAMGVYN TMQSLGLFAG GAAGGLLFQK YGFSGVFAFC SILMLLWLVI AVLSPAPKPV KNLSYPVGGV WQGNQEGLYR ALSELEGVED IGFSFDGQTV YLKVLQKGFD QAAAEKIITG V // ID Q9K0W9_NEIMB Unreviewed; 147 AA. AC Q9K0W9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40875.1}; GN OrderedLocusNames=NMB0437 {ECO:0000313|EMBL:AAF40875.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40875.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40875.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40875.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40875.1; -; Genomic_DNA. DR PIR; F81198; F81198. DR RefSeq; NP_273485.1; NC_003112.2. DR RefSeq; WP_002216546.1; NC_003112.2. DR ProteinModelPortal; Q9K0W9; -. DR STRING; 122586.NMB0437; -. DR PaxDb; Q9K0W9; -. DR EnsemblBacteria; AAF40875; AAF40875; NMB0437. DR GeneID; 902553; -. DR KEGG; nme:NMB0437; -. DR PATRIC; 20356078; VBINeiMen85645_0554. DR eggNOG; ENOG4105KPV; Bacteria. DR eggNOG; COG1959; LUCA. DR HOGENOM; HOG000249814; -. DR KO; K13771; -. DR OMA; GCEDDPP; -. DR OrthoDB; EOG6BGP3D; -. DR BioCyc; NMEN122586:GHGG-461-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR00738; rrf2_super; 1. DR PROSITE; PS51197; HTH_RRF2_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 147 AA; 16141 MW; ADEA81E2AE9BAEDC CRC64; MYLTQHTDYG LRVLIYTAIN DDALVNISTI AVTYGISKSH LMKVVTALVK GGFLHSVRGK GGGLRLAAPP DRINIGSVVR HLEPMQLVEC MGENNECLIT PSCRLTGILG GAMKSFFTYL DGFTLQDLLN KPTYDLLYEP RIPIAVQ // ID Q9JZH6_NEIMB Unreviewed; 123 AA. AC Q9JZH6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41445.1}; GN OrderedLocusNames=NMB1047 {ECO:0000313|EMBL:AAF41445.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41445.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41445.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41445.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41445.1; -; Genomic_DNA. DR PIR; G81127; G81127. DR RefSeq; NP_274081.1; NC_003112.2. DR RefSeq; WP_002217120.1; NC_003112.2. DR STRING; 122586.NMB1047; -. DR PaxDb; Q9JZH6; -. DR EnsemblBacteria; AAF41445; AAF41445; NMB1047. DR GeneID; 903184; -. DR KEGG; nme:NMB1047; -. DR PATRIC; 20357631; VBINeiMen85645_1332. DR HOGENOM; HOG000218973; -. DR OMA; GCVSEQA; -. DR OrthoDB; EOG60W7XD; -. DR BioCyc; NMEN122586:GHGG-1084-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 123 AA; 12937 MW; 4CFF2B6F4BF761A5 CRC64; MNKTLSILPV AILLGGCAAG GGNTFGSLDG GTGMGGSIVK MAVGSQCRAE LDKRSEWRLT ALAMSAEKQA EWENKICACV AQEAPERMTG NDVMQMLAPS TRNQALAALT AKTVSACFKH LYR // ID Q9JYT5_NEIMB Unreviewed; 161 AA. AC Q9JYT5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929}; DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929}; DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929}; GN Name=purE {ECO:0000256|HAMAP-Rule:MF_01929, GN ECO:0000313|EMBL:AAF41800.1}; GN OrderedLocusNames=NMB1439 {ECO:0000313|EMBL:AAF41800.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41800.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41800.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41800.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole CC ribonucleotide (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929}. CC -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxylate. {ECO:0000256|HAMAP-Rule:MF_01929}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. CC {ECO:0000256|HAMAP-Rule:MF_01929}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01929}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41800.1; -; Genomic_DNA. DR PIR; G81083; G81083. DR RefSeq; NP_274451.1; NC_003112.2. DR RefSeq; WP_002222288.1; NC_003112.2. DR ProteinModelPortal; Q9JYT5; -. DR SMR; Q9JYT5; 4-133. DR STRING; 122586.NMB1439; -. DR PaxDb; Q9JYT5; -. DR EnsemblBacteria; AAF41800; AAF41800; NMB1439. DR GeneID; 903860; -. DR KEGG; nme:NMB1439; -. DR PATRIC; 20358591; VBINeiMen85645_1807. DR eggNOG; ENOG4108UM6; Bacteria. DR eggNOG; COG0041; LUCA. DR HOGENOM; HOG000034140; -. DR KO; K01588; -. DR OMA; SDWATMR; -. DR OrthoDB; EOG6Z0QH2; -. DR BioCyc; NMEN122586:GHGG-1477-MONOMER; -. DR UniPathway; UPA00074; UER00943. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.7700; -; 1. DR HAMAP; MF_01929; PurE_classI; 1. DR InterPro; IPR024694; N5-CAIR_mutase_PurE. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR PIRSF; PIRSF001338; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. DR TIGRFAMs; TIGR01162; purE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01929}; KW Lyase {ECO:0000313|EMBL:AAF41800.1}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 153 AIRC. {ECO:0000259|SMART:SM01001}. FT BINDING 10 10 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1}. FT BINDING 13 13 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1}. FT BINDING 40 40 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01929, FT ECO:0000256|PIRSR:PIRSR001338-1}. SQ SEQUENCE 161 AA; 17124 MW; 69606CC05E0EF058 CRC64; MIQIGIIMGS NSDWPVMRQA AQFLEEFGVE YEARVVSAHR TPDLMFQYAE TARARGIKAI IAGAGGAAHL PGMVAAKTTV PVLGVPVPSK YLRGEDSLLS IVQMPKGVPV ATFAIGEAGA ANAALFAVSM LANETPELAQ KLADFRAKQE QAVLNMELEQ I // ID Q9K115_NEIMB Unreviewed; 75 AA. AC Q9K115; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40823.1}; GN OrderedLocusNames=NMB0383 {ECO:0000313|EMBL:AAF40823.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40823.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40823.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40823.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40823.1; -; Genomic_DNA. DR PIR; D81205; D81205. DR STRING; 122586.NMB0383; -. DR PaxDb; Q9K115; -. DR EnsemblBacteria; AAF40823; AAF40823; NMB0383. DR BioCyc; NMEN122586:GHGG-405-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 75 AA; 8764 MW; E0C911A187DC16C5 CRC64; MHEVSGFCTR YCCNIRETSV GIDDVKQTPA FAGFVFLGGF LKRLSSESGC RFGFGFRFRF RFRFRFRFVS HCRAL // ID Q9JXT7_NEIMB Unreviewed; 30 AA. AC Q9JXT7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42223.1}; GN OrderedLocusNames=NMB1889 {ECO:0000313|EMBL:AAF42223.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42223.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42223.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42223.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42223.1; -; Genomic_DNA. DR PIR; G81031; G81031. DR RefSeq; NP_274885.1; NC_003112.2. DR RefSeq; WP_010981003.1; NC_003112.2. DR STRING; 122586.NMB1889; -. DR PaxDb; Q9JXT7; -. DR EnsemblBacteria; AAF42223; AAF42223; NMB1889. DR GeneID; 904288; -. DR KEGG; nme:NMB1889; -. DR BioCyc; NMEN122586:GHGG-1946-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 30 AA; 3385 MW; ADCD826284F107B2 CRC64; MAVKPLGYIR GIGRQRNALK TQFEPLKAID // ID Q9JZS0_NEIMB Unreviewed; 66 AA. AC Q9JZS0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41329.1}; GN OrderedLocusNames=NMB0921 {ECO:0000313|EMBL:AAF41329.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41329.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41329.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41329.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41329.1; -; Genomic_DNA. DR PIR; C81143; C81143. DR RefSeq; NP_273961.1; NC_003112.2. DR RefSeq; WP_010980871.1; NC_003112.2. DR STRING; 122586.NMB0921; -. DR PaxDb; Q9JZS0; -. DR EnsemblBacteria; AAF41329; AAF41329; NMB0921. DR GeneID; 903042; -. DR KEGG; nme:NMB0921; -. DR BioCyc; NMEN122586:GHGG-959-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 66 AA; 7740 MW; 7026D9D3667DA837 CRC64; MPPHIRHSTS DRRQTRENHF PLPFTPPRSN TPRSNKARTK PPKYAIIATH IPRAMCSKRK NQPTRE // ID Q9JZM3_NEIMB Unreviewed; 67 AA. AC Q9JZM3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41391.1}; GN OrderedLocusNames=NMB0988 {ECO:0000313|EMBL:AAF41391.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41391.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41391.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41391.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41391.1; -; Genomic_DNA. DR PIR; E81135; E81135. DR RefSeq; NP_274024.1; NC_003112.2. DR RefSeq; WP_002225299.1; NC_003112.2. DR STRING; 122586.NMB0988; -. DR PaxDb; Q9JZM3; -. DR EnsemblBacteria; AAF41391; AAF41391; NMB0988. DR GeneID; 903108; -. DR KEGG; nme:NMB0988; -. DR PATRIC; 20357473; VBINeiMen85645_1251. DR OMA; PQMPEFE; -. DR OrthoDB; EOG69GZZ6; -. DR BioCyc; NMEN122586:GHGG-1025-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7296 MW; D093968E392A719F CRC64; MKKSLIALCV AHCAKLKNDF GVPPLPEIKI TPSPVRVGSL KQHPSLRLGK SGVAAAKRAA RKRKNRR // ID Q9K058_NEIMB Unreviewed; 152 AA. AC Q9K058; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41175.1}; GN OrderedLocusNames=NMB0762 {ECO:0000313|EMBL:AAF41175.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41175.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41175.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41175.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41175.1; -; Genomic_DNA. DR PIR; G81161; G81161. DR STRING; 122586.NMB0762; -. DR PaxDb; Q9K058; -. DR EnsemblBacteria; AAF41175; AAF41175; NMB0762. DR BioCyc; NMEN122586:GHGG-793-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 152 AA; 16781 MW; BBF3093B6AACE1BC CRC64; MCVGALLLFG NGSSVCVCGT AQTLCAEAGL LVRVAVCADG GCLCPPLRYR PAAAVNVRRL AAATRRVDGS VDAGLGTGAA AFRNWKIIRC GRIGTKSYKE RNFGYWFFRR HRFRIKPYPK FVYVSAQIPC NRTGCLWGLR LTVETLLFRS RR // ID Q9JZM9_NEIMB Unreviewed; 277 AA. AC Q9JZM9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Phosphoserine phosphatase {ECO:0000313|EMBL:AAF41385.1}; DE EC=3.1.3.3 {ECO:0000313|EMBL:AAF41385.1}; GN Name=serB {ECO:0000313|EMBL:AAF41385.1}; GN OrderedLocusNames=NMB0981 {ECO:0000313|EMBL:AAF41385.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41385.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41385.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41385.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41385.1; -; Genomic_DNA. DR PIR; G81134; G81134. DR RefSeq; NP_274018.1; NC_003112.2. DR RefSeq; WP_002225307.1; NC_003112.2. DR ProteinModelPortal; Q9JZM9; -. DR STRING; 122586.NMB0981; -. DR PaxDb; Q9JZM9; -. DR EnsemblBacteria; AAF41385; AAF41385; NMB0981. DR GeneID; 903101; -. DR KEGG; nme:NMB0981; -. DR PATRIC; 20357453; VBINeiMen85645_1241. DR eggNOG; ENOG4105EAC; Bacteria. DR eggNOG; COG0560; LUCA. DR HOGENOM; HOG000231114; -. DR KO; K01079; -. DR OMA; RVAFCAK; -. DR OrthoDB; EOG6ZPT4H; -. DR BioCyc; NMEN122586:GHGG-1018-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.150.210; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like. DR InterPro; IPR023190; Pser_Pase_dom_2. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41385.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 277 AA; 30551 MW; 08CD4085B0A22E30 CRC64; MPHALVLQFP SAAALPSDFP LRLPEPDCAD EKRMRFIVEE GFSLSEKDAA LLGSRQIDHA VLPDMDFDEL GLIVSDMDST LITIECVDEI AAGVGLKNKV AEITERSMRG ELDFEQSLRS RVALLAGLDE RVLADVYENV LKLSPGAEFL LDECKRHDVK FLLVSGGFTF FTERLQQRLG FEYQHANVLE IENGRLTGRL KGRIIDAQAK ADLLREYRSR LGLQPHQVLA VGDGANDIPM LKEAGIGVAY RAKPKARAAA DACINFGGLE RVRGLFG // ID Q9K1N0_NEIMB Unreviewed; 138 AA. AC Q9K1N0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=RNA polymerase-binding transcription factor DksA {ECO:0000256|HAMAP-Rule:MF_00926}; GN Name=dksA {ECO:0000256|HAMAP-Rule:MF_00926, GN ECO:0000313|EMBL:AAF40525.1}; GN OrderedLocusNames=NMB0056 {ECO:0000313|EMBL:AAF40525.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40525.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40525.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40525.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Transcription factor that acts by binding directly to CC the RNA polymerase (RNAP). Required for negative regulation of CC rRNA expression and positive regulation of several amino acid CC biosynthesis promoters. {ECO:0000256|HAMAP-Rule:MF_00926}. CC -!- SUBUNIT: Interacts directly with the RNA polymerase. CC {ECO:0000256|HAMAP-Rule:MF_00926}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}. CC -!- SIMILARITY: Belongs to the DksA family. {ECO:0000256|HAMAP- CC Rule:MF_00926}. CC -!- SIMILARITY: Contains 1 dksA C4-type zinc finger. CC {ECO:0000256|HAMAP-Rule:MF_00926}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40525.1; -; Genomic_DNA. DR PIR; F81243; F81243. DR RefSeq; NP_273121.1; NC_003112.2. DR RefSeq; WP_002215267.1; NC_003112.2. DR ProteinModelPortal; Q9K1N0; -. DR STRING; 122586.NMB0056; -. DR PaxDb; Q9K1N0; -. DR PRIDE; Q9K1N0; -. DR EnsemblBacteria; AAF40525; AAF40525; NMB0056. DR GeneID; 902158; -. DR KEGG; nme:NMB0056; -. DR PATRIC; 20355105; VBINeiMen85645_0090. DR eggNOG; ENOG4108V7X; Bacteria. DR eggNOG; COG1734; LUCA. DR HOGENOM; HOG000178408; -. DR KO; K06204; -. DR OMA; AQERHEK; -. DR OrthoDB; EOG6JDWD6; -. DR BioCyc; NMEN122586:GHGG-57-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00926; DksA; 1. DR InterPro; IPR012784; DksA_RNA_pol-bd. DR InterPro; IPR000962; Znf_DskA_TraR. DR Pfam; PF01258; zf-dskA_traR; 1. DR TIGRFAMs; TIGR02420; dksA; 1. DR PROSITE; PS51128; ZF_DKSA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00926}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00926}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00926}. FT DOMAIN 58 138 DksA C4-type. FT {ECO:0000259|PROSITE:PS51128}. FT ZN_FING 101 125 dksA C4-type. {ECO:0000256|HAMAP- FT Rule:MF_00926}. SQ SEQUENCE 138 AA; 15897 MW; 7C37A3B49EC73E75 CRC64; MAKLTEQDIL NWSGPEDDYM NDDHLAFFRE LLVKMQDELI ENASATTGHL QEHESAPDPA DRATQEEEYA LELRTRDRER KLLSKIQATI RNIDEGDYGF CADTGEPIGL KRLLARPTAT LSVESQERRE RMKKQFAD // ID Q9JZ75_NEIMB Unreviewed; 979 AA. AC Q9JZ75; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Type III restriction-modification system EcoPI enzyme, subunit res {ECO:0000313|EMBL:AAF41638.1}; DE EC=3.1.21.5 {ECO:0000313|EMBL:AAF41638.1}; GN Name=res {ECO:0000313|EMBL:AAF41638.1}; GN OrderedLocusNames=NMB1260 {ECO:0000313|EMBL:AAF41638.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41638.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41638.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41638.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41638.1; -; Genomic_DNA. DR PIR; G81103; G81103. DR RefSeq; NP_274282.1; NC_003112.2. DR RefSeq; WP_002222406.1; NC_003112.2. DR ProteinModelPortal; Q9JZ75; -. DR STRING; 122586.NMB1260; -. DR PaxDb; Q9JZ75; -. DR EnsemblBacteria; AAF41638; AAF41638; NMB1260. DR GeneID; 903682; -. DR KEGG; nme:NMB1260; -. DR PATRIC; 20358133; VBINeiMen85645_1578. DR eggNOG; ENOG4105D8D; Bacteria. DR eggNOG; COG3587; LUCA. DR HOGENOM; HOG000218980; -. DR KO; K01156; -. DR OMA; CIIRFGA; -. DR OrthoDB; EOG6MPWQ7; -. DR BioCyc; NMEN122586:GHGG-1298-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015668; F:Type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04851; ResIII; 1. DR SUPFAM; SSF52540; SSF52540; 5. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41638.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 11 254 ResIII. {ECO:0000259|Pfam:PF04851}. SQ SEQUENCE 979 AA; 111500 MW; 13E4AA742EA548DA CRC64; MSGFNYEKNQ PHQMRAVSAV LGVFDGATPK YRTADENPEL LFAAKQYANN ILKVQSQNGI DGRFPDRSDD QNILDISMET GTGKTYTYTQ TMFELHRWLG VFKFIVVVPT LSIKAGTQQF LQSKALAEHF EQDFGGDYEG VRLKTYVVES AKKNKGKKSN APITIEQFVK AENKKEIHVL LINAGMVNSS SMNDTGDKAL KDLFDNPVDA LAAVRPFMIV DEPHKFPTRD SAKTWGNIKR LKPQYILRYG ATFNDEYYNL LYRLTAVDAF NDGLVKGVRV FQEEMQGGMD AAVKLVSSDG KEAKFELNEK DKKQTFKLAK GEDLAQIHPA ISDLKIDKMN KTVVVLSNGL ELKTGAVINP YSYSQTVQDA MMQRAVAEHF KLERALLAER APQPKIKPLT LFFIDDIAGY RSGNELSGSL KDKFESWIRA EAARRLKTES DPFYRDYLQK TLDDVSACHG GYFSKDNTDS DDRIEQEINE ILHDKEKLLS LDNPRRFIFS KWTLREGWDN PNVFQICKLR SSGSTTSKLQ EVGRGLRLPV NELMARVRDV PYKLNYFVDS SEKDFVKQLV GEINDNSFQE EISKKFTEEL KQKILQKYPD IKPLVLVNQL FLDGIIDDNE NFAEDGYDKL KAAYPEAFPK GLDKGKVSNA KDEGKDTIIM REGKYEELKA LWELIHHKAV LQYKIKDEAE FADLFTAYLH ENAAKFPQAG IRTAVNEAYI NNGLMLSRRI DSFEDEDFIR FNTMTYREFL EKLAQTAKIR MQTLHQAFYC IRNELNIGDF LNMQTIAQIK NGFNRFLLHH SFHKFELDYR LVGSKIHPTK FTNKDGKPRA VKKADLGRFE DTEHRPAAGY LFGEIFYDSD IEHENVANNQ IEGVIVFTKI PRNSIKIPVA GGGTYSPDFA YIVKTKSGEI LNFVIEAKGT DGAEDLRKSE ERKIKHAEKL FAEISKEIKV VFKTQFDGER IAELIGQNMP AGGHSENGR // ID Q9JYE0_NEIMB Unreviewed; 251 AA. AC Q9JYE0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62335.1}; GN OrderedLocusNames=NMB1624 {ECO:0000313|EMBL:AAF62335.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62335.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62335.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62335.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62335.1; -; Genomic_DNA. DR RefSeq; NP_274630.1; NC_003112.2. DR RefSeq; WP_002220499.1; NC_003112.2. DR ProteinModelPortal; Q9JYE0; -. DR STRING; 122586.NMB1624; -. DR PaxDb; Q9JYE0; -. DR EnsemblBacteria; AAF62335; AAF62335; NMB1624. DR GeneID; 904034; -. DR KEGG; nme:NMB1624; -. DR PATRIC; 20359148; VBINeiMen85645_2085. DR eggNOG; ENOG4108Q3U; Bacteria. DR eggNOG; COG1262; LUCA. DR HOGENOM; HOG000135466; -. DR OMA; YAAFMRY; -. DR OrthoDB; EOG6ZKXPR; -. DR BioCyc; NMEN122586:GHGG-1673-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.1580.10; -; 1. DR InterPro; IPR016187; C-type_lectin_fold. DR InterPro; IPR005532; SUMF_dom. DR Pfam; PF03781; FGE-sulfatase; 1. DR SUPFAM; SSF56436; SSF56436; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 251 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332251. FT DOMAIN 20 248 FGE-sulfatase. FT {ECO:0000259|Pfam:PF03781}. SQ SEQUENCE 251 AA; 27894 MW; 66AAD05E82835E3B CRC64; MKYVRLFFLG AALAGTQAAA AEMVQIEGGS YRPLYLKKDT GLIKVKPFKL DKYPVTNAEF AEFVNSHPQW QKGRIGSKQA EPAYLKHWMK NGSRSYAPKA GELKQPVTNV SWFAANAYCA AQGKRLPTID EWEFAGLASA TQKNGSNEPG YNRTILDWYA DGGRKGLHDV GKGRPNYWGV YDMHGLIWEW TEDFNSSLLS SGNANAQMFC SGASIGSSDS SNYAAFLRYG IRTSLQSKYV LHNLGFRCTS R // ID Q9K150_NEIMB Unreviewed; 332 AA. AC Q9K150; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Putative branched-chain amino acid aminotransferase {ECO:0000313|EMBL:AAF40780.1}; GN OrderedLocusNames=NMB0337 {ECO:0000313|EMBL:AAF40780.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40780.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40780.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40780.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU004106}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40780.1; -; Genomic_DNA. DR PIR; D81211; D81211. DR RefSeq; NP_273386.1; NC_003112.2. DR RefSeq; WP_002243977.1; NC_003112.2. DR ProteinModelPortal; Q9K150; -. DR STRING; 122586.NMB0337; -. DR PaxDb; Q9K150; -. DR EnsemblBacteria; AAF40780; AAF40780; NMB0337. DR GeneID; 902452; -. DR KEGG; nme:NMB0337; -. DR PATRIC; 20355817; VBINeiMen85645_0427. DR eggNOG; ENOG4105CM2; Bacteria. DR eggNOG; COG0115; LUCA. DR HOGENOM; HOG000276704; -. DR KO; K00826; -. DR OMA; YSRAANG; -. DR OrthoDB; EOG67MF3R; -. DR BioCyc; NMEN122586:GHGG-358-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro. DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR005786; B_amino_transII. DR PANTHER; PTHR11825; PTHR11825; 1. DR Pfam; PF01063; Aminotran_4; 1. DR PIRSF; PIRSF006468; BCAT1; 1. DR SUPFAM; SSF56752; SSF56752; 1. DR TIGRFAMs; TIGR01123; ilvE_II; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:AAF40780.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40780.1}. FT MOD_RES 179 179 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR006468-1}. SQ SEQUENCE 332 AA; 36088 MW; 057325F32407E345 CRC64; MSRPVPAVFG SVFHSQMPVL AYREGKWQPT EWQSSQDLSL APGAHALHYG SECFEGLKAF RQADGKIVLF RPTANIARMR QSADILHLPR PETEAYLDAL IKLVKRAADE IPDAPAALYL RPTLIGTDPV IGKAGSPSET ALLYILASPV GDYFKVGSPV KILVETEHIR CAPHMGRVKC GGNYASAMHW VLKAKAEYGA NQVLFCPNGD VQETGASNFI LINGDEIITK PLTDEFLHGV TRDSVLTVAK DLGYTVSERN FTVDELKAAV ENGAEAILTG TAAVISPVTS FVIGGKEIEV KSQERGYAIR KAITDIQYGL AEDKYGWLVE VC // ID Q9JYZ8_NEIMB Unreviewed; 310 AA. AC Q9JYZ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41731.1}; GN OrderedLocusNames=NMB1357 {ECO:0000313|EMBL:AAF41731.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41731.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41731.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41731.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41731.1; -; Genomic_DNA. DR PIR; F81091; F81091. DR RefSeq; NP_274375.1; NC_003112.2. DR RefSeq; WP_002225149.1; NC_003112.2. DR STRING; 122586.NMB1357; -. DR PaxDb; Q9JYZ8; -. DR EnsemblBacteria; AAF41731; AAF41731; NMB1357. DR GeneID; 903779; -. DR KEGG; nme:NMB1357; -. DR PATRIC; 20358371; VBINeiMen85645_1697. DR eggNOG; ENOG4108MJ5; Bacteria. DR eggNOG; COG2990; LUCA. DR HOGENOM; HOG000218998; -. DR KO; K09824; -. DR OMA; PLHIERK; -. DR OrthoDB; EOG6TBHCV; -. DR BioCyc; NMEN122586:GHGG-1395-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007488; DUF535. DR Pfam; PF04393; DUF535; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 310 AA; 36236 MW; 794B492C918495AB CRC64; MKQNRTFTFP DFRTVYSYAP LYRLQHLKYT LRKFFGKKEI YAFEQFVNAS PIRQGLFLHC PQNAYPLLRE FVDRRFNCKR RLDAMTADFL MAEKLFGTDI LHQMEDYRFH LVLAHLSDGI SLWLNRNDNC VEEGAWSLSL RDEAGNRLYM ATFAFVGTHL LTASVQGPAG EEAKDTVRRI TKQLHGLRPQ QLMVTALQYF AAVLGLDGAM GIAQKHQVKL RWKLKKRVKM NYDAFWQEYG ASLERDGYWH LPQTPARKDL ADIESKKRSM YRKRYEMLDN MVAEMKDSLK TEARGISDGI QTEKPPRRTA // ID Q9JY90_NEIMB Unreviewed; 227 AA. AC Q9JY90; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative dedA protein {ECO:0000313|EMBL:AAF42037.1}; GN OrderedLocusNames=NMB1689 {ECO:0000313|EMBL:AAF42037.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42037.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42037.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42037.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42037.1; -; Genomic_DNA. DR PIR; B81054; B81054. DR RefSeq; NP_274693.1; NC_003112.2. DR RefSeq; WP_002224979.1; NC_003112.2. DR STRING; 122586.NMB1689; -. DR PaxDb; Q9JY90; -. DR DNASU; 903418; -. DR EnsemblBacteria; AAF42037; AAF42037; NMB1689. DR GeneID; 903418; -. DR KEGG; nme:NMB1689; -. DR PATRIC; 20359329; VBINeiMen85645_2171. DR eggNOG; ENOG4108VD1; Bacteria. DR eggNOG; COG0586; LUCA. DR HOGENOM; HOG000219073; -. DR OMA; WVYLGDF; -. DR OrthoDB; EOG613091; -. DR BioCyc; NMEN122586:GHGG-1744-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 193 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 199 226 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 227 AA; 25613 MW; 8F5A60BB067DC82F CRC64; MFAFLEAFFV EYGYAAVFFV LVICGFGVPI PEDLTLVTGG VISGMGYTNP HIMFAVGMLG VLVGDGIMFA AGRIWGQKIL RFKPIARIMT PKRYEQVQEK FDKYGNWVLF VARFLPGLRT AVFVTAGISR KVSYLRFIIM DGLAALISVP IWIYLGEYGA HNIDWLMAKM HSLQSGIFVI LGIGATVVAW IWWKKRQRIQ FYRSKLKEKR AQRKAAKAAK KAAQSKQ // ID Q9JZA3_NEIMB Unreviewed; 356 AA. AC Q9JZA3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Putative transporter {ECO:0000313|EMBL:AAF41601.1}; GN OrderedLocusNames=NMB1219 {ECO:0000313|EMBL:AAF41601.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41601.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41601.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41601.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41601.1; -; Genomic_DNA. DR PIR; E81107; E81107. DR RefSeq; NP_274244.1; NC_003112.2. DR RefSeq; WP_002225205.1; NC_003112.2. DR STRING; 122586.NMB1219; -. DR PaxDb; Q9JZA3; -. DR EnsemblBacteria; AAF41601; AAF41601; NMB1219. DR GeneID; 903641; -. DR KEGG; nme:NMB1219; -. DR PATRIC; 20358021; VBINeiMen85645_1523. DR eggNOG; ENOG4105C02; Bacteria. DR eggNOG; COG0628; LUCA. DR HOGENOM; HOG000245155; -. DR OMA; RGAADTQ; -. DR OrthoDB; EOG6J74SC; -. DR BioCyc; NMEN122586:GHGG-1256-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 234 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 295 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 307 340 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 356 AA; 38844 MW; 8007B9BDE0775D14 CRC64; MYRRKGRGIK PWMGAGAAFA ALVWLVFALG DTLTPFAVAA VLAYVLDPLV EWLQKKGLNR ASASMSVMVF SLILLLALLL IIVPMLVGQF NNLASRLPQL IGFMQNTLLP WLKNTIGGYV EIDQASIIAW LQAHTGELSN ALKAWFPVLM RQGGNIVSSI GNLLLLPLLL YYFLLDWQRW SCGIAKLVPR RFAGAYTRIT GNLNEVLGEF LRGQLLVMLI MGLVYGLGLV LVGLDSGFAI GMLAGILVFV PYLGAFTGLL LATVAALLQF GSWNGILSVW AVFAVGQFLE SFFITPKIVG DRIGLSPFWV IFSLMAFGQL MGFVGMLAGL PLAAVTLVLL REGVQKYFAG SFYRGR // ID Q7DDB0_NEIMB Unreviewed; 160 AA. AC Q7DDB0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase SlyD {ECO:0000313|EMBL:AAF41878.1}; DE EC=5.2.1.8 {ECO:0000313|EMBL:AAF41878.1}; GN Name=slyD {ECO:0000313|EMBL:AAF41878.1}; GN OrderedLocusNames=NMB1522 {ECO:0000313|EMBL:AAF41878.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41878.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41878.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41878.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41878.1; -; Genomic_DNA. DR PIR; A81075; A81075. DR RefSeq; NP_274530.1; NC_003112.2. DR RefSeq; WP_002212871.1; NC_003112.2. DR ProteinModelPortal; Q7DDB0; -. DR STRING; 122586.NMB1522; -. DR PaxDb; Q7DDB0; -. DR EnsemblBacteria; AAF41878; AAF41878; NMB1522. DR GeneID; 904012; -. DR KEGG; nme:NMB1522; -. DR PATRIC; 20358842; VBINeiMen85645_1931. DR eggNOG; ENOG4108YZY; Bacteria. DR eggNOG; COG1047; LUCA. DR HOGENOM; HOG000154889; -. DR KO; K03775; -. DR OMA; PKDVFVG; -. DR OrthoDB; EOG6Q8J79; -. DR BioCyc; NMEN122586:GHGG-1562-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PTHR10516; 2. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF41878.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 93 PPIase FKBP-type. FT {ECO:0000259|PROSITE:PS50059}. SQ SEQUENCE 160 AA; 17405 MW; 9CEB8347BBE0DDAC CRC64; MAIVKNSVVS LHYEMYDANN QLLDKTEEPI AYLHGGYDGI FPLVEEALHG KDAGDTVDVA LSPDDAFGEQ DPELVRIEDA GVFPVEVEVG MMFEADDPET GDVVVYRVTD VADGKAVVDG NHPLAGMKIR FKATVESVRD ASDEEIAHGH VHGPHGHHHH // ID Q9JZS3_NEIMB Unreviewed; 43 AA. AC Q9JZS3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41326.1}; GN OrderedLocusNames=NMB0918 {ECO:0000313|EMBL:AAF41326.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41326.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41326.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41326.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41326.1; -; Genomic_DNA. DR PIR; H81142; H81142. DR RefSeq; NP_273958.1; NC_003112.2. DR RefSeq; WP_002217434.1; NC_003112.2. DR STRING; 122586.NMB0918; -. DR PaxDb; Q9JZS3; -. DR EnsemblBacteria; AAF41326; AAF41326; NMB0918. DR GeneID; 903039; -. DR KEGG; nme:NMB0918; -. DR PATRIC; 20357273; VBINeiMen85645_1150. DR HOGENOM; HOG000220737; -. DR OrthoDB; EOG6PS62P; -. DR BioCyc; NMEN122586:GHGG-956-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 43 AA; 4753 MW; 0961440E0A367859 CRC64; MQNQNTRPVK IELKGEAGKR VLLAAARRIA KTHQKAVKAL ADK // ID Q9K028_NEIMB Unreviewed; 145 AA. AC Q9K028; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41210.1}; GN OrderedLocusNames=NMB0797 {ECO:0000313|EMBL:AAF41210.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41210.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41210.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41210.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41210.1; -; Genomic_DNA. DR PIR; D81157; D81157. DR RefSeq; NP_273839.1; NC_003112.2. DR RefSeq; WP_002223901.1; NC_003112.2. DR ProteinModelPortal; Q9K028; -. DR STRING; 122586.NMB0797; -. DR PaxDb; Q9K028; -. DR EnsemblBacteria; AAF41210; AAF41210; NMB0797. DR GeneID; 902912; -. DR KEGG; nme:NMB0797; -. DR PATRIC; 20356981; VBINeiMen85645_1009. DR eggNOG; ENOG4108Z1B; Bacteria. DR eggNOG; COG2867; LUCA. DR HOGENOM; HOG000261730; -. DR OMA; LREDACK; -. DR OrthoDB; EOG6RFZZ5; -. DR BioCyc; NMEN122586:GHGG-828-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR005031; COQ10_START. DR InterPro; IPR023393; START-like_dom. DR Pfam; PF03364; Polyketide_cyc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 136 Polyketide_cyc. FT {ECO:0000259|Pfam:PF03364}. SQ SEQUENCE 145 AA; 16929 MW; A8DD053244D35407 CRC64; MPVKKVEKNI LVLHGADKMF ELVDKVEDYP HFLPWYSKTE VIGRSGNELK ARLFMDYMHV RQSFATHNRN IPGREIRMEL LEGPFKTLRG TWKFIDLGDD MCKIEFNLEY DFSNAVLSAL ISPVFNHLST TLVEAFVKEA DRRYA // ID Q7DDU3_NEIMB Unreviewed; 441 AA. AC Q7DDU3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative membrane-bound lytic murein transglycosylase A {ECO:0000313|EMBL:AAF40504.1}; GN OrderedLocusNames=NMB0033 {ECO:0000313|EMBL:AAF40504.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40504.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40504.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40504.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40504.1; -; Genomic_DNA. DR RefSeq; NP_273099.1; NC_003112.2. DR RefSeq; WP_002221791.1; NC_003112.2. DR ProteinModelPortal; Q7DDU3; -. DR SMR; Q7DDU3; 32-441. DR STRING; 122586.NMB0033; -. DR PaxDb; Q7DDU3; -. DR EnsemblBacteria; AAF40504; AAF40504; NMB0033. DR GeneID; 902136; -. DR KEGG; nme:NMB0033; -. DR PATRIC; 20355019; VBINeiMen85645_0046. DR eggNOG; ENOG4105CA3; Bacteria. DR eggNOG; COG2821; LUCA. DR HOGENOM; HOG000255816; -. DR KO; K08304; -. DR OMA; DQNGHPY; -. DR OrthoDB; EOG6D2KR5; -. DR BioCyc; NMEN122586:GHGG-34-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro. DR Gene3D; 2.40.40.10; -; 3. DR InterPro; IPR010611; 3D_dom. DR InterPro; IPR005300; Lytic_transglycosylase_MltA. DR InterPro; IPR009009; RlpA-like_DPBB. DR Pfam; PF06725; 3D; 1. DR Pfam; PF03562; MltA; 1. DR SMART; SM00925; MltA; 1. DR SUPFAM; SSF50685; SSF50685; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 441 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287270. FT DOMAIN 144 335 MltA. {ECO:0000259|SMART:SM00925}. SQ SEQUENCE 441 AA; 48008 MW; 6F161C1B9E5C630F CRC64; MKKYLFRAAL YGIAAAILAA CQSKSIQTFP QPDTSVINGP DRPVGIPDPA GTTVGGGGAV YTVVPHLSLP HWAAQDFAKS LQSFRLGCAN LKNRQGWQDV CAQAFQTPVH SFQAKQFFER YFTPWQVAGN GSLAGTVTGY YEPVLKGDDR RTAQARFPIY GIPDDFISVP LPAGLRSGKA LVRIRQTGKN SGTIDNTGGT HTADLSRFPI TARTTAIKGR FEGSRFLPYH TRNQINGGAL DGKAPILGYA EDPVELFFMH IQGSGRLKTP SGKYIRIGYA DKNEHPYVSI GRYMADKGYL KLGQTSMQGI KSYMRQNPQR LAEVLGQNPS YIFFRELAGS SNDGPVGALG TPLMGEYAGA VDRHYITLGA PLFVATAHPV TRKALNRLIM AQDTGSAIKG AVRVDYFWGY GDEAGELAGK QKTTGYVWQL LPNGMKPEYR P // ID Q9K069_NEIMB Unreviewed; 146 AA. AC Q9K069; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Bacterioferritin comigratory protein {ECO:0000313|EMBL:AAF41163.1}; GN Name=bcp {ECO:0000313|EMBL:AAF41163.1}; GN OrderedLocusNames=NMB0750 {ECO:0000313|EMBL:AAF41163.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41163.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41163.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41163.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41163.1; -; Genomic_DNA. DR PIR; E81163; E81163. DR RefSeq; NP_273792.1; NC_003112.2. DR RefSeq; WP_010980834.1; NC_003112.2. DR ProteinModelPortal; Q9K069; -. DR STRING; 122586.NMB0750; -. DR PaxDb; Q9K069; -. DR EnsemblBacteria; AAF41163; AAF41163; NMB0750. DR GeneID; 902865; -. DR KEGG; nme:NMB0750; -. DR PATRIC; 20356871; VBINeiMen85645_0954. DR eggNOG; ENOG4108YXY; Bacteria. DR eggNOG; COG1225; LUCA. DR HOGENOM; HOG000022344; -. DR KO; K03564; -. DR OMA; YDSYGLK; -. DR OrthoDB; EOG6ZH2P1; -. DR BioCyc; NMEN122586:GHGG-781-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 146 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 146 AA; 16510 MW; E8CAB669CC2EAFBD CRC64; MDVKYEFTLP SSSGADFHSA EHLPLVVYFY PKDSTLGCTT EGLDFNARLE QFEALGYTVV GISRDGVKAH QNFCAKQGFR FELLSDKDET VCRLFDVIKL KKLYGKESLG IERSTFVLNK DGEIAHEWRK VKVAGHAQEV LETLSR // ID Q9K0D2_NEIMB Unreviewed; 203 AA. AC Q9K0D2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Cryptic protein {ECO:0000313|EMBL:AAF41098.1}; GN Name=cnp1 {ECO:0000313|EMBL:AAF41098.1}; GN OrderedLocusNames=NMB0680 {ECO:0000313|EMBL:AAF41098.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41098.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41098.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41098.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41098.1; -; Genomic_DNA. DR PIR; F81171; F81171. DR RefSeq; NP_273722.1; NC_003112.2. DR RefSeq; WP_002225499.1; NC_003112.2. DR STRING; 122586.NMB0680; -. DR PaxDb; Q9K0D2; -. DR EnsemblBacteria; AAF41098; AAF41098; NMB0680. DR GeneID; 902792; -. DR KEGG; nme:NMB0680; -. DR PATRIC; 20356669; VBINeiMen85645_0852. DR HOGENOM; HOG000218836; -. DR OMA; FCARSSI; -. DR OrthoDB; EOG66F08M; -. DR BioCyc; NMEN122586:GHGG-708-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014861; Uncharacterised_CNP1. DR Pfam; PF08750; CNP1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 203 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332290. FT DOMAIN 40 188 CNP1. {ECO:0000259|Pfam:PF08750}. SQ SEQUENCE 203 AA; 22732 MW; 771B99F5EB3B8D4E CRC64; MRRTALLLLA LAAGTSLAAG FSQKDTPINT RYRETPEEAA AREFKEHTAK LPPLPDTHSD GWFDIYVDEN YGKQPKILLD SLQIMPAPDG SIRYILNIRS DKGYDNLTAK GIFCARFSIR FGNGKPSSYK VFGYGDTVNR RWIQPRNAEW KPIGGTLSRN DALRTVLYQA FCEGGVPADT KGLVQRLKER AGRYAPSIKP HNK // ID Q9JZA8_NEIMB Unreviewed; 112 AA. AC Q9JZA8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41594.1}; GN OrderedLocusNames=NMB1212 {ECO:0000313|EMBL:AAF41594.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41594.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41594.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41594.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41594.1; -; Genomic_DNA. DR PIR; H81108; H81108. DR RefSeq; NP_274237.1; NC_003112.2. DR RefSeq; WP_002222441.1; NC_003112.2. DR STRING; 122586.NMB1212; -. DR PaxDb; Q9JZA8; -. DR EnsemblBacteria; AAF41594; AAF41594; NMB1212. DR GeneID; 903634; -. DR KEGG; nme:NMB1212; -. DR PATRIC; 20358009; VBINeiMen85645_1517. DR eggNOG; ENOG4107CEW; Bacteria. DR eggNOG; ENOG410ZBYK; LUCA. DR HOGENOM; HOG000152757; -. DR OrthoDB; EOG6SFPF4; -. DR BioCyc; NMEN122586:GHGG-1249-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 112 AA; 12666 MW; 94F10563C7AC7F9B CRC64; MKYIVSISLA MGLAACSFGG FKPNPWDAAS FWELKNYANP YPGSASAALD QYPSKARRRQ LKDMQECGYD PIDGGKSEAD ACLRKKGWCR KGFDPYPENK KYEWPREEGK TK // ID Q9K1M5_NEIMB Unreviewed; 184 AA. AC Q9K1M5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=dTDP-4-keto-6-deoxy-D-glucose-3,6-epimerase {ECO:0000313|EMBL:AAF40545.1}; GN OrderedLocusNames=NMB0081 {ECO:0000313|EMBL:AAF40545.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40545.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40545.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40545.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40545.1; -; Genomic_DNA. DR PIR; C81240; C81240. DR RefSeq; NP_273144.1; NC_003112.2. DR RefSeq; WP_009344923.1; NC_003112.2. DR ProteinModelPortal; Q9K1M5; -. DR SMR; Q9K1M5; 6-182. DR STRING; 122586.NMB0081; -. DR PaxDb; Q9K1M5; -. DR EnsemblBacteria; AAF40545; AAF40545; NMB0081. DR GeneID; 902185; -. DR KEGG; nme:NMB0081; -. DR PATRIC; 20355165; VBINeiMen85645_0116. DR eggNOG; ENOG4108URP; Bacteria. DR eggNOG; COG1898; LUCA. DR HOGENOM; HOG000227724; -. DR KO; K01790; -. DR OMA; HRSIYIS; -. DR OrthoDB; EOG6HTP2V; -. DR BioCyc; NMEN122586:GHGG-87-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR000888; dTDP_sugar_isom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR PANTHER; PTHR21047; PTHR21047; 1. DR Pfam; PF00908; dTDP_sugar_isom; 1. DR ProDom; PD001462; dTDP_sugar_isom; 1. DR SUPFAM; SSF51182; SSF51182; 1. DR TIGRFAMs; TIGR01221; rmlC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 184 AA; 21009 MW; 2528E774B8C5D921 CRC64; MKDKKMNIID TAIPDVKLLE PQVFGDARGF FMETFRDEWF KTQVCERTFV QENHSKSGKG VLRGLHYQTE NTQGKLVRVV VGEVFDVAVD MRKDSPTFGK WVGEILSAEN KRQLWVPEGF AHGFYVLSDE AEFVYKCTDY YNPKAEHSLI WNDPTVGIDW PLQGEPNLSP KDLAGKVLSE AVTF // ID Q9K0E8_NEIMB Unreviewed; 133 AA. AC Q9K0E8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41078.1}; GN OrderedLocusNames=NMB0659 {ECO:0000313|EMBL:AAF41078.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41078.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41078.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41078.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41078.1; -; Genomic_DNA. DR PIR; D81174; D81174. DR RefSeq; NP_273701.1; NC_003112.2. DR RefSeq; WP_002223957.1; NC_003112.2. DR STRING; 122586.NMB0659; -. DR PaxDb; Q9K0E8; -. DR EnsemblBacteria; AAF41078; AAF41078; NMB0659. DR GeneID; 902771; -. DR KEGG; nme:NMB0659; -. DR PATRIC; 20356615; VBINeiMen85645_0826. DR HOGENOM; HOG000219106; -. DR OMA; TANYFFE; -. DR OrthoDB; EOG683S9H; -. DR BioCyc; NMEN122586:GHGG-686-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 133 AA; 16298 MW; 80E08AA15B1FCA3D CRC64; MKIKPLQFSN NNHRFYVDKI CVTEQDVNIL ASDRNYELNI EIFIDNIIHF QITDESYKVK FSEYLFENKE KNDWDRNPAI NYFFEIIDDS YMDWLKEESF DFFEKKYYKA YIFFFSDSVI EVISSTEPVF YSK // ID Q9K1H8_NEIMB Unreviewed; 306 AA. AC Q9K1H8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Transcriptional regulator, LysR family {ECO:0000313|EMBL:AAF40630.1}; GN OrderedLocusNames=NMB0173 {ECO:0000313|EMBL:AAF40630.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40630.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40630.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40630.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3JV9} RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 88-306. RX PubMed=20478059; DOI=10.1186/1472-6807-10-10; RA Sainsbury S., Ren J., Nettleship J.E., Saunders N.J., Stuart D.I., RA Owens R.J.; RT "The structure of a reduced form of OxyR from Neisseria RT meningitidis."; RL BMC Struct. Biol. 10:10-10(2010). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40630.1; -; Genomic_DNA. DR PIR; E81230; E81230. DR RefSeq; NP_273231.1; NC_003112.2. DR RefSeq; WP_002224776.1; NC_003112.2. DR PDB; 3JV9; X-ray; 2.39 A; A/B=88-306. DR PDBsum; 3JV9; -. DR ProteinModelPortal; Q9K1H8; -. DR STRING; 122586.NMB0173; -. DR PaxDb; Q9K1H8; -. DR EnsemblBacteria; AAF40630; AAF40630; NMB0173. DR GeneID; 902280; -. DR KEGG; nme:NMB0173; -. DR PATRIC; 20355369; VBINeiMen85645_0214. DR eggNOG; ENOG4105C5Q; Bacteria. DR eggNOG; ENOG410XNR2; LUCA. DR HOGENOM; HOG000233514; -. DR KO; K04761; -. DR OMA; CPEFARF; -. DR OrthoDB; EOG6N6848; -. DR BioCyc; NMEN122586:GHGG-183-MONOMER; -. DR EvolutionaryTrace; Q9K1H8; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3JV9}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 1 58 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. FT COILED 65 92 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 306 AA; 34070 MW; 825797156064C33D CRC64; MTLTELRYIV AVAQERHFGR AARRCFVSQP TLSIAIKKLE EELAVSLFDR SSNDIITTEA GERIVAQARK VLEEAELIRH LANEEQNELE GAFKLGLIFT VAPYLLPKLI VSLRRTAPKM PLMLEENYTH TLTESLKRGD VDAIIVAEPF QEPGIVTEPL YDEPFFVIVP KGHSFEELDA VSPRMLGEEQ VLLLTEGNCM RDQVLSSCSE LAAKQRIQGL TNTLQGSSIN TIRHMVASGL AISVLPATAL TENDHMLFSI IPFEGTPPSR RVVLAYRRNF VRPKALSAMK AAIMQSQLHG VSFICD // ID Q9JYQ4_NEIMB Unreviewed; 61 AA. AC Q9JYQ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41834.1}; GN OrderedLocusNames=NMB1477 {ECO:0000313|EMBL:AAF41834.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41834.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41834.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41834.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41834.1; -; Genomic_DNA. DR PIR; C81079; C81079. DR RefSeq; NP_274486.1; NC_003112.2. DR RefSeq; WP_010980943.1; NC_003112.2. DR STRING; 122586.NMB1477; -. DR PaxDb; Q9JYQ4; -. DR EnsemblBacteria; AAF41834; AAF41834; NMB1477. DR GeneID; 903899; -. DR KEGG; nme:NMB1477; -. DR OrthoDB; EOG6FJNR0; -. DR BioCyc; NMEN122586:GHGG-1517-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 61 AA; 7049 MW; 653FFE54572695DF CRC64; MCSAFFRRIP CGLGNKIIYR LIKSGRFQLH AITFCLKIGY SCEPDGLFHS EPLFVKRKQN V // ID Q9K1C7_NEIMB Unreviewed; 53 AA. AC Q9K1C7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40690.1}; GN OrderedLocusNames=NMB0235 {ECO:0000313|EMBL:AAF40690.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40690.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40690.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40690.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40690.1; -; Genomic_DNA. DR PIR; B81221; B81221. DR STRING; 122586.NMB0235; -. DR PaxDb; Q9K1C7; -. DR EnsemblBacteria; AAF40690; AAF40690; NMB0235. DR HOGENOM; HOG000218646; -. DR OMA; IMNIINY; -. DR OrthoDB; EOG6PZXH0; -. DR BioCyc; NMEN122586:GHGG-250-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 53 AA; 6021 MW; 58E0BA846DCE2E22 CRC64; MNIINYKGDD IIISLTREEL QLLRSLVIEI YAGVCIDAEE FEIVSGIRNP KLV // ID Q7DDI8_NEIMB Unreviewed; 84 AA. AC Q7DDI8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41434.1}; GN OrderedLocusNames=NMB1035 {ECO:0000313|EMBL:AAF41434.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41434.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41434.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41434.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41434.1; -; Genomic_DNA. DR PIR; F81128; F81128. DR RefSeq; NP_274069.1; NC_003112.2. DR RefSeq; WP_002213442.1; NC_003112.2. DR STRING; 122586.NMB1035; -. DR PaxDb; Q7DDI8; -. DR EnsemblBacteria; AAF41434; AAF41434; NMB1035. DR GeneID; 903172; -. DR KEGG; nme:NMB1035; -. DR PATRIC; 20357605; VBINeiMen85645_1319. DR HOGENOM; HOG000218977; -. DR OMA; ACASTWE; -. DR OrthoDB; EOG6XQ3QV; -. DR BioCyc; NMEN122586:GHGG-1072-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 84 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004288458. SQ SEQUENCE 84 AA; 8728 MW; 706748FE261942DC CRC64; MNKLFITALS ALALSACAGT WEGAKQDTAR NLDKTQAAAE RAAEQTGNAV EKGWDKTKEA VKKGGNAVGR GISHLGGKIE NATE // ID Q9JXB5_NEIMB Unreviewed; 485 AA. AC Q9JXB5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Peptide transporter {ECO:0000313|EMBL:AAF42444.1}; GN OrderedLocusNames=NMB2136 {ECO:0000313|EMBL:AAF42444.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42444.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42444.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42444.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003755}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003755}. CC -!- SIMILARITY: Belongs to the PTR2/POT transporter (TC 2.A.17) CC family. {ECO:0000256|RuleBase:RU003755}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42444.1; -; Genomic_DNA. DR PIR; F81001; F81001. DR RefSeq; NP_275121.1; NC_003112.2. DR RefSeq; WP_002223221.1; NC_003112.2. DR ProteinModelPortal; Q9JXB5; -. DR PaxDb; Q9JXB5; -. DR EnsemblBacteria; AAF42444; AAF42444; NMB2136. DR GeneID; 903237; -. DR KEGG; nme:NMB2136; -. DR PATRIC; 20360460; VBINeiMen85645_2726. DR eggNOG; ENOG4105DUX; Bacteria. DR eggNOG; COG3104; LUCA. DR HOGENOM; HOG000243451; -. DR KO; K03305; -. DR OMA; YLFAFAK; -. DR OrthoDB; EOG6V1M5C; -. DR BioCyc; NMEN122586:GHGG-2201-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015197; F:peptide transporter activity; IEA:InterPro. DR GO; GO:0006857; P:oligopeptide transport; IEA:InterPro. DR InterPro; IPR005279; Dipep/tripep_permease. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR000109; POT_fam. DR InterPro; IPR018456; PTR2_symporter_CS. DR PANTHER; PTHR11654; PTHR11654; 2. DR Pfam; PF00854; PTR2; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR TIGRFAMs; TIGR00924; yjdL_sub1_fam; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS01023; PTR2_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003755}. FT TRANSMEM 28 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 202 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 270 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 310 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 359 379 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 385 404 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 425 443 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 455 474 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 22 482 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 485 AA; 52423 MW; 03D51420A878E2DA CRC64; MSRHPAPTGE KTFFGHPFQL STLFHIELWE RFSFYGMQGI LLIYLYYTAD KGGLGIDKTL AGGIVGAYSG SVYLSTILGA WFADRVWGAE KTLFLSGIVV MLGHIVLAAA PGLYGLLIGL IFIALGSGGV KSTASSMVGA LYEQDEMRPL RDAGFSIFYI AINIGGFLGP LLTGLLQENI GFHYGFGAAA VGMAFGLWRY SLGRKNLPHP TVPHPLSKGQ GKTAAAVGIA LIAALATAIK TGLVNLDNFS GILLSTVILA VIAYFARLLT NPRVSSDNKR HIIAYIPLFL TICMFWAVWF QIYTVATVYF DETVNRTIGS FTVPVAWKDS MQSLWVILFS GLMAAMWTKM GRKQPKTPLK FAMAVFVTGA SFLGFVPFIS SGTPMPIAVF ALIVLAITIG ELMISPIALS ISTKIAPPLF KTQMVALNFL AFSLGFTLGG VLFEKGYQAG DEIGFYRLLF YIGAATGFLL LLLVPKLNKM LEGTD // ID Q7DDS5_NEIMB Unreviewed; 504 AA. AC Q7DDS5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 86. DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498}; GN Name=kat {ECO:0000313|EMBL:AAF40672.1}; GN OrderedLocusNames=NMB0216 {ECO:0000313|EMBL:AAF40672.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40672.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40672.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40672.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC {ECO:0000256|RuleBase:RU000498}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2}; CC -!- SIMILARITY: Belongs to the catalase family. CC {ECO:0000256|RuleBase:RU000498}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40672.1; -; Genomic_DNA. DR PIR; D81224; D81224. DR RefSeq; NP_273273.1; NC_003112.2. DR RefSeq; WP_002218620.1; NC_003112.2. DR ProteinModelPortal; Q7DDS5; -. DR SMR; Q7DDS5; 11-487. DR STRING; 122586.NMB0216; -. DR PaxDb; Q7DDS5; -. DR EnsemblBacteria; AAF40672; AAF40672; NMB0216. DR GeneID; 902328; -. DR KEGG; nme:NMB0216; -. DR PATRIC; 20355500; VBINeiMen85645_0274. DR eggNOG; ENOG4105CH6; Bacteria. DR eggNOG; COG0753; LUCA. DR HOGENOM; HOG000087852; -. DR KO; K03781; -. DR OMA; QVHADFG; -. DR OrthoDB; EOG6P5Z9F; -. DR BioCyc; NMEN122586:GHGG-231-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.40.180.10; -; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR020835; Catalase-like_dom. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR PANTHER; PTHR11465; PTHR11465; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PIRSF; PIRSF038928; Catalase_clade1-3; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; SSF56634; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU000498}; KW Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2, KW ECO:0000256|RuleBase:RU000498}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000498}; KW Peroxidase {ECO:0000256|RuleBase:RU000498}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 12 396 Catalase. {ECO:0000259|SMART:SM01060}. FT ACT_SITE 59 59 {ECO:0000256|PIRSR:PIRSR038928-1}. FT ACT_SITE 132 132 {ECO:0000256|PIRSR:PIRSR038928-1}. FT METAL 342 342 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR038928-2}. SQ SEQUENCE 504 AA; 57167 MW; 26858B47446F3775 CRC64; MTTSKCPVTH LTMNNGAPVA DNQNSLTAGP RGPLLAQDLW LNEKLADFVR EVIPERRMHA KGSGAFGTFT VTHDITKYTR AKIFSEVGKK TEMFARFTTV AGERGAADAE RDIRGFALKF YTEEGNWDVV GNNTPVFFLR DPRKFPDLNK AVKRDPRTNM RSATNNWDFW TLLPEALHQV TIVMSDRGIP AGYRHMHGFG SHTYSFWNEA GERFWVKFHF RTQQGIKNLT NEEAAKIIAD DRESHQRDLY EAIERGEFPK WTMYIQVMPE ADAEKVPYHP FDLTKVWPKK DYPLIEVGEF ELNRNPENFF ADVEQSAFAP SNLVPGVGAS PDKMLQARLF NYADAQRYRL GVNFRQIPVN RPRCPVHSNQ RDGQGRADGN YGSLPHYEPN SFGQWQQQPD FAEPPLKING DAAHWDYRQD DDDYFSQPRA LFNLMNDAQK QALFGNTAAA MGDAPDFIKY RHIRNCYRCD PAYGEGVAKA LGLTVEDAQA ARATDPALGQ AGLL // ID Q9K121_NEIMB Unreviewed; 119 AA. AC Q9K121; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40815.1}; GN OrderedLocusNames=NMB0373 {ECO:0000313|EMBL:AAF40815.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40815.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40815.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40815.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40815.1; -; Genomic_DNA. DR PIR; C81207; C81207. DR RefSeq; NP_273422.1; NC_003112.2. DR RefSeq; WP_002221998.1; NC_003112.2. DR STRING; 122586.NMB0373; -. DR PaxDb; Q9K121; -. DR EnsemblBacteria; AAF40815; AAF40815; NMB0373. DR GeneID; 902488; -. DR KEGG; nme:NMB0373; -. DR eggNOG; ENOG4107BGC; Bacteria. DR eggNOG; ENOG410ZFAY; LUCA. DR HOGENOM; HOG000220768; -. DR OMA; GINMSRY; -. DR OrthoDB; EOG6MWNCH; -. DR BioCyc; NMEN122586:GHGG-395-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 119 AA; 14146 MW; B1DFED6617D1F475 CRC64; MASYVSIKGW IECSDDDIKI IQENINNFWN NCPFNIEEKE SAKIYKSGWV FPTNSFNWSS YIFFGACVKS YFIIYFEKCI KTIMELDIEI SGFFELDYYE DNYKVNWKIN NGNLIQTTN // ID Q7DDC5_NEIMB Unreviewed; 144 AA. AC Q7DDC5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41726.1}; GN OrderedLocusNames=NMB1352 {ECO:0000313|EMBL:AAF41726.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41726.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41726.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41726.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41726.1; -; Genomic_DNA. DR PIR; C81093; C81093. DR RefSeq; NP_274370.1; NC_003112.2. DR RefSeq; WP_002217013.1; NC_003112.2. DR PaxDb; Q7DDC5; -. DR EnsemblBacteria; AAF41726; AAF41726; NMB1352. DR GeneID; 903774; -. DR KEGG; nme:NMB1352; -. DR PATRIC; 20358361; VBINeiMen85645_1692. DR HOGENOM; HOG000218997; -. DR OMA; EILMNFA; -. DR OrthoDB; EOG6GBMBP; -. DR BioCyc; NMEN122586:GHGG-1390-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025392; DUF4124. DR Pfam; PF13511; DUF4124; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 144 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287538. FT DOMAIN 13 68 DUF4124. {ECO:0000259|Pfam:PF13511}. FT COILED 84 118 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 144 AA; 16042 MW; 4435F00EC0615A30 CRC64; MNFALSVIML TLASFLPVPP AGAAVFTWKD GGGNSYSDVP KQLHPDQSQI LNLRTRQTKP AVKPAQADAG KRTDGAAQEN NPDTAEKNRQ LEEEKKRIAE TERQNKEENC RISKMNLKAV GNSNAKNKDD LIRKYNNAVN KYCR // ID Q9JY28_NEIMB Unreviewed; 612 AA. AC Q9JY28; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42112.1}; GN OrderedLocusNames=NMB1772 {ECO:0000313|EMBL:AAF42112.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42112.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42112.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42112.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42112.1; -; Genomic_DNA. DR PIR; H81043; H81043. DR RefSeq; NP_274772.1; NC_003112.2. DR RefSeq; WP_002225628.1; NC_003112.2. DR STRING; 122586.NMB1772; -. DR PaxDb; Q9JY28; -. DR EnsemblBacteria; AAF42112; AAF42112; NMB1772. DR GeneID; 903327; -. DR KEGG; nme:NMB1772; -. DR PATRIC; 20359501; VBINeiMen85645_2256. DR HOGENOM; HOG000152752; -. DR OMA; SEKQGCK; -. DR BioCyc; NMEN122586:GHGG-1827-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 119 270 DUF637. {ECO:0000259|Pfam:PF04830}. FT DOMAIN 287 333 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 612 AA; 65450 MW; A6DD5448DEE13932 CRC64; MRKVCASART RSMIYGSMPS EKLTIFQTAF VMQVNIQIPY ILPRCVRAED TPYACYLKQL QVTKDVNWNQ VQLAYDKWDY KQEGLTGAGA AIIALAVTVV TAGAGAGAAL GLNGAAAAAT DAAFASLASQ ASVSLINNKG NIGNTLKELG RSSTVKNLMV AVATAGVADK IGASALNNVS DKQWINNLTV NLANAGSAAL INTAVNGGSL KDNLEANILA ALVNTAHGEA ASKIKQLDQH YITHKIAHAI AGCAAAAANK GKCQDGAIGA AVGEILGEAL LDGRDPGSLN VKDRAKIIAK AKLAAGTVAA LSKGDVNAAA NAAAVAVESN ALSKERMDKL TKCLSGKTCS TTMEKVNAIK KDEQFSKVID TEIQKVCSRN PLGDGCRNGI NMSIKYIAMP AAWKYMPTDV SRVAKEVFGY LYNSQGASTR FDKYFNTIDN RADFFAASNL YEQNLGSKAR WFGGADFVSR AAITGLGADG EASYITFAAG KVVGNPPIYE WRAASGNALI VNGFYNFRDL FNKKTNPREW DIQQLKSEQK LLQPIHQKYL SNEKDYLSLI KGVTSNKIFS IIPNPLDERK KIEDGINMLD YKSRIKYGCK LMGYSEKQGC KP // ID Q9JXA9_NEIMB Unreviewed; 248 AA. AC Q9JXA9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42451.1}; GN OrderedLocusNames=NMB2143 {ECO:0000313|EMBL:AAF42451.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42451.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42451.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42451.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42451.1; -; Genomic_DNA. DR PIR; E81002; E81002. DR RefSeq; NP_275128.1; NC_003112.2. DR RefSeq; WP_002225740.1; NC_003112.2. DR STRING; 122586.NMB2143; -. DR PaxDb; Q9JXA9; -. DR EnsemblBacteria; AAF42451; AAF42451; NMB2143. DR GeneID; 903229; -. DR KEGG; nme:NMB2143; -. DR PATRIC; 20360480; VBINeiMen85645_2736. DR eggNOG; ENOG4105GDN; Bacteria. DR eggNOG; COG3219; LUCA. DR HOGENOM; HOG000218684; -. DR KO; K09929; -. DR OMA; PLNGYAE; -. DR OrthoDB; EOG6716MP; -. DR BioCyc; NMEN122586:GHGG-2208-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR018640; DUF2063. DR Pfam; PF09836; DUF2063; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 90 DUF2063. {ECO:0000259|Pfam:PF09836}. SQ SEQUENCE 248 AA; 28683 MW; 0486C21E69B77B40 CRC64; MQPETSAQYQ HRFAQAIRGG EAADGLPQDR LNVYIRLIRN NIYSFIDRCY TETLQYFDRE EWGRLKEGFV RDACAQTPYF QEIPGEFLQY CQSLPLLDGI LALMDFEYTQ LLAEVAQIPD IPDIHYSNDS KYTPSPAAFI RQYRYDVTDD LHEAETALLI WRNAEDDVMY QTLDGFDMML LEIMGFSALS FDTLAQTLVE FMPEDDNWKN ILLGKWSGWT EQRIIIPSLS AISENMEDNS PGQNHLSA // ID Q9K136_NEIMB Unreviewed; 193 AA. AC Q9K136; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40797.1}; GN OrderedLocusNames=NMB0354 {ECO:0000313|EMBL:AAF40797.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40797.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40797.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40797.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40797.1; -; Genomic_DNA. DR PIR; A81208; A81208. DR RefSeq; NP_273403.1; NC_003112.2. DR RefSeq; WP_002231784.1; NC_003112.2. DR STRING; 122586.NMB0354; -. DR PaxDb; Q9K136; -. DR EnsemblBacteria; AAF40797; AAF40797; NMB0354. DR GeneID; 902469; -. DR KEGG; nme:NMB0354; -. DR PATRIC; 20355857; VBINeiMen85645_0447. DR eggNOG; COG3117; LUCA. DR HOGENOM; HOG000219112; -. DR KO; K11719; -. DR OMA; PENSDIH; -. DR OrthoDB; EOG680X0Z; -. DR BioCyc; NMEN122586:GHGG-375-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015221; F:lipopolysaccharide transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro. DR InterPro; IPR010664; LipoPS_assembly_LptC-rel. DR InterPro; IPR026265; LptC. DR Pfam; PF06835; LptC; 1. DR TIGRFAMs; TIGR04409; LptC_YrbK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 193 AA; 21740 MW; 6E8B3BE4820D6C2C CRC64; MKVRWRYGIA FPLILAVALG SLSAWLGRIS EVEIEEVRLN PDEPQYTMDG LDGRRFDEQG YLKEHLSAKG AKQFPESSDI HFDSPHLVFF QEGRLLYEVG SDEAVYHTEN KQVLFKNNVV LTKTADGKRQ AGKVEAEKLH VDTESQYAQT DTPVSFQYGA SHGQAGGMTY DHKTGMLNFS SKVKATIYDT KDM // ID Q7DDL1_NEIMB Unreviewed; 136 AA. AC Q7DDL1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41231.1}; GN OrderedLocusNames=NMB0818 {ECO:0000313|EMBL:AAF41231.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41231.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41231.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41231.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41231.1; -; Genomic_DNA. DR PIR; A81154; A81154. DR RefSeq; NP_273860.1; NC_003112.2. DR RefSeq; WP_002217553.1; NC_003112.2. DR STRING; 122586.NMB0818; -. DR PaxDb; Q7DDL1; -. DR EnsemblBacteria; AAF41231; AAF41231; NMB0818. DR GeneID; 902933; -. DR KEGG; nme:NMB0818; -. DR PATRIC; 20357019; VBINeiMen85645_1028. DR HOGENOM; HOG000218660; -. DR OrthoDB; EOG6WHNZZ; -. DR BioCyc; NMEN122586:GHGG-849-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007929; DUF723. DR Pfam; PF05265; DUF723; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 136 AA; 14809 MW; C92DEB829013A064 CRC64; MALTFTQAVS KLTSKFPHLN LVEFNGVRYP TVIVCPIHGR VTCSTFKSML DSKSGCPKCA SYGVNSHKIP EDTIDKLSKN TVLEDTVTGE TLTFPSRASA ARSLGINPAA ITDRIKGRVH TETLLAGRYK VHICTK // ID Q9K0T6_NEIMB Unreviewed; 31 AA. AC Q9K0T6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40922.1}; GN OrderedLocusNames=NMB0487 {ECO:0000313|EMBL:AAF40922.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40922.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40922.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40922.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40922.1; -; Genomic_DNA. DR PIR; C81193; C81193. DR STRING; 122586.NMB0487; -. DR PaxDb; Q9K0T6; -. DR EnsemblBacteria; AAF40922; AAF40922; NMB0487. DR BioCyc; NMEN122586:GHGG-512-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 31 AA; 3725 MW; C2DDCD94508838D8 CRC64; MRFSRSKPRG RLKTEKPFQT ALYIASLRRD D // ID Q9JY32_NEIMB Unreviewed; 337 AA. AC Q9JY32; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42107.1}; GN OrderedLocusNames=NMB1766 {ECO:0000313|EMBL:AAF42107.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42107.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42107.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42107.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42107.1; -; Genomic_DNA. DR PIR; D81045; D81045. DR RefSeq; NP_274766.1; NC_003112.2. DR RefSeq; WP_002225626.1; NC_003112.2. DR STRING; 122586.NMB1766; -. DR PaxDb; Q9JY32; -. DR EnsemblBacteria; AAF42107; AAF42107; NMB1766. DR GeneID; 903332; -. DR KEGG; nme:NMB1766; -. DR PATRIC; 20359493; VBINeiMen85645_2252. DR eggNOG; ENOG4106Q00; Bacteria. DR eggNOG; ENOG410YG3E; LUCA. DR OMA; NEPLENT; -. DR OrthoDB; EOG696BSN; -. DR BioCyc; NMEN122586:GHGG-1821-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 337 AA; 37758 MW; D61328591AE597FD CRC64; MAWSMFATTQ ADRAVRSATA PKEMWFHKKI IDEKTGKVSF DTRQIWSLND LSKEELASIQ DTNGKVITVS NPGIFNNRED SLSNAAKQNR NSTNGSGVIA VMNPPTGKYK SDSNNKIKDF LWLGSSLVSE LMYVGYDQLN NKVFQGYLPK TNSEKLNQDI YREVQKMGNG WSVDTSNHSR GGITASVSLK DWVNNQKQNG IAPIRKARFY GTATNVQNDY ADVLQKNGYT YTGADGKTYN SGSYSIVHDK DFVGNKWIPF LLGTNDTTQG TCKGLCYSHS SYFAEVPKAG TKEFDDYVKI WGEVEYDAQG KPINKSKPIL VEPNKTKDNE KYEKEAF // ID Q9JYH9_NEIMB Unreviewed; 217 AA. AC Q9JYH9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41931.1}; GN OrderedLocusNames=NMB1578 {ECO:0000313|EMBL:AAF41931.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41931.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41931.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41931.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41931.1; -; Genomic_DNA. DR PIR; B81067; B81067. DR RefSeq; NP_274584.1; NC_003112.2. DR RefSeq; WP_002225030.1; NC_003112.2. DR ProteinModelPortal; Q9JYH9; -. DR STRING; 122586.NMB1578; -. DR PaxDb; Q9JYH9; -. DR EnsemblBacteria; AAF41931; AAF41931; NMB1578. DR GeneID; 904204; -. DR KEGG; nme:NMB1578; -. DR PATRIC; 20359022; VBINeiMen85645_2029. DR eggNOG; ENOG4108ZX6; Bacteria. DR eggNOG; COG1999; LUCA. DR HOGENOM; HOG000258139; -. DR KO; K07152; -. DR OMA; KHAGRDY; -. DR OrthoDB; EOG6S26DB; -. DR BioCyc; NMEN122586:GHGG-1620-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.30.10; -; 2. DR InterPro; IPR003782; SCO1/SenC. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR12151; PTHR12151; 1. DR Pfam; PF02630; SCO1-SenC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 217 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327710. FT DOMAIN 54 217 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 217 AA; 23210 MW; 84FB5997D8C47AAC CRC64; MFSVPRSFLP GVFVLAALAA CKPQDNSAAQ VASSSASASA AENAAKPQTR GTDMRKEDIG GDFTLTDGEG KPFNLSDLKG KVVILSFGFT HCPDVCPTEL LTYSDTLKQL GGQAKDVKVV FVSIDPERDT PEIIGKYAKQ FNPDFIGLTA TGGQNLPVIK QQYRVVSAKV NQKDDSENYL VDHSSGAYLI DKNGEVAIFS PYGSEPETIA ADVRTLL // ID Q9K0X5_NEIMB Unreviewed; 292 AA. AC Q9K0X5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939}; DE Short=2-MIC {ECO:0000256|HAMAP-Rule:MF_01939}; DE Short=MICL {ECO:0000256|HAMAP-Rule:MF_01939}; DE EC=4.1.3.30 {ECO:0000256|HAMAP-Rule:MF_01939}; DE AltName: Full=(2R,3S)-2-methylisocitrate lyase {ECO:0000256|HAMAP-Rule:MF_01939}; GN Name=prpB {ECO:0000256|HAMAP-Rule:MF_01939}; GN OrderedLocusNames=NMB0430 {ECO:0000313|EMBL:AAF40868.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40868.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40868.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40868.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the thermodynamically favored C-C bond CC cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and CC succinate. {ECO:0000256|RuleBase:RU361121}. CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids CC (SCFA) via the 2-methylcitrate cycle (propionate degradation CC route). Catalyzes the thermodynamically favored C-C bond cleavage CC of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via CC an alpha-carboxy-carbanion intermediate. {ECO:0000256|HAMAP- CC Rule:MF_01939}. CC -!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = CC pyruvate + succinate. {ECO:0000256|HAMAP-Rule:MF_01939, CC ECO:0000256|RuleBase:RU361121}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01939}; CC -!- PATHWAY: Organic acid metabolism; propanoate degradation. CC {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_01939}. CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase CC superfamily. Methylisocitrate lyase family. {ECO:0000256|HAMAP- CC Rule:MF_01939, ECO:0000256|RuleBase:RU361121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40868.1; -; Genomic_DNA. DR PIR; H81199; H81199. DR RefSeq; NP_273478.1; NC_003112.2. DR RefSeq; WP_002212504.1; NC_003112.2. DR ProteinModelPortal; Q9K0X5; -. DR SMR; Q9K0X5; 3-290. DR STRING; 122586.NMB0430; -. DR PaxDb; Q9K0X5; -. DR PRIDE; Q9K0X5; -. DR EnsemblBacteria; AAF40868; AAF40868; NMB0430. DR GeneID; 902546; -. DR KEGG; nme:NMB0430; -. DR PATRIC; 20356060; VBINeiMen85645_0545. DR eggNOG; ENOG4105CR4; Bacteria. DR eggNOG; COG2513; LUCA. DR HOGENOM; HOG000220041; -. DR KO; K03417; -. DR OMA; MAEVNGA; -. DR OrthoDB; EOG6BGP03; -. DR BioCyc; NMEN122586:GHGG-454-MONOMER; -. DR UniPathway; UPA00946; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.60; -; 1. DR HAMAP; MF_01939; PrpB; 1. DR InterPro; IPR018523; Isocitrate_lyase_ph_CS. DR InterPro; IPR012695; PrpB. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR02317; prpB; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01939, KW ECO:0000256|RuleBase:RU361121}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}; KW Pyruvate {ECO:0000313|EMBL:AAF40868.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT REGION 46 48 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 123 124 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 210 212 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 86 86 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 88 88 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 158 158 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 188 188 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 241 241 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 270 270 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. SQ SEQUENCE 292 AA; 31714 MW; E753985E9D475FAA CRC64; MMSQHSAGAR FRQAVKESNP LAVAGCVNAY FARLATQSGF KAIYLSGGGV AACSCGIPDL GITTMEDVLI DARRITDNVD TPLLVDIDVG WGGAFNIART IRNFERAGVA AVHIEDQVAQ KRCGHRPNKA IVSKDEMVDR IKAAVDARVD ENFVIMARTD ALAVEGLDAA IERAQACVEA GADMIFPEAM TDLNMYRQFA DAVKVPVLAN ITEFGSTPLY TQSELAENGV SLVLYPLSSF RAASKAALNV YEAIMRDGTQ AAVVDSMQTR AELYEHLNYH AFEQKLDKLF QK // ID Q9JZ51_NEIMB Unreviewed; 395 AA. AC Q9JZ51; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Putative type II restriction enzyme {ECO:0000313|EMBL:AAF41665.1}; GN OrderedLocusNames=NMB1289 {ECO:0000313|EMBL:AAF41665.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41665.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41665.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41665.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41665.1; -; Genomic_DNA. DR PIR; H81100; H81100. DR RefSeq; NP_274309.1; NC_003112.2. DR RefSeq; WP_002213380.1; NC_003112.2. DR ProteinModelPortal; Q9JZ51; -. DR STRING; 122586.NMB1289; -. DR PaxDb; Q9JZ51; -. DR EnsemblBacteria; AAF41665; AAF41665; NMB1289. DR GeneID; 903711; -. DR KEGG; nme:NMB1289; -. DR PATRIC; 20358205; VBINeiMen85645_1614. DR eggNOG; ENOG4106MMT; Bacteria. DR eggNOG; ENOG410YFPN; LUCA. DR HOGENOM; HOG000218988; -. DR KO; K01155; -. DR OMA; GKSLEHH; -. DR OrthoDB; EOG6GXTXQ; -. DR BioCyc; NMEN122586:GHGG-1327-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:InterPro. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 2.40.330.10; -; 1. DR InterPro; IPR015300; DNA-bd_pseudobarrel. DR InterPro; IPR023372; Rest_endonuc_II_EcoRII_N. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR015109; Restrct_endonuc_II_EcoRII_C. DR Pfam; PF09019; EcoRII-C; 1. DR Pfam; PF09217; EcoRII-N; 1. DR SUPFAM; SSF101936; SSF101936; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 26 167 EcoRII-N. {ECO:0000259|Pfam:PF09217}. FT DOMAIN 218 386 EcoRII-C. {ECO:0000259|Pfam:PF09019}. SQ SEQUENCE 395 AA; 45198 MW; 12E0D25F60992141 CRC64; MNDLAAQTIQ VVNKSDDLVA SAIQTANKSI AVYCRYIRPN DVGTTGSHQS GFYIQKHFSD DLFDVVCQKG TNKTISIKIN WQDGSVTNSN FKYYGQGTRN EARITGFGKN FEFLSDKYSG SLLVLCRACY KDLLFHAFVL SSDEDIEIFI AETNILPGSL YLPKKQEVED NLTKLFSLFP NFPKTEEMAV LARENIALNK TNVSNVLKQW VSKEYELFSI FEKREFEIIK SKITDLDSFI NFAHSFTNRR KARAGKSLEL HLSRIFDEFS LKFETQAKTE GKKKPDFLFP GSEEYHAMDE SGNFIFQTEK LTMLGSKTTC KDRWRQVLNE ADRIPHKHLF TLQEGISDTQ IQEMSDENLT LVVPKESVKT FGTFGKTHVL TLENFIKYIK SQQVS // ID Q9JYW5_NEIMB Unreviewed; 63 AA. AC Q9JYW5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=FrpA/C-related protein {ECO:0000313|EMBL:AAF62333.1}; GN OrderedLocusNames=NMB1403 {ECO:0000313|EMBL:AAF62333.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62333.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62333.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62333.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62333.1; -; Genomic_DNA. DR RefSeq; NP_274417.1; NC_003112.2. DR RefSeq; WP_002213116.1; NC_003112.2. DR STRING; 122586.NMB1403; -. DR PaxDb; Q9JYW5; -. DR EnsemblBacteria; AAF62333; AAF62333; NMB1403. DR GeneID; 903825; -. DR KEGG; nme:NMB1403; -. DR HOGENOM; HOG000219008; -. DR OMA; TMIGSGD; -. DR OrthoDB; EOG6PCQ2M; -. DR BioCyc; NMEN122586:GHGG-1441-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 63 AA; 6781 MW; 29A151EDD751D082 CRC64; MIGSGDTKQC KKFSACDGKY HVYDPLALDL DGDGIETVTA KGFSGSLKTE RVNTMSIHSM PLN // ID Q9JXH8_NEIMB Unreviewed; 312 AA. AC Q9JXH8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 101. DE SubName: Full=Spermidine/putrescine ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF42363.1}; GN Name=potA-2 {ECO:0000313|EMBL:AAF42363.1}; GN OrderedLocusNames=NMB2042 {ECO:0000313|EMBL:AAF42363.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42363.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42363.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42363.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42363.1; -; Genomic_DNA. DR PIR; G81012; G81012. DR RefSeq; NP_275033.1; NC_003112.2. DR RefSeq; WP_002225688.1; NC_003112.2. DR ProteinModelPortal; Q9JXH8; -. DR STRING; 122586.NMB2042; -. DR PaxDb; Q9JXH8; -. DR EnsemblBacteria; AAF42363; AAF42363; NMB2042. DR GeneID; 904049; -. DR KEGG; nme:NMB2042; -. DR PATRIC; 20360230; VBINeiMen85645_2615. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR OMA; NWEHING; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-2105-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42363.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF42363.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 232 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 312 AA; 34575 MW; 0F1071B4C2791973 CRC64; MLELNGLCKR FGNKTVADNI CLTVGRGKIL AVLGRSGCGK STLLNIIAGI VRPDGGEIWL NGENITRMPP EKRRISLMFQ DYALFPHMSA LENAAFGLKM QKMPKAEAER LAMAALAEVG LENEAHRKPE KLSGGEKQRL ALARALVVRP SLLLLDESFS SLDTHLRGTL RRMTAERIRN GGIPAVLVTH SPEEACTTAD EIAVMHKGRI LQYGTPETLV KTPSCVQVAR LMGLPNTDDN RHIPQHAVRF DQDGMECRVL SRTCLPESFS LSVLHPEHGI LWLNLDMRHA GAVSGKDTVR IHIEEREIVR FR // ID Q9K1L1_NEIMB Unreviewed; 224 AA. AC Q9K1L1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40563.1}; GN OrderedLocusNames=NMB0104 {ECO:0000313|EMBL:AAF40563.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40563.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40563.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40563.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40563.1; -; Genomic_DNA. DR PIR; G81237; G81237. DR RefSeq; NP_273162.1; NC_003112.2. DR RefSeq; WP_002243942.1; NC_003112.2. DR PaxDb; Q9K1L1; -. DR EnsemblBacteria; AAF40563; AAF40563; NMB0104. DR GeneID; 902208; -. DR KEGG; nme:NMB0104; -. DR PATRIC; 20355219; VBINeiMen85645_0143. DR HOGENOM; HOG000218672; -. DR OMA; INILIYN; -. DR OrthoDB; EOG6SNDQS; -. DR BioCyc; NMEN122586:GHGG-110-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 224 AA; 24653 MW; 82516329FF135CE6 CRC64; MLAIYSINIL IYNEKSFFRV TLYFVKNFVS FSKPRKSNEM MQKHKCLIDF ILTVASQIAY ADLPLSLEEL LTDKGKFKLE SSISYINTER NQSEFANPIY VQTSATKIAT VMAMMITPVM AQNLDSQVFD SQNVKAIQLS QAEMKETQGE FVPIIAAAAF GGALGAWGYH GANLYNHGKL GTAQGAATAT GIGAATGVAA KQGWLLLPEA DWLGIWHGDR VFMH // ID Q7DDT8_NEIMB Unreviewed; 65 AA. AC Q7DDT8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40550.1}; GN OrderedLocusNames=NMB0087 {ECO:0000313|EMBL:AAF40550.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40550.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40550.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40550.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40550.1; -; Genomic_DNA. DR PIR; H81238; H81238. DR RefSeq; NP_273149.1; NC_003112.2. DR RefSeq; WP_002215316.1; NC_003112.2. DR STRING; 122586.NMB0087; -. DR PaxDb; Q7DDT8; -. DR EnsemblBacteria; AAF40550; AAF40550; NMB0087. DR GeneID; 902191; -. DR KEGG; nme:NMB0087; -. DR PATRIC; 20355179; VBINeiMen85645_0123. DR HOGENOM; HOG000218676; -. DR OMA; WVVAARL; -. DR OrthoDB; EOG61S34B; -. DR BioCyc; NMEN122586:GHGG-93-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 65 AA; 7292 MW; 34D6F8047F9C4323 CRC64; MNTVPKSRIP VKPLPEKTTD EAKVEKWRQL GAEHGLSGEW AVAVRLGENG FTEEQMENIA NLFGR // ID Q9JY25_NEIMB Unreviewed; 81 AA. AC Q9JY25; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42117.1}; GN OrderedLocusNames=NMB1777 {ECO:0000313|EMBL:AAF42117.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42117.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42117.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42117.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42117.1; -; Genomic_DNA. DR PIR; E81044; E81044. DR RefSeq; NP_274777.2; NC_003112.2. DR PaxDb; Q9JY25; -. DR EnsemblBacteria; AAF42117; AAF42117; NMB1777. DR GeneID; 903322; -. DR KEGG; nme:NMB1777; -. DR PATRIC; 20359511; VBINeiMen85645_2261. DR eggNOG; COG3792; LUCA. DR OrthoDB; EOG6SBTBF; -. DR BioCyc; NMEN122586:GHGG-1832-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3510.10; -; 1. DR InterPro; IPR023138; NMB0513-like_domain. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 81 AA; 9490 MW; 8F3DE9471EAFBCD0 CRC64; MEELLNDGSI RLHDYTDGIG IPLTGTSKEQ VQKLKDIWPT LEDAQAIWPE DPWYYLEWLW WDIACPIDLA DLPNIDIYEQ A // ID Q9JYE4_NEIMB Unreviewed; 134 AA. AC Q9JYE4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41971.1}; GN OrderedLocusNames=NMB1619 {ECO:0000313|EMBL:AAF41971.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41971.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41971.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41971.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41971.1; -; Genomic_DNA. DR PIR; A81062; A81062. DR RefSeq; NP_274625.1; NC_003112.2. DR RefSeq; WP_002225008.1; NC_003112.2. DR ProteinModelPortal; Q9JYE4; -. DR STRING; 122586.NMB1619; -. DR PaxDb; Q9JYE4; -. DR EnsemblBacteria; AAF41971; AAF41971; NMB1619. DR GeneID; 904072; -. DR KEGG; nme:NMB1619; -. DR PATRIC; 20359138; VBINeiMen85645_2080. DR eggNOG; ENOG4105KUA; Bacteria. DR eggNOG; COG0537; LUCA. DR HOGENOM; HOG000061066; -. DR OMA; FGNMVPH; -. DR OrthoDB; EOG6MM1NC; -. DR BioCyc; NMEN122586:GHGG-1668-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR InterPro; IPR026026; HIT_Hint. DR PANTHER; PTHR23089; PTHR23089; 1. DR Pfam; PF01230; HIT; 1. DR PIRSF; PIRSF000714; HIT; 1. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS51084; HIT_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 106 HIT. {ECO:0000259|PROSITE:PS51084}. SQ SEQUENCE 134 AA; 15191 MW; CFE42F875DB4D79D CRC64; MTAQPCPICT AQNEDVLLQT PNLRVIAVHN DSGSPAFCRV IWRKHIAEMT DLSAAERGEL MEMVYKVEAA MRQVFRPAKI NLASLGNVVP HLHWHIIARF ENDASFPAPI WANPVRKHGM TLPQDWTEQL KKLL // ID Q7DD46_NEIMB Unreviewed; 349 AA. AC Q7DD46; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42402.1}; GN OrderedLocusNames=NMB2085 {ECO:0000313|EMBL:AAF42402.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42402.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42402.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42402.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42402.1; -; Genomic_DNA. DR PIR; C81007; C81007. DR RefSeq; NP_275073.1; NC_003112.2. DR RefSeq; WP_002215055.1; NC_003112.2. DR ProteinModelPortal; Q7DD46; -. DR STRING; 122586.NMB2085; -. DR PaxDb; Q7DD46; -. DR EnsemblBacteria; AAF42402; AAF42402; NMB2085. DR GeneID; 903967; -. DR KEGG; nme:NMB2085; -. DR PATRIC; 20360336; VBINeiMen85645_2665. DR eggNOG; ENOG4108DNM; Bacteria. DR eggNOG; ENOG410ZRZQ; LUCA. DR HOGENOM; HOG000004258; -. DR OMA; SVLFWDE; -. DR OrthoDB; EOG6MWNC1; -. DR BioCyc; NMEN122586:GHGG-2150-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13304; AAA_21; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 29 291 ATPase_AAA_core. FT {ECO:0000259|Pfam:PF13304}. SQ SEQUENCE 349 AA; 39428 MW; D72F89A7889693CF CRC64; MSSNQYIQSL ELTNFTVLPN DTFEFSENLN VIVAENGCGK THLLKILYSL LEVTSNTKNR LLKTELQKSF ADKLLNVFRP DSLGRLSKRL QGRGRTEIVL KLQNGTTHSS LNFSSNSSSQ VNVQSIGLKE NEYTPTPIFL PSRELITLCP WFTSLYQNQS IPFEETWFDT CMQLNHPLAK GPRETKIREL LEPIENAMGG KVSEEQGRFY LSLTNTGGKI EAPLVAEGLR KFVMIARLIA TGALLDKGYL FWDEPEANLN PKLIKVAARI IWSLSQQGIQ VFIATHSLFL LRELELLKLE NNTDLPVRFF SLIASDDGTK VEQGNSINDL NTLILLDENI MQADRYLNI // ID Q9K195_NEIMB Unreviewed; 98 AA. AC Q9K195; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40726.1}; GN OrderedLocusNames=NMB0272 {ECO:0000313|EMBL:AAF40726.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40726.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40726.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40726.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40726.1; -; Genomic_DNA. DR PIR; A81219; A81219. DR PaxDb; Q9K195; -. DR EnsemblBacteria; AAF40726; AAF40726; NMB0272. DR PATRIC; 20355630; VBINeiMen85645_0339. DR HOGENOM; HOG000220685; -. DR OMA; MFTCIIA; -. DR OrthoDB; EOG65TRWG; -. DR BioCyc; NMEN122586:GHGG-287-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 96 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 11815 MW; 69042E3103753FEC CRC64; MNKKLNYIFM LDCLGLVILF TCIIATFERD YGFKIFTNSK RPEFYYWIGM FYYGIISCWF DYQLISTKAN SYKRKVKQYK IFSVIFSVLI FISTIVKL // ID Q9K087_NEIMB Unreviewed; 75 AA. AC Q9K087; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41144.1}; GN OrderedLocusNames=NMB0731 {ECO:0000313|EMBL:AAF41144.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41144.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41144.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41144.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41144.1; -; Genomic_DNA. DR PIR; F81166; F81166. DR RefSeq; NP_273773.1; NC_003112.2. DR RefSeq; WP_002244062.1; NC_003112.2. DR STRING; 122586.NMB0731; -. DR PaxDb; Q9K087; -. DR EnsemblBacteria; AAF41144; AAF41144; NMB0731. DR GeneID; 902844; -. DR KEGG; nme:NMB0731; -. DR PATRIC; 20356819; VBINeiMen85645_0930. DR HOGENOM; HOG000218855; -. DR OMA; PNEELCI; -. DR OrthoDB; EOG6QK4XV; -. DR BioCyc; NMEN122586:GHGG-760-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 74 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 75 AA; 8634 MW; EEF4CC224D200058 CRC64; MNVWYIWDRM VEIYHKYKKP CLVLAVDFVM GMVFIEPNEE PCIGRCYAPM SESPDFANAV AMAVAMICIV WIAVL // ID Q9K0N2_NEIMB Unreviewed; 228 AA. AC Q9K0N2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Putative repressor protein {ECO:0000313|EMBL:AAF40984.1}; GN OrderedLocusNames=NMB0556 {ECO:0000313|EMBL:AAF40984.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40984.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40984.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40984.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40984.1; -; Genomic_DNA. DR PIR; B81186; B81186. DR RefSeq; NP_273600.1; NC_003112.2. DR RefSeq; WP_002225569.1; NC_003112.2. DR ProteinModelPortal; Q9K0N2; -. DR STRING; 122586.NMB0556; -. DR PaxDb; Q9K0N2; -. DR EnsemblBacteria; AAF40984; AAF40984; NMB0556. DR GeneID; 902671; -. DR KEGG; nme:NMB0556; -. DR PATRIC; 20356383; VBINeiMen85645_0711. DR eggNOG; ENOG4105M7P; Bacteria. DR eggNOG; COG2932; LUCA. DR HOGENOM; HOG000008672; -. DR OMA; VGHEEPV; -. DR OrthoDB; EOG6TBHDR; -. DR BioCyc; NMEN122586:GHGG-582-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF00717; Peptidase_S24; 1. DR SUPFAM; SSF51306; SSF51306; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 142 207 Peptidase_S24. FT {ECO:0000259|Pfam:PF00717}. SQ SEQUENCE 228 AA; 25784 MW; 53629B80460B3CA4 CRC64; METFKDRLVF LWKSEARQAK IASDIEMTIA GFSRIWNEGG LPKSETLKKI KQLKGCSIDW LLTGEGNPFP DEAPKKSLAY DTLGNEVDTD EFVFVPRYDI RAAAGYGQFV DHEEPVFTMA FRRHWIENYV TRDTKNLSVI SVKGDSMEGV LNDGDSILVN HGENTPRDGL YVLRINENLL VKRLQIVPGG IINVISANEA YPAFEINLND LTDDVEIIGR VEWFGRTI // ID Q9JZJ1_NEIMB Unreviewed; 465 AA. AC Q9JZJ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|RuleBase:RU362017}; DE Short=Aspartase {ECO:0000256|RuleBase:RU362017}; DE EC=4.3.1.1 {ECO:0000256|RuleBase:RU362017}; GN Name=aspA {ECO:0000313|EMBL:AAF41428.1}; GN OrderedLocusNames=NMB1029 {ECO:0000313|EMBL:AAF41428.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41428.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41428.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41428.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: L-aspartate = fumarate + NH(3). CC {ECO:0000256|RuleBase:RU362017}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Aspartase subfamily. {ECO:0000256|RuleBase:RU362017}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41428.1; -; Genomic_DNA. DR PIR; C81130; C81130. DR RefSeq; NP_274063.1; NC_003112.2. DR RefSeq; WP_002217106.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ1; -. DR SMR; Q9JZJ1; 3-456. DR STRING; 122586.NMB1029; -. DR PaxDb; Q9JZJ1; -. DR EnsemblBacteria; AAF41428; AAF41428; NMB1029. DR GeneID; 903166; -. DR KEGG; nme:NMB1029; -. DR PATRIC; 20357593; VBINeiMen85645_1313. DR eggNOG; ENOG4108IJ0; Bacteria. DR eggNOG; COG1027; LUCA. DR HOGENOM; HOG000061737; -. DR KO; K01744; -. DR OMA; EICENYV; -. DR OrthoDB; EOG6V1M4M; -. DR BioCyc; NMEN122586:GHGG-1066-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR004708; ApsA. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00839; aspA; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000256|SAAS:SAAS00429438, KW ECO:0000313|EMBL:AAF41428.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 12 343 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 409 461 FumaraseC_C. {ECO:0000259|Pfam:PF10415}. SQ SEQUENCE 465 AA; 50762 MW; B910F8D332D353A3 CRC64; MTVRIEHDLL GDREIPAEVY WGIHTLRAIE NFKISTQKIS DVPQFVRSMV MVKKATAQAN GELGAVKPEI AAAIEKACDE VLLNNRCLDQ FPSDVYQGGA GTSVNMNTNE VIANLALEVL GYEKGRYDIV NPMDHVNASQ STNDAYPTGF RLAVYYSIGE LLDKLTVLKN AFAAKAEEFK DVLKMGRTQL QDAVPMTAGQ EFQSFQVLLE EEILNLDRTR QLLLEVNLGA TAIGTGVNTP KGYAELVVKK LSEVSGLPCK LTENLIEATS DCGAYVMVHG ALKRTAVKLS KICNDLRLLS SGPRAGLKEI NLPELQAGSS IMPAKVNPVI PEVVNQVCFK VIGNDTTITF AAEAGQLQLN VMEPVIAQCM FETISLLGNA AVNLSDKCVK GITVNREICE RYVFNSIGLV TYLNPYIGHH NGDLVGKICA QTGKGVREVV LERGLLSEEE LNRILSPENL MNPHL // ID Q9K182_NEIMB Unreviewed; 204 AA. AC Q9K182; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40738.1}; GN OrderedLocusNames=NMB0286 {ECO:0000313|EMBL:AAF40738.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40738.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40738.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40738.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40738.1; -; Genomic_DNA. DR PIR; E81216; E81216. DR RefSeq; NP_273341.1; NC_003112.2. DR RefSeq; WP_002224851.1; NC_003112.2. DR ProteinModelPortal; Q9K182; -. DR STRING; 122586.NMB0286; -. DR PaxDb; Q9K182; -. DR EnsemblBacteria; AAF40738; AAF40738; NMB0286. DR GeneID; 902397; -. DR KEGG; nme:NMB0286; -. DR PATRIC; 20355672; VBINeiMen85645_0360. DR eggNOG; ENOG4105W74; Bacteria. DR eggNOG; COG2979; LUCA. DR HOGENOM; HOG000275690; -. DR OMA; GKTEETY; -. DR OrthoDB; EOG6JX7NH; -. DR BioCyc; NMEN122586:GHGG-301-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3680.10; -; 1. DR InterPro; IPR029024; TerB-like. DR InterPro; IPR007486; YebE. DR Pfam; PF04391; DUF533; 1. DR SUPFAM; SSF158682; SSF158682; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 204 AA; 22063 MW; 540F72A3E08346C5 CRC64; MNFTRLLNQV LSTVQKKGNT FSDSPLNSFG GGALVAGVAS MLLNGKNRKT ITKIGSTAAL GYLAYRGYQM WQQNKGRATV TQSDFQPAGE TEETYSRTVL RTMIAAAASD GMIDEAERRT IEQESGTDPE TAAWLAAEYR LPASIEDIAA AVGNDEALAA EAYLAARLVC ADLSRKETVF LARLSQALKL DDNLVESLER QLGF // ID Q9JXZ5_NEIMB Unreviewed; 278 AA. AC Q9JXZ5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42159.1}; GN OrderedLocusNames=NMB1824 {ECO:0000313|EMBL:AAF42159.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42159.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42159.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42159.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42159.1; -; Genomic_DNA. DR PIR; A81040; A81040. DR RefSeq; NP_274821.1; NC_003112.2. DR RefSeq; WP_002225658.1; NC_003112.2. DR ProteinModelPortal; Q9JXZ5; -. DR STRING; 122586.NMB1824; -. DR PaxDb; Q9JXZ5; -. DR EnsemblBacteria; AAF42159; AAF42159; NMB1824. DR GeneID; 903276; -. DR KEGG; nme:NMB1824; -. DR PATRIC; 20359633; VBINeiMen85645_2322. DR eggNOG; ENOG4105DB7; Bacteria. DR eggNOG; COG0613; LUCA. DR HOGENOM; HOG000248104; -. DR KO; K07053; -. DR OMA; TRAHYAR; -. DR OrthoDB; EOG6KMB5P; -. DR BioCyc; NMEN122586:GHGG-1879-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|SAAS:SAAS00467137}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 67 POLIIIAc. {ECO:0000259|SMART:SM00481}. SQ SEQUENCE 278 AA; 30217 MW; 81AEE0B27D073B6A CRC64; MIDLHCHSTV SDGMLSPAEV VRLAHQNGCT LLALTDHDHT GGIAEARAEA DKLGLRLING VEISVTWRGR TIHVVGLDFD EQDENLQNLL AQVRKGRLKR LEAIAAKLEK KGIGGAYDGA LALAANKEMV SRTHVAEFLI QAGHVKNKQQ AFTKYLGDGK SCAVRHEWAT LEDCVSAVNG AGGMAVIAHP MRYDLSATAK RNLFEEFKNL GGAGIEVHSG NCCKNDRLNY ALLAERFGML ASAGSDFHRL NDFSGGILGA CPELPENCKP VWEHFSRY // ID Q9JY57_NEIMB Unreviewed; 142 AA. AC Q9JY57; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42072.1}; GN OrderedLocusNames=NMB1727 {ECO:0000313|EMBL:AAF42072.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42072.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42072.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42072.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42072.1; -; Genomic_DNA. DR PIR; F81048; F81048. DR RefSeq; NP_274730.1; NC_003112.2. DR RefSeq; WP_002220419.1; NC_003112.2. DR ProteinModelPortal; Q9JY57; -. DR SMR; Q9JY57; 1-141. DR PaxDb; Q9JY57; -. DR EnsemblBacteria; AAF42072; AAF42072; NMB1727. DR GeneID; 903372; -. DR KEGG; nme:NMB1727; -. DR PATRIC; 20359417; VBINeiMen85645_2214. DR eggNOG; ENOG4105WA2; Bacteria. DR eggNOG; COG3453; LUCA. DR HOGENOM; HOG000145987; -. DR OMA; DEFPRPM; -. DR OrthoDB; EOG6CGCF5; -. DR BioCyc; NMEN122586:GHGG-1782-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR005939; Beta-lactam_hydrolase-like. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR Pfam; PF04273; DUF442; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR TIGRFAMs; TIGR01244; TIGR01244; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 142 AA; 16228 MW; 488580790EF6CBD6 CRC64; MAILKLDEHL YISPQLTKAD AEQIAQLGIK TVICNRPDRE EESQPDFAQI KQWLEQAGVT GFHHQPVTAR DIQKHDVETF RQLIGQAEYP VLAYCRTGTR CSLLWGFRRA AEGMPVDEII RRAQAAGVNL ENFRERLDNA RV // ID Q9K0H0_NEIMB Unreviewed; 321 AA. AC Q9K0H0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41058.1}; GN OrderedLocusNames=NMB0635 {ECO:0000313|EMBL:AAF41058.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41058.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41058.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41058.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41058.1; -; Genomic_DNA. DR PIR; H81174; H81174. DR RefSeq; NP_273678.1; NC_003112.2. DR RefSeq; WP_002223479.1; NC_003112.2. DR ProteinModelPortal; Q9K0H0; -. DR STRING; 122586.NMB0635; -. DR PaxDb; Q9K0H0; -. DR EnsemblBacteria; AAF41058; AAF41058; NMB0635. DR GeneID; 902746; -. DR KEGG; nme:NMB0635; -. DR PATRIC; 20356569; VBINeiMen85645_0804. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; FHHERIA; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-661-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38031 MW; 9FBEC2A7AF127FBA CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS RTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JYJ7_NEIMB Unreviewed; 556 AA. AC Q9JYJ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:AAF41909.1}; DE EC=6.2.1.3 {ECO:0000313|EMBL:AAF41909.1}; GN Name=fadD-2 {ECO:0000313|EMBL:AAF41909.1}; GN OrderedLocusNames=NMB1555 {ECO:0000313|EMBL:AAF41909.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41909.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41909.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41909.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41909.1; -; Genomic_DNA. DR PIR; H81068; H81068. DR RefSeq; NP_274562.1; NC_003112.2. DR RefSeq; WP_002225041.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ7; -. DR STRING; 122586.NMB1555; -. DR PaxDb; Q9JYJ7; -. DR EnsemblBacteria; AAF41909; AAF41909; NMB1555. DR GeneID; 904112; -. DR KEGG; nme:NMB1555; -. DR PATRIC; 20358964; VBINeiMen85645_2001. DR eggNOG; ENOG4105CEY; Bacteria. DR eggNOG; COG0318; LUCA. DR HOGENOM; HOG000229983; -. DR KO; K01897; -. DR OMA; FIGDRMD; -. DR OrthoDB; EOG6MH5BV; -. DR BioCyc; NMEN122586:GHGG-1596-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF41909.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 29 461 AMP-binding. {ECO:0000259|Pfam:PF00501}. FT DOMAIN 470 544 AMP-binding_C. FT {ECO:0000259|Pfam:PF13193}. SQ SEQUENCE 556 AA; 61498 MW; FB348E134BB73EA8 CRC64; MEKIWLDSYE KGVSAEIDIT QYNSVSDVFR QSVEKFADQP AFQNMGKTLT YAETGKLATD FASYLQNVLK LPRGERVAIM LPNVLQYPVA LFGILQAGLV AVNTNPLYTP RELEHQLKDS GATAIIVLEN FANTLELVLP RTQIKHVIVA SVGEMFGLLK GSLINFVIRK IKKMVPEYRI RETVSFQTAL KEGAKHVFQP VALNREDTAL LQYTGGTTGV AKGAVLSHGN ICANMLQAKE WIKNQLREGK ETVIAALPLY HIFALTVNLM IFANAGSKII LITNPRDMKG FIGELKKQRV NVFIGVNTLF NAMVNRPDFA EVDFSELRLT LGGGMATQKA VAEKWKKITG TPIVEAYGLT EASPGVCCNP LNIESYSGSI GLPVSSTEVE LRDANGKEVP VGQPGELWVK GPQVMQGYWN RPEETAKAID ARGFLETGDI AVMDEKGWLK LVDRKKDLVV VSGFNVYPNE IEEVIAHHGK VMEVACIGVP DEKTGEALKV FVVKKDPSLT KEELIAFCRT ELTAYKVPKN IEFRDELPKS NVGKILRREL RQSTGK // ID Q9JYF2_NEIMB Unreviewed; 253 AA. AC Q9JYF2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41962.1}; GN OrderedLocusNames=NMB1610 {ECO:0000313|EMBL:AAF41962.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41962.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41962.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41962.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41962.1; -; Genomic_DNA. DR PIR; H81062; H81062. DR RefSeq; NP_274616.1; NC_003112.2. DR RefSeq; WP_002225012.1; NC_003112.2. DR STRING; 122586.NMB1610; -. DR PaxDb; Q9JYF2; -. DR EnsemblBacteria; AAF41962; AAF41962; NMB1610. DR GeneID; 904310; -. DR KEGG; nme:NMB1610; -. DR PATRIC; 20359108; VBINeiMen85645_2066. DR HOGENOM; HOG000219045; -. DR OMA; QLNILNP; -. DR OrthoDB; EOG6CZQJ9; -. DR BioCyc; NMEN122586:GHGG-1658-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 253 AA; 29098 MW; 0366FC7D7938F8A2 CRC64; MDANKEPNWE KRLENLRQTR RMKAVPTYAP LSRPSETGTD APVPKLDDES RARVLKAYLK KWQEEHNAAV ADCGEEVETD PMIVLQENWL NAQASLQMSV SEKHIESRRR IRFDTKKDSV EFETGQIESG ENADEAESGT NEPAVSENGE NDAEETLMPV QINILNPKAV NRREVFCLSE QELTERLIKR LRPHLTDTVN GIIRTAVQKQ MAVFTYQLQQ MLHEQAGAVV EDVLEHDVRK ILNDIKYELK YKR // ID Q9JXG8_NEIMB Unreviewed; 309 AA. AC Q9JXG8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=Transcriptional regulator, LysR family {ECO:0000313|EMBL:AAF42375.1}; GN OrderedLocusNames=NMB2055 {ECO:0000313|EMBL:AAF42375.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42375.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42375.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42375.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:4AB5, ECO:0000213|PDB:4AB6} RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 90-309, AND DISULFIDE BONDS. RX PubMed=22750853; DOI=10.1107/S1744309112010603; RA Sainsbury S., Ren J., Saunders N.J., Stuart D.I., Owens R.J.; RT "Structure of the regulatory domain of the LysR family regulator RT NMB2055 (MetR-like protein) from Neisseria meningitidis."; RL Acta Crystallogr. F 68:730-737(2012). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42375.1; -; Genomic_DNA. DR PIR; H81011; H81011. DR RefSeq; NP_275045.1; NC_003112.2. DR RefSeq; WP_002225700.1; NC_003112.2. DR PDB; 4AB5; X-ray; 2.51 A; A/B=90-309. DR PDB; 4AB6; X-ray; 2.80 A; A/B=90-309. DR PDBsum; 4AB5; -. DR PDBsum; 4AB6; -. DR ProteinModelPortal; Q9JXG8; -. DR STRING; 122586.NMB2055; -. DR PaxDb; Q9JXG8; -. DR EnsemblBacteria; AAF42375; AAF42375; NMB2055. DR GeneID; 904026; -. DR KEGG; nme:NMB2055; -. DR PATRIC; 20360266; VBINeiMen85645_2633. DR eggNOG; ENOG4105DZ2; Bacteria. DR eggNOG; ENOG410XQG7; LUCA. DR HOGENOM; HOG000218906; -. DR KO; K03576; -. DR OMA; ACEHLPF; -. DR OrthoDB; EOG64BQ3T; -. DR BioCyc; NMEN122586:GHGG-2118-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4AB5, ECO:0000213|PDB:4AB6}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}; KW Transcription regulation {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523926}. FT DOMAIN 5 62 HTH lysR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50931}. FT DISULFID 103 106 {ECO:0000213|PDB:4AB5}. SQ SEQUENCE 309 AA; 34831 MW; 7086861A2DE26637 CRC64; MDSIIELRHL KTLLALEETG SVSLAAKRVF LTQSALSHQI RMLENHYGTP LFERKSTPLR FTPVGERLLR LAHELIPQVA VAEWDLARIT EGEAGELRIA VECHTCFDWL MPAMGEFRPM WPQVELDIVS GFQADPVGLL LQHRADLAIV SEAEKQNGIS FQPLFAYEMV GICAPDHPLA AKNVWTAEDF IGETLITYPV PDEMLDLPKK ILIPKNINPP RRHSELTIAI IQLVASRRGI AALPYWTVMP YLEKGYVVHR QITADGLQSK LYAAIRTEDT DKSYLNNFCQ IIRERGFADL PGLSELEPV // ID Q9K098_NEIMB Unreviewed; 138 AA. AC Q9K098; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Putative cytochrome {ECO:0000313|EMBL:AAF41130.1}; GN OrderedLocusNames=NMB0717 {ECO:0000313|EMBL:AAF41130.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41130.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41130.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41130.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41130.1; -; Genomic_DNA. DR PIR; B81167; B81167. DR RefSeq; NP_273759.1; NC_003112.2. DR RefSeq; WP_010980830.1; NC_003112.2. DR ProteinModelPortal; Q9K098; -. DR STRING; 122586.NMB0717; -. DR PaxDb; Q9K098; -. DR EnsemblBacteria; AAF41130; AAF41130; NMB0717. DR GeneID; 902829; -. DR KEGG; nme:NMB0717; -. DR PATRIC; 20356785; VBINeiMen85645_0914. DR eggNOG; ENOG41083GE; Bacteria. DR eggNOG; COG2010; LUCA. DR HOGENOM; HOG000217535; -. DR OMA; KETPMNT; -. DR OrthoDB; EOG6CGCHT; -. DR BioCyc; NMEN122586:GHGG-745-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR Pfam; PF13442; Cytochrome_CBB3; 1. DR SUPFAM; SSF46626; SSF46626; 1. DR PROSITE; PS51007; CYTC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 138 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329369. FT DOMAIN 30 118 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 138 AA; 14715 MW; 947903CE2CBE6F23 CRC64; MKETPMNTTR LPTALVLGCF CAAASAADNS IMTKGQKVYE SNCVACHGKK GEGRGTMFPP LYRSDFIMKK PQVLLHSMVK GINGTIKVNG KTYNGFMPAT AISDADIAAV ATYIMNAFDN GGGSVTEKDV KQAKSKKN // ID Q9JY42_NEIMB Unreviewed; 64 AA. AC Q9JY42; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42097.1}; GN OrderedLocusNames=NMB1756 {ECO:0000313|EMBL:AAF42097.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42097.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42097.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42097.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42097.1; -; Genomic_DNA. DR PIR; C81046; C81046. DR RefSeq; NP_274756.1; NC_003112.2. DR RefSeq; WP_002219748.1; NC_003112.2. DR STRING; 122586.NMB1756; -. DR PaxDb; Q9JY42; -. DR EnsemblBacteria; AAF42097; AAF42097; NMB1756. DR GeneID; 903342; -. DR KEGG; nme:NMB1756; -. DR BioCyc; NMEN122586:GHGG-1811-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7423 MW; 314A525CFFAE7D40 CRC64; MVLFKSIKQE SISFLSEDLK KDWMFHKVKT GEKDGYGSDE MLSVPRVYLE MMSRKTGVPY SSIL // ID Q9JXW6_NEIMB Unreviewed; 192 AA. AC Q9JXW6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Modulator of drug activity B {ECO:0000313|EMBL:AAF42191.1}; GN Name=mdaB {ECO:0000313|EMBL:AAF42191.1}; GN OrderedLocusNames=NMB1857 {ECO:0000313|EMBL:AAF42191.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42191.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42191.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42191.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42191.1; -; Genomic_DNA. DR PIR; F81035; F81035. DR RefSeq; NP_274853.1; NC_003112.2. DR RefSeq; WP_002223019.1; NC_003112.2. DR ProteinModelPortal; Q9JXW6; -. DR SMR; Q9JXW6; 1-192. DR STRING; 122586.NMB1857; -. DR PaxDb; Q9JXW6; -. DR EnsemblBacteria; AAF42191; AAF42191; NMB1857. DR GeneID; 903241; -. DR KEGG; nme:NMB1857; -. DR PATRIC; 20359739; VBINeiMen85645_2375. DR eggNOG; ENOG4105NF4; Bacteria. DR eggNOG; COG2249; LUCA. DR HOGENOM; HOG000063966; -. DR KO; K03923; -. DR OMA; PTFICND; -. DR OrthoDB; EOG6ZWJFM; -. DR BioCyc; NMEN122586:GHGG-1913-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 187 Flavodoxin_2. {ECO:0000259|Pfam:PF02525}. SQ SEQUENCE 192 AA; 21730 MW; 7BCD31CA1ECACB97 CRC64; MNILLLDGGK AFGHSHGGLN RTLHKKAKEV LTALGHNVQE TVIDAGYDVE AEIEKFVWMD AVIWQMPGWW MHEPWTVKKY IDEVLTAGHG KLYQSDGRHS VNPTEGYGTG GLLQGKKHMI SLTWNAPIEA FTREGDFFEG KGVDVLYMHF HKANEFLGMT RLPTFLCNDV VKNPQVEKYL ADYQAHLEKV FG // ID Q9K1D1_NEIMB Unreviewed; 34 AA. AC Q9K1D1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40686.1}; GN OrderedLocusNames=NMB0231 {ECO:0000313|EMBL:AAF40686.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40686.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40686.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40686.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40686.1; -; Genomic_DNA. DR PIR; H81223; H81223. DR RefSeq; NP_273288.1; NC_003112.2. DR RefSeq; WP_010980761.1; NC_003112.2. DR STRING; 122586.NMB0231; -. DR PaxDb; Q9K1D1; -. DR EnsemblBacteria; AAF40686; AAF40686; NMB0231. DR GeneID; 902342; -. DR KEGG; nme:NMB0231; -. DR OrthoDB; EOG6RVG65; -. DR BioCyc; NMEN122586:GHGG-246-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 34 AA; 4161 MW; F324B38D7EB31356 CRC64; MRYFNRNGLR SSEKVQRQGS TFPIDGLMMQ HRRY // ID Q9JYZ6_NEIMB Unreviewed; 336 AA. AC Q9JYZ6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=Putative CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:AAF41733.1}; GN OrderedLocusNames=NMB1359 {ECO:0000313|EMBL:AAF41733.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41733.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41733.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41733.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000256|RuleBase:RU000392}. CC -!- SIMILARITY: Contains FAD-binding FR-type domain. CC {ECO:0000256|SAAS:SAAS00264105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41733.1; -; Genomic_DNA. DR PIR; H81091; H81091. DR RefSeq; NP_274377.1; NC_003112.2. DR RefSeq; WP_002217007.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ6; -. DR STRING; 122586.NMB1359; -. DR PaxDb; Q9JYZ6; -. DR EnsemblBacteria; AAF41733; AAF41733; NMB1359. DR GeneID; 903781; -. DR KEGG; nme:NMB1359; -. DR PATRIC; 20358377; VBINeiMen85645_1700. DR eggNOG; ENOG4108JA0; Bacteria. DR eggNOG; COG0543; LUCA. DR HOGENOM; HOG000263662; -. DR KO; K00523; -. DR OMA; RTGFVHE; -. DR OrthoDB; EOG6Q5NS6; -. DR BioCyc; NMEN122586:GHGG-1397-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR001221; Phe_hydroxylase. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00410; PHEHYDRXLASE. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU000392, ECO:0000256|SAAS:SAAS00436776}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU000392, ECO:0000256|SAAS:SAAS00436776}; KW Iron-sulfur {ECO:0000256|RuleBase:RU000392, KW ECO:0000256|SAAS:SAAS00436776}; KW Metal-binding {ECO:0000256|RuleBase:RU000392, KW ECO:0000256|SAAS:SAAS00436776}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 92 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 93 200 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. SQ SEQUENCE 336 AA; 36553 MW; 306E0BCA534A688F CRC64; MNHTVTLPDQ TTFAANDGET VLTAAARQNL NLPHSCKSGV CGQCKAELVS GDIQMGGHSE QALSEAEKAQ GKILMCCTTA QSDININIPG YKADALPVRT LPARIESIIF KHDVALLKLA LPKAPPFAFY AGQYIDLLLP GNVSRSYSIA NLPDQEGILE LHIRRHENGV CSEMIFGSEP KVKEKGIVRV KGPLGSFTLQ EDSGKPVILL ATGTGYAPIR SILLDLIRQG SNRAVHFYWG ARHQDDLYAL EEAQGLACRL KNACFTPVLS RPGEGWQGRN GHVQDIAAQD HPDLSEYEVF ACGSPAMTEQ TKNLFVQQHK LPENLFFSDA FTPSAS // ID Q9JZM2_NEIMB Unreviewed; 54 AA. AC Q9JZM2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41392.1}; GN OrderedLocusNames=NMB0989 {ECO:0000313|EMBL:AAF41392.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41392.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41392.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41392.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41392.1; -; Genomic_DNA. DR PIR; F81135; F81135. DR RefSeq; NP_274025.1; NC_003112.2. DR RefSeq; WP_002225298.1; NC_003112.2. DR RefSeq; YP_008920711.1; NC_003112.2. DR STRING; 122586.NMB0989; -. DR PaxDb; Q9JZM2; -. DR EnsemblBacteria; AAF41392; AAF41392; NMB0989. DR GeneID; 17925334; -. DR GeneID; 903109; -. DR KEGG; nme:NMB0989; -. DR KEGG; nme:NMB1083a; -. DR PATRIC; 20357475; VBINeiMen85645_1252. DR HOGENOM; HOG000218908; -. DR OrthoDB; EOG6M3PMQ; -. DR BioCyc; NMEN122586:GHGG-1026-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 54 AA; 6197 MW; D526380EC6F76A40 CRC64; MGQVAFYEKM IGLWSAKSRE ASEQADLAAF EFAEGELANY REMLKRHLQT KSVE // ID Q9JXF4_NEIMB Unreviewed; 47 AA. AC Q9JXF4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42391.1}; GN OrderedLocusNames=NMB2072 {ECO:0000313|EMBL:AAF42391.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42391.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42391.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42391.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42391.1; -; Genomic_DNA. DR PIR; G81008; G81008. DR RefSeq; NP_275062.1; NC_003112.2. DR RefSeq; WP_010981024.1; NC_003112.2. DR STRING; 122586.NMB2072; -. DR PaxDb; Q9JXF4; -. DR EnsemblBacteria; AAF42391; AAF42391; NMB2072. DR GeneID; 903995; -. DR KEGG; nme:NMB2072; -. DR BioCyc; NMEN122586:GHGG-2135-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 47 AA; 5423 MW; BDAC119A121BCD21 CRC64; MEKPAGKPCR PSRCRNQRNT RPPRCAGCRA SPKYGNRRSV LLLFEYT // ID Q4W583_NEIMB Unreviewed; 116 AA. AC Q4W583; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Site-specific DNA methylase, truncation {ECO:0000313|EMBL:AAY52156.1}; GN OrderedLocusNames=NMB0077 {ECO:0000313|EMBL:AAY52156.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52156.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52156.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52156.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52156.1; -; Genomic_DNA. DR ProteinModelPortal; Q4W583; -. DR STRING; 122586.NMB0077; -. DR PaxDb; Q4W583; -. DR EnsemblBacteria; AAY52156; AAY52156; NMB0077. DR PATRIC; 20355157; VBINeiMen85645_0112. DR HOGENOM; HOG000027827; -. DR OMA; LIENNDM; -. DR OrthoDB; EOG69WFFJ; -. DR BioCyc; NMEN122586:GHGG-83-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02086; MethyltransfD12; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAY52156.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAY52156.1}. SQ SEQUENCE 116 AA; 13313 MW; 3D30E16A3DF782A5 CRC64; MKMNKQYPKI NYIGNKEKIA SWICDQLPSD VDTVADVFSG GCSFAYEAKK RGYRVITNDI LAINYQIALA LIENNHETLN DDDVAMIFSG SPHAGFMSQR YAEKFYFHDE YQQLDL // ID Q7DD38_NEIMB Unreviewed; 114 AA. AC Q7DD38; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42431.1}; GN OrderedLocusNames=NMB2121 {ECO:0000313|EMBL:AAF42431.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42431.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42431.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42431.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42431.1; -; Genomic_DNA. DR PIR; B81005; B81005. DR RefSeq; NP_275107.1; NC_003112.2. DR RefSeq; WP_002215116.1; NC_003112.2. DR STRING; 122586.NMB2121; -. DR PaxDb; Q7DD38; -. DR EnsemblBacteria; AAF42431; AAF42431; NMB2121. DR GeneID; 903454; -. DR KEGG; nme:NMB2121; -. DR PATRIC; 20360416; VBINeiMen85645_2704. DR HOGENOM; HOG000218702; -. DR OMA; MEFEGFF; -. DR OrthoDB; EOG6J74XJ; -. DR BioCyc; NMEN122586:GHGG-2186-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 114 AA; 13882 MW; 7ED3DA2A963DB28D CRC64; MNLENYENIL IKLLFYHNNL VNEYSYFIEN KNLFKIVSRT KTSKGFFFTI EKPLNFLSKK TYFEFNFKYL HSGKERFGSF MCWINTNLME FEGVFFNDLL PDNMIINNFF EIND // ID Q7DDL7_NEIMB Unreviewed; 352 AA. AC Q7DDL7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 80. DE SubName: Full=Modification methylase HgaI-1 {ECO:0000313|EMBL:AAF41138.1}; GN OrderedLocusNames=NMB0725 {ECO:0000313|EMBL:AAF41138.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41138.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41138.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41138.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41138.1; -; Genomic_DNA. DR RefSeq; NP_273767.1; NC_003112.2. DR RefSeq; WP_002222757.1; NC_003112.2. DR ProteinModelPortal; Q7DDL7; -. DR STRING; 122586.NMB0725; -. DR PaxDb; Q7DDL7; -. DR EnsemblBacteria; AAF41138; AAF41138; NMB0725. DR GeneID; 902838; -. DR KEGG; nme:NMB0725; -. DR PATRIC; 20356807; VBINeiMen85645_0924. DR eggNOG; ENOG41081PU; Bacteria. DR eggNOG; COG0270; LUCA. DR HOGENOM; HOG000086391; -. DR KO; K00558; -. DR OMA; IVANELI; -. DR OrthoDB; EOG6BKJ40; -. DR BioCyc; NMEN122586:GHGG-754-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00675; dcm; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000313|EMBL:AAF41138.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000313|EMBL:AAF41138.1}. FT DOMAIN 5 352 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 352 AA; 40061 MW; 175F8EB34AE41C92 CRC64; MMIGASLFSS AGIAETYLHN AGIKIIAANE LVPERANLYK ALYPESKMII GDILHEEVFQ NLIQSVPNRL DFLIASPPCQ GMSVAGKNRN IQEMANDKRN HLIFRVIEFI LLKRPTFVLI ENVPFFLKIK LPYKGTLQTV EVILQDLFGC EYYIQTHIFD SADYGVAQHR KRAIIRMNKH STIWGMPEKV TKTISVRDAI SFLPSIESGQ KSNVKWHFAR THAPEHIIWL KNTPTGRSAF DNIEHYPKKK NGEKIKSYNT TYRRMEWDAP APTITIRNDA ISSQLNVHPG RSMPDGTYSD ARVLTPLELM LLTSLPIDWN IPDDTSELLI RQCIGESIPP LLIKKIVERI GK // ID Q9JXU7_NEIMB Unreviewed; 195 AA. AC Q9JXU7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Transcriptional regulator, AraC family {ECO:0000313|EMBL:AAF42212.1}; GN OrderedLocusNames=NMB1878 {ECO:0000313|EMBL:AAF42212.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42212.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42212.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42212.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH araC/xylS-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00503533}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42212.1; -; Genomic_DNA. DR PIR; D81030; D81030. DR ProteinModelPortal; Q9JXU7; -. DR STRING; 122586.NMB1878; -. DR PaxDb; Q9JXU7; -. DR EnsemblBacteria; AAF42212; AAF42212; NMB1878. DR PATRIC; 20359789; VBINeiMen85645_2400. DR eggNOG; ENOG41081TV; Bacteria. DR eggNOG; COG2207; LUCA. DR OMA; PSAGEIX; -. DR OrthoDB; EOG63Z765; -. DR BioCyc; NMEN122586:GHGG-1934-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR Pfam; PF12833; HTH_18; 1. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 2. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}; KW Transcription regulation {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}. FT DOMAIN 98 195 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 195 AA; 22305 MW; 22E40A7BE7EF2DCF CRC64; MCALHLDFSL EKLRRWHDEG LLDERLFSPQ TIGRFALQRL AQNAAALTAA ACPLLQRPFE SDGFGLLADE AAALELSARL LRFTFRRHDN GYRRRRIDEA ADILQHEFAR PLTIAEIARR VGLNECYLKR YFKAQTGETV AGCLRRLRLE HALALIESGS TVQAAMHFCG YRHAGRFNEA FRRHYGFLPS DVKKC // ID Q7DDS2_NEIMB Unreviewed; 206 AA. AC Q7DDS2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40693.1}; GN OrderedLocusNames=NMB0239 {ECO:0000313|EMBL:AAF40693.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40693.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40693.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40693.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40693.1; -; Genomic_DNA. DR PIR; E81221; E81221. DR RefSeq; NP_273295.1; NC_003112.2. DR RefSeq; WP_002215603.1; NC_003112.2. DR STRING; 122586.NMB0239; -. DR PaxDb; Q7DDS2; -. DR EnsemblBacteria; AAF40693; AAF40693; NMB0239. DR GeneID; 902350; -. DR KEGG; nme:NMB0239; -. DR PATRIC; 20355554; VBINeiMen85645_0301. DR eggNOG; ENOG4107WTK; Bacteria. DR eggNOG; ENOG410XQ7D; LUCA. DR HOGENOM; HOG000218643; -. DR OMA; LAPYFGN; -. DR OrthoDB; EOG62NX0Q; -. DR BioCyc; NMEN122586:GHGG-254-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 198 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 206 AA; 22298 MW; EF4FA35A7B6E6CC9 CRC64; MNSTASKTLK GLSLVFFASG FCALIYQVSW QRLLFSHIGI DLSSITVIIS VFMVGLGVGA YFGGRIADRF PSSIIPLFCI AEVSIGLFGL VSRGLISGLG HLLVEADLPI IAAANFLLLL LPTFMMGATL PLLTCFFNRK IHNVGESIGT LYFFNTLGAA LGSLAAAEFF YVFFTLSQTI ALTACFNLLI AASVWLRYRK DGYSEH // ID Q9K172_NEIMB Unreviewed; 68 AA. AC Q9K172; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62307.1}; GN OrderedLocusNames=NMB0301 {ECO:0000313|EMBL:AAF62307.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62307.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62307.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62307.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62307.1; -; Genomic_DNA. DR PaxDb; Q9K172; -. DR EnsemblBacteria; AAF62307; AAF62307; NMB0301. DR PATRIC; 20355715; VBINeiMen85645_0377. DR OrthoDB; EOG6VF349; -. DR BioCyc; NMEN122586:GHGG-321-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 68 AA; 7764 MW; 755B895747EFB8C1 CRC64; MFDGAKVVRR VEGNLWVFGM VALEKTCFKG QMPSENRFQT AFSVYLKQTG KGSNILQSSY SHKRFIVN // ID Q9JYR2_NEIMB Unreviewed; 107 AA. AC Q9JYR2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41825.1}; GN OrderedLocusNames=NMB1468 {ECO:0000313|EMBL:AAF41825.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41825.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41825.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41825.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41825.1; -; Genomic_DNA. DR PIR; G81080; G81080. DR RefSeq; NP_274477.1; NC_003112.2. DR RefSeq; WP_002225099.1; NC_003112.2. DR STRING; 122586.NMB1468; -. DR PaxDb; Q9JYR2; -. DR EnsemblBacteria; AAF41825; AAF41825; NMB1468. DR GeneID; 903890; -. DR KEGG; nme:NMB1468; -. DR PATRIC; 20358701; VBINeiMen85645_1860. DR HOGENOM; HOG000027846; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NMEN122586:GHGG-1508-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 107 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327717. FT COILED 44 105 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 107 AA; 10855 MW; 42F26B60A14E0B8A CRC64; MKKLLIAAMM AAALAACSQE AKQEVKEAVQ AVESDVKDTA ASAAESAASA VEEAKDQVKD AAADAKASAE EAVTEAKEAV TEAAKDTLNK AADATQEAAD KMKDAAK // ID Q9JXX5_NEIMB Unreviewed; 114 AA. AC Q9JXX5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42182.1}; GN OrderedLocusNames=NMB1848 {ECO:0000313|EMBL:AAF42182.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42182.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42182.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42182.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42182.1; -; Genomic_DNA. DR PIR; E81034; E81034. DR STRING; 122586.NMB1848; -. DR PaxDb; Q9JXX5; -. DR EnsemblBacteria; AAF42182; AAF42182; NMB1848. DR eggNOG; ENOG4107JRT; Bacteria. DR eggNOG; ENOG4112323; LUCA. DR HOGENOM; HOG000198792; -. DR OMA; SGIPISY; -. DR OrthoDB; EOG6KT2N3; -. DR BioCyc; NMEN122586:GHGG-1904-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 114 AA; 11347 MW; 0CC00D75C7F58B23 CRC64; MGIPESSGIP ESSGIPESSG IPESSGIPES SGIPESSGIP ESSGIPESSG IPESSGIPES SGIPESSGIP ESSGIPESSG IPESSGIPES SGIPEPSFPR RRESRPVGAE TYRV // ID Q9JZR8_NEIMB Unreviewed; 273 AA. AC Q9JZR8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=Oxidoreductase, short-chain dehydrogenase/reductase family {ECO:0000313|EMBL:AAF41332.1}; GN OrderedLocusNames=NMB0924 {ECO:0000313|EMBL:AAF41332.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41332.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41332.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41332.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000256|RuleBase:RU000363}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41332.1; -; Genomic_DNA. DR PIR; H81140; H81140. DR RefSeq; NP_273964.1; NC_003112.2. DR RefSeq; WP_002222631.1; NC_003112.2. DR ProteinModelPortal; Q9JZR8; -. DR STRING; 122586.NMB0924; -. DR PaxDb; Q9JZR8; -. DR EnsemblBacteria; AAF41332; AAF41332; NMB0924. DR GeneID; 903045; -. DR KEGG; nme:NMB0924; -. DR PATRIC; 20357297; VBINeiMen85645_1162. DR eggNOG; ENOG4105EMU; Bacteria. DR eggNOG; COG4221; LUCA. DR KO; K00540; -. DR OMA; DWENMID; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NMEN122586:GHGG-962-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 273 AA; 30119 MW; 24411163F8E4A1F2 CRC64; MAVLITGASA GFGEAMCRAF VGAGYRVIGA ARRADRLQAL ADELGALFYP LEMDVSRRES VENALNGIPD EFSDIDCLIN NAGLALGLDT ADKADFEDWE TMIQTNVLGL TFLTRKILPQ MVERGGGYVM NLGSIAGNYA YAGSNVYGAT KAFVRQFSLN LRAELADKNI RVTNIEPGLC GNTEFSNVRF KGDDERAAGV YEGVEFIRPE DIAETALWLY QRPAHMNVNT IEIMPVAQTF AGMKVIKKAV PEVREDFEKQ SMSLFSRIRS WFK // ID Q9JYR4_NEIMB Unreviewed; 243 AA. AC Q9JYR4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41823.1}; GN OrderedLocusNames=NMB1466 {ECO:0000313|EMBL:AAF41823.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41823.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41823.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41823.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41823.1; -; Genomic_DNA. DR PIR; E81080; E81080. DR RefSeq; NP_274475.1; NC_003112.2. DR RefSeq; WP_002225101.1; NC_003112.2. DR STRING; 122586.NMB1466; -. DR PaxDb; Q9JYR4; -. DR DNASU; 903888; -. DR EnsemblBacteria; AAF41823; AAF41823; NMB1466. DR GeneID; 903888; -. DR KEGG; nme:NMB1466; -. DR PATRIC; 20358695; VBINeiMen85645_1857. DR eggNOG; ENOG4105EF5; Bacteria. DR eggNOG; ENOG410XR26; LUCA. DR HOGENOM; HOG000220756; -. DR KO; K07280; -. DR OMA; ARYGSHM; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NMEN122586:GHGG-1506-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 243 AA; 28228 MW; 1A95DC6A1CB750BA CRC64; MSREINAGRH HFLYGGISGG GVHYWDNKDF SEQSLRLSFG YKNRSVTRSF GIVPFVEQNL LGGSRYNFVG GFNADFSQRL SERWRLTLNA GNMWKHYQED RTAARYDSHM PLAGATLMYS APKDWLLYGG ADWSHNITKE AEQASIRKGL RVGAVKTFDG GLGLRANLRY TRRMFDAPGT IVYRFPRKDH EYQANLSLWH DKISWKGFTP QLNFRYLKID SNMKSFYTRK NMQIFMSVEK DFK // ID Q9JZP8_NEIMB Unreviewed; 587 AA. AC Q9JZP8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|RuleBase:RU362051}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051}; GN Name=sdhA {ECO:0000313|EMBL:AAF41356.1}; GN OrderedLocusNames=NMB0950 {ECO:0000313|EMBL:AAF41356.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41356.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41356.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41356.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC {ECO:0000256|RuleBase:RU362051}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU362051}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC fumarate from succinate (bacterial route): step 1/1. CC {ECO:0000256|RuleBase:RU362051}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU362051}; Cytoplasmic side CC {ECO:0000256|RuleBase:RU362051}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU362051}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41356.1; -; Genomic_DNA. DR PIR; F81138; F81138. DR RefSeq; NP_273988.1; NC_003112.2. DR RefSeq; WP_010980875.1; NC_003112.2. DR ProteinModelPortal; Q9JZP8; -. DR SMR; Q9JZP8; 1-587. DR STRING; 122586.NMB0950; -. DR PaxDb; Q9JZP8; -. DR PRIDE; Q9JZP8; -. DR EnsemblBacteria; AAF41356; AAF41356; NMB0950. DR GeneID; 903070; -. DR KEGG; nme:NMB0950; -. DR PATRIC; 20357383; VBINeiMen85645_1206. DR eggNOG; ENOG4105C00; Bacteria. DR eggNOG; COG1053; LUCA. DR HOGENOM; HOG000160475; -. DR KO; K00239; -. DR OMA; PSVYEIG; -. DR OrthoDB; EOG6M3PC4; -. DR BioCyc; NMEN122586:GHGG-987-MONOMER; -. DR UniPathway; UPA00223; UER01005. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR030664; SdhA/FrdA/AprA. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. DR InterPro; IPR011281; Succ_DH_flav_su_fwd. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF56425; SSF56425; 1. DR TIGRFAMs; TIGR01816; sdhA_forward; 1. DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU362051}; KW Cell membrane {ECO:0000256|RuleBase:RU362051}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|RuleBase:RU362051}; KW FAD {ECO:0000256|RuleBase:RU362051}; KW Flavoprotein {ECO:0000256|RuleBase:RU362051}; KW Membrane {ECO:0000256|RuleBase:RU362051}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362051, KW ECO:0000313|EMBL:AAF41356.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transport {ECO:0000256|RuleBase:RU362051}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}. FT DOMAIN 9 404 FAD_binding_2. FT {ECO:0000259|Pfam:PF00890}. FT DOMAIN 459 587 Succ_DH_flav_C. FT {ECO:0000259|Pfam:PF02910}. SQ SEQUENCE 587 AA; 64502 MW; 9581701B08069003 CRC64; MGFPVRKFDA VIVGGGGAGL RAALQLSKSG LNCAVLSKVF PTRSHTVAAQ GGISASLGNV QEDRWDWHMY DTVKGSDWLG DQDAIEFMCR AAPEAVIELE HMGMPFDRVE SGKIYQRPFG GHTAEHGKRA VERACAVADR TGHAMLHTLY QQNVRANTQF FVEWTAQDLI RDENGDVVGV TAMEMETGEV YIFHAKAVMF ATGGGGRIYA SSTNAYMNTG DGLGICARAG IPLEDMEFWQ FHPTGVAGAG VLITEGVRGE GGILLNADGE RFMERYAPTV KDLASRDVVS RAMAMEIYEG RGCGKNKDHV LLKIDHIGAE KIMEKLPGIR EISIQFAGID PIKDPIPVVP TTHYMMGGIP TNYHGEVVVP QGEDYEVPVK GLYAAGECAC ASVHGANRLG TNSLLDLVVF GKAAGDSMIK FIKEQSDWKP LPANAGELTR QRIERLDNQT DGENVDALRR ELQRSVQLHA GVFRTDEILS KGVREVMAIA ERVKRTEIKD KSKVWNTARI EALELDNLIE VAKATLVSAE ARKESRGAHA SDDHPERDDE NWMKHTLYHS DINTLSYKPV HTKPLSVEYI KPAKRVY // ID Q9JY82_NEIMB Unreviewed; 252 AA. AC Q9JY82; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:AAF42046.1}; GN OrderedLocusNames=NMB1698 {ECO:0000313|EMBL:AAF42046.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42046.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42046.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42046.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42046.1; -; Genomic_DNA. DR PIR; D81052; D81052. DR RefSeq; NP_274702.1; NC_003112.2. DR RefSeq; WP_002222117.1; NC_003112.2. DR ProteinModelPortal; Q9JY82; -. DR STRING; 122586.NMB1698; -. DR PaxDb; Q9JY82; -. DR DNASU; 903405; -. DR EnsemblBacteria; AAF42046; AAF42046; NMB1698. DR GeneID; 903405; -. DR KEGG; nme:NMB1698; -. DR PATRIC; 20359353; VBINeiMen85645_2183. DR eggNOG; ENOG4108AZT; Bacteria. DR eggNOG; COG0204; LUCA. DR HOGENOM; HOG000282170; -. DR OMA; GQMIIAN; -. DR OrthoDB; EOG6F55DN; -. DR BioCyc; NMEN122586:GHGG-1753-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAF42046.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42046.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 36 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 85 193 PlsC. {ECO:0000259|SMART:SM00563}. SQ SEQUENCE 252 AA; 28477 MW; 846C2B564480F04C CRC64; MDKLDYCRRF FATWLGFVIF GVGGIMMKLV LLPYTLNGTS GSVARQLAAR RIIGTSWRLF VAYLKWSGVL EVSFKGVEKL NRPGQLILAN HPSLLDVVLL VGHVPEMNCI VKKDLQHNPA MSSQIKGAGY IPNEESEAML ETVKAVFDSG QSLLVFPEGT RTGWDGRVKM HRGAVSLGLR YAEVITPVCI KMNPPNFKKG QPWYRIPPKR IRYEITVGDD ILPQDWLAEK PLPIAARRLN EYLQDYFTRK TI // ID Q7DD64_NEIMB Unreviewed; 288 AA. AC Q7DD64; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=ATP synthase subunit a {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}; DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000256|HAMAP-Rule:MF_01393}; DE AltName: Full=F-ATPase subunit 6 {ECO:0000256|HAMAP-Rule:MF_01393}; GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_01393, GN ECO:0000313|EMBL:AAF42269.1}; GN OrderedLocusNames=NMB1940 {ECO:0000313|EMBL:AAF42269.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42269.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42269.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42269.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Key component of the proton channel; it plays a direct CC role in the translocation of protons across the membrane. CC {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000256|HAMAP- CC Rule:MF_01393}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01393}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU000483}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000483}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42269.1; -; Genomic_DNA. DR PIR; E81025; E81025. DR RefSeq; NP_274934.1; NC_003112.2. DR RefSeq; WP_002214802.1; NC_003112.2. DR ProteinModelPortal; Q7DD64; -. DR STRING; 122586.NMB1940; -. DR PaxDb; Q7DD64; -. DR EnsemblBacteria; AAF42269; AAF42269; NMB1940. DR GeneID; 904211; -. DR KEGG; nme:NMB1940; -. DR PATRIC; 20359927; VBINeiMen85645_2468. DR eggNOG; ENOG4107RAZ; Bacteria. DR eggNOG; COG0356; LUCA. DR HOGENOM; HOG000253872; -. DR KO; K02108; -. DR OMA; LIYVGQA; -. DR OrthoDB; EOG6K4054; -. DR BioCyc; NMEN122586:GHGG-1997-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.220; -; 1. DR HAMAP; MF_01393; ATP_synth_a_bact; 1. DR InterPro; IPR000568; ATPase_F0-cplx_asu. DR InterPro; IPR023011; ATPase_F0-cplx_asu_AS. DR PANTHER; PTHR11410; PTHR11410; 2. DR Pfam; PF00119; ATP-synt_A; 1. DR SUPFAM; SSF81336; SSF81336; 1. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01393}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01393}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01393}; KW CF(0) {ECO:0000256|HAMAP-Rule:MF_01393, KW ECO:0000256|RuleBase:RU000483}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393, KW ECO:0000256|RuleBase:RU000483}; KW Hydrolase {ECO:0000313|EMBL:AAF42269.1}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01393, KW ECO:0000256|RuleBase:RU000483}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01393}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01393}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01393}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01393, KW ECO:0000256|RuleBase:RU000483}. FT TRANSMEM 39 59 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 102 122 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 145 165 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 222 242 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 246 266 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 267 287 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01393}. SQ SEQUENCE 288 AA; 31418 MW; F1E9B4459D71A929 CRC64; MAGETITAAD YIKHHLQSLT SLSDVTQGQG LKNIADFSFI NLDAVFFAVL LGVIGSFLLW RGAKKATAGV PGRFQAAVEI LFEFVDDMCK SIIHNEKSRK AVAPLGLTLF VWIFLMNAMD MLPVDLLPMV WQGITGNHHA LLRVVPTADL NTTLALAVGV LLICIYYNIK IKGLGGWFHE LFSAPFGAKL APANFLLNLV EFLSKTVSHG MRLFGNMYAG ELVFLLIALL GGAWAASGSV EVMDPILFVF HIIAGLAWAI FHILVITLQA FIFMALAFVY IGQAHDAH // ID Q9JZ87_NEIMB Unreviewed; 102 AA. AC Q9JZ87; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41623.1}; GN OrderedLocusNames=NMB1242 {ECO:0000313|EMBL:AAF41623.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41623.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41623.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41623.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41623.1; -; Genomic_DNA. DR PIR; G81105; G81105. DR RefSeq; NP_274266.1; NC_003112.2. DR RefSeq; WP_002217140.1; NC_003112.2. DR STRING; 122586.NMB1242; -. DR PaxDb; Q9JZ87; -. DR EnsemblBacteria; AAF41623; AAF41623; NMB1242. DR GeneID; 903664; -. DR KEGG; nme:NMB1242; -. DR PATRIC; 20358081; VBINeiMen85645_1553. DR HOGENOM; HOG000218966; -. DR OMA; LKHISEF; -. DR OrthoDB; EOG6130DH; -. DR BioCyc; NMEN122586:GHGG-1279-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 102 AA; 11784 MW; 696ED69F16768B3D CRC64; MTLKTDLLPK INNEDYQRLI LKHSAEFSGG EIRLLNEILE KFNFDVVQAQ ALAQAVMQQI RFDPNAYHID SDDEDTTGIC PHCINPPMPP LRDYLVWRET RG // ID Q9JY69_NEIMB Unreviewed; 99 AA. AC Q9JY69; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=L-lactate permease-related protein {ECO:0000313|EMBL:AAF42059.1}; GN OrderedLocusNames=NMB1712 {ECO:0000313|EMBL:AAF42059.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42059.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42059.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42059.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42059.1; -; Genomic_DNA. DR PIR; B81051; B81051. DR RefSeq; NP_274715.1; NC_003112.2. DR RefSeq; WP_010980977.1; NC_003112.2. DR STRING; 122586.NMB1712; -. DR PaxDb; Q9JY69; -. DR EnsemblBacteria; AAF42059; AAF42059; NMB1712. DR GeneID; 903390; -. DR KEGG; nme:NMB1712; -. DR PATRIC; 20359383; VBINeiMen85645_2197. DR eggNOG; COG1620; LUCA. DR HOGENOM; HOG000219080; -. DR OMA; FFLALTK; -. DR OrthoDB; EOG6NKR31; -. DR BioCyc; NMEN122586:GHGG-1767-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003804; Lactate_perm. DR PANTHER; PTHR30003; PTHR30003; 1. DR Pfam; PF02652; Lactate_perm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 85 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 99 AA; 11146 MW; F3993CFBC7EF0C71 CRC64; MQRCFNWFDH YCRRLEKYFR RCSIMETWVQ NYTAIGGSLY LTAAAALLPI VFFFAALTVL KLKGYQAGLY TLLIALAVAV FGFGMPTGMA VSSLPPQPH // ID Q9JZQ9_NEIMB Unreviewed; 434 AA. AC Q9JZQ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41342.1}; GN OrderedLocusNames=NMB0936 {ECO:0000313|EMBL:AAF41342.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41342.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41342.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41342.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41342.1; -; Genomic_DNA. DR PIR; E81139; E81139. DR STRING; 122586.NMB0936; -. DR PaxDb; Q9JZQ9; -. DR EnsemblBacteria; AAF41342; AAF41342; NMB0936. DR HOGENOM; HOG000218899; -. DR OMA; INICRIG; -. DR OrthoDB; EOG6T7N45; -. DR BioCyc; NMEN122586:GHGG-973-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 434 AA; 48811 MW; 66D263CC5F49F61E CRC64; MDILVLRVDV PKEGFARKLG AHETVFAADD GAVGKVQQLV EVLLRHERDF DEADGCRLKN IAVVLQGILR NNAALFEAVD DLRPRQQQCH RAACLSPHFQ PLCPNIAPIA EKQPFGGVFF GQHQPLSQGF SIETDGFAVI TFAYQPAAFF AETHKPKIFL NTLLRRRHQM QPFIAFLRAQ IFPIQPKRLV SADNVQHIFG QVAGKSFDDD IGNRRGINIC RIGMPSADMN ILMNAGNIGQ IRAKRTQGGH IVRPQMHLPT EFAVQNTGEP PRNADVAEIV DDLAKNPTDK RRSIHRNNGN GLKRAKIVEQ IHNQQNNRNK QQHSLTFQIK LLFQMMLDGV EKDEFKQKRR FAGKDDAVDQ MLEFVFGRIG GENGKRRQRD EADGKPADKQ VSGHCKAFKK AKRHYRPKRT PCLTDAPEMP SEALPQENAA PPNL // ID Q7DDK0_NEIMB Unreviewed; 427 AA. AC Q7DDK0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 88. DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369}; GN Name=gltA {ECO:0000313|EMBL:AAF41360.1}; GN OrderedLocusNames=NMB0954 {ECO:0000313|EMBL:AAF41360.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41360.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41360.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41360.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate + CC CoA. {ECO:0000256|RuleBase:RU003370}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC isocitrate from oxaloacetate: step 1/2. CC {ECO:0000256|RuleBase:RU003370}. CC -!- SIMILARITY: Belongs to the citrate synthase family. CC {ECO:0000256|PIRNR:PIRNR001369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41360.1; -; Genomic_DNA. DR PIR; B81139; B81139. DR RefSeq; NP_273992.1; NC_003112.2. DR RefSeq; WP_002213761.1; NC_003112.2. DR ProteinModelPortal; Q7DDK0; -. DR SMR; Q7DDK0; 6-421. DR STRING; 122586.NMB0954; -. DR PaxDb; Q7DDK0; -. DR PRIDE; Q7DDK0; -. DR EnsemblBacteria; AAF41360; AAF41360; NMB0954. DR GeneID; 903074; -. DR KEGG; nme:NMB0954; -. DR PATRIC; 20357389; VBINeiMen85645_1209. DR eggNOG; ENOG4105BZN; Bacteria. DR eggNOG; COG0372; LUCA. DR HOGENOM; HOG000021224; -. DR KO; K01647; -. DR OMA; NKEDGVR; -. DR OrthoDB; EOG6P8TP4; -. DR BioCyc; NMEN122586:GHGG-991-MONOMER; -. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.230.10; -; 1. DR Gene3D; 1.10.580.10; -; 1. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR019810; Citrate_synthase_AS. DR InterPro; IPR024176; Citrate_synthase_bac-typ. DR InterPro; IPR010953; Citrate_synthase_typ-I. DR PANTHER; PTHR11739; PTHR11739; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PIRSF; PIRSF001369; Citrate_synth; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; SSF48256; 1. DR TIGRFAMs; TIGR01798; cit_synth_I; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:AAF41360.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41360.1}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003370}. FT ACT_SITE 304 304 {ECO:0000256|PIRSR:PIRSR001369-1}. FT ACT_SITE 362 362 {ECO:0000256|PIRSR:PIRSR001369-1}. SQ SEQUENCE 427 AA; 48121 MW; AA6BBA166E00247D CRC64; MSKSIKLNVP GQAGLELPVL EASIGHDVVD IRGLTKNTGL FSFDPGFVST ASCESKITYI DGDQGLLYYR GYPIEQLAEK SDYLEVCYLL IYGELPTPEQ KAEFDNTVRR HTMVHEQLTW FFRGFRRDAH PMAMMVGVVG ALSAFYQDSL DISNPEHRKI AIYRLISKIP TIAAMCYRYS NGLPFNYPKN NLSYSENFLH MMFATPCEDY KPNPVLARAL DRIFILHADH EQNASTSTVR LAGSSGANPF ACIAAGIACL WGASHGGANE AVLKMLDEIG DVSNVAAYME GVKQRKYRLM GFGHRVYRNM DPRASIMRET CYEVLKELGL EDSPKFKLAM ELEQIALKDP FFIERKLYPN VDFYSGIVLS ALGIPTEMFT VIFALSRSVG WISHWHEMIS DPSLKIGRPR QLYTGSERRD YVPPGER // ID Q9JZE3_NEIMB Unreviewed; 516 AA. AC Q9JZE3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41486.1}; GN OrderedLocusNames=NMB1094 {ECO:0000313|EMBL:AAF41486.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41486.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41486.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41486.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41486.1; -; Genomic_DNA. DR PIR; H81123; H81123. DR RefSeq; NP_274126.1; NC_003112.2. DR RefSeq; WP_010980890.1; NC_003112.2. DR STRING; 122586.NMB1094; -. DR PaxDb; Q9JZE3; -. DR EnsemblBacteria; AAF41486; AAF41486; NMB1094. DR GeneID; 903515; -. DR KEGG; nme:NMB1094; -. DR PATRIC; 20357749; VBINeiMen85645_1391. DR eggNOG; ENOG4105CCM; Bacteria. DR eggNOG; ENOG410XNW6; LUCA. DR HOGENOM; HOG000218944; -. DR OMA; EMERGAQ; -. DR OrthoDB; EOG632D1D; -. DR BioCyc; NMEN122586:GHGG-1130-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006517; Arc_phage_psiM2_terminase_lsu. DR TIGRFAMs; TIGR01630; psiM2_ORF9; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 516 AA; 58634 MW; AE1F24C0FAA7F388 CRC64; MDGFDASPKA IAARRAKVFD PVGGYEYFVN TYFPHYIRSP EKSELHAFLF SRLPEIIRSP KGENEAVGAP RGEGKSTKVT QLFTLWCIVT GQKHYAVIVM DSIDQAYPML EAIKAELEFN PRLKTDFPEV CGQGRVWQAG TIVTANDVKV QVAGSGKKLR GLRHGPYRPD LTVLDDIEND EQVRNPEQRD KLNAWLTKTV LPLGGVGQKY DVIYIGTILH YDSVLNRTLN NPFWHGIKFK AMKRWPDRMD LWDRWEELFR NDGETVAEAF YQANKDEMER GAVTSWAARG VLALMKIRAR DGHATFDSEY QNDPVSGEDA PFAKSMKFWN DLPSDLVYFG ALDPSLGKAG ASRDPSAIII GGYQRVTGKL YVVEAQIKKR LPDLIIEDVI RLHRQYRCKL WFVETVQFQE FLKDELVKRS AARGIPVPAR AVKPVSDKLL RIETLQPHMA NGLILLNESQ QTLIQQFRHF PKADHDDGPD AVHMLWSGAV ANCVPIEWQS PTDNDFDDEI KSKWSR // ID Q7DD61_NEIMB Unreviewed; 160 AA. AC Q7DD61; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42289.1}; GN OrderedLocusNames=NMB1960 {ECO:0000313|EMBL:AAF42289.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42289.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42289.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42289.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42289.1; -; Genomic_DNA. DR PIR; A81022; A81022. DR RefSeq; NP_274954.1; NC_003112.2. DR RefSeq; WP_002219878.1; NC_003112.2. DR STRING; 122586.NMB1960; -. DR PaxDb; Q7DD61; -. DR EnsemblBacteria; AAF42289; AAF42289; NMB1960. DR GeneID; 904190; -. DR KEGG; nme:NMB1960; -. DR PATRIC; 20359981; VBINeiMen85645_2495. DR eggNOG; ENOG4106HVU; Bacteria. DR eggNOG; ENOG410Y4X4; LUCA. DR HOGENOM; HOG000218746; -. DR OMA; QMFREWF; -. DR OrthoDB; EOG6WT8DD; -. DR BioCyc; NMEN122586:GHGG-2017-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 160 AA; 18508 MW; 6939DA255365BA61 CRC64; MPSENPCSDG IPFCRNGQSE TTDWAIISFL RIPRDSKGKT MYEVNRSVFV LIPLEPFWNW LQTLPGNHLD GLTLEDIQAD ANSYLVRPCE TADEVWDEIE ARFEDIFAAE LADWCEDERE WPALDADIFN EWFDIQLSTV ITDLEHEPLA REAFQPINLN // ID Q7DDA9_NEIMB Unreviewed; 206 AA. AC Q7DDA9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41886.1}; GN OrderedLocusNames=NMB1531 {ECO:0000313|EMBL:AAF41886.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41886.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41886.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41886.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41886.1; -; Genomic_DNA. DR PIR; G81071; G81071. DR RefSeq; NP_274538.1; NC_003112.2. DR RefSeq; WP_002225057.1; NC_003112.2. DR STRING; 122586.NMB1531; -. DR PaxDb; Q7DDA9; -. DR EnsemblBacteria; AAF41886; AAF41886; NMB1531. DR GeneID; 904052; -. DR KEGG; nme:NMB1531; -. DR PATRIC; 20358868; VBINeiMen85645_1943. DR eggNOG; ENOG4108TJP; Bacteria. DR eggNOG; ENOG4111GE4; LUCA. DR HOGENOM; HOG000219025; -. DR OMA; FCPEDIP; -. DR OrthoDB; EOG6CCH4G; -. DR BioCyc; NMEN122586:GHGG-1572-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019722; G6PD_bac. DR Pfam; PF10786; G6PD_bact; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 206 AA; 24471 MW; 955C3B1B819AE56A CRC64; MLTPKSCDLF NIPFFQFSQL KKYQPESIPQ IKADYKENWQ IWQQLIQQVA AELGAPFAPP HIERWCNGWQ VRAHFFAYFK YEQYKNSAAI LSILLNRRRL SVSLDWHCYK ADVSPIALPD YNRWLDNFDT EKYASFDMWH GAESEYDDYR TVAQQNESDR KLQNDEDFFC IGKHIERDDL GRQDVAKWIA ETVEDLLPLY EACHGK // ID Q9JZX2_NEIMB Unreviewed; 39 AA. AC Q9JZX2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41273.1}; GN OrderedLocusNames=NMB0862 {ECO:0000313|EMBL:AAF41273.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41273.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41273.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41273.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41273.1; -; Genomic_DNA. DR PIR; A81151; A81151. DR RefSeq; NP_273903.1; NC_003112.2. DR RefSeq; WP_010980863.1; NC_003112.2. DR STRING; 122586.NMB0862; -. DR PaxDb; Q9JZX2; -. DR EnsemblBacteria; AAF41273; AAF41273; NMB0862. DR GeneID; 902976; -. DR KEGG; nme:NMB0862; -. DR BioCyc; NMEN122586:GHGG-893-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 39 AA; 4408 MW; E618986A6A11E1DB CRC64; MTIFKLLDLQ SDLPIEIGCA TYVLSRALIF QPCNPKELL // ID Q9K123_NEIMB Unreviewed; 135 AA. AC Q9K123; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40813.1}; GN OrderedLocusNames=NMB0371 {ECO:0000313|EMBL:AAF40813.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40813.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40813.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40813.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40813.1; -; Genomic_DNA. DR PIR; A81207; A81207. DR RefSeq; NP_273420.1; NC_003112.2. DR RefSeq; WP_002224903.1; NC_003112.2. DR STRING; 122586.NMB0371; -. DR PaxDb; Q9K123; -. DR EnsemblBacteria; AAF40813; AAF40813; NMB0371. DR GeneID; 902486; -. DR KEGG; nme:NMB0371; -. DR PATRIC; 20355901; VBINeiMen85645_0468. DR eggNOG; ENOG41077X7; Bacteria. DR eggNOG; ENOG410Z4X8; LUCA. DR HOGENOM; HOG000219105; -. DR OMA; DYSEWND; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NMEN122586:GHGG-393-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 135 AA; 16815 MW; 992E601713F5EF96 CRC64; MCEFKDFRRN IPCFKEYDEN SFIGKWYDDG VWDDEEYWKL ENDLIEVRKK YPYPMDIPRD IVIGIGTIID FLMVQNWKLF EIKASTWLPK SVKINERYER FRVMLRYIFT DLDVEDWKFF YFPIQHSKGR LRRKV // ID Q7DD57_NEIMB Unreviewed; 251 AA. AC Q7DD57; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42328.1}; GN OrderedLocusNames=NMB2001 {ECO:0000313|EMBL:AAF42328.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42328.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42328.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42328.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42328.1; -; Genomic_DNA. DR RefSeq; NP_274993.1; NC_003112.2. DR RefSeq; WP_002219917.1; NC_003112.2. DR ProteinModelPortal; Q7DD57; -. DR STRING; 122586.NMB2001; -. DR MEROPS; C40.006; -. DR PaxDb; Q7DD57; -. DR EnsemblBacteria; AAF42328; AAF42328; NMB2001. DR GeneID; 904124; -. DR KEGG; nme:NMB2001; -. DR PATRIC; 20360101; VBINeiMen85645_2555. DR eggNOG; ENOG4105K4H; Bacteria. DR eggNOG; COG0791; LUCA. DR HOGENOM; HOG000229978; -. DR OrthoDB; EOG6GTZPF; -. DR BioCyc; NMEN122586:GHGG-2058-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.1720.10; -; 1. DR InterPro; IPR000064; NLP_P60_dom. DR Pfam; PF00877; NLPC_P60; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 134 239 NLPC_P60. {ECO:0000259|Pfam:PF00877}. SQ SEQUENCE 251 AA; 27620 MW; 658EC0F88184F451 CRC64; MDSFFKPAVW AVLWLMFAVR PALADELTNL LSSREQILRQ FAEDEQPVLP INRAPARRAG NADELIGSAM GLNEQPVLPV NRVPARRAGN ADELIGNAMG LNEQPVLPVN RAPARRAGNA DELIGNAMGL LGIAYRYGGT SVSTGFDCSG FMQHIFKRAM GINLPRTSAE QARMGTPVAR SELQPGDMVF FRTLGGSRIS HVGLYIGNNR FIHAPRTGKN IEITSLSHKY WSGKYAFARR VKKNDPSRFL N // ID Q9JZP3_NEIMB Unreviewed; 296 AA. AC Q9JZP3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha {ECO:0000256|RuleBase:RU000699}; DE EC=6.2.1.5 {ECO:0000256|RuleBase:RU000699}; GN Name=sucD {ECO:0000313|EMBL:AAF41366.1}; GN OrderedLocusNames=NMB0960 {ECO:0000313|EMBL:AAF41366.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41366.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41366.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41366.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. {ECO:0000256|RuleBase:RU000699}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000256|RuleBase:RU000699}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha CC subunit family. {ECO:0000256|RuleBase:RU000677}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41366.1; -; Genomic_DNA. DR PIR; G81137; G81137. DR RefSeq; NP_273998.1; NC_003112.2. DR RefSeq; WP_002222615.1; NC_003112.2. DR ProteinModelPortal; Q9JZP3; -. DR SMR; Q9JZP3; 2-291. DR STRING; 122586.NMB0960; -. DR PaxDb; Q9JZP3; -. DR PRIDE; Q9JZP3; -. DR EnsemblBacteria; AAF41366; AAF41366; NMB0960. DR GeneID; 903080; -. DR KEGG; nme:NMB0960; -. DR PATRIC; 20357401; VBINeiMen85645_1215. DR eggNOG; ENOG4105CH8; Bacteria. DR eggNOG; COG0074; LUCA. DR HOGENOM; HOG000239685; -. DR KO; K01902; -. DR OMA; QATFHSE; -. DR OrthoDB; EOG644ZT0; -. DR BioCyc; NMEN122586:GHGG-997-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.261; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR005810; CoA_lig_alpha. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001553; SucCS_alpha; 1. DR PRINTS; PR01798; SCOASYNTHASE. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01019; sucCoAalpha; 1. DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1. DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000699}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000256|RuleBase:RU000677, ECO:0000313|EMBL:AAF41366.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000699}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 100 CoA_binding. {ECO:0000259|SMART:SM00881}. FT ACT_SITE 249 249 Tele-phosphohistidine intermediate. FT {ECO:0000256|PIRSR:PIRSR001553-1}. SQ SEQUENCE 296 AA; 30548 MW; FBF333089C23BE9F CRC64; MSVLINKDTK VLVQGFTGKN GTFHSEQALA YGTKVVGGVT PGKGGQTHLN LPVFNTMKEA VKETGADASV IYVPAPFVLD SIVEAVDSGV GLVVVITEGV PTLDMLKAKR YLETNGNGTR LVGPNCPGVI TPGECKIGIM PGHIHTPGRI GIISRSGTLT YEAVAQTTKL GLGQSTCIGI GGDPIPGMNQ IDALKLFQED PDTDAIIMIG EIGGTAEEEA AEYIQSNVSK PVVGYIAGVT APKGKRMGHA GAIISGGKGT AEEKFAAFEK AGIAYTRSPA ELGTTMLEVL KAKGLA // ID Q7DD75_NEIMB Unreviewed; 391 AA. AC Q7DD75; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Pilin glycosylation protein PglC {ECO:0000313|EMBL:AAF42156.1}; GN Name=pglC {ECO:0000313|EMBL:AAF42156.1}; GN OrderedLocusNames=NMB1821 {ECO:0000313|EMBL:AAF42156.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42156.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42156.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42156.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. CC {ECO:0000256|RuleBase:RU004508}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42156.1; -; Genomic_DNA. DR RefSeq; NP_274818.1; NC_003112.2. DR RefSeq; WP_002222986.1; NC_003112.2. DR ProteinModelPortal; Q7DD75; -. DR STRING; 122586.NMB1821; -. DR PaxDb; Q7DD75; -. DR EnsemblBacteria; AAF42156; AAF42156; NMB1821. DR GeneID; 903279; -. DR KEGG; nme:NMB1821; -. DR PATRIC; 20359627; VBINeiMen85645_2319. DR eggNOG; ENOG4105CF4; Bacteria. DR eggNOG; COG0399; LUCA. DR HOGENOM; HOG000230163; -. DR OMA; IGHIGAW; -. DR OrthoDB; EOG6MPWRD; -. DR BioCyc; NMEN122586:GHGG-1876-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000653; DegT/StrS_aminotransferase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF01041; DegT_DnrJ_EryC1; 1. DR PIRSF; PIRSF000390; PLP_StrS; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-1, KW ECO:0000256|RuleBase:RU004508, ECO:0000256|SAAS:SAAS00486653}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT MOD_RES 185 185 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR000390-1}. SQ SEQUENCE 391 AA; 43398 MW; 66BCD932C4A8B64F CRC64; MLNTFLSPWP CFTQEEADAV SKVLLSNKVN YWTGNECREF EKEFAAFAGT RYAVALANGT LALDVALKAM GIGAGDDVIV TSRTFLASAS CIVNAGANPV FADVDLNSQN ISAETVKAAL TPTTKAVIVV HLAGMPAEMD GIMALAKEHN LWVIEDCAQA HGAKYKGKSV GSIGHVGAWS FCQDKIMTTG GEGGMVTTND KTLWEKMWSY KDHGKSYDAV YNHEHAPGFR WLHESFGTNW RMMEMQAVIG RIQLKRLPEW TARRRENAAK LAESLGKFSS IRLVEVADYI GHAQYKFYAF VKPEHLKDGW TRDRIVGELN ARKVPCYQGS CSEVYLEKAF DNTPWRPKER LTNAVELGDT SLMFLVHPTL TDDEIAFCKK HIEAVLTEAA R // ID Q7DD74_NEIMB Unreviewed; 636 AA. AC Q7DD74; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Pilin glycosylation protein PglD {ECO:0000313|EMBL:AAF42157.1}; GN Name=pglD {ECO:0000313|EMBL:AAF42157.1}; GN OrderedLocusNames=NMB1822 {ECO:0000313|EMBL:AAF42157.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42157.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42157.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42157.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42157.1; -; Genomic_DNA. DR RefSeq; NP_274819.1; NC_003112.2. DR RefSeq; WP_002222987.1; NC_003112.2. DR ProteinModelPortal; Q7DD74; -. DR STRING; 122586.NMB1822; -. DR PaxDb; Q7DD74; -. DR DNASU; 903278; -. DR EnsemblBacteria; AAF42157; AAF42157; NMB1822. DR GeneID; 903278; -. DR KEGG; nme:NMB1822; -. DR PATRIC; 20359629; VBINeiMen85645_2320. DR eggNOG; ENOG4105C5E; Bacteria. DR eggNOG; COG1086; LUCA. DR HOGENOM; HOG000257078; -. DR OMA; FNPTDGI; -. DR OrthoDB; EOG6WQD59; -. DR BioCyc; NMEN122586:GHGG-1877-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003869; Polysac_CapD-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02719; Polysacc_synt_2; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 130 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 282 576 Polysacc_synt_2. FT {ECO:0000259|Pfam:PF02719}. SQ SEQUENCE 636 AA; 70955 MW; 3FBE52289890096F CRC64; MNLETLIALP RNIKKICFLI HDFLMIFIAF WFTQSLKADY SDEWFDFANW QSFLLTALLT ITLFIRMGLY HAVTRFVSFR ILTTALAGSL ASAVLFFLNT LIFEERLRLA LPIVYFLLLF VSVTGSRMVL RGLLSEHPKK QMIPVIIYGA GRSGRQLLEA VKQMREYSAA AFVDDDPKLW HTVIYDLAVY QPDAIAFLIE RYGVEKILLA IPGATQEQRR RIINKLEAYP CEVLTIPGMK DLMDGKISIG TLKKISVSDL LGRDSVAPDD RLMSADIEGK TVMVTGAGGS IGSELCRQII RRRPEKLLLF ELSEFALYAI EKELRETCIQ KRLDTEILPF LGSVQNRTLL EHVMTAFSVA TVYHAAAYKH VPMVEFNTVE GIRNNIFGTL ECALAATTSG VRTFVLISTD KAVRPTNTMG ASKRMAELCL QALAAEPGQK TRFSMVRFGN VLGSSGSVVP LFEKQIAEGG PLTLTHPEIT RYFMTIPEAA QLVIQAGAMG TGGDVFVLDM GESVKIIDLA RQMITLSGLK PNTPEQPDGD IEILITGLRP GEKLYEELLI GDNVRKTGHP RIMTANETML PWHELSALLD RIRAACDRYD QQAIRTLLIN APTGFAPSDG ICDLLWVRET HRKNAV // ID Q9JXG2_NEIMB Unreviewed; 462 AA. AC Q9JXG2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42383.1}; GN OrderedLocusNames=NMB2064 {ECO:0000313|EMBL:AAF42383.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42383.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42383.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42383.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42383.1; -; Genomic_DNA. DR PIR; D81010; D81010. DR RefSeq; NP_275054.1; NC_003112.2. DR RefSeq; WP_002225704.1; NC_003112.2. DR STRING; 122586.NMB2064; -. DR PaxDb; Q9JXG2; -. DR EnsemblBacteria; AAF42383; AAF42383; NMB2064. DR GeneID; 904014; -. DR KEGG; nme:NMB2064; -. DR PATRIC; 20360288; VBINeiMen85645_2644. DR eggNOG; ENOG4105D3Y; Bacteria. DR eggNOG; COG2056; LUCA. DR HOGENOM; HOG000279369; -. DR KO; K07084; -. DR OMA; NHIYDTC; -. DR OrthoDB; EOG6D5G41; -. DR BioCyc; NMEN122586:GHGG-2127-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR018461; Na/H_Antiport_NhaC-like_C. DR InterPro; IPR032813; Na_H_antiport_N. DR Pfam; PF13726; Na_H_antiport_2; 1. DR Pfam; PF03553; Na_H_antiporter; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 207 229 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 299 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 334 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 409 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 444 461 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 100 Na_H_antiport_2. FT {ECO:0000259|Pfam:PF13726}. FT DOMAIN 166 456 Na_H_antiporter. FT {ECO:0000259|Pfam:PF03553}. SQ SEQUENCE 462 AA; 48097 MW; 6F239E03A2BB8ED1 CRC64; MNAVVVAVIV MLVLSLSRVH VVLSLTVGAF VGGAVAGMPL QNIADAAGQV SQAGIIPVFN KGLEGGAKIA LSYAMLGAFA MAITHSGLPQ QLAGAVVRKL NRGGMPDSVR SGEGAVKWLL LSIILVMGMM SQNIIPIHIA FIPMIVPPLL LVFNRLKIDR RLIACVITFG LVTTYMFLPY GFGAIFLNEI LLGNIHSAAP QLDVKNINVM AAMAIPALGM LAGLLLAFVH YRKPRLYQSN NADTAGNADA ANRPQPSAYR SLAAAVAIAV CFAIQLMYED SLVLGAMLGF AVFMMLGVIN RDKANDVFGE GIKMMAMVGF IMIAAQGFAA VMNATGHIQP LVESSMAIFG NSKGMAALAM LVVGLLVTMG IGSSFSTLPI IAAIYVPLCV GLGFSPLATV AIVGTAGALG DAGSPASDST LGPTMGLNAD GQHDHIRDSV IPTFIHYNIP LLIAGWIAAM VL // ID Q9K1L0_NEIMB Unreviewed; 280 AA. AC Q9K1L0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=PhnO-related protein {ECO:0000313|EMBL:AAF40564.1}; GN OrderedLocusNames=NMB0105 {ECO:0000313|EMBL:AAF40564.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40564.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40564.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40564.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40564.1; -; Genomic_DNA. DR PIR; H81237; H81237. DR RefSeq; NP_273163.1; NC_003112.2. DR RefSeq; WP_002215334.1; NC_003112.2. DR ProteinModelPortal; Q9K1L0; -. DR STRING; 122586.NMB0105; -. DR PaxDb; Q9K1L0; -. DR EnsemblBacteria; AAF40564; AAF40564; NMB0105. DR GeneID; 902209; -. DR KEGG; nme:NMB0105; -. DR PATRIC; 20355223; VBINeiMen85645_0145. DR eggNOG; ENOG4105MF0; Bacteria. DR eggNOG; ENOG4111ZKF; LUCA. DR HOGENOM; HOG000218668; -. DR OMA; QNDPANE; -. DR OrthoDB; EOG6SBT62; -. DR BioCyc; NMEN122586:GHGG-111-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR021969; DUF3579. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF00583; Acetyltransf_1; 1. DR Pfam; PF12112; DUF3579; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 136 280 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 280 AA; 31581 MW; 83F95ED704C65D3C CRC64; MLVCNPYEVV IHGTTSSGKI FRPSDWAERL CGILSSFTKD HRLSYSKWVR PILVDNIRCV AVDKKLETDN PQMFRFLMDF AADNDLRVID CKALLEEREQ GGQNNPADEH VMLAQAIEEK HAAEKAQEQT ASGASYVLRE IGADDTATAF AALSVLRSAL TDINRFTEQI NKVQRPQGYR LLGIFEEGKH NAVAVCGFRE ACTLASGRHI HIDDIVTLPQ SRRKGYASRL LEEVRKIGAE TGVTKIHLNV HVNHDRADAH RLYFKNGFEI CAYHFRCDPK // ID Q9JXI6_NEIMB Unreviewed; 413 AA. AC Q9JXI6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Tryptophan transporter {ECO:0000313|EMBL:AAF42353.1}; GN Name=mtr {ECO:0000313|EMBL:AAF42353.1}; GN OrderedLocusNames=NMB2031 {ECO:0000313|EMBL:AAF42353.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42353.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42353.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42353.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42353.1; -; Genomic_DNA. DR PIR; E81013; E81013. DR RefSeq; NP_275023.1; NC_003112.2. DR RefSeq; WP_002225681.1; NC_003112.2. DR STRING; 122586.NMB2031; -. DR PaxDb; Q9JXI6; -. DR EnsemblBacteria; AAF42353; AAF42353; NMB2031. DR GeneID; 904070; -. DR KEGG; nme:NMB2031; -. DR PATRIC; 20360179; VBINeiMen85645_2589. DR eggNOG; ENOG4105CIC; Bacteria. DR eggNOG; COG0814; LUCA. DR HOGENOM; HOG000269674; -. DR KO; K03835; -. DR OMA; IWLLGTM; -. DR OrthoDB; EOG60394J; -. DR BioCyc; NMEN122586:GHGG-2093-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002091; ArAA_permease. DR InterPro; IPR013061; Trp/try_permease_CS. DR InterPro; IPR013059; Trp_tyr_transpt. DR InterPro; IPR018227; Tryptophan/tyrosine_permease. DR Pfam; PF03222; Trp_Tyr_perm; 1. DR PRINTS; PR00166; AROAAPRMEASE. DR TIGRFAMs; TIGR00837; araaP; 1. DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 167 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 285 310 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 344 365 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 399 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 413 AA; 44107 MW; F575AD99CCED65C4 CRC64; MPNKTPSLFG GAMIIAGTVI GAGMLANPTA TSGVWFTGSL AVLLYTWFSM LSSGLMILEV NTHYPHGASF DTMVKDLLGR GWNIINGIAV AFVLYLLTYA YIFVGGDLTA KGLGSAAGGD VSLTVGQLVF FGILAFCVWA SARLVDRFTG VLIGGMVLTF IWAAGGLIAD AKPSVLFDTQ APAGTNYWIY AATALPVCLA SFGFHGNVSS LLKYFKGDAP KVAKSIWTGT LIALVIYVLW QTAIQGNLPR NEFAPVIAAE GQVSVLIETL SKFAQTGNMD KILSLFSYMA IATSFLGVTL GLFDYIADIF KWNDSISGRT KTAALTFLPP LISCLLFPTG FVTAIGYVGL AATVWTGIIP AMLLYRSRKK FGAGKTYKVY GGLWLMVWVF LFGIVNIAAQ VLSQMELVPV FKG // ID Q9JXZ4_NEIMB Unreviewed; 67 AA. AC Q9JXZ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42160.1}; GN OrderedLocusNames=NMB1825 {ECO:0000313|EMBL:AAF42160.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42160.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42160.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42160.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42160.1; -; Genomic_DNA. DR PIR; F81037; F81037. DR RefSeq; NP_274822.1; NC_003112.2. DR RefSeq; WP_002225659.1; NC_003112.2. DR PaxDb; Q9JXZ4; -. DR EnsemblBacteria; AAF42160; AAF42160; NMB1825. DR GeneID; 903275; -. DR KEGG; nme:NMB1825; -. DR PATRIC; 20359635; VBINeiMen85645_2323. DR eggNOG; ENOG410ZF5P; LUCA. DR HOGENOM; HOG000218770; -. DR OMA; WAEDENA; -. DR OrthoDB; EOG6VF37H; -. DR BioCyc; NMEN122586:GHGG-1880-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR019180; Oxidoreductase-like_N. DR Pfam; PF09791; Oxidored-like; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 19 58 Oxidoreductase-like. FT {ECO:0000259|Pfam:PF09791}. SQ SEQUENCE 67 AA; 7570 MW; A0F482D38A0DEC86 CRC64; MDTTLKYKAE ALLGEPLLDE PVRPESWECC GSDCGEACIQ TIYWADKAKY DVQRQKLKEA GWSDDAV // ID Q9JZJ2_NEIMB Unreviewed; 291 AA. AC Q9JZJ2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41427.1}; GN OrderedLocusNames=NMB1028 {ECO:0000313|EMBL:AAF41427.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41427.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41427.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41427.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41427.1; -; Genomic_DNA. DR PIR; B81130; B81130. DR RefSeq; NP_274062.1; NC_003112.2. DR RefSeq; WP_002219215.1; NC_003112.2. DR STRING; 122586.NMB1028; -. DR PaxDb; Q9JZJ2; -. DR EnsemblBacteria; AAF41427; AAF41427; NMB1028. DR GeneID; 903165; -. DR KEGG; nme:NMB1028; -. DR PATRIC; 20357591; VBINeiMen85645_1312. DR eggNOG; ENOG4108TZV; Bacteria. DR eggNOG; ENOG4111H5E; LUCA. DR HOGENOM; HOG000218978; -. DR OMA; FNYITAI; -. DR OrthoDB; EOG6BW4ZJ; -. DR BioCyc; NMEN122586:GHGG-1065-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 21 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 224 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 236 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 283 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 291 AA; 31023 MW; BCFBA1533F0FE8B0 CRC64; MAYLLISIVF SVSVSILLKM ARKKKIDIAQ AVAVNYVVAV ILTLLVLKPD IGNIGAFLPT WPLFAALGVL LPSVFVIMGK SVEAAGIVKS DAAQRLSLFL PIVAALTLFG EKLSEGKLIG LCLAFAALFC LLWKHSGGKK SGSAWRQAAL LLGVWAGYGI IDILFKQLAK SGTAFAGNLL VAFVLAGVLM FACLFAKSVR WRVESVVGGI FLGGLNFMNI VTYITAHQMM KDNPTLVFAG MNIGVIVLGT LSGALFFKEK INTINTAGIV LALCSIACLF YWGEVKVLFG I // ID Q9JXJ9_NEIMB Unreviewed; 230 AA. AC Q9JXJ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42331.1}; GN OrderedLocusNames=NMB2004 {ECO:0000313|EMBL:AAF42331.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42331.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42331.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42331.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42331.1; -; Genomic_DNA. DR PIR; B81017; B81017. DR RefSeq; NP_274996.1; NC_003112.2. DR RefSeq; WP_002214916.1; NC_003112.2. DR STRING; 122586.NMB2004; -. DR PaxDb; Q9JXJ9; -. DR EnsemblBacteria; AAF42331; AAF42331; NMB2004. DR GeneID; 904117; -. DR KEGG; nme:NMB2004; -. DR PATRIC; 20360107; VBINeiMen85645_2558. DR eggNOG; ENOG41067MG; Bacteria. DR eggNOG; COG1346; LUCA. DR HOGENOM; HOG000253604; -. DR OMA; QMHQIRA; -. DR OrthoDB; EOG6NPMDR; -. DR BioCyc; NMEN122586:GHGG-2061-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007300; CidB/LrgB. DR Pfam; PF04172; LrgB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 225 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 230 AA; 24584 MW; AE9AA98A40A83DE8 CRC64; MNEILRQPSV LLFLTLAVYA LAIIVRTRTG NIFCNPVLVS TIVLIAYLKI LGIDYAVYHN AAQFIDFWLK PAVVVLAVPL YQNRRKIFNQ WLPVIVSQLA GSVTGIVTGM YFAKWLGAER EVVLSLASKS VTNPIAIEIT RSIGGIPAIT AATVIIAGLV GQIAGYKMLK NTVVMPSSVG MSLGTASHAM GIAASLERSR RMAAYAGLGL TFNGVLTALI APLLIPVLGF // ID Q9JYX4_NEIMB Unreviewed; 183 AA. AC Q9JYX4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41751.1}; GN OrderedLocusNames=NMB1387 {ECO:0000313|EMBL:AAF41751.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41751.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41751.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41751.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41751.1; -; Genomic_DNA. DR PIR; B81089; B81089. DR RefSeq; NP_274401.1; NC_003112.2. DR RefSeq; WP_009348591.1; NC_003112.2. DR STRING; 122586.NMB1387; -. DR PaxDb; Q9JYX4; -. DR EnsemblBacteria; AAF41751; AAF41751; NMB1387. DR GeneID; 903809; -. DR KEGG; nme:NMB1387; -. DR PATRIC; 20358455; VBINeiMen85645_1739. DR HOGENOM; HOG000219003; -. DR OMA; HVCSAAM; -. DR OrthoDB; EOG6SR8ZV; -. DR BioCyc; NMEN122586:GHGG-1425-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009739; DUF1311. DR Pfam; PF07007; DUF1311; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 149 176 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 183 AA; 20978 MW; 2774C361CCE2D46B CRC64; MPSERRPFQT AFLSNRKTVG KLAERVQSRY DGLHKFKHIC SAAMALIKEP LDKVKQRNEE LEAAEEAAAQ EALGREQEAA RVSEWEERYK LSRSEFEQFW KGLPQTVQNK LQASQKTWKS GMDKICANNA KAEGKTPNGI KFSELACKTA KTEARLEELH NRKKALIDEM AREADKKELS KRL // ID Q9K0S7_NEIMB Unreviewed; 1978 AA. AC Q9K0S7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 2. DT 16-MAR-2016, entry version 78. DE SubName: Full=Hemagglutinin/hemolysin-related protein {ECO:0000313|EMBL:AAF40929.2}; GN OrderedLocusNames=NMB0497 {ECO:0000313|EMBL:AAF40929.2}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40929.2, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40929.2, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40929.2, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40929.2; -; Genomic_DNA. DR PIR; B81192; B81192. DR RefSeq; NP_273543.2; NC_003112.2. DR RefSeq; WP_002225630.1; NC_003112.2. DR ProteinModelPortal; Q9K0S7; -. DR STRING; 122586.NMB0497; -. DR PaxDb; Q9K0S7; -. DR EnsemblBacteria; AAF40929; AAF40929; NMB0497. DR GeneID; 902613; -. DR KEGG; nme:NMB0497; -. DR PATRIC; 20356244; VBINeiMen85645_0642. DR eggNOG; ENOG4108XKC; Bacteria. DR eggNOG; COG3210; LUCA. DR HOGENOM; HOG000218788; -. DR OMA; PDNNIDI; -. DR OrthoDB; EOG69SK6F; -. DR BioCyc; NMEN122586:GHGG-522-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR006915; DUF637_hemagglutn_put. DR InterPro; IPR008619; Filamentous_hemagglutn_rpt. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04830; DUF637; 1. DR Pfam; PF05594; Fil_haemagg; 2. DR Pfam; PF05860; Haemagg_act; 1. DR Pfam; PF04829; PT-VENN; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 93 201 Haemagg_act. {ECO:0000259|SMART:SM00912}. SQ SEQUENCE 1978 AA; 205041 MW; 8328BC1ACAC45741 CRC64; MNKGLHRIIF SKKHSTMVAV AETANSQGKG KQAGSSVSVS LKTSGDLCGK LKTTLKTLVC SLVSLSMVLP AHAQITTDKS APKNQQVVIL KTNTGAPLVN IQTPNGRGLS HNRYTQFDVD NKGAVLNNDR NNNPFVVKGS AQLILNEVRG TASKLNGIVT VGGQKADVII ANPNGITVNG GGFKNVGRGI LTTGAPQIGK DGALTGFDVR QGTLTVGAAG WNDKGGADYT GVLARAVALQ GKLQGKNLAV STGPQKVDYA SGEISAGTAA GTKPTIALDT AALGGMYADS ITLIANEKGV GVKNAGTLEA AKQLIVTSSG RIENSGRIAT TADGTEASPT YLSIETTEKG AAGTFISNGG RIESKGLLVI ETGEDISLRN GAVVQNNGSR PATTVLNAGH NLVIESKTNV NNAKGPATLS ADGRTVIKEA SIQTGTTVYS SSKGNAELGN NTRITGADVT VLSNGTISSS AVIDAKDTAH IEAGKPLSLE ASTVTSDIRL NGGSIKGGKQ LALLADDNIT AKTTNLNTPG NLYVHTGKDL NLNVDKDLSA ASIHLKSDNA AHITGTSKTL TASKDMGVEA GSLNVTNTNL RTNSGNLHIQ AAKGNIQLRN TKLNAAKALE TTALQGNIVS DGLHAVSADG HVSLLANGNA DFTGHNTLTA KADVNAGSVG KGRLKADNTN ITSSSGDITL VAGNGIQLGD GKQRNSINGK HISIKNNGGN ADLKNLNVHA KSGALNIHSD RALSIENTKL ESTHNTHLNA QHERVTLNQV DAYAHRHLSI TGSQIWQNDK LPSANKLVAN GVLALNARYS QIADNTTLRA GAINLTAGTA LVKRGNINWS TVSTKTLEDN AELKPLAGRL NIEAGSGTLT IEPANRISAH TDLSIKTGGK LLLSAKGGNA GAPSAQVSSL EAKGNIRLVT GETDLRGSKI TAGKNLVVAT TKGKLNIEAV NNSFSNYFPT QKAAELNQKS KELEQQIAQL KKSSPKSKLI PTLQEERDRL AFYIQAINKE VKGKKPKGKE YLQAKLSAQN IDLISAQGIE ISGSDITASK KLNLHAAGVL PKAADSEAAA ILIDGITDQY EIGKPTYKSH YDKAALNKPS RLTGRTGVSI HAAAALDDAR IIIGASEIKA PSGSIDIKAH SDIVLEAGQN DAYTFLKTKG KSGKIIRKTK FTSTRDHLIM PAPVELTANG ITLQAGGNIE ANTTRFNAPA GKVTLVAGEE LQLLAEEGIH KHELDVQKSR RFIGIKVGKS NYSKNELNET KLPVRVVAQT AATRSGWDTV LEGTEFKTTL AGADIQAGVG EKARADAKII LKGIVNRIQS EEKLETNSTV WQKQAGRGST IETLKLPSFE SPTPPKLTAP GGYIVDIPKG NLKTEIEKLA KQPEYAYLKQ LQVAKNVNWN QVQLAYDKWD YKQEGLTRAG AAIVTIIVTA LTYGYGATAA GGVAASGSST AAAAGTAATT TAAATTVSTA TAMQTAALAS LYSQAAVSII NNKGDVGKAL KDLGTSDTVK QIVTSALTAG ALNQMGADIA QLNSKVRTEL FSSTGNQTIA NLGGRLATNL SNAGISAGIN TAVNGGSLKD NLGNAALGAL VNSFQGEAAS KIKTTFSDDY VAKQFAHALA GCVSGLVQGK CKDGAIGAAV GEIVADSMLG GRNPATLSDA EKHKVISYSK IIAGSVAALN GGDVNTAANA AEVAVVNNAL NFDSTPTNAK KHQPQKPDKT ALEKIIQGIM PAHAAGAMTN PQDKDAAIWI SNIRNGITGP IVITSYGVYA AGWTAPLIGT AGKLAISTCM ANPSGCTVMV TQAAEAGAGI ATGAVTVGNA WEAPVGALSK AKAAKQAIPT QTVKELDGLL QESKNIGAVN TRINIANSTT RYTPMRQTGQ PVSAGFEHVL EGHFHRPIAN NRSVFTISPN ELKVILQSNK VVSSPVSMTP DGQYMRTVDV GKVIGTTSIK EGGQPTTTIK VFTDKSGNLI TTYPVKGN // ID Q7DD58_NEIMB Unreviewed; 223 AA. AC Q7DD58; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42311.1}; GN OrderedLocusNames=NMB1983 {ECO:0000313|EMBL:AAF42311.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42311.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42311.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42311.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42311.1; -; Genomic_DNA. DR PIR; C81019; C81019. DR RefSeq; NP_274976.1; NC_003112.2. DR RefSeq; WP_002225856.1; NC_003112.2. DR ProteinModelPortal; Q7DD58; -. DR STRING; 122586.NMB1983; -. DR PaxDb; Q7DD58; -. DR EnsemblBacteria; AAF42311; AAF42311; NMB1983. DR GeneID; 904154; -. DR KEGG; nme:NMB1983; -. DR PATRIC; 20360047; VBINeiMen85645_2528. DR eggNOG; ENOG4108XQ5; Bacteria. DR eggNOG; ENOG4111MJJ; LUCA. DR HOGENOM; HOG000271058; -. DR OMA; NDAVNGM; -. DR OrthoDB; EOG6KHG1J; -. DR BioCyc; NMEN122586:GHGG-2040-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 81 216 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 223 AA; 24811 MW; E37325D47606D098 CRC64; MFPDKYKLSL KENIFLAKKV LVAQIHNLSR FENCQTTLLQ TEQIIHGKNV ASASLEDIQT ILNLKRAYQY VISHISNGEP VDISLLKKIN NIVAKDDSLA PGDFRTGSVG VTLLDGSRHA PNPVKEIEVA RVLQNIGLQS GSTTEAAVRF MLYCMRQQVF WDGNKRTATL FANGLMMAGG CGILEISEMQ MPQFNEKLSA FYRSGDDTDI SKFVYQNCIS GID // ID Q9JZU4_NEIMB Unreviewed; 126 AA. AC Q9JZU4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41305.1}; GN OrderedLocusNames=NMB0897 {ECO:0000313|EMBL:AAF41305.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41305.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41305.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41305.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41305.1; -; Genomic_DNA. DR PIR; F81143; F81143. DR RefSeq; NP_273937.1; NC_003112.2. DR RefSeq; WP_002220683.1; NC_003112.2. DR ProteinModelPortal; Q9JZU4; -. DR PaxDb; Q9JZU4; -. DR EnsemblBacteria; AAF41305; AAF41305; NMB0897. DR GeneID; 903018; -. DR KEGG; nme:NMB0897; -. DR PATRIC; 20357223; VBINeiMen85645_1125. DR eggNOG; ENOG4105TWM; Bacteria. DR eggNOG; COG3692; LUCA. DR HOGENOM; HOG000152348; -. DR OMA; CDMIYTV; -. DR OrthoDB; EOG6K6V8J; -. DR BioCyc; NMEN122586:GHGG-935-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 2.30.30.110; -; 1. DR InterPro; IPR003477; PemK-like. DR InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib. DR Pfam; PF02452; PemK_toxin; 1. DR SUPFAM; SSF50118; SSF50118; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 126 AA; 14418 MW; 0A8DCC6B2E23BA73 CRC64; MPLKFQPRER SVIMCDFRGY EEPEMVKKRP VVVIARNRHN GKLVTVVPLS STEPVPLADY HHKMSGNPLP DKPHIQCWAK CDMTATVGLA RLDRYKPKGR DRCIPIISEE DFQAIKTAVA KAFKLY // ID Q9K0I3_NEIMB Unreviewed; 419 AA. AC Q9K0I3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884}; DE AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884}; GN Name=rho {ECO:0000256|HAMAP-Rule:MF_01884, GN ECO:0000313|EMBL:AAF41043.1}; GN OrderedLocusNames=NMB0617 {ECO:0000313|EMBL:AAF41043.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41043.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41043.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41043.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Facilitates transcription termination by a mechanism CC that involves Rho binding to the nascent RNA, activation of Rho's CC RNA-dependent ATPase activity, and release of the mRNA from the CC DNA template. {ECO:0000256|HAMAP-Rule:MF_01884}. CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring CC structure. {ECO:0000256|HAMAP-Rule:MF_01884}. CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000256|HAMAP- CC Rule:MF_01884}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41043.1; -; Genomic_DNA. DR PIR; F81177; F81177. DR RefSeq; NP_273661.1; NC_003112.2. DR RefSeq; WP_002219650.1; NC_003112.2. DR ProteinModelPortal; Q9K0I3; -. DR SMR; Q9K0I3; 1-417. DR STRING; 122586.NMB0617; -. DR PaxDb; Q9K0I3; -. DR EnsemblBacteria; AAF41043; AAF41043; NMB0617. DR GeneID; 902730; -. DR KEGG; nme:NMB0617; -. DR PATRIC; 20356523; VBINeiMen85645_0781. DR eggNOG; ENOG4105C4P; Bacteria. DR eggNOG; COG1158; LUCA. DR HOGENOM; HOG000076952; -. DR KO; K03628; -. DR OMA; FLRAPDY; -. DR OrthoDB; EOG6N681W; -. DR BioCyc; NMEN122586:GHGG-643-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01884; Rho; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011112; Rho_N. DR InterPro; IPR011113; Rho_RNA-bd. DR InterPro; IPR004665; Term_rho. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF07498; Rho_N; 1. DR Pfam; PF07497; Rho_RNA_bind; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00959; Rho_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF68912; SSF68912; 1. DR TIGRFAMs; TIGR00767; rho; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01884}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription termination {ECO:0000256|HAMAP-Rule:MF_01884}. FT DOMAIN 5 47 Rho_N. {ECO:0000259|SMART:SM00959}. FT DOMAIN 52 118 CSP. {ECO:0000259|SMART:SM00357}. FT DOMAIN 170 355 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 169 174 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT NP_BIND 181 186 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT BINDING 212 212 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. SQ SEQUENCE 419 AA; 47306 MW; 95982734F5CE5087 CRC64; MHVSELQTLH ISKLLELAEE HGIENANRFR KQDLVFAIVR QMMKKGEGFT CSGTLEILPD GFGFLRSADT SYLAGPDDIY VSPTQIRRFN LHTGDTIEGS VRVPKDNERY FALVRLDTIN GDHPEVCRHK ILFENLTPLF PTEQLKLERD LKSEENLTGR AIDLISPIGK GQRALLVAPP KSGKTVMLQN IAHAVTANYP EVELIVLLID ERPEEVTEMS RSVRGEVVSS TFDEPAQRHV QVAEMVLEKA KRMVEHKKDV VILLDSITRL ARAYNTVVPT SGKILTGGVD ANALHRPKRF FGAARNVEEG GSLTIIATAL VETGSRMDDV IYEEFKGTGN MELHLDRRMA EKRLFPAINI NKSGTRREEL LVPNDQLQRM WLLRKFLHPM DEIEAAEFLI GKIKASKNND DFFELMRGK // ID Q9K163_NEIMB Unreviewed; 430 AA. AC Q9K163; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40760.1}; GN OrderedLocusNames=NMB0315 {ECO:0000313|EMBL:AAF40760.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40760.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40760.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40760.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40760.1; -; Genomic_DNA. DR PIR; A81214; A81214. DR RefSeq; NP_273364.1; NC_003112.2. DR RefSeq; WP_002224862.1; NC_003112.2. DR ProteinModelPortal; Q9K163; -. DR STRING; 122586.NMB0315; -. DR MEROPS; M23.009; -. DR PaxDb; Q9K163; -. DR DNASU; 902431; -. DR EnsemblBacteria; AAF40760; AAF40760; NMB0315. DR GeneID; 902431; -. DR KEGG; nme:NMB0315; -. DR PATRIC; 20355759; VBINeiMen85645_0399. DR eggNOG; ENOG4105DR5; Bacteria. DR eggNOG; COG0739; LUCA. DR HOGENOM; HOG000281148; -. DR OMA; NARVSSH; -. DR OrthoDB; EOG61KBD1; -. DR BioCyc; NMEN122586:GHGG-335-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01551; Peptidase_M23; 1. DR SUPFAM; SSF51261; SSF51261; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 294 387 Peptidase_M23. FT {ECO:0000259|Pfam:PF01551}. SQ SEQUENCE 430 AA; 46440 MW; 1E820D559436BCA3 CRC64; MAVFPLSAKH RKYALRALAV SIILVSAAYI ASTERTERVR PQRVEQNLPP LSWGGSGVQT AYWVQEAVQP GDSLADVLAR SGMARDEIAR ITEKYGGEAD LRHLRADQSV HVLVGGDGGA REVQFFTDED GERNLVALEK KGGIWRRSAS EADMKVLPTL RSVVVKTSAR GSLARAEVPV EIRESLSGIF AGRFSLDGLK EGDAVRLMYD SLYFHGQQVA AGDILAAEVV KGGTRHQAFY YRSDKEGGGG GNYYDEDGKV LQEKGGFNIE PLVYTRISSP FGYRMHPILH TWRLHTGIDY AAPQGTPVRA SADGVITFKG RKGGYGNAVM IRHANGVETL YAHLSAFSQA EGNVRGGEVI GFVGSTGRST GPHLHYEARI NGQPVNPVSV ALPTPELTQA DKAAFAAQKQ KADALLARLR GIPVTVSQSD // ID Q7DDC4_NEIMB Unreviewed; 390 AA. AC Q7DDC4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:AAF62327.1}; DE EC=1.1.2.3 {ECO:0000313|EMBL:AAF62327.1}; GN Name=lldD {ECO:0000313|EMBL:AAF62327.1}; GN OrderedLocusNames=NMB1377 {ECO:0000313|EMBL:AAF62327.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62327.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62327.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62327.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62327.1; -; Genomic_DNA. DR RefSeq; NP_274393.1; NC_003112.2. DR RefSeq; WP_002220815.1; NC_003112.2. DR ProteinModelPortal; Q7DDC4; -. DR STRING; 122586.NMB1377; -. DR PaxDb; Q7DDC4; -. DR EnsemblBacteria; AAF62327; AAF62327; NMB1377. DR GeneID; 903799; -. DR KEGG; nme:NMB1377; -. DR PATRIC; 20358431; VBINeiMen85645_1727. DR eggNOG; ENOG4105DMF; Bacteria. DR eggNOG; COG1304; LUCA. DR HOGENOM; HOG000217464; -. DR KO; K00101; -. DR OMA; AWIKEQW; -. DR OrthoDB; EOG6HMXBG; -. DR BioCyc; NMEN122586:GHGG-1415-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000313|EMBL:AAF62327.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 18 381 FMN_dh. {ECO:0000259|Pfam:PF01070}. FT ACT_SITE 280 280 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000138-1}. SQ SEQUENCE 390 AA; 43501 MW; 6E8E928CE0FA6F80 CRC64; MKRDLSKMTC IEDLRRVAKR KMPRMFYDYI DSGSWTETTY RENTSDFKDI RFRQKVLVNM EGRSLETKMI GQDVKMPVAI APTGFTGMAH ADGEILAARA AEKFGIPFTL STMSICSIED VAENTSAPFW FQLYVMRDRE FMENLIKRAK DAKCSALVLT ADLQVLGQRH KDIKNGLSAP PKPTIANLIN LATKPEWCMK MLNTERRTFR NIVGHAKNVG DLSSLSSWTS EQFDPRLSWD DVARIKDLWG GKLIIKGIME PEDAEKAAKS GADALIVSNH GGRQLDDTVS AIKALPDIVS AVGSDIEVWM DSGIRSGQDI LKAWALGAKG TMIGRAFLYG LGAYGEEGVT RALEILYKEM DISMAFTGHR DIQDVDASIL RGKDWGRETV // ID Q9JZD8_NEIMB Unreviewed; 160 AA. AC Q9JZD8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41491.1}; GN OrderedLocusNames=NMB1100 {ECO:0000313|EMBL:AAF41491.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41491.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41491.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41491.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41491.1; -; Genomic_DNA. DR PIR; A81121; A81121. DR RefSeq; NP_274131.1; NC_003112.2. DR RefSeq; WP_010980891.1; NC_003112.2. DR STRING; 122586.NMB1100; -. DR PaxDb; Q9JZD8; -. DR EnsemblBacteria; AAF41491; AAF41491; NMB1100. DR GeneID; 903522; -. DR KEGG; nme:NMB1100; -. DR PATRIC; 20357764; VBINeiMen85645_1398. DR OMA; ARPAACY; -. DR OrthoDB; EOG6G4W47; -. DR BioCyc; NMEN122586:GHGG-1136-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 46 94 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 160 AA; 17586 MW; 1C1C3333CF2E6F59 CRC64; MLPHTGLFLL GKVALQMRIR RRLKQGVIMA KTNNKPETAE TAAPSFEDIK AELDAVQAEL AAARNDVEML TTALEKAEDD KKALSAELAE LKVQHTQRAA DALADSRDVM LVSTGADGKE FWRGGLLFDG GWREVKRAEV GEAVWKAICA EPMLQRKAVE // ID Q4W559_NEIMB Unreviewed; 463 AA. AC Q4W559; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=ATP-dependent RNA helicase HrpA, truncation {ECO:0000313|EMBL:AAY52151.1}; GN OrderedLocusNames=NMB2007 {ECO:0000313|EMBL:AAY52151.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52151.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52151.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52151.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52151.1; -; Genomic_DNA. DR RefSeq; NP_274999.1; NC_003112.2. DR RefSeq; WP_002223142.1; NC_003112.2. DR ProteinModelPortal; Q4W559; -. DR STRING; 122586.NMB2007; -. DR PaxDb; Q4W559; -. DR EnsemblBacteria; AAY52151; AAY52151; NMB2007. DR GeneID; 903117; -. DR KEGG; nme:NMB2007; -. DR PATRIC; 20360115; VBINeiMen85645_2562. DR eggNOG; ENOG4105CQ7; Bacteria. DR eggNOG; COG1643; LUCA. DR HOGENOM; HOG000175261; -. DR OMA; HFLQSAF; -. DR OrthoDB; EOG6PP9H5; -. DR BioCyc; NMEN122586:GHGG-2064-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010222; RNA_helicase_HrpA. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01967; DEAH_box_HrpA; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAY52151.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|RuleBase:RU000452, ECO:0000313|EMBL:AAY52151.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAY52151.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAY52151.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 69 232 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 256 429 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 463 AA; 51694 MW; 24E849F0F172C429 CRC64; MFPDFSQTLS KDRHFLRSAF KNPNKYGGLS KIEEKYRKSH EIFLKRLAAL PKPEFDNTLP VHEKLEEIKK AIAKNQVTII CGETGSGKTT QLPKICLELG RGAAGLIGHT QPRRLAARSV AERIAEELKS EIGSAVGYKV RFTDHTSRDA CVKLMTDGIL LAETQTDRYL AAYDTIIIDE AHERSLNIDF LLGYLKQLLP RRPDLKVIIT SATIDAERFS RHFNGAPVLE VSGRTYPVEI LYRPLTGKDE DDAEVELTDA IVDAADELAR HGEGDILVFL PGEREIRETA EALRKSTLRR NDEILPLFAR LSHAEQHKIF HPSGAKRRIV LATNVAETSL TVPGIKYVID TGLARVKRYS ARAKVEQLHI EKISQAAARQ RSGRCGRVSA GVCIRLFSEE DFNSRPEFTD PEIVRSNLAA VILRMAALKL GDVAAFPFLE MPDSRYINDG FQVLLELGAV EAV // ID Q9JYK4_NEIMB Unreviewed; 737 AA. AC Q9JYK4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Lactoferrin-binding protein B {ECO:0000313|EMBL:AAF41896.1}; GN Name=lbpB {ECO:0000313|EMBL:AAF41896.1}; GN OrderedLocusNames=NMB1541 {ECO:0000313|EMBL:AAF41896.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41896.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41896.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41896.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41896.1; -; Genomic_DNA. DR PIR; H81070; H81070. DR RefSeq; NP_274548.1; NC_003112.2. DR RefSeq; WP_002225048.1; NC_003112.2. DR ProteinModelPortal; Q9JYK4; -. DR STRING; 122586.NMB1541; -. DR PaxDb; Q9JYK4; -. DR EnsemblBacteria; AAF41896; AAF41896; NMB1541. DR GeneID; 904078; -. DR KEGG; nme:NMB1541; -. DR PATRIC; 20358908; VBINeiMen85645_1968. DR HOGENOM; HOG000219027; -. DR OMA; DFGHPDK; -. DR OrthoDB; EOG6423BR; -. DR BioCyc; NMEN122586:GHGG-1582-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR001677; Solute-bd_prot_TBP-like. DR Pfam; PF01298; Lipoprotein_5; 1. DR SUPFAM; SSF56925; SSF56925; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 737 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332256. SQ SEQUENCE 737 AA; 81131 MW; 590AAE5B5E3129A9 CRC64; MCKPNYGGIV LLPLLLASCI GGNFGVQPVV ESTPTAYPVT FKSKDVPTPP PAGSSVETTP VNRPAVGAAM RLPRRNIASY KQDGTEIPDK HQAEEHLPLK EKDILFLDGT LKEQADKLKK KINERYSDVR VITSKKEEEK YQYQFVRAGY VFTRAEGKDN EKEKTSDGKE FVNRFSYDGF VYYSGERPSQ SLPSAGTVQY SGNWQYMTDA KRHRTGKAVS STDLGYTTYY GNEIGATSYE ARDADDREKH PAEYTVDFDN KTLNGKLIKN QYVQNKSNPN EPKKPLTIYD ITATLDGNRF TGSAKVSTEV KTQHADKEYL FFHTDADQRL EGGFFGDNGE ELAGRFISND NSVFGVFAGK QKTETENAAD TKPALSSGKH TKILDSLKIS VDEASDKNPR EFAISSMPDF GHPDKLLVEG REIPLVNKEQ TIELADGRKT TIRTCCDFLT YVKIGRMQTE RPAAKPKAQD EERDEEDTGV DSVEEGEDEI DDEEGTEDAA VKDEGSEEDE AVEGEDEAEE PEEESPTEEG GSGSDGILPA PEAPKGRNID LFLKGIRTAE TDIPKTGEAH YTGTWEARIG KPIQWDNQAD KEAAKAVFTV DFGKKSISGT LTEENGVEPA FHIENGKIEG NGFYATARTR ENGINLSGNG STDPKTFQAS NLRVEGGFYG PQAEELGGII FNNDGKSLGI TEGTENKVDV EAEVDAEVDV GKQLESEVKH QFGVVFGAKK DMQEVEK // ID Q9JZN0_NEIMB Unreviewed; 513 AA. AC Q9JZN0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203}; DE EC=1.6.1.2 {ECO:0000256|PIRNR:PIRNR000203}; GN Name=pntA {ECO:0000313|EMBL:AAF41384.1}; GN OrderedLocusNames=NMB0980 {ECO:0000313|EMBL:AAF41384.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41384.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41384.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41384.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane. {ECO:0000256|PIRNR:PIRNR000203}. CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC {ECO:0000256|PIRNR:PIRNR000203}. CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. CC {ECO:0000256|PIRNR:PIRNR000203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41384.1; -; Genomic_DNA. DR PIR; F81134; F81134. DR RefSeq; NP_274017.1; NC_003112.2. DR RefSeq; WP_002225308.1; NC_003112.2. DR ProteinModelPortal; Q9JZN0; -. DR SMR; Q9JZN0; 2-377. DR STRING; 122586.NMB0980; -. DR PaxDb; Q9JZN0; -. DR EnsemblBacteria; AAF41384; AAF41384; NMB0980. DR GeneID; 903100; -. DR KEGG; nme:NMB0980; -. DR PATRIC; 20357449; VBINeiMen85645_1239. DR eggNOG; ENOG4108IIE; Bacteria. DR eggNOG; COG3288; LUCA. DR HOGENOM; HOG000022121; -. DR KO; K00324; -. DR OMA; AGNNFGR; -. DR OrthoDB; EOG61P6S9; -. DR BioCyc; NMEN122586:GHGG-1017-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0015992; P:proton transport; IEA:InterPro. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR008142; AlaDH/PNT_CS1. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR026255; NADP_transhyd_a. DR InterPro; IPR024605; NADP_transhyd_a_C. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR Pfam; PF12769; PNTB_4TM; 1. DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00561; pntA; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW NAD {ECO:0000256|PIRNR:PIRNR000203}; KW NADP {ECO:0000256|PIRNR:PIRNR000203}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000203}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000203, KW ECO:0000313|EMBL:AAF41384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 405 424 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 430 448 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 455 474 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 480 502 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 137 AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}. FT DOMAIN 146 312 AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}. SQ SEQUENCE 513 AA; 53852 MW; 618DAC660A316BA1 CRC64; MKIGIPRESL SGETRVACTP ATVALLGKLG FETVVESGAG LAASLDDAAY QTAGATVADK AAVWVCPLIY KVNAPSEQEL PLLNEGQTIV SFLWPRQNEA LVEALRAKKV NALAMDMVPR ISRAQALDAL SSMANISGYR AVIEAANAFG RFFTGQITAA GKVPPAQVLV IGAGVAGLAA IGTANSLGAV VRAFDTRLEV AEQIESMGGK FLKLDFPQES GGSGDGYAKV MSDEFIAAEM KLFAEQAKEV DIIITTAAIP GKPAPKLITK EMVESMKSGS VIVDLAAATG GNCELTRPGE LSVTGNGVKI IGYTDMANRL AGQSSQLYAT NLVNLTKLLS PNKDGEITLD FEDVIIRNMT VTHDGEITFP PPPIQVSAQP QQTPSEKAVP AAKPEPKPVP LWKKLAPAVI AAVLVLWVGA VAPAAFLNHF IVFVLACVIG YYVVWNVSHS LHTPLMSVTN AISGIIVVGA LLQIGQGNGF VSLLSFVAIL IAGINIFGGF AVTRRMLNMF KKG // ID Q7DDR6_NEIMB Unreviewed; 231 AA. AC Q7DDR6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488}; GN Name=dsbA-2 {ECO:0000313|EMBL:AAF40745.1}; GN OrderedLocusNames=NMB0294 {ECO:0000313|EMBL:AAF40745.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40745.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40745.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40745.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}. CC -!- SIMILARITY: Belongs to the thioredoxin family. CC {ECO:0000256|PIRNR:PIRNR001488}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40745.1; -; Genomic_DNA. DR RefSeq; NP_273348.1; NC_003112.2. DR RefSeq; WP_002215704.1; NC_003112.2. DR ProteinModelPortal; Q7DDR6; -. DR STRING; 122586.NMB0294; -. DR PaxDb; Q7DDR6; -. DR EnsemblBacteria; AAF40745; AAF40745; NMB0294. DR GeneID; 902405; -. DR KEGG; nme:NMB0294; -. DR PATRIC; 20355690; VBINeiMen85645_0369. DR eggNOG; ENOG4107WU4; Bacteria. DR eggNOG; ENOG410ZVW5; LUCA. DR HOGENOM; HOG000265318; -. DR KO; K03673; -. DR OMA; FENTWTA; -. DR OrthoDB; EOG68Q0Q6; -. DR BioCyc; NMEN122586:GHGG-309-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR023205; DsbA/DsbL. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF13462; Thioredoxin_4; 1. DR PIRSF; PIRSF001488; Tdi_protein; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488}; KW Periplasm {ECO:0000256|PIRNR:PIRNR001488}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 231 Thiol:disulfide interchange protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287268. FT DOMAIN 32 228 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 76 79 Redox-active. FT {ECO:0000256|PIRSR:PIRSR001488-1}. SQ SEQUENCE 231 AA; 25420 MW; A5893B240C76F948 CRC64; MKLKTLALTS LTLLALAACS KQAETSVPAD SAQSSSSAPA APAELNEGVN YTVLSTPIPQ QQAGKIEVLE FFGYFCPHCA HLEPVLSEHI KTFKDDTYMR REHVVWGDEM KPLARLAAAV EMAGESDKAN SHIFDAMVNQ KINLADTDTL KKWLSEQTAF DGKKVLAAFE APESQARAAQ MEELTNKFQI SGTPTVIVGG KYQVEFKDWQ SGMTTIDQLV DKVREEQKKP Q // ID Q9JYG0_NEIMB Unreviewed; 335 AA. AC Q9JYG0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=IS1106 transposase {ECO:0000313|EMBL:AAF41954.1}; GN OrderedLocusNames=NMB1601 {ECO:0000313|EMBL:AAF41954.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41954.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41954.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41954.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41954.1; -; Genomic_DNA. DR PIR; D81064; D81064. DR RefSeq; NP_274607.1; NC_003112.2. DR RefSeq; WP_009348805.1; NC_003112.2. DR STRING; 122586.NMB1601; -. DR PaxDb; Q9JYG0; -. DR EnsemblBacteria; AAF41954; AAF41954; NMB1601. DR GeneID; 904284; -. DR KEGG; nme:NMB1601; -. DR PATRIC; 20359082; VBINeiMen85645_2053. DR eggNOG; ENOG4105F2I; Bacteria. DR eggNOG; COG3039; LUCA. DR HOGENOM; HOG000218682; -. DR KO; K07481; -. DR OMA; CSGNSEH; -. DR OrthoDB; EOG6RZB5B; -. DR BioCyc; NMEN122586:GHGG-1649-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR002559; Transposase_11. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF01609; DDE_Tnp_1; 1. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 51 122 DUF772. {ECO:0000259|Pfam:PF05598}. FT DOMAIN 138 322 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 335 AA; 38516 MW; 9F6C05D9FE6E85C4 CRC64; MSTFFQQTAQ AMIAKHIDRF PLLKLDRVID WQLIEQYLNR QKTRYLRDHR GRPAYPLLSM FKAVLLGQWH SLSDPELEHS LITRIDFNLF CRFDELSIPD YSTLCRYRNR LAQDNTLSEL LELINRQLTE KGLKIEKASA AVVDATIIQT AGSKQRQAIE VDEEGQISGQ TTPSKDSDAR WIKKNGLYKL GYKQHTRTDA EGYIEKLHIT PANAHECKHL SPLLEGLPKG TTVYADKGYD SAENRQHLEE HQLQDGIMRK ACRNRPLSEV QTKRNRYLSK TRYVVEQSFG TLHRKFRYAR AAYFGLIKVS AQSHLKAMCL NLLKAANRLS APAAA // ID Q9JXU4_NEIMB Unreviewed; 107 AA. AC Q9JXU4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42215.1}; GN OrderedLocusNames=NMB1881 {ECO:0000313|EMBL:AAF42215.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42215.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42215.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42215.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2I45} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS). RA Chang C., Hatzos C., Bargassa M., Joachimiak A.; RT "Crystal structure of protein NMB1881 from Neisseria meningitidis."; RL Submitted (AUG-2006) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42215.1; -; Genomic_DNA. DR PIR; G81030; G81030. DR RefSeq; NP_274877.1; NC_003112.2. DR RefSeq; WP_002225791.1; NC_003112.2. DR PDB; 2I45; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-107. DR PDBsum; 2I45; -. DR ProteinModelPortal; Q9JXU4; -. DR SMR; Q9JXU4; 4-102. DR STRING; 122586.NMB1881; -. DR PaxDb; Q9JXU4; -. DR EnsemblBacteria; AAF42215; AAF42215; NMB1881. DR GeneID; 904300; -. DR KEGG; nme:NMB1881; -. DR PATRIC; 20359797; VBINeiMen85645_2404. DR eggNOG; ENOG4108Z28; Bacteria. DR eggNOG; COG0662; LUCA. DR HOGENOM; HOG000031295; -. DR OMA; KGEFVWH; -. DR OrthoDB; EOG6K6VBF; -. DR BioCyc; NMEN122586:GHGG-1937-MONOMER; -. DR EvolutionaryTrace; Q9JXU4; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2I45}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 41 91 Cupin_2. {ECO:0000259|Pfam:PF07883}. SQ SEQUENCE 107 AA; 11996 MW; D2EA3619C6765B69 CRC64; MQNETINLKQ HLAAIKEYWQ PEIINRHGFQ FHLVKLLGDY GWHTHGYSDK VLFAVEGDMA VDFADGGSMT IREGEMAVVP KSVSHRPRSE NGCSLVLIEL SDPSEAV // ID Q9JY92_NEIMB Unreviewed; 256 AA. AC Q9JY92; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42035.1}; GN OrderedLocusNames=NMB1687 {ECO:0000313|EMBL:AAF42035.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42035.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42035.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42035.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42035.1; -; Genomic_DNA. DR PIR; H81053; H81053. DR RefSeq; NP_274691.1; NC_003112.2. DR RefSeq; WP_002222128.1; NC_003112.2. DR ProteinModelPortal; Q9JY92; -. DR STRING; 122586.NMB1687; -. DR PaxDb; Q9JY92; -. DR DNASU; 903420; -. DR EnsemblBacteria; AAF42035; AAF42035; NMB1687. DR GeneID; 903420; -. DR KEGG; nme:NMB1687; -. DR PATRIC; 20359325; VBINeiMen85645_2169. DR eggNOG; ENOG4105TRG; Bacteria. DR eggNOG; COG0084; LUCA. DR HOGENOM; HOG000201521; -. DR KO; K03424; -. DR OMA; GAATWPQ; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; NMEN122586:GHGG-1742-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005902; DNase_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 256 AA; 28432 MW; DC9953F0815FC742 CRC64; MNFTDTHCHL ADPALRENLP HILTAARKVG VKRFIVPATR PQDWQDVADL AEMPSEHGQI RIALGIHPWF SDGIAERDFV RLETMLAHYP QAWVGEIGLD FYDKTQTSQQ RERQIQVFVR QLEIAQTLRR RVIIHNLKAT ADIAAAVKQT GFAQGGIVHA FSGSAEEARV LTKLGFKIGI GSLLLNPNAR KVRDTLKALN DGDFVLETDS PFMLKKEINT PANIPGIAKI AAEIRGTCVE EIAKVTERNA DALLGR // ID Q9JZX4_NEIMB Unreviewed; 125 AA. AC Q9JZX4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41270.1}; GN OrderedLocusNames=NMB0859 {ECO:0000313|EMBL:AAF41270.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41270.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41270.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41270.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41270.1; -; Genomic_DNA. DR PIR; F81150; F81150. DR STRING; 122586.NMB0859; -. DR PaxDb; Q9JZX4; -. DR EnsemblBacteria; AAF41270; AAF41270; NMB0859. DR PATRIC; 20357111; VBINeiMen85645_1074. DR HOGENOM; HOG000218878; -. DR OMA; FRNIYRI; -. DR OrthoDB; EOG67T5KM; -. DR BioCyc; NMEN122586:GHGG-890-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 125 AA; 14913 MW; DF1B0804B6AE85FF CRC64; MSFGYLIATS QPCELLTKSR GETFSLIMDK MDLWIYFRFC EGNIYTIRKN ETESCLTERG GEWLKHIYEF NRGSFIFSYV LLKKRESEEN FTEIVLKSIK NNKILTVKVR SGLHFDLRNI YRIEM // ID Q9JXN2_NEIMB Unreviewed; 92 AA. AC Q9JXN2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42291.1}; GN OrderedLocusNames=NMB1962 {ECO:0000313|EMBL:AAF42291.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42291.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42291.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42291.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42291.1; -; Genomic_DNA. DR PIR; C81022; C81022. DR RefSeq; NP_274956.1; NC_003112.2. DR RefSeq; WP_002218074.1; NC_003112.2. DR STRING; 122586.NMB1962; -. DR PaxDb; Q9JXN2; -. DR EnsemblBacteria; AAF42291; AAF42291; NMB1962. DR GeneID; 904187; -. DR KEGG; nme:NMB1962; -. DR PATRIC; 20359985; VBINeiMen85645_2497. DR eggNOG; COG3113; LUCA. DR HOGENOM; HOG000218745; -. DR KO; K07122; -. DR OMA; RADSACM; -. DR OrthoDB; EOG6VMTP1; -. DR BioCyc; NMEN122586:GHGG-2019-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.750.24; -; 1. DR InterPro; IPR002645; STAS_dom. DR Pfam; PF13466; STAS_2; 1. DR SUPFAM; SSF52091; SSF52091; 1. DR PROSITE; PS50801; STAS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 41 92 STAS. {ECO:0000259|PROSITE:PS50801}. SQ SEQUENCE 92 AA; 10033 MW; 4F6F6C6A3746F647 CRC64; MHTELKNGIL HIGGDITVKT LTAAAFTRFR QQCRLKDTCA VDLSGVGRAD SACVSLLLEV LRGCKGSVRL TGIPESVRAL SELYEIKDWL KS // ID Q9K009_NEIMB Unreviewed; 130 AA. AC Q9K009; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41232.1}; GN OrderedLocusNames=NMB0819 {ECO:0000313|EMBL:AAF41232.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41232.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41232.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41232.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41232.1; -; Genomic_DNA. DR PIR; B81154; B81154. DR RefSeq; NP_273861.1; NC_003112.2. DR RefSeq; WP_002232189.1; NC_003112.2. DR STRING; 122586.NMB0819; -. DR PaxDb; Q9K009; -. DR EnsemblBacteria; AAF41232; AAF41232; NMB0819. DR GeneID; 902934; -. DR KEGG; nme:NMB0819; -. DR PATRIC; 20357021; VBINeiMen85645_1029. DR HOGENOM; HOG000218660; -. DR OMA; MYPLDIH; -. DR OrthoDB; EOG6VQPVF; -. DR BioCyc; NMEN122586:GHGG-850-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007929; DUF723. DR Pfam; PF05265; DUF723; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 130 AA; 14210 MW; CBF05E93111B9740 CRC64; MAKSFNQAAS ELTDIFPNIS LTGFDGVNYP VTVNCPMHGN VRYSTFNALI KSKYGCPECA KMSKTQTPPN VGKPLLILDT TTNETLTFPS VTAAGAALGV HFQQINHRLK GRTSPDNLIS NRYKVLGYDR // ID Q9JY13_NEIMB Unreviewed; 314 AA. AC Q9JY13; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAF42131.1}; GN OrderedLocusNames=NMB1792 {ECO:0000313|EMBL:AAF42131.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42131.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42131.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42131.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00102782}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42131.1; -; Genomic_DNA. DR PIR; G81041; G81041. DR RefSeq; NP_274791.2; NC_003112.2. DR ProteinModelPortal; Q9JY13; -. DR STRING; 122586.NMB1792; -. DR PaxDb; Q9JY13; -. DR EnsemblBacteria; AAF42131; AAF42131; NMB1792. DR GeneID; 903307; -. DR KEGG; nme:NMB1792; -. DR PATRIC; 20359549; VBINeiMen85645_2280. DR eggNOG; ENOG4105DHQ; Bacteria. DR eggNOG; ENOG410XS4R; LUCA. DR HOGENOM; HOG000223178; -. DR KO; K07645; -. DR OMA; FRAVFNI; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NMEN122586:GHGG-1847-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAF42131.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAF42131.1}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 37 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 98 312 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 314 AA; 35231 MW; 2D81808BDB44C159 CRC64; MQENEYREDL AADAARQSVL PLLAALPLMI LLTVWITHKA MRPVRKLSQS LEQRRINDLS ALSVDNIPSE IRGFVTAINL LLKRADEDIR HRQRFVADAA HELRTPMTAL PLQAERLNNM PLPPDAARQP AVLQQSIRRN KHLLEQLLAL ARSQSDEIPL TKTTFGLQSR FRQVLQELMP LALEKCQDIG VAVGGDVEVS ADETEIYTLI KTFADNAVRY TPPEGRIDLG FTDEGKYLAV WVEDNGKGIP ESERARVLDP FYRILGTEQQ GTGLGLSIAD TLAKKYGGYL ELSDSRRFGR GLLIRALLDK ETLK // ID Q9JZ15_NEIMB Unreviewed; 218 AA. AC Q9JZ15; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Putative isomerase {ECO:0000313|EMBL:AAF41713.1}; GN OrderedLocusNames=NMB1338 {ECO:0000313|EMBL:AAF41713.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41713.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41713.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41713.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41713.1; -; Genomic_DNA. DR PIR; B81094; B81094. DR RefSeq; NP_274357.1; NC_003112.2. DR RefSeq; WP_002222354.1; NC_003112.2. DR ProteinModelPortal; Q9JZ15; -. DR STRING; 122586.NMB1338; -. DR PaxDb; Q9JZ15; -. DR EnsemblBacteria; AAF41713; AAF41713; NMB1338. DR GeneID; 903760; -. DR KEGG; nme:NMB1338; -. DR PATRIC; 20358331; VBINeiMen85645_1677. DR eggNOG; ENOG4105FBJ; Bacteria. DR eggNOG; COG0179; LUCA. DR HOGENOM; HOG000063753; -. DR OMA; LTKDMIF; -. DR OrthoDB; EOG657J9Z; -. DR BioCyc; NMEN122586:GHGG-1376-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.850.10; -; 1. DR InterPro; IPR011234; Fumarylacetoacetase_C-rel. DR Pfam; PF01557; FAA_hydrolase; 1. DR SUPFAM; SSF56529; SSF56529; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF41713.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 216 FAA_hydrolase. FT {ECO:0000259|Pfam:PF01557}. SQ SEQUENCE 218 AA; 23059 MW; BA531FCD9C010BD9 CRC64; MASVFLEGEA VEVGNIFCIG RNYAAHIEEL KNEIPSEPVV FMKPSGSILN SGGTILLPEF SRDVQFECEL VLLVGKDSDG TGEGKDILGC VAGYGVGLDL TARDIQCRLK EKGLPWLKAK GFRHSACVSD FAAAGRIGNP EKVLFSLKQN GVLKQRGDTG LMIYPIREIL HKLAADYGLG KGDLVFTGTP SGVGAIGAGD NLALELDGLV RASFTVGC // ID Q7DD82_NEIMB Unreviewed; 56 AA. AC Q7DD82; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42121.1}; GN OrderedLocusNames=NMB1781 {ECO:0000313|EMBL:AAF42121.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42121.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42121.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42121.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42121.1; -; Genomic_DNA. DR PIR; G81042; G81042. DR RefSeq; NP_274781.1; NC_003112.2. DR RefSeq; WP_002214450.1; NC_003112.2. DR STRING; 122586.NMB1781; -. DR PaxDb; Q7DD82; -. DR EnsemblBacteria; AAF42121; AAF42121; NMB1781. DR GeneID; 903318; -. DR KEGG; nme:NMB1781; -. DR PATRIC; 20359519; VBINeiMen85645_2265. DR HOGENOM; HOG000218786; -. DR OrthoDB; EOG6S26K1; -. DR BioCyc; NMEN122586:GHGG-1836-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 51 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 56 AA; 6768 MW; DF1039181936662A CRC64; MMFAKHYQFI ALGIMLLLYM LILYTTDFSN LTYWMLFFIC FITGKILARL LEKSFK // ID Q9K1N9_NEIMB Unreviewed; 282 AA. AC Q9K1N9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40513.1}; GN OrderedLocusNames=NMB0042 {ECO:0000313|EMBL:AAF40513.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40513.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40513.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40513.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40513.1; -; Genomic_DNA. DR PIR; D81245; D81245. DR RefSeq; NP_273108.1; NC_003112.2. DR RefSeq; WP_002215243.1; NC_003112.2. DR ProteinModelPortal; Q9K1N9; -. DR STRING; 122586.NMB0042; -. DR PaxDb; Q9K1N9; -. DR EnsemblBacteria; AAF40513; AAF40513; NMB0042. DR GeneID; 902145; -. DR KEGG; nme:NMB0042; -. DR PATRIC; 20355041; VBINeiMen85645_0057. DR eggNOG; ENOG4105D64; Bacteria. DR eggNOG; COG0668; LUCA. DR HOGENOM; HOG000110051; -. DR KO; K03442; -. DR OMA; SNNTACR; -. DR OrthoDB; EOG61GG69; -. DR BioCyc; NMEN122586:GHGG-43-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR011066; MscC_channel_C. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR011014; MscS_channel_TM-2. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82689; SSF82689; 1. DR SUPFAM; SSF82861; SSF82861; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 111 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 282 AA; 30796 MW; 4B1326A28C13BC49 CRC64; MDFKQFDFLH LISVSGWEHL AEKAWAFGLN LAAALLIFLV GKWAAKRIVA VMRAAMTRAQ VDATLISFLC NVANIGLLIL VIIAALGRLG VSTTSVTALI GGAGLAVALS LKDQLSNFAA GALIILFRPF KVGDFIRVGG FEGYVREIKM VQTSLRTTDN EEVVLPNSVV MGNSIVNRST LPLCRAQVIV GVDYNCDLKV AKEAVLKAAV EHPLSVQNEE RQAAAYITAL GDNAIEITLW AWANEADRWT LQCDLNEQVV ENLRKVNINI PFPQRDIHII NS // ID Q9K154_NEIMB Unreviewed; 286 AA. AC Q9K154; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794}; DE EC=2.1.1.- {ECO:0000256|RuleBase:RU003794}; DE EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794}; GN Name=pilD {ECO:0000313|EMBL:AAF40775.1}; GN OrderedLocusNames=NMB0332 {ECO:0000313|EMBL:AAF40775.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40775.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40775.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40775.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates CC the N-terminal (generally Phe) residue. CC {ECO:0000256|RuleBase:RU003794}. CC -!- CATALYTIC ACTIVITY: Typically cleaves a -Gly-|-Phe- bond to CC release an N-terminal, basic peptide of 5-8 residues from type IV CC prepilin, and then N-methylates the new N-terminal amino group, CC the methyl donor being S-adenosyl-L-methionine. CC {ECO:0000256|RuleBase:RU003794}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003794}. CC -!- SIMILARITY: Belongs to the peptidase A24 family. CC {ECO:0000256|RuleBase:RU003793}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40775.1; -; Genomic_DNA. DR PIR; B53374; B53374. DR PIR; G81210; G81210. DR RefSeq; NP_273381.1; NC_003112.2. DR RefSeq; WP_002212335.1; NC_003112.2. DR STRING; 122586.NMB0332; -. DR PaxDb; Q9K154; -. DR EnsemblBacteria; AAF40775; AAF40775; NMB0332. DR GeneID; 902447; -. DR KEGG; nme:NMB0332; -. DR PATRIC; 20355803; VBINeiMen85645_0420. DR eggNOG; ENOG4105EHH; Bacteria. DR eggNOG; COG1989; LUCA. DR HOGENOM; HOG000248584; -. DR KO; K02654; -. DR OMA; RCAYCHE; -. DR OrthoDB; EOG6F55M8; -. DR BioCyc; NMEN122586:GHGG-353-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR010627; Pept_A24A_N. DR InterPro; IPR014032; Peptidase_A24A_bac. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF06750; DiS_P_DiS; 1. DR Pfam; PF01478; Peptidase_A24; 1. DR PRINTS; PR00864; PREPILNPTASE. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU003794}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|RuleBase:RU003794}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794}; KW Protease {ECO:0000256|RuleBase:RU003794}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003794}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 128 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 202 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 269 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 124 DiS_P_DiS. {ECO:0000259|Pfam:PF06750}. FT DOMAIN 134 242 Peptidase_A24. FT {ECO:0000259|Pfam:PF01478}. SQ SEQUENCE 286 AA; 31305 MW; 7EBBE92B6F1BA4FE CRC64; MSDLSVLSPF AVPLAAVFGL LVGSFLNVVI YRVPVMMERG WTVFAKEYLN LPLTEEESRT FNLMKPDSCC PKCRVPIRAW QNIPIVSYLL LRGKCASCQT KISIRYPLIE LLTGVLFGLV AWQYGWSWIT LGGLVLTAFL ISLTFIDADT QYLPDSMTLP LIWLGLIFNL DGGFVPLQSA VLGAVAGYGS LWLLCAVYKL LTGKTGMGNG DFKLIAALGA WLGISALPVL IFVSSLIGLV AAIVMRVAKG QHFAFGPALT VSGWIIFTAN DSVWRAVNWW LTHPVL // ID Q9JZV7_NEIMB Unreviewed; 110 AA. AC Q9JZV7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41293.1}; GN OrderedLocusNames=NMB0882 {ECO:0000313|EMBL:AAF41293.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41293.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41293.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41293.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41293.1; -; Genomic_DNA. DR PIR; E81147; E81147. DR RefSeq; NP_273923.1; NC_003112.2. DR RefSeq; WP_002225363.1; NC_003112.2. DR STRING; 122586.NMB0882; -. DR PaxDb; Q9JZV7; -. DR EnsemblBacteria; AAF41293; AAF41293; NMB0882. DR GeneID; 903001; -. DR KEGG; nme:NMB0882; -. DR PATRIC; 20357169; VBINeiMen85645_1098. DR HOGENOM; HOG000218892; -. DR OrthoDB; EOG6MPWXT; -. DR BioCyc; NMEN122586:GHGG-918-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 110 AA; 12189 MW; 14EADD6EA68EBED8 CRC64; MQILSFQPDI AERMLEGTEG ESVNENAQFV RTDNGYWIAW HEGVAALLAP DMPPGIPCFW VEGAESLEEL CVMVERGEFD EVEEFDGDDD EWLETAQGCG HHGDACACGH // ID Q9JYU0_NEIMB Unreviewed; 508 AA. AC Q9JYU0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Cardiolipin synthetase family protein {ECO:0000313|EMBL:AAF41795.1}; GN OrderedLocusNames=NMB1434 {ECO:0000313|EMBL:AAF41795.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41795.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41795.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41795.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41795.1; -; Genomic_DNA. DR PIR; B81083; B81083. DR RefSeq; NP_274446.1; NC_003112.2. DR RefSeq; WP_010980938.1; NC_003112.2. DR ProteinModelPortal; Q9JYU0; -. DR STRING; 122586.NMB1434; -. DR PaxDb; Q9JYU0; -. DR EnsemblBacteria; AAF41795; AAF41795; NMB1434. DR GeneID; 903855; -. DR KEGG; nme:NMB1434; -. DR PATRIC; 20358581; VBINeiMen85645_1802. DR eggNOG; ENOG4107RZC; Bacteria. DR eggNOG; COG1502; LUCA. DR HOGENOM; HOG000157571; -. DR KO; K06132; -. DR OMA; YIFKTDA; -. DR OrthoDB; EOG6VF309; -. DR BioCyc; NMEN122586:GHGG-1472-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR InterPro; IPR025202; PLD-like_dom. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR Pfam; PF13091; PLDc_2; 2. DR SMART; SM00155; PLDc; 2. DR PROSITE; PS50035; PLD; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 508 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327849. FT DOMAIN 163 190 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. FT DOMAIN 401 428 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. SQ SEQUENCE 508 AA; 57350 MW; A2DE6CAC47CA25D5 CRC64; MKTRSLISLL CLLLCSCSSW LPPLEERTES RHFNTSKPVR LDNILQIRHT PHTNGLSDIY LLNDPHEAFA ARAALIESAE HSLDLQYYIW RNDISGRLLF NLVYLAAERG VRVRLLLDDN NTRGLDDLLL ALDSHPNIEV RLFNPFVLRK WRALGYLTDF PRLNRRMHNK SFTADNRATI LGGRNIGDEY FKVGEDTVFA DLDILATGSV VGEVSHDFDR YWASHSAHNA TRIIRSGDIG KGLQALGYND ETSRHALLRY RETVEQSPLY QKIQTGCIDW QSVRTRLISD DPAKGLDRDR RKPPIAGRLQ DALKQPEKSV YLVSPYFVPT KSGTDALAKL VQDGIDVTVL TNSLQATDVA AVHSGYVKYR KPLLKAGIKL YELQPNHAVP ATKDKGLTGS SVTSLHAKTF IVDGKRIFIG SFNLDPRSAR LNTEMGVVIE SPKIAEQMER TLADTTPAYA YRVTLDRHNR LQWHDPATRK TYPNEPEAKL WKRIAAKILS LLPIEGLL // ID Q9JYV0_NEIMB Unreviewed; 336 AA. AC Q9JYV0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000256|HAMAP-Rule:MF_02042}; DE EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621}; GN Name=dusB {ECO:0000256|HAMAP-Rule:MF_02042}; GN OrderedLocusNames=NMB1421 {ECO:0000313|EMBL:AAF41782.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41782.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41782.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41782.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. {ECO:0000256|HAMAP- CC Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil in tRNA + NAD(P)(+) = uracil CC in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02042}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02042, CC ECO:0000256|PIRNR:PIRNR006621}; CC -!- SIMILARITY: Belongs to the Dus family. DusB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02042}. CC -!- SIMILARITY: Belongs to the dus family. CC {ECO:0000256|PIRNR:PIRNR006621}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41782.1; -; Genomic_DNA. DR PIR; G81085; G81085. DR RefSeq; NP_274433.1; NC_003112.2. DR RefSeq; WP_002225123.1; NC_003112.2. DR ProteinModelPortal; Q9JYV0; -. DR STRING; 122586.NMB1421; -. DR PaxDb; Q9JYV0; -. DR EnsemblBacteria; AAF41782; AAF41782; NMB1421. DR GeneID; 903843; -. DR KEGG; nme:NMB1421; -. DR PATRIC; 20358529; VBINeiMen85645_1776. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR HOGENOM; HOG000217855; -. DR KO; K05540; -. DR OMA; PVGIQIF; -. DR OrthoDB; EOG6VHZFQ; -. DR BioCyc; NMEN122586:GHGG-1459-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1200.80; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02042; DusB_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR032887; DusB. DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C. DR InterPro; IPR004652; tRNA_dU_NifR3. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00737; nifR3_yhdG; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02042, KW ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02042}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02042, KW ECO:0000256|PIRNR:PIRNR006621}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02042, KW ECO:0000256|PIRNR:PIRNR006621}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}. FT NP_BIND 16 18 FMN. {ECO:0000256|HAMAP-Rule:MF_02042}. FT NP_BIND 200 202 FMN. {ECO:0000256|HAMAP-Rule:MF_02042}. FT NP_BIND 224 225 FMN. {ECO:0000256|HAMAP-Rule:MF_02042}. FT ACT_SITE 100 100 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_02042, FT ECO:0000256|PIRSR:PIRSR006621-1}. FT BINDING 70 70 FMN. {ECO:0000256|HAMAP-Rule:MF_02042}. FT BINDING 139 139 FMN. {ECO:0000256|HAMAP-Rule:MF_02042}. SQ SEQUENCE 336 AA; 36775 MW; 985AA2FB24F11DF6 CRC64; MHIGGYFIDN PIALAPMAGI TDKPFRRLCR DFGAGWAVCE MLTSDPTLRN TRKTLHRSDF ADEGGIVAVQ IAGSDPQQMA DAARYNVSLG AQLIDINMGC PAKKVCNVQA GSALMQNEPL VAAILEAVVR AAGVPVTLKT RLGWHDDHQN LPVIAKIAED CGIAALAVHG RTRTQMYKGE ARYELIAETK CRLNIPVWVN GDITSPQKAQ AVLKQTAADG IMIGRGAQGR PWFFRDLKHY AEHGVLPPAL SLAECAAAIL NHIRAIHAFY GDTAGVRIAR KHIGWYIDEM PDGEQTRREI NRLDSAAAQY DMLAGYLERL AEKTDSWACA YRPNAF // ID Q7DD71_NEIMB Unreviewed; 363 AA. AC Q7DD71; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944}; GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944}; GN OrderedLocusNames=NMB1838 {ECO:0000313|EMBL:AAF42173.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42173.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42173.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42173.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S CC ribosomal subunit in a nucleotide-independent manner. CC {ECO:0000256|HAMAP-Rule:MF_00944}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. YchF/OLA1 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00944}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42173.1; -; Genomic_DNA. DR PIR; D81037; D81037. DR RefSeq; NP_274835.1; NC_003112.2. DR RefSeq; WP_002225667.1; NC_003112.2. DR ProteinModelPortal; Q7DD71; -. DR SMR; Q7DD71; 1-363. DR STRING; 122586.NMB1838; -. DR PaxDb; Q7DD71; -. DR EnsemblBacteria; AAF42173; AAF42173; NMB1838. DR GeneID; 903261; -. DR KEGG; nme:NMB1838; -. DR PATRIC; 20359683; VBINeiMen85645_2347. DR eggNOG; ENOG4105C3G; Bacteria. DR eggNOG; COG0012; LUCA. DR HOGENOM; HOG000087628; -. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR BioCyc; NMEN122586:GHGG-1893-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.300; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1. DR InterPro; IPR004396; ATPase_YchF/OLA1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR013029; DUF933. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR023192; TGS-like_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF06071; YchF-GTPase_C; 1. DR PIRSF; PIRSF006641; CHP00092; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00092; TIGR00092; 1. DR PROSITE; PS51710; G_OBG; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00944}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00944}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 256 OBG-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51710}. FT NP_BIND 12 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00944}. SQ SEQUENCE 363 AA; 39376 MW; CFBC0A68F1701DDE CRC64; MSLKCGIVGL PNVGKSTLFN ALTQSGIEAA NYPFCTIEPN VGIVEVPDPR MAELAKIVNP QKMQPAIVEF VDIAGLVAGA SKGEGLGNQF LANIRETDAI VNVVRCFDDD NIVHVAGRVD PIADIETIGT ELALADLASV EKAIVREEKR ARSGDKDAQK LVDLCKKLLP HLDEGKPVRS FGLDAEERAM LKPLFLLTAK PAMYVGNVAE DGFENNPHLD RLKELAAKEN APVVAVCAAM ESEIAELEDD EKAEFLAEMG LEEPGLNRLI RAGYDLLGLQ TYFTAGVKEV RAWTIHKGDT APQAAGVIHT DFERGFIRAQ VISYDDFVSL GGEAKAKEAG KMRVEGKEYV VQDGDVMHFL FNV // ID Q9JYP0_NEIMB Unreviewed; 22 AA. AC Q9JYP0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41848.1}; GN OrderedLocusNames=NMB1492 {ECO:0000313|EMBL:AAF41848.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41848.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41848.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41848.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41848.1; -; Genomic_DNA. DR PIR; B81078; B81078. DR RefSeq; NP_274500.1; NC_003112.2. DR RefSeq; WP_010980948.1; NC_003112.2. DR STRING; 122586.NMB1492; -. DR PaxDb; Q9JYP0; -. DR EnsemblBacteria; AAF41848; AAF41848; NMB1492. DR GeneID; 903914; -. DR KEGG; nme:NMB1492; -. DR BioCyc; NMEN122586:GHGG-1532-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 22 AA; 2390 MW; 4735893BDFE4A1DD CRC64; MPERRETAEP SAGTGTNRSL ND // ID Q9JYR9_NEIMB Unreviewed; 462 AA. AC Q9JYR9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743}; DE Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743}; DE EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743}; GN Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743, GN ECO:0000313|EMBL:AAF41817.1}; GN OrderedLocusNames=NMB1458 {ECO:0000313|EMBL:AAF41817.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41817.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41817.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41817.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)- CC malate from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743, CC ECO:0000256|SAAS:SAAS00219779}. CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic CC A site, and the non-catalytic B site that may play a role in the CC transfer of substrate or product between the active site and the CC solvent. Alternatively, the B site may bind allosteric effectors. CC {ECO:0000256|HAMAP-Rule:MF_00743}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Fumarase subfamily. {ECO:0000256|HAMAP-Rule:MF_00743}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41817.1; -; Genomic_DNA. DR PIR; C81082; C81082. DR RefSeq; NP_274469.1; NC_003112.2. DR RefSeq; WP_002225106.1; NC_003112.2. DR ProteinModelPortal; Q9JYR9; -. DR SMR; Q9JYR9; 4-459. DR STRING; 122586.NMB1458; -. DR PaxDb; Q9JYR9; -. DR EnsemblBacteria; AAF41817; AAF41817; NMB1458. DR GeneID; 903880; -. DR KEGG; nme:NMB1458; -. DR PATRIC; 20358659; VBINeiMen85645_1839. DR eggNOG; ENOG4105C9Q; Bacteria. DR eggNOG; COG0114; LUCA. DR HOGENOM; HOG000061737; -. DR KO; K01679; -. DR OMA; FELNVYN; -. DR OrthoDB; EOG6V1M4M; -. DR BioCyc; NMEN122586:GHGG-1498-MONOMER; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.275.10; -; 1. DR HAMAP; MF_00743; FumaraseC; 1. DR InterPro; IPR005677; Fum_hydII. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00979; fumC_II; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00429438, KW ECO:0000313|EMBL:AAF41817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}. FT DOMAIN 11 341 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 407 460 FumaraseC_C. {ECO:0000259|Pfam:PF10415}. FT REGION 128 131 B site. {ECO:0000256|HAMAP- FT Rule:MF_00743}. FT REGION 138 140 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00743}. FT BINDING 99 99 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00743}. SQ SEQUENCE 462 AA; 49332 MW; 4E44AD0D3489F250 CRC64; MSTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV KKAAAATNVS LGRIKPEQAD LITQAADDVL SGKLDGQFPL VVWQTGSGTQ SNMNMNEVLA NRANEIAGTG LAAYQPVHPN DHVNHAQSTN DAFPTAIHVA AAIEINRHLI PAVKALRDTL DKKAQAFAPI VKIGRTHLQD ATPLTLGQEF SGYVSQLDHG LGRLNDALKD LYELALGGTA VGTGLNSHPE YAEKAAAKLA ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG ASGNFELNVY MPVIAYNLLQ SIHLLGDACN SFNEHCAIGI EPVPEKIDYF LHHSLMLVTA LNRKIGYENA AKVAKTAYKN NKSLRETAVE LGLLTGEEFD ELVVPADMVH PR // ID Q9JZ13_NEIMB Unreviewed; 76 AA. AC Q9JZ13; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41715.1}; GN OrderedLocusNames=NMB1340 {ECO:0000313|EMBL:AAF41715.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41715.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41715.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41715.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41715.1; -; Genomic_DNA. DR PIR; D81094; D81094. DR STRING; 122586.NMB1340; -. DR PaxDb; Q9JZ13; -. DR EnsemblBacteria; AAF41715; AAF41715; NMB1340. DR HOGENOM; HOG000027831; -. DR OMA; EIFVFAY; -. DR OrthoDB; EOG6ZKZ0Z; -. DR BioCyc; NMEN122586:GHGG-1378-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 76 AA; 9200 MW; C54981A975881420 CRC64; MVICQQTRLL IGFRVEQIEH FFQVFPCFQN FYNFLKTLNL NYFFRFDLEI FVFAYYFSQT KIKGLATPSL PIKHST // ID Q9JXN5_NEIMB Unreviewed; 127 AA. AC Q9JXN5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42286.1}; GN OrderedLocusNames=NMB1957 {ECO:0000313|EMBL:AAF42286.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42286.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42286.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42286.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42286.1; -; Genomic_DNA. DR PIR; F81021; F81021. DR ProteinModelPortal; Q9JXN5; -. DR PaxDb; Q9JXN5; -. DR EnsemblBacteria; AAF42286; AAF42286; NMB1957. DR PATRIC; 20359973; VBINeiMen85645_2491. DR HOGENOM; HOG000027852; -. DR OMA; HIGRGAY; -. DR OrthoDB; EOG6PZXGR; -. DR BioCyc; NMEN122586:GHGG-2014-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR SUPFAM; SSF51161; SSF51161; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 127 AA; 14044 MW; D3211CB06086E3AB CRC64; MMGSKFFFLL LRFAGSGLPP SHMRGIGIVG RRVRGFLARR VSPHIGRGVN IERGAYVFPD TVLGDGSGIG ANCEICRGLV VGKNVMMEPE CLFYSNNHKF DRSKNALRAT RKSVRLRWRT MSGRGTG // ID Q7DD59_NEIMB Unreviewed; 258 AA. AC Q7DD59; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42294.1}; GN OrderedLocusNames=NMB1965 {ECO:0000313|EMBL:AAF42294.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42294.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42294.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42294.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU362044}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362044}. CC -!- SIMILARITY: Belongs to the MlaE permease family. CC {ECO:0000256|RuleBase:RU362044}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU362044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42294.1; -; Genomic_DNA. DR PIR; F81022; F81022. DR RefSeq; NP_274959.1; NC_003112.2. DR RefSeq; WP_002219882.1; NC_003112.2. DR STRING; 122586.NMB1965; -. DR PaxDb; Q7DD59; -. DR EnsemblBacteria; AAF42294; AAF42294; NMB1965. DR GeneID; 904180; -. DR KEGG; nme:NMB1965; -. DR PATRIC; 20359991; VBINeiMen85645_2500. DR eggNOG; ENOG4105CY3; Bacteria. DR eggNOG; COG0767; LUCA. DR HOGENOM; HOG000255130; -. DR KO; K02066; -. DR OMA; MEIGYSS; -. DR OrthoDB; EOG6RJV8Q; -. DR BioCyc; NMEN122586:GHGG-2022-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR003453; ABC_MlaE_Proteobac. DR InterPro; IPR030802; Permease_MalE. DR PANTHER; PTHR30188; PTHR30188; 1. DR Pfam; PF02405; MlaE; 1. DR TIGRFAMs; TIGR00056; TIGR00056; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU362044}; KW Cell membrane {ECO:0000256|RuleBase:RU362044}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU362044}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362044}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 46 70 Helical. {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 155 177 Helical. {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 197 216 Helical. {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 237 256 Helical. {ECO:0000256|RuleBase:RU362044}. SQ SEQUENCE 258 AA; 27399 MW; 63ACAE66F1E4D878 CRC64; MNFIRSVGAK TLGLIQSLGS ITLFLLNILA KSGTAFVRPR LSVRQVYFAG VLSVLIVAVS GLFVGMVLGL QGYTQLSKFK SADILGYMVA ASLLRELGPV LAAILFASSA GGAMTSEIGL MKTTEQLEAM NVMAVNPVAR VVAPRFWAGV FSMPLLASIF NVAGIFGAYL VGVTWLGLDS GIFWSQMQNN ITIHYDVING LIKSAAFGVA VTLIAVHQGF HCVPTSEGIL RASTRTVVSS ALTILAVDFI LTAWMFTD // ID Q9JY12_NEIMB Unreviewed; 52 AA. AC Q9JY12; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42133.1}; GN OrderedLocusNames=NMB1795 {ECO:0000313|EMBL:AAF42133.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42133.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42133.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42133.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42133.1; -; Genomic_DNA. DR PIR; A81042; A81042. DR STRING; 122586.NMB1795; -. DR PaxDb; Q9JY12; -. DR EnsemblBacteria; AAF42133; AAF42133; NMB1795. DR PATRIC; 20359555; VBINeiMen85645_2283. DR OMA; SAHRDEC; -. DR BioCyc; NMEN122586:GHGG-1850-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 52 AA; 6018 MW; 280F5A2090A82D7B CRC64; MIGAVSFESA HRDECPRAVP IPIYRLFRIG CRCEMTDGCR NGGRRKWEEM TD // ID Q9K0Y7_NEIMB Unreviewed; 58 AA. AC Q9K0Y7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40855.1}; GN OrderedLocusNames=NMB0417 {ECO:0000313|EMBL:AAF40855.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40855.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40855.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40855.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40855.1; -; Genomic_DNA. DR PIR; E81202; E81202. DR RefSeq; NP_273465.1; NC_003112.2. DR RefSeq; WP_002218790.1; NC_003112.2. DR STRING; 122586.NMB0417; -. DR PaxDb; Q9K0Y7; -. DR EnsemblBacteria; AAF40855; AAF40855; NMB0417. DR GeneID; 902533; -. DR KEGG; nme:NMB0417; -. DR PATRIC; 20356028; VBINeiMen85645_0529. DR HOGENOM; HOG000219097; -. DR OrthoDB; EOG6PW24H; -. DR BioCyc; NMEN122586:GHGG-441-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 58 AA; 6398 MW; 27B295981AFA8879 CRC64; MKSRRFFKAL LLIAALVGAF YAGMRTQAYL YEDLCLDLGG GKNPGSYPIC VIEKVPAR // ID Q9JZJ7_NEIMB Unreviewed; 321 AA. AC Q9JZJ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41422.1}; GN OrderedLocusNames=NMB1022 {ECO:0000313|EMBL:AAF41422.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41422.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41422.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41422.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41422.1; -; Genomic_DNA. DR PIR; E81129; E81129. DR RefSeq; NP_274056.1; NC_003112.2. DR RefSeq; WP_002222411.1; NC_003112.2. DR ProteinModelPortal; Q9JZJ7; -. DR STRING; 122586.NMB1022; -. DR PaxDb; Q9JZJ7; -. DR EnsemblBacteria; AAF41422; AAF41422; NMB1022. DR GeneID; 903160; -. DR KEGG; nme:NMB1022; -. DR PATRIC; 20357579; VBINeiMen85645_1306. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; SVHHEIV; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-1059-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38002 MW; 9E1C52A7AFAFEFBA CRC64; MSYTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS QTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLCK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRALKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JYF8_NEIMB Unreviewed; 314 AA. AC Q9JYF8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Putative tellurite resistance protein {ECO:0000313|EMBL:AAF41955.1}; GN OrderedLocusNames=NMB1603 {ECO:0000313|EMBL:AAF41955.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41955.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41955.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41955.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41955.1; -; Genomic_DNA. DR PIR; E81064; E81064. DR RefSeq; NP_274609.1; NC_003112.2. DR RefSeq; WP_002225019.1; NC_003112.2. DR STRING; 122586.NMB1603; -. DR PaxDb; Q9JYF8; -. DR DNASU; 904294; -. DR EnsemblBacteria; AAF41955; AAF41955; NMB1603. DR GeneID; 904294; -. DR KEGG; nme:NMB1603; -. DR PATRIC; 20359086; VBINeiMen85645_2055. DR eggNOG; ENOG4107X5E; Bacteria. DR eggNOG; COG1275; LUCA. DR HOGENOM; HOG000120585; -. DR KO; K03304; -. DR OMA; TIAGISW; -. DR OrthoDB; EOG6P0709; -. DR BioCyc; NMEN122586:GHGG-1651-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004695; Voltage-dep_anion_channel. DR Pfam; PF03595; SLAC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 281 303 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 314 AA; 32843 MW; 169AF5192BB36E53 CRC64; MSASKKFPIP LSYFSIALGL FALGLSWRYG ASVGLLPALA AESLLAAASV VWLLLVAAYL IKMFAYRNDF LSDLRDLVQC CFISAIPITA MLEGLALKPY QAGAAAVLIY VGVAGQLAFS MYRAAGLWRG LHSLEATTPI IYLPTVATNF VSASSLAALG HHDYAALFFG AGMFSWLSLE ASILGRLRTA APVGTAARGV VGIQLAPAFV GCGAYFAVGG KVDGFALALI GYGCLQLLFL LRLTRWFWEG GFTMSFWGFS FGFAAMAGCG LHLAASGVLS GLGLTLATAG SAGVALLLVG TLHRIATGRF LVRS // ID Q9JYW2_NEIMB Unreviewed; 120 AA. AC Q9JYW2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41769.1}; GN OrderedLocusNames=NMB1406 {ECO:0000313|EMBL:AAF41769.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41769.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41769.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41769.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41769.1; -; Genomic_DNA. DR PIR; C81087; C81087. DR PaxDb; Q9JYW2; -. DR EnsemblBacteria; AAF41769; AAF41769; NMB1406. DR BioCyc; NMEN122586:GHGG-1444-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 115 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 120 AA; 14532 MW; C0E0144357DCFD57 CRC64; MIAKSLFFRC QKIYFIYFIL FICLYLNISY DGEIFIYFII NFTHLLICHG ILLVFCRIFP YENIPFTIFL NFISLFLIFL PLIFTIRELI DSYYIESIIN LFLILIPHVI FLIYLKGKQI // ID Q7DD47_NEIMB Unreviewed; 259 AA. AC Q7DD47; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=Exodeoxyribonuclease {ECO:0000313|EMBL:AAF42400.1}; DE EC=3.1.11.2 {ECO:0000313|EMBL:AAF42400.1}; GN Name=exoA {ECO:0000313|EMBL:AAF42400.1}; GN OrderedLocusNames=NMB2082 {ECO:0000313|EMBL:AAF42400.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42400.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42400.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42400.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2JC5} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RX PubMed=17318183; DOI=10.1038/sj.emboj.7601593; RA Carpenter E.P., Corbett A., Thomson H., Adacha J., Jensen K., RA Bergeron J., Kasampalidis I., Exley R., Winterbotham M., Tang C., RA Baldwin G.S., Freemont P.; RT "AP endonuclease paralogues with distinct activities in DNA repair and RT bacterial pathogenesis."; RL EMBO J. 26:1363-1372(2007). RN [3] {ECO:0000213|PDB:4B5F, ECO:0000213|PDB:4B5G, ECO:0000213|PDB:4B5H} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RX PubMed=23035246; DOI=10.1073/pnas.1206563109; RA Lu D., Silhan J., MacDonald J.T., Carpenter E.P., Jensen K., RA Tang C.M., Baldwin G.S., Freemont P.S.; RT "Structural basis for the recognition and cleavage of abasic DNA in RT Neisseria meningitidis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:16852-16857(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42400.1; -; Genomic_DNA. DR PIR; H81009; H81009. DR RefSeq; NP_275071.1; NC_003112.2. DR RefSeq; WP_002225717.1; NC_003112.2. DR PDB; 2JC5; X-ray; 1.50 A; A=1-259. DR PDB; 4B5F; X-ray; 2.00 A; A=1-259. DR PDB; 4B5G; X-ray; 2.75 A; A/B/C=1-259. DR PDB; 4B5H; X-ray; 3.05 A; A=1-259. DR PDB; 4B5I; X-ray; 2.56 A; A=1-259. DR PDB; 4B5J; X-ray; 2.10 A; A=1-259. DR PDB; 4B5M; X-ray; 2.76 A; A/B/C=1-259. DR PDBsum; 2JC5; -. DR PDBsum; 4B5F; -. DR PDBsum; 4B5G; -. DR PDBsum; 4B5H; -. DR PDBsum; 4B5I; -. DR PDBsum; 4B5J; -. DR PDBsum; 4B5M; -. DR ProteinModelPortal; Q7DD47; -. DR SMR; Q7DD47; 1-259. DR STRING; 122586.NMB2082; -. DR PaxDb; Q7DD47; -. DR EnsemblBacteria; AAF42400; AAF42400; NMB2082. DR GeneID; 903973; -. DR KEGG; nme:NMB2082; -. DR PATRIC; 20360332; VBINeiMen85645_2663. DR eggNOG; ENOG4105CGK; Bacteria. DR eggNOG; COG0708; LUCA. DR HOGENOM; HOG000034586; -. DR KO; K01142; -. DR OMA; PDQYTWW; -. DR OrthoDB; EOG6TBHJS; -. DR BioCyc; NMEN122586:GHGG-2148-MONOMER; -. DR EvolutionaryTrace; Q7DD47; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.60.10.10; -; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR PANTHER; PTHR22748; PTHR22748; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; SSF56219; 1. DR TIGRFAMs; TIGR00633; xth; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2JC5, ECO:0000213|PDB:4B5F, KW ECO:0000213|PDB:4B5G, ECO:0000213|PDB:4B5H}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF42400.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 247 Endo/exonuclease/phosphatase. FT {ECO:0000259|Pfam:PF03372}. SQ SEQUENCE 259 AA; 29659 MW; 4718246210AD55E6 CRC64; MLKIISANVN GIRSAYKKGF YEYIAASGAD IVCVQELKAQ EADLSADMKN PHGMHGHWHC AEKRGYSGVA VYSKRKPDNV QIGMGIEEFD REGRFVRCDF GRLSVISLYL PSGSSAEERQ QVKYRFLDAF YPMLEAMKNE GRDIVVCGDW NIAHQNIDLK NWKGNQKNSG FLPEEREWIG KVIHKLGWTD MWRTLYPDVP GYTWWSNRGQ AYAKDVGWRI DYQMVTPELA AKAVSAHVYK DEKFSDHAPL VVEYDYAAE // ID Q9JZ79_NEIMB Unreviewed; 225 AA. AC Q9JZ79; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41633.1}; GN OrderedLocusNames=NMB1253 {ECO:0000313|EMBL:AAF41633.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41633.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41633.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41633.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41633.1; -; Genomic_DNA. DR PIR; F81104; F81104. DR RefSeq; NP_274276.1; NC_003112.2. DR RefSeq; WP_002222408.1; NC_003112.2. DR PaxDb; Q9JZ79; -. DR EnsemblBacteria; AAF41633; AAF41633; NMB1253. DR GeneID; 903676; -. DR KEGG; nme:NMB1253; -. DR PATRIC; 20358111; VBINeiMen85645_1567. DR HOGENOM; HOG000218969; -. DR OMA; GWMNIAS; -. DR OrthoDB; EOG6NGVQR; -. DR BioCyc; NMEN122586:GHGG-1291-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 225 AA; 24285 MW; 378CE7D92AC26C1A CRC64; MPAALIKDFL LTQGLKLPLD EVRAAYLTAQ TVMDMGTASI DRSVLWRSDE GWKLADYLSC DNVREDALKR LFMALDSVFS RSTGVRSAAV YALMPSENQA FQLICLSRQG EVLENLWDLD EAAGKVSLAC RSAQSGWMNV ASDVRRWLDL GELSGERNHA SAAQISIPVC TESGGVLGVV HVEFECAECA GTAAQVEWVA LALALSEPLK LLLGMSAGKD GSEDV // ID Q9JXB2_NEIMB Unreviewed; 297 AA. AC Q9JXB2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42447.1}; GN OrderedLocusNames=NMB2139 {ECO:0000313|EMBL:AAF42447.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42447.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42447.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42447.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42447.1; -; Genomic_DNA. DR PIR; A81002; A81002. DR RefSeq; NP_275124.1; NC_003112.2. DR RefSeq; WP_002244359.1; NC_003112.2. DR ProteinModelPortal; Q9JXB2; -. DR PaxDb; Q9JXB2; -. DR EnsemblBacteria; AAF42447; AAF42447; NMB2139. DR GeneID; 903233; -. DR KEGG; nme:NMB2139; -. DR PATRIC; 20360470; VBINeiMen85645_2731. DR eggNOG; ENOG4105D78; Bacteria. DR eggNOG; COG1752; LUCA. DR HOGENOM; HOG000261884; -. DR KO; K07001; -. DR OMA; ILFRRGN; -. DR OrthoDB; EOG6KDKSZ; -. DR BioCyc; NMEN122586:GHGG-2204-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR002641; Patatin/PLipase_A2-rel. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; SSF52151; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 297 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328291. FT DOMAIN 45 202 Patatin. {ECO:0000259|Pfam:PF01734}. SQ SEQUENCE 297 AA; 30963 MW; 76012701A91278EB CRC64; MVTFSKIRPL LAIAAAALLA ACGTAGNNAV RKPVQTAKPA AVVGLALGGG ASKGFAHVGI IKVLKENGIP VKVVTGTSAG SIVGSLFASG MSPDRLELEA EILGKTDLVD LTLSTSGFIK GEKLQNYINR KVGGRQIQQF PIKFAAVATD FETGKAVAFN QGNAGQAVRA SAAIPNVFQP VIIGRHTYVD GGLSQPVPVS AARRQGANFV IAVDISARPG KNISQGFFSY LDQTLNVMSV SALQNELGQA DVVIKPQVLD LGAVGGFDQK KRAIRLGEEA ARAALPEIKR KLAAYRY // ID Q9K164_NEIMB Unreviewed; 322 AA. AC Q9K164; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40759.1}; GN OrderedLocusNames=NMB0314 {ECO:0000313|EMBL:AAF40759.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40759.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40759.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40759.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40759.1; -; Genomic_DNA. DR PIR; H81213; H81213. DR RefSeq; NP_273363.1; NC_003112.2. DR RefSeq; WP_002224861.1; NC_003112.2. DR STRING; 122586.NMB0314; -. DR PaxDb; Q9K164; -. DR EnsemblBacteria; AAF40759; AAF40759; NMB0314. DR GeneID; 902430; -. DR KEGG; nme:NMB0314; -. DR PATRIC; 20355757; VBINeiMen85645_0398. DR eggNOG; COG4255; LUCA. DR HOGENOM; HOG000219117; -. DR OMA; FTEYGWQ; -. DR OrthoDB; EOG6X6RD6; -. DR BioCyc; NMEN122586:GHGG-334-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR016631; Regulatory_RpfE. DR PIRSF; PIRSF015283; Regulatory_RpfE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 322 AA; 36760 MW; 5A9D24D16DB487A7 CRC64; MKLTLAIPSL NLDEDEIRIP LCLHAFNKIL QYGSLHRQSC TASAFYARYL WCGRLVERAA QSLNMPSEAV ALATPVWQKM GMHQANVLTA EYLNVGTDEA ERICRDLSAF YGDIPWRFVP VLPELWLVSL PCAYRWGAKP VLDLGGLLGA DDQPDGEDAL EWLRVQTEIQ MWLAAHPVNH NRKKRGLPEL NGLWLWDGTN GGAQGGTLFA DTVWSRFHSD RRALPDNFRA YEETAAHLPD THHILFMDDL RLTALTGDRE RYAAILQQWE ERWFAPIYEA VRTGKIKRLD ITTDGQHGGT LTFKPADRWK FWRGAKTFDG IW // ID Q9JZG8_NEIMB Unreviewed; 118 AA. AC Q9JZG8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079}; DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079}; GN Name=folB {ECO:0000313|EMBL:AAF41459.1}; GN OrderedLocusNames=NMB1063 {ECO:0000313|EMBL:AAF41459.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41459.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41459.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41459.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6- CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8- CC dihydropterin + glycolaldehyde. {ECO:0000256|RuleBase:RU362079}. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2- CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate CC from 7,8-dihydroneopterin triphosphate: step 3/4. CC {ECO:0000256|RuleBase:RU362079}. CC -!- SIMILARITY: Belongs to the DHNA family. CC {ECO:0000256|RuleBase:RU362079}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41459.1; -; Genomic_DNA. DR PIR; A81127; A81127. DR RefSeq; NP_274096.1; NC_003112.2. DR RefSeq; WP_002221051.1; NC_003112.2. DR ProteinModelPortal; Q9JZG8; -. DR STRING; 122586.NMB1063; -. DR PaxDb; Q9JZG8; -. DR EnsemblBacteria; AAF41459; AAF41459; NMB1063. DR GeneID; 903480; -. DR KEGG; nme:NMB1063; -. DR PATRIC; 20357669; VBINeiMen85645_1351. DR eggNOG; ENOG4107ZVW; Bacteria. DR eggNOG; COG1539; LUCA. DR HOGENOM; HOG000217627; -. DR KO; K01633; -. DR OMA; DYASVST; -. DR OrthoDB; EOG6ND0KG; -. DR BioCyc; NMEN122586:GHGG-1100-MONOMER; -. DR UniPathway; UPA00077; UER00154. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR006156; Dihydroneopterin_aldolase. DR InterPro; IPR006157; FolB_dom. DR Pfam; PF02152; FolB; 1. DR SMART; SM00905; FolB; 1. DR TIGRFAMs; TIGR00525; folB; 1. DR TIGRFAMs; TIGR00526; folB_dom; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Folate biosynthesis {ECO:0000256|RuleBase:RU362079}; KW Lyase {ECO:0000256|RuleBase:RU362079, ECO:0000313|EMBL:AAF41459.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 113 FolB. {ECO:0000259|SMART:SM00905}. SQ SEQUENCE 118 AA; 13381 MW; AAE9C987AEDCDCBC CRC64; MDKIFLHGMK ADTLIGVYGW ERERLQTLIV DLDIGVPEKA GSDDDIANTV HYAEVCETLR RHLKEQDFLL LEALAEYIAD LVLGYFGAVW VRVKIVKPGI LEGVREVGVE IERGKRED // ID Q9K0F6_NEIMB Unreviewed; 139 AA. AC Q9K0F6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41071.1}; GN OrderedLocusNames=NMB0650 {ECO:0000313|EMBL:AAF41071.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41071.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41071.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41071.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41071.1; -; Genomic_DNA. DR PIR; E81173; E81173. DR RefSeq; NP_273692.1; NC_003112.2. DR RefSeq; WP_010980821.1; NC_003112.2. DR STRING; 122586.NMB0650; -. DR PaxDb; Q9K0F6; -. DR EnsemblBacteria; AAF41071; AAF41071; NMB0650. DR GeneID; 902762; -. DR KEGG; nme:NMB0650; -. DR PATRIC; 20356599; VBINeiMen85645_0818. DR eggNOG; ENOG4106FJ1; Bacteria. DR eggNOG; ENOG410XUYE; LUCA. DR HOGENOM; HOG000218830; -. DR OMA; IDNIYNI; -. DR OrthoDB; EOG62ZHWC; -. DR BioCyc; NMEN122586:GHGG-677-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 139 AA; 16062 MW; A756DAC86BC3A064 CRC64; MGSNEQRKVT MWKIIKEDSD DLEFAIKCLF SQSIDLNEFK LWIEQVIRDM PIEDIPFYIF DLADFDGGIA DIDNIVGFVS SCRLSKSKKN ALTGIAFLRG IDVYDPPISK EKALKALEKH PEIYQKFQHF FPFVELPPL // ID Q9JXG7_NEIMB Unreviewed; 109 AA. AC Q9JXG7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42379.1}; GN OrderedLocusNames=NMB2059 {ECO:0000313|EMBL:AAF42379.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42379.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42379.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42379.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42379.1; -; Genomic_DNA. DR PIR; D81012; D81012. DR RefSeq; NP_275049.1; NC_003112.2. DR RefSeq; WP_002215012.1; NC_003112.2. DR STRING; 122586.NMB2059; -. DR PaxDb; Q9JXG7; -. DR EnsemblBacteria; AAF42379; AAF42379; NMB2059. DR GeneID; 904021; -. DR KEGG; nme:NMB2059; -. DR PATRIC; 20360274; VBINeiMen85645_2637. DR HOGENOM; HOG000218720; -. DR OrthoDB; EOG6GTZMF; -. DR BioCyc; NMEN122586:GHGG-2122-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 19 57 {ECO:0000256|SAM:Coils}. FT COILED 59 93 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 109 AA; 12792 MW; C46FADFB65582800 CRC64; MKQNIEKLES SVYTLVQKFE TLVSENRRLK ETVAELKRAH ERQKLEHETA VDELSEALLV QVGKLKEDLQ NKIDSLTEEN TRYRSLLEQS REKISALAAR LPQWQETQQ // ID Q9K135_NEIMB Unreviewed; 254 AA. AC Q9K135; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 108. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF40799.1}; GN OrderedLocusNames=NMB0356 {ECO:0000313|EMBL:AAF40799.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40799.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40799.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40799.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40799.1; -; Genomic_DNA. DR PIR; C81208; C81208. DR RefSeq; NP_273405.1; NC_003112.2. DR RefSeq; WP_002224886.1; NC_003112.2. DR ProteinModelPortal; Q9K135; -. DR STRING; 122586.NMB0356; -. DR PaxDb; Q9K135; -. DR EnsemblBacteria; AAF40799; AAF40799; NMB0356. DR GeneID; 902471; -. DR KEGG; nme:NMB0356; -. DR PATRIC; 20355861; VBINeiMen85645_0449. DR eggNOG; ENOG4108IUZ; Bacteria. DR eggNOG; COG1137; LUCA. DR KO; K06861; -. DR OMA; YYLGDNF; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NMEN122586:GHGG-377-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR032823; BCA_ABC_TP_C. DR InterPro; IPR030921; LPS_export_LptB. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF12399; BCA_ABC_TP_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04406; LPS_export_lptB; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40799.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40799.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 18 250 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 254 AA; 28173 MW; 5684BE6FE15F0925 CRC64; MPTEDIEEIF MSANVSRLVV QNLQKSFKKR QVVKSFSLEI ESGEVIGLLG PNGAGKTTSF YMIVGLIAAD AGSVTLDGQE LRHLPIHERA RLGVGYLPQE ASIFRKMTVE QNIRAILEIR TKDKNQIDRE IEKLLADLNI GHLRRSPAPS LSGGERRRVE IARVLAMKPH FILLDEPFAG VDPIAVIDIQ KIIGFLKSRG IGVLITDHNV RETLSICDRA YIISDGTVLA SGKPDDLVGN EQVRSVYLGK NFKY // ID Q9JXR7_NEIMB Unreviewed; 129 AA. AC Q9JXR7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42245.1}; GN OrderedLocusNames=NMB1915 {ECO:0000313|EMBL:AAF42245.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42245.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42245.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42245.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42245.1; -; Genomic_DNA. DR PIR; B81029; B81029. DR RefSeq; NP_274909.1; NC_003112.2. DR RefSeq; WP_010981007.1; NC_003112.2. DR STRING; 122586.NMB1915; -. DR PaxDb; Q9JXR7; -. DR EnsemblBacteria; AAF42245; AAF42245; NMB1915. DR GeneID; 904247; -. DR KEGG; nme:NMB1915; -. DR PATRIC; 20359875; VBINeiMen85645_2442. DR OMA; TVYFKKG; -. DR OrthoDB; EOG6CK7RH; -. DR BioCyc; NMEN122586:GHGG-1972-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 14476 MW; 9E3C9D4AD49DB213 CRC64; MKTSTVVFGG FFMADNGERI QIPVLENPDI REINHFFSVS NFEKKTGVLV FRIIPEPEFG NTELTVYFKK GYYSGLTKTS TALPRLAVLV FVNPLYQTKT NTRANSLTAT RQSKCRLKQL GLSDGISFA // ID Q9JYK2_NEIMB Unreviewed; 404 AA. AC Q9JYK2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41898.1}; GN OrderedLocusNames=NMB1543 {ECO:0000313|EMBL:AAF41898.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41898.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41898.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41898.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41898.1; -; Genomic_DNA. DR PIR; B81071; B81071. DR RefSeq; NP_274550.1; NC_003112.2. DR RefSeq; WP_002221956.1; NC_003112.2. DR STRING; 122586.NMB1543; -. DR PaxDb; Q9JYK2; -. DR EnsemblBacteria; AAF41898; AAF41898; NMB1543. DR GeneID; 904083; -. DR KEGG; nme:NMB1543; -. DR PATRIC; 20358920; VBINeiMen85645_1974. DR eggNOG; ENOG4105HKQ; Bacteria. DR eggNOG; COG2946; LUCA. DR HOGENOM; HOG000218820; -. DR KO; K07467; -. DR OMA; TEWHEST; -. DR OrthoDB; EOG651SRG; -. DR BioCyc; NMEN122586:GHGG-1584-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR InterPro; IPR003491; Rep_trans. DR Pfam; PF02486; Rep_trans; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 404 AA; 47114 MW; BB0EF3716E70CABB CRC64; MSEVEYFSHF ISDGKGKLLE IPQRRGKQDG VFVDWISFTF HEDTLLKVSG CPLFSDAEYM YVLSRKLEEI LGFGITRKCK SRGNKFYESM YRLGSDDVDY GEVHFGGQRN TVLVELKGTG CSVASPGWEL RLKQFLDDSI RTRITRIDLA LDFFDGEYTP DQALLDHDNG FFDNSNQRPK SETIGTAWRN EDGSGKTFYV GRKKNSRFVR VYEKGRQLGD KESKWVRFEI QFNYGDIEIP LDILINQGSY FCGAFPICRK FKNMPVPERF DQRKKKLNLT FEHKLHYAKN AVGKLVNFMI EMGFDNSEIV ESLKADSGFP KGLEPEKYAL EMLRDGLKHG FIHEQPDIDL EIELDELGVI AFKNSDKFDR EKRLFSPDYD VEKERKYQEY LSKVYHQNVD YDYF // ID Q9JZP6_NEIMB Unreviewed; 393 AA. AC Q9JZP6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138}; DE EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138}; DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138}; GN Name=sucB {ECO:0000313|EMBL:AAF41362.1}; GN OrderedLocusNames=NMB0956 {ECO:0000313|EMBL:AAF41362.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41362.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41362.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41362.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). CC {ECO:0000256|RuleBase:RU361138}. CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)- CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S- CC succinyldihydrolipoyl)lysine. {ECO:0000256|RuleBase:RU361138}. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000256|RuleBase:RU361138}; CC Note=Binds 1 lipoyl cofactor covalently. CC {ECO:0000256|RuleBase:RU361138}; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. CC {ECO:0000256|RuleBase:RU361138}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000256|RuleBase:RU003423}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. CC {ECO:0000256|RuleBase:RU361138}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41362.1; -; Genomic_DNA. DR PIR; D81139; D81139. DR RefSeq; NP_273994.1; NC_003112.2. DR RefSeq; WP_002225318.1; NC_003112.2. DR ProteinModelPortal; Q9JZP6; -. DR SMR; Q9JZP6; 161-393. DR STRING; 122586.NMB0956; -. DR PaxDb; Q9JZP6; -. DR EnsemblBacteria; AAF41362; AAF41362; NMB0956. DR GeneID; 903076; -. DR KEGG; nme:NMB0956; -. DR PATRIC; 20357393; VBINeiMen85645_1211. DR eggNOG; ENOG4105C7S; Bacteria. DR eggNOG; COG0508; LUCA. DR HOGENOM; HOG000281563; -. DR KO; K00658; -. DR OMA; HRYYDIG; -. DR OrthoDB; EOG610413; -. DR BioCyc; NMEN122586:GHGG-993-MONOMER; -. DR UniPathway; UPA00868; UER00840. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. DR Gene3D; 4.10.320.10; -; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR004167; E3-bd. DR InterPro; IPR011053; Single_hybrid_motif. DR InterPro; IPR006255; SucB. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR01347; sucB; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU003765, KW ECO:0000313|EMBL:AAF41362.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lipoyl {ECO:0000256|RuleBase:RU003765, ECO:0000256|SAAS:SAAS00065550}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003765, KW ECO:0000313|EMBL:AAF41362.1}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}. FT DOMAIN 2 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 393 AA; 41517 MW; 748E1D04420B2A0E CRC64; MIIDVKVPML SESVSEGTLL EWKKKVGEAV ARDEILIDIE TDKVVLEVPS PQAGVLVEIV AQDGETVVAD QVLARVDTAA TAAAEAPAAA PAEAAPAAAP AATQNNAAMP AAAKLAAETG VDVNALQGSG RDGRVLKEDV QNAAAKPAGA AAPAVALPAG ARPEERVPMS RLRARVAERL LASQQENAIL TTFNEVNMKP IMDLRAKYKE KFEKEHGVKL GFMSFFVKAA VAALKKYPVV NASVDGKDIV YHGYFDIGIA IGSPRGLVVP ILRDADQMSI ADIEQAIVDY AKKAKDGKIA IEDLTGGTFS ITNGGTFGSM MSTPIINPPQ SAILGMHATK ERAVVENGQV VVRPMMYLAL SYDHRIIDGR EAVLTLVAIK DALEDPARLL LDL // ID Q9JY60_NEIMB Unreviewed; 365 AA. AC Q9JY60; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Cytochrome c oxidase, subunit III {ECO:0000313|EMBL:AAF42068.1}; DE EC=1.9.3.1 {ECO:0000313|EMBL:AAF42068.1}; GN Name=fixP {ECO:0000313|EMBL:AAF42068.1}; GN OrderedLocusNames=NMB1723 {ECO:0000313|EMBL:AAF42068.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42068.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42068.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42068.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42068.1; -; Genomic_DNA. DR PIR; C81050; C81050. DR RefSeq; NP_274726.1; NC_003112.2. DR RefSeq; WP_002244268.1; NC_003112.2. DR ProteinModelPortal; Q9JY60; -. DR STRING; 122586.NMB1723; -. DR PaxDb; Q9JY60; -. DR EnsemblBacteria; AAF42068; AAF42068; NMB1723. DR GeneID; 903379; -. DR KEGG; nme:NMB1723; -. DR PATRIC; 20359407; VBINeiMen85645_2209. DR eggNOG; ENOG4105D6P; Bacteria. DR eggNOG; COG2010; LUCA. DR HOGENOM; HOG000277942; -. DR KO; K00406; -. DR OMA; QTEFSNG; -. DR OrthoDB; EOG6H4K86; -. DR BioCyc; NMEN122586:GHGG-1778-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 1.10.760.10; -; 3. DR InterPro; IPR032858; CcoP_N. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR008168; Cyt_C_IC. DR InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3. DR Pfam; PF13442; Cytochrome_CBB3; 2. DR Pfam; PF14715; FixP_N; 1. DR PRINTS; PR00605; CYTCHROMECIC. DR SUPFAM; SSF46626; SSF46626; 3. DR TIGRFAMs; TIGR00782; ccoP; 1. DR PROSITE; PS51007; CYTC; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAF42068.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 88 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 134 213 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. FT DOMAIN 222 305 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 365 AA; 40039 MW; AF344435A51EB4A2 CRC64; MNTTSQFTSN FWNIYIAVIV LLSFIALAWL LLSQNVVKRP KKGEEVQTTG HEWDGIAEYD NPLPRWWFWL CVLTWLFGIG YLVMYPGVGD YKGLLKWTSH NQYEKEVKKA DEQYGKLYAK FADMPIEKVA KDPQAKQIAQ NLFNTYCIQC HGSDAKGSKG FPNLTDSDWL WGGDPDKIHE TIEKGRVATM PAWGPALGEE GVKDVAHYVM SLSKPEGQYD EERAARGQAL FSGPPANCFT CHGDKGQGIQ GLGPNLTDDV WLWGGTQKSI IETITNGRSS QMPAWGHFLD KDKLHIMTAY VWGLSDKDGK APVKKAEPAP TPAPAAEPAA SAPAEAAQAV SEAKPAAAEP KAEEKAAPAA KADGK // ID Q7DDB4_NEIMB Unreviewed; 248 AA. AC Q7DDB4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 85. DE SubName: Full=Amino acid ABC transporter, permease protein {ECO:0000313|EMBL:AAF41865.1}; GN OrderedLocusNames=NMB1509 {ECO:0000313|EMBL:AAF41865.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41865.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41865.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41865.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41865.1; -; Genomic_DNA. DR PIR; A81076; A81076. DR RefSeq; NP_274517.1; NC_003112.2. DR RefSeq; WP_002216849.1; NC_003112.2. DR ProteinModelPortal; Q7DDB4; -. DR STRING; 122586.NMB1509; -. DR PaxDb; Q7DDB4; -. DR EnsemblBacteria; AAF41865; AAF41865; NMB1509. DR GeneID; 903968; -. DR KEGG; nme:NMB1509; -. DR PATRIC; 20358804; VBINeiMen85645_1912. DR eggNOG; ENOG4105E5Q; Bacteria. DR eggNOG; COG0765; LUCA. DR HOGENOM; HOG000267552; -. DR KO; K02029; -. DR OMA; YKAEETQ; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NMEN122586:GHGG-1549-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 15 46 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 67 94 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 218 239 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 19 236 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 248 AA; 27820 MW; 3156570A0E0049B8 CRC64; MDFRFDIIYE YRWMFLYGAL TTLGLTVVAT AGGSVLGLLL ALARLIHLEK AGAPMRVLAW ALRKVSLLYV TLFRGTPLFV QIVIWAYVWF PFFVHPSDGI LVSGEAAIAL RRGYGPLIAG SLALIANSGA YICEIFRAGI QSIDKGQMEA ARSLGLTYPQ AMRYVILPQA LRRMLPPLAS EFITLLKDSS LLSVIAVAEL AYVQNTITGR YSVYEEPLYT VALIYLLMTT FLGWIFLRLE KRYNPQHR // ID Q7DDL9_NEIMB Unreviewed; 38 AA. AC Q7DDL9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41095.1}; GN OrderedLocusNames=NMB0677 {ECO:0000313|EMBL:AAF41095.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41095.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41095.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41095.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41095.1; -; Genomic_DNA. DR PIR; C81171; C81171. DR STRING; 122586.NMB0677; -. DR PaxDb; Q7DDL9; -. DR EnsemblBacteria; AAF41095; AAF41095; NMB0677. DR PATRIC; 20356659; VBINeiMen85645_0848. DR OrthoDB; EOG679TK5; -. DR BioCyc; NMEN122586:GHGG-704-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 38 AA; 4399 MW; 9AA1EA9CAE6F7083 CRC64; MHKSILLEDV AVRNISIQEE KKCLIGYNQG KSYFISKD // ID Q9JXI9_NEIMB Unreviewed; 531 AA. AC Q9JXI9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=ABC transporter, permease protein {ECO:0000313|EMBL:AAF42349.1}; GN OrderedLocusNames=NMB2026 {ECO:0000313|EMBL:AAF42349.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42349.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42349.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42349.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42349.1; -; Genomic_DNA. DR PIR; E81015; E81015. DR RefSeq; NP_275018.1; NC_003112.2. DR RefSeq; WP_002225678.1; NC_003112.2. DR ProteinModelPortal; Q9JXI9; -. DR STRING; 122586.NMB2026; -. DR PaxDb; Q9JXI9; -. DR EnsemblBacteria; AAF42349; AAF42349; NMB2026. DR GeneID; 904080; -. DR KEGG; nme:NMB2026; -. DR PATRIC; 20360167; VBINeiMen85645_2583. DR eggNOG; ENOG4106SMU; Bacteria. DR eggNOG; COG1178; LUCA. DR HOGENOM; HOG000218723; -. DR KO; K02063; -. DR OMA; RWAVWGA; -. DR OrthoDB; EOG6TN430; -. DR BioCyc; NMEN122586:GHGG-2088-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 24 50 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 70 95 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 107 131 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 143 163 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 199 223 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 243 267 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 288 314 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 334 357 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 369 389 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 395 412 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 456 475 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 498 519 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 70 260 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. FT DOMAIN 335 519 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 531 AA; 57351 MW; FD8F131318F7A61A CRC64; MWGLLGTIAT SVFQVGKAMD GRRWVVWGAF ALLPSAFLAV MVVAPLWAVA AYDGLAWRAV LSDAYMLKRL AWTVFQAAAT CVLVLPLGVP VAWVLARLAF PGRALVLRLL MLPFVMPTLV AGVGVLALFG ADGLLWRGRQ DTPYLLLYGN VFFNLPVLVR AAYQGFVQVP AARLQTARTL GAGAWRRFWD IEMPVLRPWL AGGVCLVFLY CFSGFGLALL LGGSRYATVE VEIYQLVMFE LDMAVASVLV WLVLGVTAAA GLLYAWFGRR AVSDKAVSPV MPSPPQSVGE YVLLAFAAAV LSVCCLFPLL AIVVKAWSAG ESWRVLMESE TWQAVWNTLR FSAAAVYAAA VLGVVYAAAA RRSAWMRGLM FLPFMVSPVC VSAGVLLLYP QWTASLPLLL AMYALLAYPF VAKDVLSAWD ALPPDYGRAA AGLGANGFQT ACRITFPLLK PALRRGLTLA AATCVGEFAA TLFLSRPEWQ TLTTLIYAYL GRAGEDNYAR AMVLTLLLAA FALGIFLLLD GGEGGKQTET L // ID Q9JYW0_NEIMB Unreviewed; 142 AA. AC Q9JYW0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=FrpA/C-related protein {ECO:0000313|EMBL:AAF41771.1}; GN OrderedLocusNames=NMB1409 {ECO:0000313|EMBL:AAF41771.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41771.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41771.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41771.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41771.1; -; Genomic_DNA. DR PIR; E81087; E81087. DR STRING; 122586.NMB1409; -. DR PaxDb; Q9JYW0; -. DR EnsemblBacteria; AAF41771; AAF41771; NMB1409. DR PATRIC; 20358499; VBINeiMen85645_1761. DR eggNOG; COG2931; LUCA. DR OMA; KQITINV; -. DR OrthoDB; EOG690MC5; -. DR BioCyc; NMEN122586:GHGG-1447-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 142 AA; 16047 MW; 7ED218F91FED7444 CRC64; MSTDSTNYAA KHESLGKSVQ RELQKTQSQL RQVVRKMQSK YNINNKARVA EISLLRQMQS QFSRKYVNKN LGNSNTLAQQ GSYTKKDGTT AQAGDLLLAA DNLHSRLTDK MLSISHVREN TISPFVLGCL KQITINAYHY LK // ID Q9JYW7_NEIMB Unreviewed; 742 AA. AC Q9JYW7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=ABC transporter family protein {ECO:0000313|EMBL:AAF41764.1}; GN OrderedLocusNames=NMB1400 {ECO:0000313|EMBL:AAF41764.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41764.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41764.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41764.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41764.1; -; Genomic_DNA. DR PIR; H81088; H81088. DR RefSeq; NP_274414.1; NC_003112.2. DR RefSeq; WP_002244161.1; NC_003112.2. DR ProteinModelPortal; Q9JYW7; -. DR SMR; Q9JYW7; 502-741. DR STRING; 122586.NMB1400; -. DR PaxDb; Q9JYW7; -. DR EnsemblBacteria; AAF41764; AAF41764; NMB1400. DR GeneID; 903822; -. DR KEGG; nme:NMB1400; -. DR PATRIC; 20358487; VBINeiMen85645_1755. DR eggNOG; ENOG4108JJA; Bacteria. DR eggNOG; COG2274; LUCA. DR KO; K11004; -. DR OMA; LMKGEMT; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-1438-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR010132; ATPase_T1SS_HlyB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF03412; Peptidase_C39; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 350 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 35 160 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. FT DOMAIN 192 471 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 503 738 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 742 AA; 82320 MW; D0D8C1E66EF07B62 CRC64; MRSAVLFIYF FLLNIFLFQP AVIHIQSNYI LFMSIVSAPL PALSALIILA HYHGIAANPA DIQHEFCTSA QSDLNETQWL LAAKSLGLKA KVVRQPIKRL AMATLPALVW CDDGNHFILA KTDGEGEHAQ FLIQDLVTNK SAVLSFAEFS NRYSGKLILV ASRASVLGSL AKFDFTWFIP AVIKYRRLFF EVLVVSVVLQ LFALITPLFF QVVMDKVLVH RGFSTLDVVS VALLVVSLFE IVLGGLRTYL FAHTTSRIDV ELGARLFRHL LSLPLSYFEH RRVGDTVARV RELEQIRNFL TGQALTSVLD LAFSFIFLAV MWYYSSTLTW VVLASLPAYA FWSAFISPIL RTRLNDKFAR NADNQSFLVE SITAVGTVKA MAVEPQMTQR WDNQLAAYVA SGFRVTKLAV VGQQGVQLIQ KLVTVATLWI GARLVIESKL TVGQLIAFNM LSGQVAAPVI RLAQLWQDFQ QVGISVARLG DILNAPTENA SSHLALPDIR GEITFEHVDF RYKADGRLIL QDLNLRIRAG EVLGIVGRSG SGKSTLTKLV QRLYVPEQGR VLVDGNDLAL AAPAWLRRQV GVVLQENVLL NRSIRDNIAL TDTGMPLERI IEAAKLAGAH EFIMELPEGY GTVVGEQGAG LSGGQRQRIA IARALITNPR ILIFDEATSA LDYESERAIM QNMQAICANR TVLIIAHRLS TVKTAHRIIA MDKGRIVEAG TQQELLAKPN GYYRYLYDLQ NG // ID Q9JZ73_NEIMB Unreviewed; 305 AA. AC Q9JZ73; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 69. DE SubName: Full=CobW-related protein {ECO:0000313|EMBL:AAF41640.1}; GN OrderedLocusNames=NMB1263 {ECO:0000313|EMBL:AAF41640.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41640.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41640.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41640.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41640.1; -; Genomic_DNA. DR PIR; A81104; A81104. DR RefSeq; NP_274284.1; NC_003112.2. DR RefSeq; WP_002222404.1; NC_003112.2. DR ProteinModelPortal; Q9JZ73; -. DR STRING; 122586.NMB1263; -. DR PaxDb; Q9JZ73; -. DR EnsemblBacteria; AAF41640; AAF41640; NMB1263. DR GeneID; 903685; -. DR KEGG; nme:NMB1263; -. DR PATRIC; 20358141; VBINeiMen85645_1582. DR eggNOG; ENOG4105CKI; Bacteria. DR eggNOG; COG0523; LUCA. DR HOGENOM; HOG000294929; -. DR OMA; WHKELYN; -. DR OrthoDB; EOG6N3CQV; -. DR BioCyc; NMEN122586:GHGG-1301-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011629; Cbl_biosynth_CobW-like_C. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02492; cobW; 1. DR Pfam; PF07683; CobW_C; 1. DR SMART; SM00833; CobW_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90002; SSF90002; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 218 304 CobW C-terminal. FT {ECO:0000259|SMART:SM00833}. SQ SEQUENCE 305 AA; 33741 MW; 574936FF13787148 CRC64; MKKTKVHLIS GFLGTGKTTA LKSLMAQKDP NEKWVIIVNE FGEIGIDGAV LSDNGIPVAE IAGGCLCCTA GPQMGVTVQK MLRDAKPDRL MIEASGLAHA ASVIDELKTK PLDSLLEIGA VFTVVDPRQF INPDYAQQAL YKDQIGICDV LVASKTDLCT PEQLAEFHDK AAKLFPPKAK VVEVQNAQLD IQWLDIPVIE KSRYRLKALP DNTMGFQSQG FTFPAGRDFD GEKLTNFFND LPNMTEGLVR AKGVFQVLGT WVWLNWVDGQ WGANQVSWRR DSRFELIAKS FDADLIEQKL KDALE // ID Q9K1G4_NEIMB Unreviewed; 140 AA. AC Q9K1G4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40646.1}; GN OrderedLocusNames=NMB0189 {ECO:0000313|EMBL:AAF40646.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40646.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40646.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40646.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40646.1; -; Genomic_DNA. DR PIR; B81227; B81227. DR PaxDb; Q9K1G4; -. DR EnsemblBacteria; AAF40646; AAF40646; NMB0189. DR PATRIC; 20355405; VBINeiMen85645_0231. DR HOGENOM; HOG000218657; -. DR OMA; HDAFACA; -. DR OrthoDB; EOG6742XQ; -. DR BioCyc; NMEN122586:GHGG-200-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 111 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 140 AA; 15368 MW; FE6FB798BB7EAE5E CRC64; MFVNEKYPYA ALFAGLVFLT LPFALAVHDA FALAFGRTGL LVSVSDGGFG WRGGWDGTVW FVFGVFAFLN VVVSAGLTKL AYKKMMRRHS RYTLFLSGVA ACAAAAVAWI FELLLGSGAL GGLRGRRCWN MRLPCGWWRC // ID Q9JYL5_NEIMB Unreviewed; 336 AA. AC Q9JYL5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=ADP-heptose--LPS heptosyltransferase II {ECO:0000313|EMBL:AAF41882.1}; GN Name=rfaF {ECO:0000313|EMBL:AAF41882.1}; GN OrderedLocusNames=NMB1527 {ECO:0000313|EMBL:AAF41882.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41882.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41882.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41882.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41882.1; -; Genomic_DNA. DR PIR; C81073; C81073. DR RefSeq; NP_274534.1; NC_003112.2. DR RefSeq; WP_002225061.1; NC_003112.2. DR ProteinModelPortal; Q9JYL5; -. DR STRING; 122586.NMB1527; -. DR PaxDb; Q9JYL5; -. DR EnsemblBacteria; AAF41882; AAF41882; NMB1527. DR GeneID; 904029; -. DR KEGG; nme:NMB1527; -. DR PATRIC; 20358852; VBINeiMen85645_1936. DR eggNOG; ENOG4105XA0; Bacteria. DR eggNOG; COG0859; LUCA. DR HOGENOM; HOG000237541; -. DR KO; K02843; -. DR OMA; IAFCPGA; -. DR OrthoDB; EOG64N9TX; -. DR BioCyc; NMEN122586:GHGG-1567-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:InterPro. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR InterPro; IPR002201; Glyco_trans_9. DR InterPro; IPR011910; LipoPS_heptosylTferase-II. DR Pfam; PF01075; Glyco_transf_9; 1. DR TIGRFAMs; TIGR02195; heptsyl_trn_II; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41882.1}. SQ SEQUENCE 336 AA; 37538 MW; 930DDC643D317E4D CRC64; MSIKILIISP SWIGDCVMTQ PLFRRLKELH PGCTIDVFAP KWSMAVFERM PEVNEILENS FGHGALELKR RWRVGRDLGR RGYDQVIVLP GSLKSAIIAL ATGIGKRTGY VGESRYFLLN DIRRLDKERL PLMVDRYTAL AHPSQEDFDG HSGFPEFSID ERRREISVET FGLDIGKPVL AFCPGAEFGP AKRWPTRHFA ELGKHYLAAG WQVWLFGSQK DDEIAEEINR LSDGMCVNLC GKTDLSQAMD LLSLADTVVC NDSGLMHLAA ALGRKVVAVY GSSSPTHTPP LSDRAKIVSL HLECSPCFKR ECPLGHTDCL NRLYPEKIVQ AVEEAV // ID Q9JXC4_NEIMB Unreviewed; 124 AA. AC Q9JXC4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42434.1}; GN OrderedLocusNames=NMB2125 {ECO:0000313|EMBL:AAF42434.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42434.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42434.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42434.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42434.1; -; Genomic_DNA. DR PIR; E81005; E81005. DR RefSeq; NP_275111.1; NC_003112.2. DR RefSeq; WP_002224193.1; NC_003112.2. DR STRING; 122586.NMB2125; -. DR PaxDb; Q9JXC4; -. DR EnsemblBacteria; AAF42434; AAF42434; NMB2125. DR GeneID; 903416; -. DR KEGG; nme:NMB2125; -. DR PATRIC; 20360424; VBINeiMen85645_2708. DR HOGENOM; HOG000218700; -. DR OMA; TYIFRNS; -. DR OrthoDB; EOG6CP3X6; -. DR BioCyc; NMEN122586:GHGG-2190-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 124 AA; 14750 MW; 83A2684418DAAC1D CRC64; MIIQNEFNLY PSNMLPERFC YPEKYVRISN DTSLIPYIQP HNFHWWFENY GTEGAEVAYI FRNSILPDLN LIPFASNGEW EAYFDGNDVT GNSRVIVINL DNIENHEFFN SFEDWLELAI KDTW // ID Q7DDQ7_NEIMB Unreviewed; 244 AA. AC Q7DDQ7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-APR-2016, entry version 86. DE SubName: Full=Transcriptional regulator, Crp/Fnr family {ECO:0000313|EMBL:AAF40820.1}; GN OrderedLocusNames=NMB0380 {ECO:0000313|EMBL:AAF40820.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40820.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40820.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40820.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH crp-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00433475}. CC -!- SIMILARITY: Contains cyclic nucleotide-binding domain. CC {ECO:0000256|SAAS:SAAS00443679}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40820.1; -; Genomic_DNA. DR PIR; A81205; A81205. DR RefSeq; NP_273429.1; NC_003112.2. DR RefSeq; WP_002212452.1; NC_003112.2. DR ProteinModelPortal; Q7DDQ7; -. DR STRING; 122586.NMB0380; -. DR PaxDb; Q7DDQ7; -. DR EnsemblBacteria; AAF40820; AAF40820; NMB0380. DR GeneID; 902495; -. DR KEGG; nme:NMB0380; -. DR PATRIC; 20355925; VBINeiMen85645_0480. DR eggNOG; ENOG4105DS0; Bacteria. DR eggNOG; COG0664; LUCA. DR HOGENOM; HOG000186461; -. DR KO; K01420; -. DR OMA; ARCSVCA; -. DR OrthoDB; EOG6RVFWF; -. DR BioCyc; NMEN122586:GHGG-402-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF13545; HTH_Crp_2; 1. DR PRINTS; PR00034; HTHCRP. DR SMART; SM00100; cNMP; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51206; SSF51206; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|SAAS:SAAS00433748}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00433813}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00433813}. FT DOMAIN 24 94 Cyclic nucleotide-binding. FT {ECO:0000259|PROSITE:PS50042}. FT DOMAIN 158 231 HTH crp-type DNA-binding. FT {ECO:0000259|PROSITE:PS51063}. SQ SEQUENCE 244 AA; 27416 MW; E10C22A3159E5D99 CRC64; MASHNTTHQM KTLCSSCSLR ELCLPVGLLP NELSQLDAVI RQSRRLKKGE YLFCVGEAFT SLFAIRSGFF KTTVASQDGR DQVTGFFMSG ELIGMDGICS HVHSCDAVAL EDSEVCELPF THIEELGQNI PSLRTHFFRM MSREIVRDQG VMLLLGNMRA EERIAAFLLN LSQRLYSRGF AANDFILRMS REEIGSYLGL KLETVSRTLS KFHQEGLISV EHKHIKILNL QVLKKMVSGC SHAI // ID Q9JYH1_NEIMB Unreviewed; 80 AA. AC Q9JYH1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41942.1}; GN OrderedLocusNames=NMB1589 {ECO:0000313|EMBL:AAF41942.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41942.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41942.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41942.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41942.1; -; Genomic_DNA. DR PIR; G81065; G81065. DR STRING; 122586.NMB1589; -. DR PaxDb; Q9JYH1; -. DR EnsemblBacteria; AAF41942; AAF41942; NMB1589. DR BioCyc; NMEN122586:GHGG-1637-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 80 AA; 9395 MW; 8FBC5E79AB29DCEA CRC64; MVCRHKLSAV VRRFYCTLPD GISRTRKNIR ICGIDRYRPQ PQRTGNQTGC RRAALPAFLL WVRQFVHRRQ YRQNHQGGAG // ID Q9JZZ1_NEIMB Unreviewed; 238 AA. AC Q9JZZ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41252.1}; GN OrderedLocusNames=NMB0841 {ECO:0000313|EMBL:AAF41252.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41252.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41252.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41252.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41252.1; -; Genomic_DNA. DR PIR; F81151; F81151. DR RefSeq; NP_273882.1; NC_003112.2. DR RefSeq; WP_002244078.1; NC_003112.2. DR STRING; 122586.NMB0841; -. DR PaxDb; Q9JZZ1; -. DR EnsemblBacteria; AAF41252; AAF41252; NMB0841. DR GeneID; 902955; -. DR KEGG; nme:NMB0841; -. DR PATRIC; 20357069; VBINeiMen85645_1053. DR eggNOG; ENOG4106SSJ; Bacteria. DR eggNOG; ENOG410YKJ2; LUCA. DR HOGENOM; HOG000218871; -. DR OMA; QTITRKH; -. DR OrthoDB; EOG6H1PZZ; -. DR BioCyc; NMEN122586:GHGG-872-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 238 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327871. FT TRANSMEM 212 233 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 238 AA; 26136 MW; 7DCBD0ADC9447E6F CRC64; MLFRKTTAAV LAATLMLNGC TLMLWGMNNP VSETITRKHV DKDQIRAFGV VAEDNAQLEK GSLVMMGGKY WFVVNPEDSA KLTGILKAGL DKPFQIVEDT PSYARHQALP VKLESPGSQN FSTEGLCLRY DTDKPADIAK LKQLGFEAVK LDNRTIYTRC VSAKGKYYAT PQKLNADYHF EQSVPADIYY TVTEEHTDKS KLFANILYTP PFLILDAAGA VLALPAAALG AVVDAARK // ID Q9JY33_NEIMB Unreviewed; 99 AA. AC Q9JY33; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42106.1}; GN OrderedLocusNames=NMB1765 {ECO:0000313|EMBL:AAF42106.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42106.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42106.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42106.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42106.1; -; Genomic_DNA. DR PIR; C81045; C81045. DR RefSeq; NP_274765.1; NC_003112.2. DR RefSeq; WP_002238274.1; NC_003112.2. DR STRING; 122586.NMB1765; -. DR PaxDb; Q9JY33; -. DR EnsemblBacteria; AAF42106; AAF42106; NMB1765. DR GeneID; 903333; -. DR KEGG; nme:NMB1765; -. DR BioCyc; NMEN122586:GHGG-1820-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 99 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332240. SQ SEQUENCE 99 AA; 11345 MW; DDE0151A2A71C738 CRC64; MKKKLSKYSL FLSSVFCLTA CATTLLGTVV VGTALYGTSS NWTTTDKEHQ EIMNCLDKAL VKLNIYFEND EEKYKNKTVM DIYYQCIKNP NYVVTHNNL // ID Q9K147_NEIMB Unreviewed; 875 AA. AC Q9K147; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=TspA protein {ECO:0000313|EMBL:AAF40784.1}; GN OrderedLocusNames=NMB0341 {ECO:0000313|EMBL:AAF40784.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40784.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40784.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40784.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40784.1; -; Genomic_DNA. DR PIR; C81209; C81209. DR RefSeq; NP_273390.1; NC_003112.2. DR RefSeq; WP_010980781.1; NC_003112.2. DR STRING; 122586.NMB0341; -. DR PaxDb; Q9K147; -. DR EnsemblBacteria; AAF40784; AAF40784; NMB0341. DR GeneID; 902456; -. DR KEGG; nme:NMB0341; -. DR PATRIC; 20355829; VBINeiMen85645_0433. DR eggNOG; COG3170; LUCA. DR HOGENOM; HOG000219116; -. DR KO; K07288; -. DR OMA; ASFQAYA; -. DR OrthoDB; EOG61ZTJ4; -. DR BioCyc; NMEN122586:GHGG-362-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR020011; Motility_prot_FimV_C. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF01476; LysM; 1. DR TIGRFAMs; TIGR03504; FimV_Cterm; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 371 394 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 828 861 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 875 AA; 92489 MW; 1F921520C167D090 CRC64; MPAGRLPRRC PMMTKFTDCT RSNRIQPPTH RGYILKNNRQ IKLIAASVAV AASFQAHAGL GGLNIQSNLD EPFSGSITVT GEEAKALLGG GSVTVSEKGL TAKVHKLGDK AVIAVSSEQA VRDPVLVFRI GAGAQVREYT AILDPVGYSP KTKSALSDGK THRKTAPTAE SQENQNAKAL RKTDKKDSAN AAVKPAYNGK THTVRKGETV KQIAAAIRPK HLTLEQVADA LLKANPNVSA HGRLRAGSVL HIPNLNRIKA EQPKPQTAKP KAETASMPSE PSKQATVEKP VEKPEAKVAA PEAKAEKPAV RPEPVPAANT AASETAAESA PQEAAASAID TPTDETGNAV SEPVEQVSAE EETESGLFDG LFGGSYTLLL AGGGAALIAL LLLLRLAQSK RARRTEESVP EEEPDLDDAA DDGIEITFAE VETPATPEPA PKNDVNDTLA LDGESEEELS AKQTFDVETD TPSNRIDLDF DSLAAAQNGI LSGALTQDEE TQKRADADWN AIESTDSVYE PETFNPYNPV EIVIDTPEPE SVAQTAENKP ETVDTDFSDN LPSNNHIGTE ETASAKPASP SGLAGFLKAS SPETILEKTV AEVQTPEELH DFLKVYETDA VAETAPETPD FNAAADDLSA LLQPAEAPSV EENITETVAE TPDFNATADD LSALLQPSKV PAVEENAAET VADDLSALLQ PAEAPAVEEN VTETVAETPD FNATADDLSA LLQPSEAPAV EENAAETVAD DLSALLQPAE APAVEENAAE ITLETPDSNT SEADALPDFL KDGEEETVDW SIYLSEENIP NNADTSFPSE SVGSDAPSEA KYDLAEMYLE IGDRDAAAET VQKLLEEAEG DVLKRAQALA QELGI // ID Q7DD81_NEIMB Unreviewed; 100 AA. AC Q7DD81; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42122.1}; GN OrderedLocusNames=NMB1782 {ECO:0000313|EMBL:AAF42122.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42122.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42122.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42122.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42122.1; -; Genomic_DNA. DR RefSeq; NP_274782.1; NC_003112.2. DR RefSeq; WP_002221436.1; NC_003112.2. DR STRING; 122586.NMB1782; -. DR PaxDb; Q7DD81; -. DR EnsemblBacteria; AAF42122; AAF42122; NMB1782. DR GeneID; 903317; -. DR KEGG; nme:NMB1782; -. DR PATRIC; 20359521; VBINeiMen85645_2266. DR OMA; GNAXQSS; -. DR OrthoDB; EOG60390D; -. DR BioCyc; NMEN122586:GHGG-1837-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 100 AA; 10887 MW; 7D87B18A310BE9C3 CRC64; MTWVGGSGNA QQSSYYCEIC ESAGLNDTGN PDKSLGLPNN TFSNPPGWGA TIGALAGSRI GMPEFGTFAS HAIENFDWSW YRRYREIAET IEREYSGGLP // ID Q9K0Q0_NEIMB Unreviewed; 426 AA. AC Q9K0Q0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Glucose/galactose transporter {ECO:0000313|EMBL:AAF40964.1}; GN Name=gluP {ECO:0000313|EMBL:AAF40964.1}; GN OrderedLocusNames=NMB0535 {ECO:0000313|EMBL:AAF40964.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40964.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40964.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40964.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40964.1; -; Genomic_DNA. DR PIR; F81187; F81187. DR RefSeq; NP_273580.1; NC_003112.2. DR RefSeq; WP_002225587.1; NC_003112.2. DR ProteinModelPortal; Q9K0Q0; -. DR STRING; 122586.NMB0535; -. DR PaxDb; Q9K0Q0; -. DR EnsemblBacteria; AAF40964; AAF40964; NMB0535. DR GeneID; 902650; -. DR KEGG; nme:NMB0535; -. DR PATRIC; 20356325; VBINeiMen85645_0681. DR eggNOG; ENOG4105EDR; Bacteria. DR eggNOG; COG0738; LUCA. DR HOGENOM; HOG000267862; -. DR KO; K02429; -. DR OMA; FESCIFP; -. DR OrthoDB; EOG661H8H; -. DR BioCyc; NMEN122586:GHGG-561-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005354; F:galactose transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR005964; Glc/Gal_transptr_bac. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR01272; gluP; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 216 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 272 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 284 302 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 362 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 374 394 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 400 422 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 31 426 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 426 AA; 45614 MW; 4991CBBE20B8EE21 CRC64; MSISIFLKRV IFRHHERQIM SAQSQNNHTS PLVVLTTLFF MMGFITCMND ILIPHLKEIF DLSYVQAMLI QFCFFTAYAV MSIPMGAFVG KVGYKNGVIG GFLLTAVGCL LFYPAAGSHS YAVFLGALFI LASGVTLLQV AGNPYVTLLA KPGKESATLT LVQAFNALGT TIAPQIGAFL ILADATQTVS KAEQISSVQI PYLGLAGLLI ILAVFVKMIR LPDARKIAAE ESAHNHDGKT SVWQYKHLVF GTAGIFCYVG AEVSIGSLMV NVLGYLKGLD HASAAHYLSF YWGGAMVGRF LGSAVMAKFA PNRYLAFNAS AAVVLLAVAM ATGSGNADVA MWSLLAIGFF NSIMFPTIFS LATKGLGKFT NAASGVLCTA IVGGAVVPVV QGWVADTYTL MSSFVVSVIC YLYIVFFAVY GYRADK // ID Q9K0C3_NEIMB Unreviewed; 165 AA. AC Q9K0C3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Putative colicin V production protein {ECO:0000313|EMBL:AAF62316.1}; GN OrderedLocusNames=NMB0691 {ECO:0000313|EMBL:AAF62316.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62316.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62316.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62316.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62316.1; -; Genomic_DNA. DR RefSeq; NP_273733.1; NC_003112.2. DR RefSeq; WP_002225491.1; NC_003112.2. DR STRING; 122586.NMB0691; -. DR PaxDb; Q9K0C3; -. DR EnsemblBacteria; AAF62316; AAF62316; NMB0691. DR GeneID; 902803; -. DR KEGG; nme:NMB0691; -. DR PATRIC; 20356711; VBINeiMen85645_0877. DR eggNOG; COG1286; LUCA. DR HOGENOM; HOG000162044; -. DR KO; K03558; -. DR OMA; IIAECLF; -. DR OrthoDB; EOG6W4609; -. DR BioCyc; NMEN122586:GHGG-719-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro. DR InterPro; IPR003825; Colicin-V_CvpA. DR Pfam; PF02674; Colicin_V; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 124 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 165 AA; 17455 MW; B9C0C31F5CAE6287 CRC64; MNSLPIADLL VSAVIAACIV LSAMRGVIAE AGSMAAWVVS FFFAKLFAAS FADLAFASFQ PRLFALALSF ISLFVIACLI QKMLRSLLTS AVSAVGLGFA NRILGGVFGA LKGVLIVTLL VMLASKTDLP DTEEWRQSYT LPFFVSLSEA VLNHSGGTAE TPEDD // ID Q9K1E3_NEIMB Unreviewed; 328 AA. AC Q9K1E3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40669.1}; GN OrderedLocusNames=NMB0213 {ECO:0000313|EMBL:AAF40669.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40669.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40669.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40669.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40669.1; -; Genomic_DNA. DR PIR; E81225; E81225. DR RefSeq; NP_273270.1; NC_003112.2. DR RefSeq; WP_002215545.1; NC_003112.2. DR ProteinModelPortal; Q9K1E3; -. DR STRING; 122586.NMB0213; -. DR PaxDb; Q9K1E3; -. DR EnsemblBacteria; AAF40669; AAF40669; NMB0213. DR GeneID; 902325; -. DR KEGG; nme:NMB0213; -. DR PATRIC; 20355482; VBINeiMen85645_0265. DR eggNOG; ENOG4108R7A; Bacteria. DR eggNOG; COG0668; LUCA. DR HOGENOM; HOG000218655; -. DR OMA; GSEPHIH; -. DR OrthoDB; EOG67MF3D; -. DR BioCyc; NMEN122586:GHGG-228-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR006685; MscS_channel. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 115 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 328 AA; 36887 MW; 65B2558F3E2C89B9 CRC64; MKRYVCLRHQ VGDCPVKWQK RFFATKIYTL YFSDRGAEME IWNMLDTWLG AVPIRAEAVE SVAAVAALLL ARALLLNIHF KRHPDFGIES KRRFLVASRN ITLLLVLFSL AFIWSAQIQT LALSMFAVAA AVVVATKELI MCLSGSILRS ATQQYSVGDY IEINGLRGRV VDINLLNTLM MQVGPNPLVG QLAGTTVSFP NSLLLSHPVR RDNILGDYVI HTVEIPVPIH LDSDEAVCRL KAVLEPLCAP YIPAIQRHLE NVQAEKLFIT PAARPRVTRV PYDDKAYRII VRFASPVSKR LEIQQAVMDE FLRVQYRLLN HPAGSETL // ID Q9JZ82_NEIMB Unreviewed; 234 AA. AC Q9JZ82; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Riboflavin synthase, alpha subunit {ECO:0000313|EMBL:AAF41628.1}; DE EC=2.5.1.9 {ECO:0000313|EMBL:AAF41628.1}; GN Name=ribE {ECO:0000313|EMBL:AAF41628.1}; GN OrderedLocusNames=NMB1247 {ECO:0000313|EMBL:AAF41628.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41628.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41628.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41628.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41628.1; -; Genomic_DNA. DR PIR; D81106; D81106. DR RefSeq; NP_274271.2; NC_003112.2. DR ProteinModelPortal; Q9JZ82; -. DR SMR; Q9JZ82; 30-231. DR STRING; 122586.NMB1247; -. DR PaxDb; Q9JZ82; -. DR EnsemblBacteria; AAF41628; AAF41628; NMB1247. DR GeneID; 903669; -. DR KEGG; nme:NMB1247; -. DR PATRIC; 20358091; VBINeiMen85645_1558. DR eggNOG; ENOG4108R6K; Bacteria. DR eggNOG; COG0307; LUCA. DR HOGENOM; HOG000151758; -. DR KO; K00793; -. DR OMA; HILSGHV; -. DR OrthoDB; EOG6VMTQH; -. DR BioCyc; NMEN122586:GHGG-1284-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.20; -; 2. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR001783; Lumazine-bd. DR InterPro; IPR026017; Lumazine-bd_dom. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR21098; PTHR21098; 1. DR Pfam; PF00677; Lum_binding; 2. DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1. DR SUPFAM; SSF63380; SSF63380; 2. DR TIGRFAMs; TIGR00187; ribE; 1. DR PROSITE; PS51177; LUMAZINE_BIND; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41628.1}. FT DOMAIN 30 127 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT DOMAIN 128 224 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT REGION 33 35 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 78 80 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 92 97 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. SQ SEQUENCE 234 AA; 25790 MW; 3ADE68578A6506BB CRC64; MLSEGISDGI FRGEMLQFAP FLPTQGNRIM FTGIVQGLGK LTAIHRPSEA FHTYVVELPQ EAADNLQRGA SVANNGCCLT ITEIEGNRVS FDLMAETLAK TNLGLLKEGD CVNIERAARF GDEIGGHVMS GHIMATVPIV EIERDGFNRT VWFSLPHELK PYILTKGFVG LDGCSLTIGK VEDGRFNVHL IPETLERTLF GSRKVGDRIN IEIDPNTQAI VDTVERLMAQ RYAK // ID Q9K1Q7_NEIMB Unreviewed; 149 AA. AC Q9K1Q7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40492.1}; GN OrderedLocusNames=NMB0013 {ECO:0000313|EMBL:AAF40492.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40492.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40492.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40492.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40492.1; -; Genomic_DNA. DR PIR; C81248; C81248. DR RefSeq; NP_273079.1; NC_003112.2. DR RefSeq; WP_002225757.1; NC_003112.2. DR STRING; 122586.NMB0013; -. DR PaxDb; Q9K1Q7; -. DR EnsemblBacteria; AAF40492; AAF40492; NMB0013. DR GeneID; 902116; -. DR KEGG; nme:NMB0013; -. DR PATRIC; 20354957; VBINeiMen85645_0014. DR eggNOG; ENOG4106EV1; Bacteria. DR eggNOG; COG3399; LUCA. DR HOGENOM; HOG000218690; -. DR KO; K09943; -. DR OMA; FDMVIFP; -. DR OrthoDB; EOG6N685J; -. DR BioCyc; NMEN122586:GHGG-14-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007418; DUF474. DR PIRSF; PIRSF015875; UCP015875; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 147 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 149 AA; 16565 MW; CAB2C1E8B3EB7DD4 CRC64; MSIYAVAHIV HLYCAIAFVG GVFFEVLVLS VLHTGRVSRE ARREVEKAMS YRAVRVMPFV VGLLFASGIV MAANRYLSIL GEPFATSFGT MLTLKILLAF SVLAHFAIAV VKMARSTLTV GWSKYIHAVV FTHMLLIVFL AKAMFYISW // ID Q9K0M1_NEIMB Unreviewed; 119 AA. AC Q9K0M1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40999.1}; GN OrderedLocusNames=NMB0571 {ECO:0000313|EMBL:AAF40999.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40999.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40999.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40999.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40999.1; -; Genomic_DNA. DR PIR; F81182; F81182. DR RefSeq; NP_273615.1; NC_003112.2. DR RefSeq; WP_002222875.1; NC_003112.2. DR STRING; 122586.NMB0571; -. DR PaxDb; Q9K0M1; -. DR EnsemblBacteria; AAF40999; AAF40999; NMB0571. DR GeneID; 902686; -. DR KEGG; nme:NMB0571; -. DR PATRIC; 20356423; VBINeiMen85645_0731. DR eggNOG; ENOG4105WD1; Bacteria. DR eggNOG; COG2832; LUCA. DR HOGENOM; HOG000277594; -. DR KO; K09790; -. DR OMA; CVLVWLW; -. DR OrthoDB; EOG6KMB9V; -. DR BioCyc; NMEN122586:GHGG-597-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007401; DUF454. DR Pfam; PF04304; DUF454; 1. DR PIRSF; PIRSF016789; DUF454; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 114 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 119 AA; 13835 MW; 1F1E8666941E3A1E CRC64; MIRYLLIACG CISLLLGIIG IFLPLLPTTP FVLLSAACWA KASPRFYRWL HRHRYFGPMV HNWEQNGAVP RKAKIFAISM MTASCLIMFW QFPQRWWVGA VSSVFCSLVA IWMWRRPES // ID Q7DDK8_NEIMB Unreviewed; 90 AA. AC Q7DDK8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41274.1}; GN OrderedLocusNames=NMB0863 {ECO:0000313|EMBL:AAF41274.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41274.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41274.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41274.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41274.1; -; Genomic_DNA. DR PIR; B81151; B81151. DR STRING; 122586.NMB0863; -. DR PaxDb; Q7DDK8; -. DR EnsemblBacteria; AAF41274; AAF41274; NMB0863. DR PATRIC; 20357117; VBINeiMen85645_1077. DR HOGENOM; HOG000218881; -. DR OMA; NVIIGYV; -. DR OrthoDB; EOG6BPDN2; -. DR BioCyc; NMEN122586:GHGG-894-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 82 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 90 AA; 10200 MW; 14B7423399BED4D8 CRC64; MFAVIFFSTL GCILAWIRDI PKIKSKKILA RSLYIIGIIN VIISYVLIKN ILVSVSDGGG IKYVAIYLSN LFFWTVLMYV LVKRLSKKPS // ID Q9JZT0_NEIMB Unreviewed; 321 AA. AC Q9JZT0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transposase, IS30 family {ECO:0000313|EMBL:AAF41319.1}; GN OrderedLocusNames=NMB0911 {ECO:0000313|EMBL:AAF41319.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41319.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41319.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41319.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41319.1; -; Genomic_DNA. DR PIR; D81145; D81145. DR RefSeq; NP_273951.1; NC_003112.2. DR RefSeq; WP_002248700.1; NC_003112.2. DR ProteinModelPortal; Q9JZT0; -. DR STRING; 122586.NMB0911; -. DR PaxDb; Q9JZT0; -. DR EnsemblBacteria; AAF41319; AAF41319; NMB0911. DR GeneID; 903032; -. DR KEGG; nme:NMB0911; -. DR PATRIC; 20357255; VBINeiMen85645_1141. DR eggNOG; ENOG4105F9F; Bacteria. DR eggNOG; COG2826; LUCA. DR HOGENOM; HOG000114768; -. DR KO; K07482; -. DR OMA; ISERPAM; -. DR OrthoDB; EOG693GNH; -. DR BioCyc; NMEN122586:GHGG-949-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 155 316 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 321 AA; 38059 MW; 8DC4C90480FFE0B5 CRC64; MSHTQLTQGE RYHIQYLSRH CTVTEIAKQL NRHKSTISRE IRRHRTQGQQ YSAEKAQRQS QTIKQRKRQP YKLDSQLIQH IDPLIRRKLS PEQVCAYLRK HHQITLHHST IYRYLRQDKS NGSTLWQHLR ICSKPYRKRY GSTWTRGKVP NRVGIENRPA IVDQKSRIGD WEADTIVGKG QKSALLTLVE RVTRYTIICK LDSLKAEDTA RAAVRTLKAH KDRVHTITMD NGKEFYQHTK ITKALKAETY FCRPYHSWEK GLNENTNGLI RQYFPKQTDF RNISDREIRR VQDELNHRPR KTLGYETPSV LFLNLFQPLI H // ID Q9JYE6_NEIMB Unreviewed; 289 AA. AC Q9JYE6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Putative tellurite resistance protein {ECO:0000313|EMBL:AAF41969.1}; GN OrderedLocusNames=NMB1617 {ECO:0000313|EMBL:AAF41969.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41969.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41969.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41969.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41969.1; -; Genomic_DNA. DR PIR; G81061; G81061. DR RefSeq; NP_274623.1; NC_003112.2. DR RefSeq; WP_010980965.1; NC_003112.2. DR ProteinModelPortal; Q9JYE6; -. DR STRING; 122586.NMB1617; -. DR PaxDb; Q9JYE6; -. DR EnsemblBacteria; AAF41969; AAF41969; NMB1617. DR GeneID; 904150; -. DR KEGG; nme:NMB1617; -. DR PATRIC; 20359134; VBINeiMen85645_2078. DR eggNOG; ENOG4108IHG; Bacteria. DR eggNOG; COG3615; LUCA. DR HOGENOM; HOG000120596; -. DR KO; K16868; -. DR OMA; LHKTDEN; -. DR OrthoDB; EOG6C2WG4; -. DR BioCyc; NMEN122586:GHGG-1666-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro. DR GO; GO:0046690; P:response to tellurium ion; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR015392; DUF1971. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR015985; TehB-like_dom. DR InterPro; IPR004537; Tellurite-R_MeTrfase_TehB. DR InterPro; IPR014431; Tellurite-R_TehB-2. DR Pfam; PF09313; DUF1971; 1. DR Pfam; PF03848; TehB; 1. DR PIRSF; PIRSF005215; TehB; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00477; tehB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 91 DUF1971. {ECO:0000259|Pfam:PF09313}. FT DOMAIN 93 284 TehB. {ECO:0000259|Pfam:PF03848}. SQ SEQUENCE 289 AA; 31711 MW; CDF9498B98A24B90 CRC64; MKERIVGQSG ELFCFGQMPV WKVENLPEVL LSGYSSEEGE WVCLNVLQGD VEVRAPDGSA EVWSADGGDC VFAPQQVFSV KPKTDDAEIR LSLYCAAADY FHKKYGMSAT HSAVAAARDT VPAGRALDMG CGQGRNALFL GLKGFEVTAV DHNPAALANV AELAEAEGLN VRTLEYDLNA AALQGEFDYI VATVVLMFLM PQRVPDVIAD MQAHTAAGGY NLIVSAMDTA DFPCPMPFPF KFKEGELKDY YRDWELVEYK EELGSMHAKD ENGNPIRFKF VTMLAKKPE // ID Q9K0N1_NEIMB Unreviewed; 154 AA. AC Q9K0N1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40986.1}; GN OrderedLocusNames=NMB0558 {ECO:0000313|EMBL:AAF40986.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40986.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40986.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40986.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40986.1; -; Genomic_DNA. DR PIR; A81184; A81184. DR RefSeq; NP_273602.1; NC_003112.2. DR RefSeq; WP_002225568.1; NC_003112.2. DR STRING; 122586.NMB0558; -. DR PaxDb; Q9K0N1; -. DR EnsemblBacteria; AAF40986; AAF40986; NMB0558. DR GeneID; 902673; -. DR KEGG; nme:NMB0558; -. DR PATRIC; 20356389; VBINeiMen85645_0714. DR HOGENOM; HOG000218805; -. DR OMA; EEKCTWE; -. DR OrthoDB; EOG67HJW7; -. DR BioCyc; NMEN122586:GHGG-584-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 151 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 154 AA; 17589 MW; DF0FE13E3A99FA10 CRC64; MIEMSKDYRN DLYDVYVSYP PQVDRGLIRE CLKENLGEEK AEGLIESLDS KPQVLVEEKC TWAKREELHD YFSYLGLDII TRRYMELETV VPPEEGEGEG EGADGEMPEY LELHGGREDD ISAPSQPEPP SRNIKLLVFG LLIAFLGYLL GKIF // ID Q9K189_NEIMB Unreviewed; 232 AA. AC Q9K189; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Thiol:disulfide interchange protein DsbA {ECO:0000313|EMBL:AAF40732.1}; GN Name=dsbA-1 {ECO:0000313|EMBL:AAF40732.1}; GN OrderedLocusNames=NMB0278 {ECO:0000313|EMBL:AAF40732.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40732.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40732.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40732.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3DVW, ECO:0000213|PDB:3HZ8} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 41-232, AND DISULFIDE BONDS. RX PubMed=19631659; DOI=10.1016/j.jmb.2009.07.056; RA Lafaye C., Iwema T., Carpentier P., Jullian-Binard C., Kroll J.S., RA Collet J.F., Serre L.; RT "Biochemical and structural study of the homologues of the thiol- RT disulfide oxidoreductase DsbA in Neisseria meningitidis."; RL J. Mol. Biol. 392:952-966(2009). RN [3] {ECO:0000213|PDB:3A3T} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 42-232, AND DISULFIDE BONDS. RX PubMed=19815019; DOI=10.1016/j.jmb.2009.09.065; RA Vivian J.P., Scoullar J., Rimmer K., Bushell S.R., Beddoe T., RA Wilce M.C., Byres E., Boyle T.P., Doak B., Simpson J.S., Graham B., RA Heras B., Kahler C.M., Rossjohn J., Scanlon M.J.; RT "Structure and function of the oxidoreductase DsbA1 from Neisseria RT meningitidis."; RL J. Mol. Biol. 394:931-943(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40732.1; -; Genomic_DNA. DR PIR; C81217; C81217. DR RefSeq; NP_273334.1; NC_003112.2. DR RefSeq; WP_002224844.1; NC_003112.2. DR PDB; 3A3T; X-ray; 2.10 A; A/B/C/D/E/F=42-232. DR PDB; 3DVW; X-ray; 1.50 A; A=41-232. DR PDB; 3HZ8; X-ray; 1.45 A; A=41-232. DR PDBsum; 3A3T; -. DR PDBsum; 3DVW; -. DR PDBsum; 3HZ8; -. DR ProteinModelPortal; Q9K189; -. DR STRING; 122586.NMB0278; -. DR PaxDb; Q9K189; -. DR EnsemblBacteria; AAF40732; AAF40732; NMB0278. DR GeneID; 902389; -. DR KEGG; nme:NMB0278; -. DR PATRIC; 20355646; VBINeiMen85645_0347. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000265318; -. DR KO; K03673; -. DR OMA; NAIHKQK; -. DR OrthoDB; EOG68Q0Q6; -. DR BioCyc; NMEN122586:GHGG-293-MONOMER; -. DR EvolutionaryTrace; Q9K189; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR023205; DsbA/DsbL. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF13462; Thioredoxin_4; 1. DR PIRSF; PIRSF001488; Tdi_protein; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3A3T, ECO:0000213|PDB:3DVW, KW ECO:0000213|PDB:3HZ8}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 232 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332314. FT DOMAIN 26 229 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 75 78 {ECO:0000213|PDB:3A3T, FT ECO:0000213|PDB:3HZ8}. FT DISULFID 75 78 Redox-active. FT {ECO:0000256|PIRSR:PIRSR001488-1}. SQ SEQUENCE 232 AA; 25250 MW; 186EF798E448A2B7 CRC64; MKSRHLALGV AALFALAACD SKVQTSVPAD SAPAASAAAA PAGLVEGQNY TVLANPIPQQ QAGKVEVLEF FGYFCPHCAH LEPVLSKHAK SFKDDMYLRT EHVVWQKEML TLARLAAAVD MAAADSKDVA NSHIFDAMVN QKIKLQNPEV LKKWLGEQTA FDGKKVLAAY ESPESQARAD KMQELTETFQ IDGTPTVIVG GKYKVEFADW ESGMNTIDLL ADKVREEQKA AQ // ID Q7DD73_NEIMB Unreviewed; 430 AA. AC Q7DD73; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Valine--pyruvate aminotransferase {ECO:0000313|EMBL:AAF42158.1}; DE EC=2.6.1.66 {ECO:0000313|EMBL:AAF42158.1}; GN Name=avtA {ECO:0000313|EMBL:AAF42158.1}; GN OrderedLocusNames=NMB1823 {ECO:0000313|EMBL:AAF42158.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42158.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42158.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42158.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42158.1; -; Genomic_DNA. DR RefSeq; NP_274820.1; NC_003112.2. DR RefSeq; WP_002225657.1; NC_003112.2. DR ProteinModelPortal; Q7DD73; -. DR STRING; 122586.NMB1823; -. DR PaxDb; Q7DD73; -. DR EnsemblBacteria; AAF42158; AAF42158; NMB1823. DR GeneID; 903277; -. DR KEGG; nme:NMB1823; -. DR PATRIC; 20359631; VBINeiMen85645_2321. DR eggNOG; ENOG4105JKW; Bacteria. DR eggNOG; COG3977; LUCA. DR HOGENOM; HOG000269357; -. DR KO; K00835; -. DR OMA; HAHQCLR; -. DR OrthoDB; EOG6QCD62; -. DR BioCyc; NMEN122586:GHGG-1878-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 4: Predicted; KW Aminotransferase {ECO:0000313|EMBL:AAF42158.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Pyruvate {ECO:0000313|EMBL:AAF42158.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42158.1}. FT DOMAIN 51 419 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 430 AA; 47076 MW; 25E90E77C1BEC8AF CRC64; MQFSAFGEKF TQHSGILQLM DDLGDALKSD KPVNMLGGGN PARIPEIDQA FADIFSKLAA EHAVENIGNY SNPQGDAVLI DALTAFLNRE YSWNLTADNI ALTNGSQNAF FYLFNLFGGK FNLSDGTSAE KAILLPLAPE YIGYADVHVE GQHFVSVKPK IENVEHEGEA GFFKYRVDFD ALENLPELKA GKIGAICCSR PTNPTGNVLT DGEMARLDAL AREHGIPLII DNAYGMPFPN IIYSDVTLNW HENIILCFSL SKVGLPGVRT GIIVAAPEVV KAVSSLNAIV NLAPTRFGAA IATPLLESGE MKRLADQVIR PFYRNQAQTA VSLLKRELGA YPMKIHKPEG AIFLWLWFEN LPVSSQTLYE MLKAEGTLII PGEHFFVGID TQDYPHAGEC IRMSIAQDAQ TLEKGIAAIG KTVRKLYDNV // ID Q9K0Z7_NEIMB Unreviewed; 106 AA. AC Q9K0Z7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40843.1}; GN OrderedLocusNames=NMB0404 {ECO:0000313|EMBL:AAF40843.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40843.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40843.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40843.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40843.1; -; Genomic_DNA. DR PIR; A81203; A81203. DR RefSeq; NP_273453.1; NC_003112.2. DR RefSeq; WP_002212476.1; NC_003112.2. DR STRING; 122586.NMB0404; -. DR PaxDb; Q9K0Z7; -. DR DNASU; 902518; -. DR EnsemblBacteria; AAF40843; AAF40843; NMB0404. DR GeneID; 902518; -. DR KEGG; nme:NMB0404; -. DR PATRIC; 20355991; VBINeiMen85645_0513. DR eggNOG; ENOG4105W0Z; Bacteria. DR eggNOG; COG2960; LUCA. DR HOGENOM; HOG000265044; -. DR KO; K09806; -. DR OMA; EFDVQQE; -. DR OrthoDB; EOG6V1MB8; -. DR BioCyc; NMEN122586:GHGG-426-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007475; BMFP. DR Pfam; PF04380; BMFP; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 81 104 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 106 AA; 11646 MW; 119695871827939F CRC64; MFGKQLFEEV GSKISETIAN SPAKDVEKNI KAMLGGAFNR MDLVTREEFD IQQQVLIKTR TKLAALEARL EKLEAAQNPE RAALEAAEAA AEEAVAEIRQ QTEAGE // ID Q9JY87_NEIMB Unreviewed; 704 AA. AC Q9JY87; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42041.1}; GN OrderedLocusNames=NMB1693 {ECO:0000313|EMBL:AAF42041.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42041.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42041.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42041.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42041.1; -; Genomic_DNA. DR PIR; G81051; G81051. DR RefSeq; NP_274697.1; NC_003112.2. DR RefSeq; WP_002222123.1; NC_003112.2. DR STRING; 122586.NMB1693; -. DR PaxDb; Q9JY87; -. DR EnsemblBacteria; AAF42041; AAF42041; NMB1693. DR GeneID; 903412; -. DR KEGG; nme:NMB1693; -. DR PATRIC; 20359339; VBINeiMen85645_2176. DR eggNOG; ENOG4108WB6; Bacteria. DR eggNOG; COG2982; LUCA. DR HOGENOM; HOG000219074; -. DR OMA; PTALKQN; -. DR OrthoDB; EOG67Q964; -. DR BioCyc; NMEN122586:GHGG-1748-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007844; AsmA. DR Pfam; PF05170; AsmA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 615 AsmA. {ECO:0000259|Pfam:PF05170}. SQ SEQUENCE 704 AA; 77609 MW; 440F653D11F6CD13 CRC64; MDLLSVFHKY RLKYAVAVLT ILLLAAVGLH ASVYRTFTPE NIRSRLQQSI AHTHRKISFD ADIQRRLLPR PTVILKNLTI TEPGGDQTAV SVQETKIGLS WKNLWSDQIQ IEKWVVSSAE LALTRDGKGV WNIQDLIDSQ KRQASVNRII VENSTVRLNF LQEQLILKEI NLNLQSPDSS GQPFESSGIL VWGKLSVPWK SRGLFLSNGI GPPEISPFHF EASTSLDGHG ITISTTGSPS VRFNAGGADA AGLGLRADTS FRNLHLTAQI PALALRNNSI KIETVNGAFT AGGEYARWDG SFKLDKANLH SGIANIGNAE ISGSFKTPRH QTNFSLNSPL VWTENKGLDA PRLYVSTLQD TVNRLPQPRF ISRLDGSLSV PNLQNWNAEL NGTFDRQTVA AKFRYTHEDA PHLEAAVALQ KLNLTPYLDD VRQQNGKIFP DTLAKLSGDI EAHLKIGKVQ LPGLQLDDME TYLHADKGHI ALSRFKSGLY GGHTEGGISI ANTRPATYRL QQNASNIQIQ PLLQDLFGFH SFSGNGDAVI DLTAGGETRK ELIRSLQGSL SLNISNGAWH GIDMDNILKN GISGKTADNA APSTPFHRFT LNSEISDGIS RHIDTELFSD SLYVTSNGYT NLDTQELSED VLIRNAVHPK NKPIPLKITG TVDKPSITVD YGRLTGGINS RKEKQKILED TLLEQWQWLK PKEP // ID Q9K033_NEIMB Unreviewed; 251 AA. AC Q9K033; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 106. DE SubName: Full=Amino acid ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41202.1}; GN OrderedLocusNames=NMB0789 {ECO:0000313|EMBL:AAF41202.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41202.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41202.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41202.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41202.1; -; Genomic_DNA. DR PIR; B81159; B81159. DR RefSeq; NP_273831.1; NC_003112.2. DR RefSeq; WP_010980846.1; NC_003112.2. DR ProteinModelPortal; Q9K033; -. DR SMR; Q9K033; 1-246. DR STRING; 122586.NMB0789; -. DR PaxDb; Q9K033; -. DR EnsemblBacteria; AAF41202; AAF41202; NMB0789. DR GeneID; 902904; -. DR KEGG; nme:NMB0789; -. DR PATRIC; 20356965; VBINeiMen85645_1001. DR eggNOG; ENOG4105CDA; Bacteria. DR eggNOG; COG1126; LUCA. DR KO; K10010; -. DR OMA; DLFDHPK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-820-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030679; ABC_ATPase_HisP-typ. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41202.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41202.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 251 AA; 27999 MW; 5B19A289CA54EC00 CRC64; MIKIRNIHKT FGENTILRGI DLDVCKGQVV VILGPSGSGK TTFLRCLNAL EMPEDGQIEF DNERPLKIDF SKKPSKHDIL ALRRKSGMVF QQYNLFPHKT ALENVMEGPV AVQGKPAAQA REEALKLLEK VGLGDKVDLY PYQLSGGQQQ RVGIARALAI QPELMLFDEP TSALDPELVQ DVLDTMKELA QEGWTMVVVT HEIKFALEVA TTVVVMDGGV IVEQGSPQDL FDHPKHERTR RFLSQIQSTK I // ID Q7DD54_NEIMB Unreviewed; 128 AA. AC Q7DD54; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 66. DE RecName: Full=Ribosomal silencing factor RsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN Name=rsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN OrderedLocusNames=NMB2023 {ECO:0000313|EMBL:AAF42346.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42346.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42346.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42346.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Functions as a ribosomal silencing factor. Interacts CC with ribosomal protein L14 (rplN), blocking formation of CC intersubunit bridge B8. Prevents association of the 30S and 50S CC ribosomal subunits and the formation of functional ribosomes, thus CC repressing translation. {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SUBUNIT: Interacts with ribosomal protein L14 (rplN). CC {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000256|HAMAP- CC Rule:MF_01477}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42346.1; -; Genomic_DNA. DR PIR; B81015; B81015. DR RefSeq; NP_275015.1; NC_003112.2. DR RefSeq; WP_002225676.1; NC_003112.2. DR ProteinModelPortal; Q7DD54; -. DR SMR; Q7DD54; 8-124. DR STRING; 122586.NMB2023; -. DR PaxDb; Q7DD54; -. DR EnsemblBacteria; AAF42346; AAF42346; NMB2023. DR GeneID; 904084; -. DR KEGG; nme:NMB2023; -. DR PATRIC; 20360161; VBINeiMen85645_2580. DR eggNOG; ENOG4105KEM; Bacteria. DR eggNOG; COG0799; LUCA. DR HOGENOM; HOG000016051; -. DR KO; K09710; -. DR OMA; YNVEGLW; -. DR OrthoDB; EOG6J48TR; -. DR BioCyc; NMEN122586:GHGG-2085-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01477; Iojap_RsfS; 1. DR InterPro; IPR004394; Iojap/RsfS/C7orf30. DR PANTHER; PTHR21043; PTHR21043; 1. DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_01477}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_01477}. SQ SEQUENCE 128 AA; 13944 MW; E04A497837663BDF CRC64; MNEQELQDLQ KMVGVAVNAL GDIKAKDISV LETQDKTSLF ARMIIASGDS TRQVKALANN VAVDLKEAGF EILSTEGDSG EWTLVDAGDL VVHVMLPAVR DFYDIDTLWG GEKPSFHAGM QKPWHAAD // ID Q9JZ69_NEIMB Unreviewed; 151 AA. AC Q9JZ69; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Low molecular weight protein tyrosine-phosphatase {ECO:0000313|EMBL:AAF41644.1}; DE EC=3.1.3.48 {ECO:0000313|EMBL:AAF41644.1}; GN OrderedLocusNames=NMB1267 {ECO:0000313|EMBL:AAF41644.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41644.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41644.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41644.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41644.1; -; Genomic_DNA. DR PIR; E81102; E81102. DR RefSeq; NP_274288.1; NC_003112.2. DR RefSeq; WP_002222400.1; NC_003112.2. DR ProteinModelPortal; Q9JZ69; -. DR STRING; 122586.NMB1267; -. DR PaxDb; Q9JZ69; -. DR EnsemblBacteria; AAF41644; AAF41644; NMB1267. DR GeneID; 903689; -. DR KEGG; nme:NMB1267; -. DR PATRIC; 20358149; VBINeiMen85645_1586. DR eggNOG; ENOG4105KJF; Bacteria. DR eggNOG; COG0394; LUCA. DR HOGENOM; HOG000273094; -. DR KO; K01104; -. DR OMA; FRHLVND; -. DR OrthoDB; EOG6MH5JB; -. DR BioCyc; NMEN122586:GHGG-1305-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR InterPro; IPR023485; Ptyr_pPase_SF. DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt. DR Pfam; PF01451; LMWPc; 1. DR PRINTS; PR00719; LMWPTPASE. DR SMART; SM00226; LMWPc; 1. DR SUPFAM; SSF52788; SSF52788; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41644.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 148 LMWPc. {ECO:0000259|SMART:SM00226}. SQ SEQUENCE 151 AA; 16931 MW; AFFE4AA1FC2408DB CRC64; MKKPKILFVC LGNICRSPMA EYILRRRAAE AGIPLEADSA GTSGWHDGED MHRETAKILK KHGIDASGFT SRKIRQSDAA AFDCIIAMDG KNLSELERTF GRRPEKIFKL TDLIPESGYD HVPDPWYTGD FEETFRLADA GCRALLEKIS K // ID Q9JXV1_NEIMB Unreviewed; 245 AA. AC Q9JXV1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Putative DNA polymerase, bacteriophage-type {ECO:0000313|EMBL:AAF42207.1}; GN OrderedLocusNames=NMB1873 {ECO:0000313|EMBL:AAF42207.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42207.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42207.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42207.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42207.1; -; Genomic_DNA. DR PIR; G81032; G81032. DR RefSeq; NP_274869.1; NC_003112.2. DR RefSeq; WP_002225788.1; NC_003112.2. DR ProteinModelPortal; Q9JXV1; -. DR STRING; 122586.NMB1873; -. DR PaxDb; Q9JXV1; -. DR EnsemblBacteria; AAF42207; AAF42207; NMB1873. DR GeneID; 904315; -. DR KEGG; nme:NMB1873; -. DR PATRIC; 20359777; VBINeiMen85645_2394. DR eggNOG; COG1573; LUCA. DR HOGENOM; HOG000218759; -. DR KO; K02334; -. DR OMA; AMIETLC; -. DR OrthoDB; EOG63RGQ3; -. DR BioCyc; NMEN122586:GHGG-1929-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.470.10; -; 1. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR Pfam; PF03167; UDG; 1. DR SUPFAM; SSF52141; SSF52141; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 102 232 UDG. {ECO:0000259|Pfam:PF03167}. SQ SEQUENCE 245 AA; 26160 MW; D0098BFFF88A84C9 CRC64; MLSARYLHLH EALGLGPMWL KQAAAVLPPK NTPAPSAQAR PQTVRAAPIR PSQPHNGQAR LETMKALETA AVPTRKPAPE TETPLPGLSD GIAPVPAASG ITKLAVVSLC PPIEDAVYGQ LFHGKAGILL DNILKAVGLD AAYVHKTCWV KTAAVGNPMP SEQAVANALG QIARELDGCR APAVLFLGQA FVQPERQTMI ETLCGSRPFF IIDHPARLLR QPELKARAWQ VLKQLKRALR QGGGS // ID Q9JXU3_NEIMB Unreviewed; 725 AA. AC Q9JXU3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAF42216.1}; GN OrderedLocusNames=NMB1882 {ECO:0000313|EMBL:AAF42216.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42216.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42216.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42216.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU003357}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC {ECO:0000256|RuleBase:RU003357}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42216.1; -; Genomic_DNA. DR PIR; H81030; H81030. DR RefSeq; NP_274878.1; NC_003112.2. DR RefSeq; WP_002225792.1; NC_003112.2. DR ProteinModelPortal; Q9JXU3; -. DR STRING; 122586.NMB1882; -. DR PaxDb; Q9JXU3; -. DR EnsemblBacteria; AAF42216; AAF42216; NMB1882. DR GeneID; 904299; -. DR KEGG; nme:NMB1882; -. DR PATRIC; 20359799; VBINeiMen85645_2405. DR eggNOG; ENOG4105CNM; Bacteria. DR eggNOG; COG4773; LUCA. DR HOGENOM; HOG000218756; -. DR KO; K16088; -. DR OMA; GETHTDP; -. DR OrthoDB; EOG67DPGD; -. DR BioCyc; NMEN122586:GHGG-1938-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015891; P:siderophore transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010105; TonB_sidphr_rcpt. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01783; TonB-siderophor; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Receptor {ECO:0000313|EMBL:AAF42216.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 725 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327829. FT DOMAIN 68 168 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 480 723 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 725 AA; 80479 MW; D3953D4485FD8FAF CRC64; MTRFKYSLLF AALLPVYAQA DVSVSDDPKP QESTELPTIT VTADRTASSN DGYTVSGTHT PLGLPMTLRE IPQSVSVITS QQMRDQNIKT LDRALLQATG TSRQIYGSDR AGYNYLFARG SRIANYQING IPVADALADT GNANTAAYER VEVVRGVAGL LDGTGEPSAT VNLVRKRLTR KPLFEVRAEA GNRKHFGLDA DVSGSLNTEG TLRGRLVSTF GRGDSWRRRE RSRDAELYGI LEYDIAPQTR VHAGMDYQQA KETADAPLSY AVYDSQGYAT AFGPKDNPAT NWANSRHRAL NLFAGIEHRF NQDWKLKAEY DYTRSRFRQP YGVAGVLSID HNTAATDLIP GYWHADPRTH SASVSLIGKY RLFGREHDLI AGINGYKYAS NKYGERSIIP NAIPNAYEFS RTGAYPQPAS FAQTIPQYGT RRQIGGYLAT RFRAADNLSL ILGGRYTRYR TGSYDSRTQG MTYVSANRFT PYTGIVFDLT GNLSLYGSYS SLFVPQSQKD EHGSYLKPVT GNNLEAGIKG EWLEGRLNAS AAVYRARKNN LATAAGRDPS GNTYYRAANQ AKTHGWEIEV GGRITPEWQI QAGYSQSKTR DQDGSRLNPD SVPERSFKLF TAYHFAPEAP SGWTIGAGVR WQSETHTDPA TLRIPNPAAK ARAADNSRQK AYAVADIMAR YRFNPRAELS LNVDNLFNKH YRTQPDRHSY GALRTVNAAF TYRFK // ID Q9JZX0_NEIMB Unreviewed; 157 AA. AC Q9JZX0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41276.1}; GN OrderedLocusNames=NMB0865 {ECO:0000313|EMBL:AAF41276.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41276.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41276.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41276.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41276.1; -; Genomic_DNA. DR PIR; A81148; A81148. DR RefSeq; NP_273906.1; NC_003112.2. DR RefSeq; WP_002244512.1; NC_003112.2. DR STRING; 122586.NMB0865; -. DR PaxDb; Q9JZX0; -. DR EnsemblBacteria; AAF41276; AAF41276; NMB0865. DR GeneID; 902979; -. DR KEGG; nme:NMB0865; -. DR eggNOG; ENOG4107AP1; Bacteria. DR eggNOG; ENOG410Z5UK; LUCA. DR HOGENOM; HOG000218889; -. DR OrthoDB; EOG61P6VJ; -. DR BioCyc; NMEN122586:GHGG-896-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 157 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328350. FT TRANSMEM 57 75 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 157 AA; 16205 MW; 948F3A2BA3E29F49 CRC64; MKKQITAAVM MLSMIAPAMA NGLDNQAFEK YVFHTQADAP MQLAELSQKE MKETEGAFLP IVAGALMGGA ISAWANHGIS KIKTGQFAST RSTLAATAGG MIGGGYSSAM LRGAGITTSV FARSAWKGGN AIPNAVIRAN GAALNQSSSA AMGKHRR // ID Q9JX95_NEIMB Unreviewed; 334 AA. AC Q9JX95; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 97. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160}; GN Name=gapA-2 {ECO:0000313|EMBL:AAF42467.1}; GN OrderedLocusNames=NMB2159 {ECO:0000313|EMBL:AAF42467.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42467.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42467.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42467.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {ECO:0000256|RuleBase:RU361160}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42467.1; -; Genomic_DNA. DR PIR; E81001; E81001. DR RefSeq; NP_275144.1; NC_003112.2. DR RefSeq; WP_010981034.1; NC_003112.2. DR ProteinModelPortal; Q9JX95; -. DR SMR; Q9JX95; 4-332. DR STRING; 122586.NMB2159; -. DR PaxDb; Q9JX95; -. DR PRIDE; Q9JX95; -. DR EnsemblBacteria; AAF42467; AAF42467; NMB2159. DR GeneID; 903213; -. DR KEGG; nme:NMB2159; -. DR PATRIC; 20360516; VBINeiMen85645_2754. DR eggNOG; ENOG4105C17; Bacteria. DR eggNOG; COG0057; LUCA. DR HOGENOM; HOG000071678; -. DR KO; K00134; -. DR OMA; MKAASSE; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; NMEN122586:GHGG-2224-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160, KW ECO:0000313|EMBL:AAF42467.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 151 Gp_dh_N. {ECO:0000259|SMART:SM00846}. FT ACT_SITE 151 151 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR000149-1}. FT SITE 178 178 Activates thiol group during catalysis. FT {ECO:0000256|PIRSR:PIRSR000149-4}. SQ SEQUENCE 334 AA; 35845 MW; EC33464350094B9F CRC64; MSIKVAINGF GRIGRLALRQ IEKAHDIEVV AVNDLTPAEM LLHLFKYDST QGRFQGTAEL KDDAIVVNGK EIKVFANPNP EELPWGELGV DVILECTGFF TNKTKAEAHI RAGARKVVIS APGGNDVKTV VYGVNQDILD GSETVISAAS CTTNCLAPMA AVLQKEFGVV EGLMTTIHAY TGDQNTLDAP HRKGDLRRAR AAALNIVPNS TGAAKAIGLV IPELNGKLDG SAQRVPVASG SLTELVSILE RPVTKEEINA AMKAAASESY GYNEDQIVSS DVVGIEYGSL FDATQTRVMT VGGKQLVKTV AWYDNEMSYT CQLVRTLEYF AGKI // ID Q9K1G7_NEIMB Unreviewed; 265 AA. AC Q9K1G7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938}; DE EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938}; GN Name=cdsA {ECO:0000313|EMBL:AAF40642.1}; GN OrderedLocusNames=NMB0185 {ECO:0000313|EMBL:AAF40642.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40642.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40642.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40642.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP- CC diacylglycerol. {ECO:0000256|RuleBase:RU003938}. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC {ECO:0000256|RuleBase:RU003938}. CC -!- SIMILARITY: Belongs to the CDS family. CC {ECO:0000256|RuleBase:RU003938}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40642.1; -; Genomic_DNA. DR PIR; B81229; B81229. DR RefSeq; NP_273243.1; NC_003112.2. DR RefSeq; WP_002239446.1; NC_003112.2. DR STRING; 122586.NMB0185; -. DR PaxDb; Q9K1G7; -. DR EnsemblBacteria; AAF40642; AAF40642; NMB0185. DR GeneID; 902292; -. DR KEGG; nme:NMB0185; -. DR PATRIC; 20355395; VBINeiMen85645_0227. DR eggNOG; ENOG4105KNE; Bacteria. DR eggNOG; COG0575; LUCA. DR HOGENOM; HOG000006168; -. DR KO; K00981; -. DR OMA; WEWGRLN; -. DR OrthoDB; EOG6TBHJT; -. DR BioCyc; NMEN122586:GHGG-195-MONOMER; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR000374; PC_trans. DR PROSITE; PS01315; CDS; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938, KW ECO:0000313|EMBL:AAF40642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU003938, KW ECO:0000313|EMBL:AAF40642.1}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 220 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 265 AA; 29221 MW; 0A4FE7DB21A4429D CRC64; MLKQRVITAM WLLPLMLGML FYAPQWLWAA FCGLIALIAL WEYARMGGLC KIKTNHYLAA TLVFGVVAYA GGWMLPNLVW YVVLAFWLAV MPLWLRFKWR LNGGWQVYAV GWLLVMPFWF ALVSLRPHPD DALPLLAVMG LVWVADICAY FSGKAFGKHK IAPAISPGKS WEGAIGGAVC VAVYMTAVRS AGWLAFDTGW FDTVLIGLVL TVVSVCGDLL ESWLKRAAGI KDSSKLLPGH GGVFDRTDSL IAVISVYAAM MSVLN // ID Q7DDM7_NEIMB Unreviewed; 164 AA. AC Q7DDM7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41008.1}; GN OrderedLocusNames=NMB0580 {ECO:0000313|EMBL:AAF41008.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41008.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41008.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41008.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41008.1; -; Genomic_DNA. DR PIR; G81183; G81183. DR RefSeq; NP_273624.1; NC_003112.2. DR RefSeq; WP_002221353.1; NC_003112.2. DR ProteinModelPortal; Q7DDM7; -. DR STRING; 122586.NMB0580; -. DR PaxDb; Q7DDM7; -. DR EnsemblBacteria; AAF41008; AAF41008; NMB0580. DR GeneID; 902695; -. DR KEGG; nme:NMB0580; -. DR PATRIC; 20356443; VBINeiMen85645_0741. DR eggNOG; ENOG4108X6V; Bacteria. DR eggNOG; COG4314; LUCA. DR HOGENOM; HOG000146264; -. DR KO; K19342; -. DR OMA; TLMPDQP; -. DR OrthoDB; EOG6GJBT9; -. DR BioCyc; NMEN122586:GHGG-606-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008719; N2O_reductase_NosL. DR Pfam; PF05573; NosL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 164 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287541. SQ SEQUENCE 164 AA; 18154 MW; 213CC71F950FA6CD CRC64; MKKTLLAIVA VSALSACRQA EEGPPPLPRQ ISDRSVGHYC SMNLTEHNGP KAQIFLNGKP DQPVWFSTIK QMFGYTKLPE EPKGIRVIYV TDMGNVTDWT NPNADTEWMD AKKAFYVIDS GFIGGMGAED ALPFGNKEQA EKFAKDKGGK VVGFDDMPDT YIFK // ID Q9JY47_NEIMB Unreviewed; 361 AA. AC Q9JY47; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42092.1}; GN OrderedLocusNames=NMB1749 {ECO:0000313|EMBL:AAF42092.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42092.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42092.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42092.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42092.1; -; Genomic_DNA. DR PIR; D81048; D81048. DR RefSeq; NP_274750.1; NC_003112.2. DR RefSeq; WP_002219739.1; NC_003112.2. DR ProteinModelPortal; Q9JY47; -. DR STRING; 122586.NMB1749; -. DR PaxDb; Q9JY47; -. DR EnsemblBacteria; AAF42092; AAF42092; NMB1749. DR GeneID; 903348; -. DR KEGG; nme:NMB1749; -. DR PATRIC; 20359465; VBINeiMen85645_2238. DR eggNOG; ENOG4108UST; Bacteria. DR eggNOG; ENOG4111MTZ; LUCA. DR HOGENOM; HOG000218807; -. DR OMA; TAPFEHS; -. DR OrthoDB; EOG6QP0WW; -. DR BioCyc; NMEN122586:GHGG-1804-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008900; Zona_occludens_tox. DR Pfam; PF05707; Zot; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 218 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 361 AA; 40979 MW; B6BFBD53530B41BB CRC64; MIYLFTGNMG TGKTSRVVSM ILNNEDGLFK MKLEDGTEVD RPLYFCHIDG LDKRQFKAHE LTEEQIMSAP LRDVIPEGAV LIVDEAHYTY PVRAAGRPVP PYIQELTELR HHGHTVILMT QHPSQLDIFV RNLVSKHVHL ERKAIGMKQY YWYKCVTSLD NPAGVSGVEV ASWKPPKEAF KYYKSASQHQ KFKKKVPWAV WALIAIVGFV GWKSYGIFKV YSKATDSRIE QEAQKESVVQ TMTEQPASSE EMPLKNSDNL KPEDFVPTLP EKPESKPIYN TVRQVKTFEQ IAGCIDGGKS DCTCYSNQGT PLKEITKIMC KEYVKNGLPF NPYKDEQQRT EQVEQSAKAD KPQVLVMGGK P // ID Q9JZF3_NEIMB Unreviewed; 661 AA. AC Q9JZF3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Bacteriophage transposase {ECO:0000313|EMBL:AAF41473.1}; GN OrderedLocusNames=NMB1081 {ECO:0000313|EMBL:AAF41473.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41473.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41473.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41473.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41473.1; -; Genomic_DNA. DR PIR; A81125; A81125. DR RefSeq; NP_274113.1; NC_003112.2. DR RefSeq; WP_002225252.1; NC_003112.2. DR ProteinModelPortal; Q9JZF3; -. DR STRING; 122586.NMB1081; -. DR PaxDb; Q9JZF3; -. DR EnsemblBacteria; AAF41473; AAF41473; NMB1081. DR GeneID; 903498; -. DR KEGG; nme:NMB1081; -. DR PATRIC; 20357717; VBINeiMen85645_1375. DR eggNOG; ENOG4105DU7; Bacteria. DR eggNOG; COG2801; LUCA. DR HOGENOM; HOG000218935; -. DR KO; K07497; -. DR OMA; HERYEWL; -. DR OrthoDB; EOG6C0130; -. DR BioCyc; NMEN122586:GHGG-1117-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.30.30.130; -; 1. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR003314; Mu-type_HTH. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR015378; Transposase-like_Mu_C. DR InterPro; IPR009004; Transposase_Mu_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02316; HTH_Tnp_Mu_1; 1. DR Pfam; PF09299; Mu-transpos_C; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50610; SSF50610; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS51702; HTH_MU; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 69 HTH Mu-type. FT {ECO:0000259|PROSITE:PS51702}. FT DOMAIN 281 399 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 661 AA; 73928 MW; 8B2E98DF25CEEFD0 CRC64; MKISASDIAK LGIPSLPTDR QGIEYHAKKN NWQHCFEQKG RGRPKKLYEI ASLPAEIRAA IMKRQSDELA EKMPKMLPKV RPGTAMSAQA LAEAAKLLNE KQRSVADARC AVVAAVLGIK YEYDCSAKAA VAQFLGLLAE GKLDAVTLGN LEKANDRSRT AKVGERTLDG WISAYLKAEN ATERLVALAP KTTKAVKPIE SYGWLPMFMQ FHNIPSAPKL AHSYRWFVQW AEAENMPVND VPNLSMVRRV WEKLPLIMQE RGRKTGAAYK SLLPYVKRDW GALKPNDVWI GDGHSFKAKV AHPVHGRPFK PEVTVIIDGC TRFVVGFSVS LAESCVAVSD AMRIGVKHFG LPIIYYSDNG GGQTGKTIDH EITGITSRPG IRHETGIAGN PQGRGIIERW WKDNLIEMAR QYETFAGAGM DSSTKNLMYR KMESAFNALE KGKDLTEEQQ KYLKKLPSWS RFIADVVKCI DEYNNRPHGE LPRHPDGGHY TPKAYREMRL EQDGIAPDML SAQELATMFM PQEVRKVQRG WLDLFNNSYF STELAEYHKD EVRVSYDLSD ASAVNVFDMD GKFITKAQAN GNTREAFPTA RIDQLAEKRR KGKIKRAENA IKLANAEVNP ALEQAAVWDE LGHLGGNDIE AEYAVLPKTG TDDFVLFEAD R // ID Q9K0P4_NEIMB Unreviewed; 165 AA. AC Q9K0P4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40970.1}; GN OrderedLocusNames=NMB0541 {ECO:0000313|EMBL:AAF40970.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40970.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40970.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40970.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3VJZ} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS). RX PubMed=22373915; DOI=10.1093/nar/gks177; RA Wang H.C., Ko T.P., Wu M.L., Ku S.C., Wu H.J., Wang A.H.; RT "Neisseria conserved protein DMP19 is a DNA mimic protein that RT prevents DNA binding to a hypothetical nitrogen-response transcription RT factor."; RL Nucleic Acids Res. 40:5718-5730(2012). RN [3] {ECO:0000213|PDB:3WUR} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX PubMed=25287606; DOI=10.1002/anie.201405664; RA Lee C.C., Maestre-Reyna M., Hsu K.C., Wang H.C., Liu C.I., Jeng W.Y., RA Lin L.L., Wood R., Chou C.C., Yang J.M., Wang A.H.; RT "Crowning proteins: modulating the protein surface properties using RT crown ethers."; RL Angew. Chem. Int. Ed. 53:13054-13058(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40970.1; -; Genomic_DNA. DR PIR; C81186; C81186. DR RefSeq; NP_273586.1; NC_003112.2. DR RefSeq; WP_002225584.1; NC_003112.2. DR PDB; 3VJZ; X-ray; 1.80 A; A/B=1-165. DR PDB; 3WUR; X-ray; 1.45 A; A/B=1-165. DR PDBsum; 3VJZ; -. DR PDBsum; 3WUR; -. DR STRING; 122586.NMB0541; -. DR PaxDb; Q9K0P4; -. DR EnsemblBacteria; AAF40970; AAF40970; NMB0541. DR GeneID; 902656; -. DR KEGG; nme:NMB0541; -. DR PATRIC; 20356341; VBINeiMen85645_0689. DR eggNOG; ENOG4108ZUT; Bacteria. DR eggNOG; ENOG4111PBT; LUCA. DR HOGENOM; HOG000218796; -. DR OMA; FVQLIQN; -. DR OrthoDB; EOG6JX7K2; -. DR BioCyc; NMEN122586:GHGG-567-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025402; DUF4375. DR Pfam; PF14300; DUF4375; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3VJZ, ECO:0000213|PDB:3WUR}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 39 159 DUF4375. {ECO:0000259|Pfam:PF14300}. SQ SEQUENCE 165 AA; 18512 MW; 491B755652F254BB CRC64; MTALTLPEDI RQQEPSALLY TLVSAYLEHT AQTGDESLSC LSDDQHTLTA FCYLDSQVEE GGFVQLIASG YGEYIFRNPL ADSLRRWKIK AVPKVLDKAK ALYEQHGKTI ETLADGGADI PSLRKQFPEF EEWDGAYYEA AEQDLPLLAE HIQSNWETFA HIGQA // ID Q9JYS5_NEIMB Unreviewed; 379 AA. AC Q9JYS5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41811.1}; GN OrderedLocusNames=NMB1452 {ECO:0000313|EMBL:AAF41811.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41811.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41811.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41811.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41811.1; -; Genomic_DNA. DR PIR; E81081; E81081. DR RefSeq; NP_274463.1; NC_003112.2. DR RefSeq; WP_010980940.1; NC_003112.2. DR ProteinModelPortal; Q9JYS5; -. DR STRING; 122586.NMB1452; -. DR PaxDb; Q9JYS5; -. DR EnsemblBacteria; AAF41811; AAF41811; NMB1452. DR GeneID; 903874; -. DR KEGG; nme:NMB1452; -. DR PATRIC; 20358645; VBINeiMen85645_1832. DR eggNOG; ENOG4107SK8; Bacteria. DR eggNOG; COG2070; LUCA. DR HOGENOM; HOG000123286; -. DR KO; K00459; -. DR OMA; SNCVSPC; -. DR OrthoDB; EOG6C013S; -. DR BioCyc; NMEN122586:GHGG-1492-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004136; NMO. DR Pfam; PF03060; NMO; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 334 NMO. {ECO:0000259|Pfam:PF03060}. SQ SEQUENCE 379 AA; 40598 MW; 4AD1B572D9FE93B5 CRC64; MQNIFDPLVI RGKSLTPIVQ GGMGVGVSAS GLSSAVAREN GIGTIASVDL RHLHEDLLAE SQINPSEEKY TSLNCTALDR EIQKAKSASE GKGLIAVNVM KAVKDHAAYV RQACESGADA VVMGAGLPLD LPEMTEGYHK DVALLPILSE SRGINIVLKR WMKKGILPDA IVVEHPAHAA GHLGASTVEG VNDAKFDFKR VIEETFEVFK SLGLESEKIP LILAGGMANF EKVKTALKNW GASAVQIGTA FAVTEEGDAH LNFKKTLAGA ETEKVVEFMS VAGLPARGVR TKFLDSYIKR ESKLQTNAKA DPRRCTQGLN CLTSCGLRDG LSKAGQFCID IQLAAAFRGE VDKGLFFRGK DRCPSAMPSA PSARRYNIC // ID Q7DD56_NEIMB Unreviewed; 72 AA. AC Q7DD56; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42329.1}; GN OrderedLocusNames=NMB2002 {ECO:0000313|EMBL:AAF42329.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42329.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42329.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42329.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42329.1; -; Genomic_DNA. DR PIR; H81016; H81016. DR RefSeq; NP_274994.1; NC_003112.2. DR RefSeq; WP_002214913.1; NC_003112.2. DR STRING; 122586.NMB2002; -. DR PaxDb; Q7DD56; -. DR EnsemblBacteria; AAF42329; AAF42329; NMB2002. DR GeneID; 904123; -. DR KEGG; nme:NMB2002; -. DR PATRIC; 20360103; VBINeiMen85645_2556. DR eggNOG; ENOG4105W2U; Bacteria. DR eggNOG; ENOG41122R4; LUCA. DR HOGENOM; HOG000218730; -. DR OMA; LMGCDEQ; -. DR OrthoDB; EOG6MM1RZ; -. DR BioCyc; NMEN122586:GHGG-2059-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 72 AA; 8310 MW; 794ED3461AC89470 CRC64; MSMPEMPKWY DDDGQIVSCT EKVKVMSENM AELYQTAQDA FEDALLMGCG ERQLRDYLLA LIEGLENPYR KV // ID Q9K125_NEIMB Unreviewed; 129 AA. AC Q9K125; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40811.1}; GN OrderedLocusNames=NMB0369 {ECO:0000313|EMBL:AAF40811.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40811.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40811.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40811.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40811.1; -; Genomic_DNA. DR PIR; G81206; G81206. DR RefSeq; NP_273418.1; NC_003112.2. DR RefSeq; WP_002224900.1; NC_003112.2. DR ProteinModelPortal; Q9K125; -. DR STRING; 122586.NMB0369; -. DR PaxDb; Q9K125; -. DR EnsemblBacteria; AAF40811; AAF40811; NMB0369. DR GeneID; 902484; -. DR KEGG; nme:NMB0369; -. DR PATRIC; 20355895; VBINeiMen85645_0465. DR OMA; DEASGKM; -. DR OrthoDB; EOG60GRTJ; -. DR BioCyc; NMEN122586:GHGG-391-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR030934; Intein_C. DR SUPFAM; SSF51294; SSF51294; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 129 AA; 14419 MW; 197FA617599F0D6F CRC64; MKAGSRLLSE SGRTQTVRKT VVKPKPLKAY NLTVADWHTY FVKGNQAETE GVWVHNSCPP KRTGSSKNEK HGDGGRSQIS AESKIAELTN KIIPGMSKNE RLKIKQKIRN IAKNANRKTK GEEHGRRGR // ID Q9JZH9_NEIMB Unreviewed; 68 AA. AC Q9JZH9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41441.1}; GN OrderedLocusNames=NMB1043 {ECO:0000313|EMBL:AAF41441.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41441.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41441.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41441.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41441.1; -; Genomic_DNA. DR PIR; C81127; C81127. DR STRING; 122586.NMB1043; -. DR PaxDb; Q9JZH9; -. DR EnsemblBacteria; AAF41441; AAF41441; NMB1043. DR BioCyc; NMEN122586:GHGG-1080-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 62 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 8154 MW; D1887E7F628C0135 CRC64; MRKKIKKWIY AINGIMMSIW IIFFPNTGSV YDGGRTTIFN ENHPFHFIFC ITFLIGTIFL IYHEYNDN // ID Q9JXD0_NEIMB Unreviewed; 83 AA. AC Q9JXD0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42423.1}; GN OrderedLocusNames=NMB2109 {ECO:0000313|EMBL:AAF42423.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42423.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42423.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42423.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42423.1; -; Genomic_DNA. DR PIR; B81004; B81004. DR STRING; 122586.NMB2109; -. DR PaxDb; Q9JXD0; -. DR EnsemblBacteria; AAF42423; AAF42423; NMB2109. DR PATRIC; 20360392; VBINeiMen85645_2692. DR eggNOG; ENOG4107C2N; Bacteria. DR eggNOG; ENOG410Z5S0; LUCA. DR HOGENOM; HOG000218707; -. DR OrthoDB; EOG6Z3KP4; -. DR BioCyc; NMEN122586:GHGG-2174-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 83 AA; 9664 MW; E18092B859042854 CRC64; MDNTRIMAAR EAGVKVEANV HNFNDRLSSK ERIRFKHDGI EPQTWGEAIQ LRIRKQETQK GVPEGWSKRF PNGSIYDVKV LRK // ID Q9JZY4_NEIMB Unreviewed; 234 AA. AC Q9JZY4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41259.1}; GN OrderedLocusNames=NMB0848 {ECO:0000313|EMBL:AAF41259.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41259.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41259.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41259.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41259.1; -; Genomic_DNA. DR PIR; C81149; C81149. DR RefSeq; NP_273889.1; NC_003112.2. DR RefSeq; WP_002225397.1; NC_003112.2. DR STRING; 122586.NMB0848; -. DR PaxDb; Q9JZY4; -. DR EnsemblBacteria; AAF41259; AAF41259; NMB0848. DR GeneID; 902962; -. DR KEGG; nme:NMB0848; -. DR PATRIC; 20357087; VBINeiMen85645_1062. DR eggNOG; COG3471; LUCA. DR HOGENOM; HOG000218873; -. DR OMA; YPRYGKD; -. DR OrthoDB; EOG6RJV4P; -. DR BioCyc; NMEN122586:GHGG-879-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007497; DUF541. DR Pfam; PF04402; SIMPL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 234 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328353. SQ SEQUENCE 234 AA; 25573 MW; 3F7887C1C4F26BAC CRC64; MLRLVLAASL SAVSFPAAAE ALNYNIVEFS ESAGVEVAQD TMSARFQVTA EGRDKNAVNA EFVKKFNKFI RKSKNGSFKT ELVSRSAMPR YQYTNGRRIQ TGWEERAEFK VEGRDFDELN RFIADIQADA ALEYTDFHVS RERRNEVIDQ VSKDAVLRFK ARAEKLAGVL GASGYKIVKL NLGHIGSHIA GGGAAQAKML RAMPMAASVN MEGADSAAPG VEEISISVNG TVQF // ID Q9JZJ4_NEIMB Unreviewed; 120 AA. AC Q9JZJ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41425.1}; GN OrderedLocusNames=NMB1025 {ECO:0000313|EMBL:AAF41425.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41425.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41425.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41425.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3KJJ, ECO:0000213|PDB:3KJK} RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS). RA Ren J., Sainsbury S., Owens R.J.; RT "Crystal structure of NMB1025, a member of YjgF protein family, from RT Neisseria meningitidis."; RL Submitted (NOV-2009) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41425.1; -; Genomic_DNA. DR PIR; H81129; H81129. DR RefSeq; NP_274059.1; NC_003112.2. DR RefSeq; WP_002222561.1; NC_003112.2. DR PDB; 3KJJ; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-120. DR PDB; 3KJK; X-ray; 2.29 A; A/B/C/D/E/F/G/H/I/J/K/L=1-120. DR PDBsum; 3KJJ; -. DR PDBsum; 3KJK; -. DR ProteinModelPortal; Q9JZJ4; -. DR STRING; 122586.NMB1025; -. DR PaxDb; Q9JZJ4; -. DR EnsemblBacteria; AAF41425; AAF41425; NMB1025. DR GeneID; 903163; -. DR KEGG; nme:NMB1025; -. DR PATRIC; 20357585; VBINeiMen85645_1309. DR eggNOG; ENOG4105M4H; Bacteria. DR eggNOG; COG0251; LUCA. DR HOGENOM; HOG000267214; -. DR OMA; KTRILMC; -. DR OrthoDB; EOG6QVRPF; -. DR BioCyc; NMEN122586:GHGG-1062-MONOMER; -. DR EvolutionaryTrace; Q9JZJ4; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.1330.40; -; 1. DR InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like. DR InterPro; IPR019897; RidA_CS. DR InterPro; IPR006175; YjgF/YER057c/UK114. DR PANTHER; PTHR11803; PTHR11803; 1. DR Pfam; PF01042; Ribonuc_L-PSP; 1. DR SUPFAM; SSF55298; SSF55298; 1. DR PROSITE; PS01094; UPF0076; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3KJJ, ECO:0000213|PDB:3KJK}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 120 AA; 13147 MW; F532D2E88649092C CRC64; MDIRYFGTTP RYSEAVGANG LIFLSGMVPE NGETAAEQTA DVLAQIDRWL AECGSDKAHV LDAVIYLRDM GDYAEMNGVW DAWVAAGRTP ARACVEARLA RPEWRVEIKI TAVKRDAATA // ID Q9JXD5_NEIMB Unreviewed; 196 AA. AC Q9JXD5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42415.1}; GN OrderedLocusNames=NMB2098 {ECO:0000313|EMBL:AAF42415.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42415.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42415.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42415.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42415.1; -; Genomic_DNA. DR PIR; C81006; C81006. DR RefSeq; NP_275086.1; NC_003112.2. DR RefSeq; WP_002225722.1; NC_003112.2. DR ProteinModelPortal; Q9JXD5; -. DR STRING; 122586.NMB2098; -. DR PaxDb; Q9JXD5; -. DR EnsemblBacteria; AAF42415; AAF42415; NMB2098. DR GeneID; 903946; -. DR KEGG; nme:NMB2098; -. DR PATRIC; 20360366; VBINeiMen85645_2680. DR eggNOG; ENOG4108SGY; Bacteria. DR eggNOG; COG1670; LUCA. DR HOGENOM; HOG000078520; -. DR OMA; LWKLWYT; -. DR OrthoDB; EOG64FKJW; -. DR BioCyc; NMEN122586:GHGG-2163-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF13302; Acetyltransf_3; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 15 176 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 196 AA; 21876 MW; 6D29F28D73C16000 CRC64; MSEKIILPVL SLGGVRLEPL DVHHETGLRE AVCDGEVWKL GVTSAPHPDR VADYIGTALA TRLAFAVVDE EAGRVVGTTA YYHFEPQIPR LDIGFTWYAA SARRTRINTC CKIMLLDSAF DVLACRCVGW RTDILNLASQ RAIERLGAEK DGVLRMHMLR KDGSVRDTVV YSMLREDWCK NREILTGRLA GYGVQV // ID Q9JY40_NEIMB Unreviewed; 70 AA. AC Q9JY40; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42099.1}; GN OrderedLocusNames=NMB1758 {ECO:0000313|EMBL:AAF42099.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42099.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42099.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42099.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42099.1; -; Genomic_DNA. DR PIR; E81046; E81046. DR STRING; 122586.NMB1758; -. DR PaxDb; Q9JY40; -. DR EnsemblBacteria; AAF42099; AAF42099; NMB1758. DR HOGENOM; HOG000095290; -. DR OMA; FYIRLCF; -. DR OrthoDB; EOG6FZ4PB; -. DR BioCyc; NMEN122586:GHGG-1813-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 70 AA; 8113 MW; 3A317AA6DE5CBD6A CRC64; MRSRSVRLSQ MLSSPFVPIC FYIRLCFSNL LISIICKGKD NYFPVRNKPI LLNTLKPNTP INTILKHSLF // ID Q9JZ18_NEIMB Unreviewed; 186 AA. AC Q9JZ18; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=CreA protein {ECO:0000313|EMBL:AAF41710.1}; GN Name=creA {ECO:0000313|EMBL:AAF41710.1}; GN OrderedLocusNames=NMB1335 {ECO:0000313|EMBL:AAF41710.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41710.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41710.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41710.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41710.1; -; Genomic_DNA. DR PIR; G81093; G81093. DR RefSeq; NP_274354.1; NC_003112.2. DR RefSeq; WP_002222356.1; NC_003112.2. DR STRING; 122586.NMB1335; -. DR PaxDb; Q9JZ18; -. DR EnsemblBacteria; AAF41710; AAF41710; NMB1335. DR GeneID; 903757; -. DR KEGG; nme:NMB1335; -. DR PATRIC; 20358325; VBINeiMen85645_1674. DR eggNOG; ENOG4108RH0; Bacteria. DR eggNOG; COG3045; LUCA. DR HOGENOM; HOG000257967; -. DR KO; K05805; -. DR OMA; SPQNSVT; -. DR OrthoDB; EOG6MD95K; -. DR BioCyc; NMEN122586:GHGG-1373-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR010292; Uncharacterised_CreA. DR Pfam; PF05981; CreA; 1. DR PIRSF; PIRSF003174; CreA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 186 AA; 19989 MW; 87CE4960F6110844 CRC64; MNRLLLLSAA VLLTACGSGE TDKIGRASTV FNILGKNDRI EVEGFDDPDV QGVACYISYA KKGGLKEMVN LEEDASDASV SCVQTASSIS FDETAVRKPK EVFKHGASFA FKSRQIVRYY DPKRKTFAYL VYSDKIIQGS PKNSLSAVSC FGGGIPQTDG VQADTSGNLL AGACMISNPI ENLDKR // ID Q9JYB7_NEIMB Unreviewed; 394 AA. AC Q9JYB7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase {ECO:0000313|EMBL:AAF42007.1}; GN Name=coaBC {ECO:0000313|EMBL:AAF42007.1}; GN OrderedLocusNames=NMB1658 {ECO:0000313|EMBL:AAF42007.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42007.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42007.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42007.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42007.1; -; Genomic_DNA. DR PIR; A81058; A81058. DR RefSeq; NP_274663.1; NC_003112.2. DR RefSeq; WP_002222148.1; NC_003112.2. DR ProteinModelPortal; Q9JYB7; -. DR STRING; 122586.NMB1658; -. DR PaxDb; Q9JYB7; -. DR EnsemblBacteria; AAF42007; AAF42007; NMB1658. DR GeneID; 903453; -. DR KEGG; nme:NMB1658; -. DR PATRIC; 20359254; VBINeiMen85645_2135. DR eggNOG; ENOG4105CJS; Bacteria. DR eggNOG; COG0452; LUCA. DR HOGENOM; HOG000037525; -. DR KO; K13038; -. DR OMA; VRFIGNH; -. DR OrthoDB; EOG6FFSBB; -. DR BioCyc; NMEN122586:GHGG-1712-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:InterPro. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:InterPro. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:InterPro. DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 1. DR InterPro; IPR005252; CoaBC. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF42007.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 130 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 182 364 DFP. {ECO:0000259|Pfam:PF04127}. SQ SEQUENCE 394 AA; 42212 MW; B427D1901932AB91 CRC64; MGKHILLGVT GSIAAYKSCE LVRLLKKQGH SVTVVMSRSA TEFVSPLTFQ ALSGNPVLTD THGGNGSNGM EHINLTRNAD VFLIAPASMN TVAKICNGVA DNLLTSLAAA RKCPLAIAPA MNVEMWLNPA NQRNIAQLVS DGITVYMPGL GEQACGENGM GRMPEPAELL DLLPDLWTPK ILKGKKVLIT AGATFEAIDP VRGITNISSG KMGVALARAC RAAGAEVSLI HGQLQTALPF GISDTVQAVS AENMHRAVHR LIDKQDAFIS VAAVSDYRVK NRSTQKFKKD KNAKPLSIEL DENPDILASI ASLPNPPFCI GFAAETENVM TYAREKRIKK KLPMIVANDV SIAMGKPTNR ITIIGDDGEL SFPETSKDEA AMRIVERLAV YLSK // ID Q9K146_NEIMB Unreviewed; 92 AA. AC Q9K146; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40786.1}; GN OrderedLocusNames=NMB0343 {ECO:0000313|EMBL:AAF40786.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40786.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40786.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40786.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40786.1; -; Genomic_DNA. DR PIR; E81209; E81209. DR RefSeq; NP_273392.1; NC_003112.2. DR RefSeq; WP_010980782.1; NC_003112.2. DR ProteinModelPortal; Q9K146; -. DR SMR; Q9K146; 3-91. DR STRING; 122586.NMB0343; -. DR PaxDb; Q9K146; -. DR EnsemblBacteria; AAF40786; AAF40786; NMB0343. DR GeneID; 902458; -. DR KEGG; nme:NMB0343; -. DR PATRIC; 20355833; VBINeiMen85645_0435. DR eggNOG; ENOG4105K9H; Bacteria. DR eggNOG; COG2350; LUCA. DR HOGENOM; HOG000118146; -. DR KO; K09780; -. DR OMA; MWYMISS; -. DR OrthoDB; EOG6423NJ; -. DR BioCyc; NMEN122586:GHGG-364-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR005545; YCII. DR Pfam; PF03795; YCII; 1. DR SUPFAM; SSF54909; SSF54909; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 88 YCII. {ECO:0000259|Pfam:PF03795}. SQ SEQUENCE 92 AA; 10116 MW; 5EAA7A65B84584E3 CRC64; MLLATDGEDV HEARMAARPE HLKRLETLKS EGRLLTAGPN PLPEDSNRVS GSLIVAQFES LDAAQAWAED DPYVHAGVYS EVLIKPFKAV FK // ID Q9K032_NEIMB Unreviewed; 471 AA. AC Q9K032; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Transporter, NadC family {ECO:0000313|EMBL:AAF41205.1}; GN OrderedLocusNames=NMB0792 {ECO:0000313|EMBL:AAF41205.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41205.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41205.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41205.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41205.1; -; Genomic_DNA. DR PIR; G81156; G81156. DR RefSeq; NP_273834.1; NC_003112.2. DR RefSeq; WP_002223903.1; NC_003112.2. DR STRING; 122586.NMB0792; -. DR PaxDb; Q9K032; -. DR EnsemblBacteria; AAF41205; AAF41205; NMB0792. DR GeneID; 902907; -. DR KEGG; nme:NMB0792; -. DR PATRIC; 20356971; VBINeiMen85645_1004. DR eggNOG; ENOG4105C8P; Bacteria. DR eggNOG; COG0471; LUCA. DR HOGENOM; HOG000278433; -. DR KO; K14445; -. DR OMA; RTNFSIC; -. DR OrthoDB; EOG6GN72M; -. DR BioCyc; NMEN122586:GHGG-823-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR001898; Na/sul_symport. DR InterPro; IPR031312; Na/sul_symport_CS. DR Pfam; PF00939; Na_sulph_symp; 1. DR TIGRFAMs; TIGR00785; dass; 1. DR PROSITE; PS01271; NA_SULFATE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 209 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 381 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 387 404 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 411 430 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 450 470 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 471 AA; 50648 MW; 2DBC53ECCC51CE04 CRC64; MNLHAKDKTQ HPENVELLSA QKPITDFKGL LTTIISAVVC FGIYHILPYS PDANKGIALL IFVAALWFTE AVHITVTALM VPILAVVLGF PDMDIKKAMA DFSNPIIYIF FGGFALATAL HMQRLDRKIA VSLLRLSRGN MKVAVLMLFL VTAFLSMWIS NTATAAMMLP LAMGMLSHLD QEKEHKTYVF LLLGIAYCAS IGGLGTLVGS PPNLIAAKAL NLDFVGWMKL GLPMMLLILP LMLLSLYVIL KPNLNERVEI KAESIPWTLH RVIALLIFLA TAAAWIFSSK IKTAFGISNP DTVIALSAAV AVVVFGVAQW KEVARNTDWG VLMLFGGGIS LSTLLKTSGA SEALGQQVAA TFSGAPAFLV ILIVAAFIIF LTEFTSNTAS AALLVPIFSG IAMQMGLPEQ VLVFVIGIGA SCAFMLPVAT PPNAIVFGTG LIKQREMMNV GILLNILCVV LVALWAYAVL M // ID Q7DD69_NEIMB Unreviewed; 151 AA. AC Q7DD69; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxyl carrier protein {ECO:0000313|EMBL:AAF42194.1}; GN Name=accB {ECO:0000313|EMBL:AAF42194.1}; GN OrderedLocusNames=NMB1860 {ECO:0000313|EMBL:AAF42194.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42194.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42194.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42194.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42194.1; -; Genomic_DNA. DR PIR; E81033; E81033. DR RefSeq; NP_274856.1; NC_003112.2. DR RefSeq; WP_002214627.1; NC_003112.2. DR ProteinModelPortal; Q7DD69; -. DR SMR; Q7DD69; 79-150. DR STRING; 122586.NMB1860; -. DR PaxDb; Q7DD69; -. DR EnsemblBacteria; AAF42194; AAF42194; NMB1860. DR GeneID; 903238; -. DR KEGG; nme:NMB1860; -. DR PATRIC; 20359745; VBINeiMen85645_2378. DR eggNOG; ENOG4105KM4; Bacteria. DR eggNOG; COG0511; LUCA. DR HOGENOM; HOG000008875; -. DR KO; K02160; -. DR OMA; KMFNQIE; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; NMEN122586:GHGG-1916-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR InterPro; IPR001249; AcCoA_biotinCC. DR InterPro; IPR001882; Biotin_BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR PRINTS; PR01071; ACOABIOTINCC. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00531; BCCP; 1. DR PROSITE; PS00188; BIOTIN; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. PE 4: Predicted; KW Biotin {ECO:0000256|RuleBase:RU000428}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 69 151 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 151 AA; 15679 MW; CCF77115FABE9E72 CRC64; MDLRKLKKLI DLVEESGIAE IEVTEGEEKV RITRTIAAAP VYAAPVPAAA PAVTPAAAPV AASAPAAAPA ARDLSDAQKS PMVGTFYRAP GPNAAPFVEV GQQVKAGDTL CIIEAMKLMN EIEAEKSGTV KEILVENGTP VEFGEPLFII G // ID Q9JZ27_NEIMB Unreviewed; 720 AA. AC Q9JZ27; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 119. DE SubName: Full=Cation transport ATPase, E1-E2 family {ECO:0000313|EMBL:AAF41700.1}; GN OrderedLocusNames=NMB1325 {ECO:0000313|EMBL:AAF41700.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41700.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41700.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41700.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IB subfamily. CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Contains 1 HMA domain. CC {ECO:0000256|RuleBase:RU362081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41700.1; -; Genomic_DNA. DR PIR; D81097; D81097. DR RefSeq; NP_274344.1; NC_003112.2. DR RefSeq; WP_002222365.1; NC_003112.2. DR ProteinModelPortal; Q9JZ27; -. DR STRING; 122586.NMB1325; -. DR PaxDb; Q9JZ27; -. DR EnsemblBacteria; AAF41700; AAF41700; NMB1325. DR GeneID; 903747; -. DR KEGG; nme:NMB1325; -. DR PATRIC; 20358301; VBINeiMen85645_1662. DR eggNOG; ENOG4105C59; Bacteria. DR eggNOG; COG2217; LUCA. DR HOGENOM; HOG000250397; -. DR KO; K17686; -. DR OMA; TLPKFSD; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NMEN122586:GHGG-1363-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR Gene3D; 2.70.150.10; -; 1. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR InterPro; IPR027256; P-typ_ATPase_IB. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|RuleBase:RU362081}; KW Membrane {ECO:0000256|RuleBase:RU362081}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362081}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 89 108 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 114 136 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 148 170 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 182 200 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 334 356 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 362 387 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 671 688 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 694 712 Helical. {ECO:0000256|RuleBase:RU362081}. FT DOMAIN 4 70 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 720 AA; 76329 MW; 2F51048108B4FC73 CRC64; MQQKIRFQIE GMTCQACASR IEKVLNKKDF VESAGVNFAS EEAQVVFDDS KTSVADIAKI IEKTGYGAKE KTEDTLPQPE AEHHIGWRLW LLFTINVPFL IGMAGMMIGR HDWMIPPLWQ FALASVVQLW LAIPFYKSAW ASIKGGLANM DVLVTIGTVS IYLYSVYMLF FSPHAAYGMA HVYFEVGVMV IGFVSLGKFL EHRTKKSSLN SLGLLLKLTP TQVNVQRNGE WKQLPIDQVQ IGDLIRANHG ERIAADGIIE SGSGWADESH LTGESNPEEK KAGGKVLAGA LMTEGSVVYR ATQLGSQTQL GDMMNALSEA QGSKAPIARV ADKAAAVFVP AVVGIALLTF IVTWLIKGDW TVALMHAVAV LVIACPCALG LATPAAIMVG MGKAVKHGIW FKDAAAMEEA AHVDAVVLDK TGTLTEGSPQ VAAVYCVPDS GFDEDALYRI AAAVEQNAAH PLARAIVSAA QARGLDIPAA QNAQTVVGAG ITAEVEGVGL VKAGKAEFAE LALPKFLDGV WDIASIVAVS VDNKPIGAFA LADALKADTA EAIGRLKKHN IDVYIMSGDN QGTVEYVAKQ LGIAHAFGNM SPRDKAAEVQ KLKAAGKTVA MVGDGINDAP ALAAANVSFA MKGGADVAEH TASATLMQHS VNQLADALLV SQATLKNIKQ NLFFAFFYNI LGIPLAALGF LNPVIAGAAM AASSVSVLSN ALRLKRVKID // ID Q4W587_NEIMB Unreviewed; 198 AA. AC Q4W587; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 44. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52144.1}; GN OrderedLocusNames=NMB0024 {ECO:0000313|EMBL:AAY52144.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52144.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52144.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52144.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52144.1; -; Genomic_DNA. DR RefSeq; WP_002221783.1; NC_003112.2. DR RefSeq; YP_338289.1; NC_003112.2. DR ProteinModelPortal; Q4W587; -. DR SMR; Q4W587; 5-104. DR STRING; 122586.NMB0024; -. DR PaxDb; Q4W587; -. DR EnsemblBacteria; AAY52144; AAY52144; NMB0024. DR GeneID; 902127; -. DR KEGG; nme:NMB0024; -. DR PATRIC; 20354995; VBINeiMen85645_0034. DR eggNOG; COG4969; LUCA. DR HOGENOM; HOG000218691; -. DR OMA; DAASAIC; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-25-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 198 AA; 22343 MW; A8C30B13A0E66B61 CRC64; MTGFNDAAGV ASSSDIKGKY VEKVEVKNGV VTATMLSSGV NKEIKGKKLS LWAKRQNGSV KWFCGQPVTR NDTATATATD VAAANGKTDD KINTKHLPST CRDDSSTGCI ETPRADFKHF QKISRYRVLP ESRQMAEKLR HSRKSGNLVR WFQLFRINFE TLIPSFPRKW ESRTQNLKKP FYPISFRTDR PGFPPARE // ID Q9JXY3_NEIMB Unreviewed; 84 AA. AC Q9JXY3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42172.1}; GN OrderedLocusNames=NMB1837 {ECO:0000313|EMBL:AAF42172.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42172.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42172.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42172.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42172.1; -; Genomic_DNA. DR PIR; C81037; C81037. DR RefSeq; NP_274834.1; NC_003112.2. DR RefSeq; WP_010980996.1; NC_003112.2. DR STRING; 122586.NMB1837; -. DR PaxDb; Q9JXY3; -. DR EnsemblBacteria; AAF42172; AAF42172; NMB1837. DR GeneID; 903262; -. DR KEGG; nme:NMB1837; -. DR PATRIC; 20359679; VBINeiMen85645_2345. DR OMA; PICPPRF; -. DR OrthoDB; EOG68Q0VK; -. DR BioCyc; NMEN122586:GHGG-1892-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 84 AA; 9552 MW; BB8146360F7635C6 CRC64; MIFGVSRTAG MQPHQNKLPP AFPICPPRFL QNKPPAPPLR EAVRHSEYPD PRYEMTFQTA FAPPRFEYSG LTLNQDKATK PQTV // ID Q9K196_NEIMB Unreviewed; 262 AA. AC Q9K196; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40725.1}; GN OrderedLocusNames=NMB0271 {ECO:0000313|EMBL:AAF40725.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40725.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40725.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40725.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40725.1; -; Genomic_DNA. DR PIR; H81218; H81218. DR RefSeq; NP_273327.1; NC_003112.2. DR RefSeq; WP_002224840.1; NC_003112.2. DR ProteinModelPortal; Q9K196; -. DR STRING; 122586.NMB0271; -. DR PaxDb; Q9K196; -. DR EnsemblBacteria; AAF40725; AAF40725; NMB0271. DR GeneID; 902382; -. DR KEGG; nme:NMB0271; -. DR PATRIC; 20355626; VBINeiMen85645_0337. DR eggNOG; COG0500; LUCA. DR HOGENOM; HOG000219127; -. DR KO; K02169; -. DR OMA; NAPGHIL; -. DR OrthoDB; EOG63VBXF; -. DR BioCyc; NMEN122586:GHGG-286-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 262 AA; 29400 MW; 8BF816998F075536 CRC64; MNHQDARWQV HRHLAEHTDQ RLTLVRNAPK HILLAGADAD ISRSLLAKRY PQAVFEEYDS RADFLAAAAA ARKGGFWQRF TGKGVVQHCQ SPIAPLPEAC ADMLWSNLGL LAAEQILPVL HNWARALKTD GLLFFTCFGR DTLAELKCRL KENGIESRSA LFPDMHDLGD MLAENGFYDP VTDTAKLVLD YKKAETFWAD MDTLGVWRAM AWNDENAARS CVGTIFEREG GLGITLETVY GHAVKKLMLP QGENVVQFFP KR // ID Q9K0E2_NEIMB Unreviewed; 428 AA. AC Q9K0E2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Cell division protein ZipA {ECO:0000256|RuleBase:RU003612}; GN OrderedLocusNames=NMB0667 {ECO:0000313|EMBL:AAF41085.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41085.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41085.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41085.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ CC protofilaments by cross-linking them and that serves as a CC cytoplasmic membrane anchor for the Z ring. Also required for the CC recruitment to the septal ring of downstream cell division CC proteins. {ECO:0000256|RuleBase:RU003612}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU003613}; Single-pass type I membrane CC protein {ECO:0000256|RuleBase:RU003613}. CC -!- SIMILARITY: Belongs to the ZipA family. CC {ECO:0000256|RuleBase:RU003612}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41085.1; -; Genomic_DNA. DR PIR; G81172; G81172. DR RefSeq; NP_273709.1; NC_003112.2. DR RefSeq; WP_002247799.1; NC_003112.2. DR ProteinModelPortal; Q9K0E2; -. DR STRING; 122586.NMB0667; -. DR PaxDb; Q9K0E2; -. DR EnsemblBacteria; AAF41085; AAF41085; NMB0667. DR GeneID; 902778; -. DR KEGG; nme:NMB0667; -. DR PATRIC; 20356635; VBINeiMen85645_0836. DR HOGENOM; HOG000218832; -. DR OMA; MIAMIYI; -. DR OrthoDB; EOG63JR6H; -. DR BioCyc; NMEN122586:GHGG-694-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR Gene3D; 3.30.1400.10; -; 1. DR InterPro; IPR007449; ZipA_FtsZ-bd_C. DR Pfam; PF04354; ZipA_C; 1. DR ProDom; PD035754; ZipA_Fts_Z_bd_C; 1. DR SMART; SM00771; ZipA_C; 1. DR SUPFAM; SSF64383; SSF64383; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|RuleBase:RU003612}; KW Cell division {ECO:0000256|RuleBase:RU003612}; KW Cell inner membrane {ECO:0000256|RuleBase:RU003613}; KW Cell membrane {ECO:0000256|RuleBase:RU003613}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU003613}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Septation {ECO:0000256|RuleBase:RU003612}; KW Transmembrane {ECO:0000256|RuleBase:RU003613}. FT DOMAIN 279 404 ZipA_C. {ECO:0000259|SMART:SM00771}. SQ SEQUENCE 428 AA; 47009 MW; DFCAC4A26982A195 CRC64; MIYIVLFLAV VLAVVAYNMY QENQYRKKVR DQFGHSDKDA LLNSKTSHVR DGKPSGGSVM MPKPQPAVKK TAKPQDPAMR NLQEQDAVYI AKQKQAKASP FKTEIETALE ESGIIGNSAH TVSEPQTGHS APKPADAPAK PAPVPQTPAK PLITLKELSK VELPWFDVRF DFISYIALTE AKELHALPRL SNRCRYQIVG CTMDDHFQIA EPIPGIRYQA FIVGIQAVSR NGLASQEELS AFNRQVDAFA QSMGGQTLHT DLAAFIEVAS ALDAFCARVD QTIAIHLVSP TSISGVELRS AVTGVGFVLE DDGAFHYTDT SGSTMFSICS LNNEPFTNAL LDNQSYKGFS MLLDIPHSPA GEKTFDDLFM DLAVRLSGQL NLNLVNDKME EVSTQWLKDV RTYVLARQSE MLKVGIEPGG KTALRLFS // ID Q9JYB0_NEIMB Unreviewed; 82 AA. AC Q9JYB0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Antitoxin {ECO:0000256|RuleBase:RU362080}; GN OrderedLocusNames=NMB1666 {ECO:0000313|EMBL:AAF42015.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42015.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42015.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42015.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC {ECO:0000256|RuleBase:RU362080}. CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. CC {ECO:0000256|RuleBase:RU362080}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42015.1; -; Genomic_DNA. DR PIR; D81056; D81056. DR RefSeq; NP_274671.1; NC_003112.2. DR RefSeq; WP_002212658.1; NC_003112.2. DR ProteinModelPortal; Q9JYB0; -. DR STRING; 122586.NMB1666; -. DR PaxDb; Q9JYB0; -. DR EnsemblBacteria; AAF42015; AAF42015; NMB1666. DR GeneID; 903444; -. DR KEGG; nme:NMB1666; -. DR PATRIC; 20359272; VBINeiMen85645_2144. DR eggNOG; ENOG4105W17; Bacteria. DR eggNOG; ENOG410XV7S; LUCA. DR HOGENOM; HOG000211899; -. DR OMA; TYNIHEA; -. DR OrthoDB; EOG6FRD41; -. DR BioCyc; NMEN122586:GHGG-1720-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.1620.10; -; 1. DR InterPro; IPR006442; Antitoxin_Phd/YefM. DR Pfam; PF02604; PhdYeFM_antitox; 1. DR TIGRFAMs; TIGR01552; phd_fam; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 82 AA; 9094 MW; 88C34A9358ED6E5C CRC64; MFQANIHQAK TNLSQLIQRA EAGEIVIIAK AGKPCVQLIG IEKPARNAGR LKKFSHMENT DISRILEDDN ETAALFFEES AL // ID Q9JYZ0_NEIMB Unreviewed; 157 AA. AC Q9JYZ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41739.1}; GN OrderedLocusNames=NMB1365 {ECO:0000313|EMBL:AAF41739.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41739.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41739.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41739.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41739.1; -; Genomic_DNA. DR PIR; B81090; B81090. DR RefSeq; NP_274383.1; NC_003112.2. DR RefSeq; WP_002225143.1; NC_003112.2. DR ProteinModelPortal; Q9JYZ0; -. DR STRING; 122586.NMB1365; -. DR PaxDb; Q9JYZ0; -. DR EnsemblBacteria; AAF41739; AAF41739; NMB1365. DR GeneID; 903787; -. DR KEGG; nme:NMB1365; -. DR PATRIC; 20358393; VBINeiMen85645_1708. DR eggNOG; ENOG4105FJH; Bacteria. DR eggNOG; COG2846; LUCA. DR HOGENOM; HOG000286324; -. DR KO; K07322; -. DR OMA; ACGTWTA; -. DR OrthoDB; EOG68DD4M; -. DR BioCyc; NMEN122586:GHGG-1403-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF01814; Hemerythrin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 16 153 Hemerythrin. {ECO:0000259|Pfam:PF01814}. SQ SEQUENCE 157 AA; 18023 MW; 5EE112C267E42CF9 CRC64; MTDFSVWETA PFGATVDHIL QRYHNVHRAQ FEELVPLAQK VAQVHADTFP AEIAELLAYM QNELLMHMMK EERMLFPMIN QGVGRGAAMP IGVMMHEHEE HDRAIARLKE LTDNFQPPEG ACGSWTRLYA LAKEMVEDLN DHIHLENDIL FARVLDS // ID Q9K057_NEIMB Unreviewed; 301 AA. AC Q9K057; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41177.1}; GN OrderedLocusNames=NMB0764 {ECO:0000313|EMBL:AAF41177.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41177.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41177.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41177.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41177.1; -; Genomic_DNA. DR PIR; A81162; A81162. DR RefSeq; NP_273806.1; NC_003112.2. DR RefSeq; WP_010980841.1; NC_003112.2. DR STRING; 122586.NMB0764; -. DR PaxDb; Q9K057; -. DR EnsemblBacteria; AAF41177; AAF41177; NMB0764. DR GeneID; 902879; -. DR KEGG; nme:NMB0764; -. DR PATRIC; 20356899; VBINeiMen85645_0968. DR eggNOG; ENOG4107XS3; Bacteria. DR eggNOG; COG0697; LUCA. DR HOGENOM; HOG000218860; -. DR OMA; KTHEIEP; -. DR OrthoDB; EOG6SJJQC; -. DR BioCyc; NMEN122586:GHGG-795-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 185 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 295 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 19 144 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 157 292 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 301 AA; 32079 MW; 7768A0920A8A010E CRC64; MGKGGDIVVG NGKKYAAPLL VLGCVVFGLG SLIVRSVPVG SYAIAFWRLL ISVFVFWFLA RFFRQKFPKN RKTVRYALTA GVFLAFDLAL WHESIHAVGP GISTLLNSLQ IFFLSAIGVF FFGERLSGLK KAGLISAVAG VAMIAGAEFG YNGNAVWGFA SGLVSGLMLA LSMVFVRKTH EIEPVALFPS MMILSLGGAV SLVVPALLMD GGALYPTTWK DAGLVLVYGV VMQCFAWAMV AYAIPLLSLS LTGLLLLSEP VAALFIDYFG LGKPIEGVQW AGVALTLSAI YLGSLKRQSS H // ID Q9JZD7_NEIMB Unreviewed; 140 AA. AC Q9JZD7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41492.1}; GN OrderedLocusNames=NMB1101 {ECO:0000313|EMBL:AAF41492.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41492.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41492.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41492.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41492.1; -; Genomic_DNA. DR PIR; B81121; B81121. DR RefSeq; NP_274132.1; NC_003112.2. DR RefSeq; WP_002225240.1; NC_003112.2. DR STRING; 122586.NMB1101; -. DR PaxDb; Q9JZD7; -. DR EnsemblBacteria; AAF41492; AAF41492; NMB1101. DR GeneID; 903523; -. DR KEGG; nme:NMB1101; -. DR PATRIC; 20357766; VBINeiMen85645_1399. DR eggNOG; ENOG4105Y5J; Bacteria. DR eggNOG; COG4387; LUCA. DR HOGENOM; HOG000013806; -. DR OMA; ARYHACT; -. DR OrthoDB; EOG6JTCCG; -. DR BioCyc; NMEN122586:GHGG-1137-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009752; Phage_Mu_Gp36. DR Pfam; PF07030; DUF1320; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15600 MW; 968FEA9E12F451B2 CRC64; MAYATVEDMV ARFGELEVLQ LTDRNNEGLI DREVAQTALV DATAEIDAYL GRFRRPFEDL PPILVRLCCD IARYRLTAAQ GVLITDEIRN RYKIDVLDLL RAMAKGEVQL GVDDSGEEVA AGEDGIVFVN GKNKVFGRDH // ID Q9K1N2_NEIMB Unreviewed; 135 AA. AC Q9K1N2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40523.1}; GN OrderedLocusNames=NMB0054 {ECO:0000313|EMBL:AAF40523.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40523.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40523.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40523.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40523.1; -; Genomic_DNA. DR PIR; D81243; D81243. DR RefSeq; NP_273119.1; NC_003112.2. DR RefSeq; WP_002243932.1; NC_003112.2. DR STRING; 122586.NMB0054; -. DR PaxDb; Q9K1N2; -. DR EnsemblBacteria; AAF40523; AAF40523; NMB0054. DR GeneID; 902156; -. DR KEGG; nme:NMB0054; -. DR PATRIC; 20355101; VBINeiMen85645_0088. DR HOGENOM; HOG000218680; -. DR OMA; FTVAGCQ; -. DR OrthoDB; EOG61ZTGT; -. DR BioCyc; NMEN122586:GHGG-55-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 135 AA; 15298 MW; 0780989AB7F4E7EF CRC64; MEIRAIKYTA MAALLAFTVA GCRLAGWYEC SSLTGWCKPR KPAAIDFWDI GGESPPSLGD YEIPLSDGNR SVRANEYESA QQSYFYRKIG KFEACGLDWR TRDGKPLIET FKQGGFDCLE KQGLRRNGLS ERVRW // ID Q9JYA4_NEIMB Unreviewed; 183 AA. AC Q9JYA4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=DNA-3-methyladenine glycosylase I {ECO:0000313|EMBL:AAF42022.1}; DE EC=3.2.2.20 {ECO:0000313|EMBL:AAF42022.1}; GN Name=tag {ECO:0000313|EMBL:AAF42022.1}; GN OrderedLocusNames=NMB1673 {ECO:0000313|EMBL:AAF42022.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42022.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42022.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42022.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42022.1; -; Genomic_DNA. DR PIR; C81057; C81057. DR RefSeq; NP_274678.1; NC_003112.2. DR RefSeq; WP_002220466.1; NC_003112.2. DR ProteinModelPortal; Q9JYA4; -. DR STRING; 122586.NMB1673; -. DR PaxDb; Q9JYA4; -. DR EnsemblBacteria; AAF42022; AAF42022; NMB1673. DR GeneID; 903437; -. DR KEGG; nme:NMB1673; -. DR PATRIC; 20359288; VBINeiMen85645_2152. DR eggNOG; ENOG4108R3E; Bacteria. DR eggNOG; COG2818; LUCA. DR HOGENOM; HOG000220753; -. DR KO; K01246; -. DR OMA; NEFLMST; -. DR OrthoDB; EOG661HDB; -. DR BioCyc; NMEN122586:GHGG-1727-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.340.30; -; 1. DR InterPro; IPR005019; Adenine_glyco. DR InterPro; IPR011257; DNA_glycosylase. DR Pfam; PF03352; Adenine_glyco; 1. DR SUPFAM; SSF48150; SSF48150; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosidase {ECO:0000313|EMBL:AAF42022.1}; KW Hydrolase {ECO:0000313|EMBL:AAF42022.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 183 AA; 21307 MW; DB481F2C83AF0DE8 CRC64; MNYCEFAASL PENTDNPNKH YHDTQYGFPI EDDNELFERL VLEINQAGLN WTLMLKKRQA FQTAFEGFDI DTVAAFDDTD RERLLADAGI VRNRLKIDAA IFNARQIQAL QQEYGSFKNW LDTHHPRSKD EWVKLFKKHF KFVGGEIVGE FLMSTGYLKG AHAESCPVYR ETLKYHPKWL DAI // ID Q9K086_NEIMB Unreviewed; 433 AA. AC Q9K086; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834}; DE EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834}; GN Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834, GN ECO:0000313|EMBL:AAF41145.1}; GN OrderedLocusNames=NMB0732 {ECO:0000313|EMBL:AAF41145.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41145.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41145.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41145.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S- CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only CC animotransferase known to utilize SAM as an amino donor. CC {ECO:0000256|HAMAP-Rule:MF_00834}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7- CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8- CC diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00834}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8- CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step CC 1/1. {ECO:0000256|HAMAP-Rule:MF_00834}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00834}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41145.1; -; Genomic_DNA. DR PIR; D81164; D81164. DR RefSeq; NP_273774.1; NC_003112.2. DR RefSeq; WP_002225455.1; NC_003112.2. DR ProteinModelPortal; Q9K086; -. DR SMR; Q9K086; 10-432. DR STRING; 122586.NMB0732; -. DR PaxDb; Q9K086; -. DR EnsemblBacteria; AAF41145; AAF41145; NMB0732. DR GeneID; 902845; -. DR KEGG; nme:NMB0732; -. DR PATRIC; 20356823; VBINeiMen85645_0932. DR eggNOG; ENOG4108JPX; Bacteria. DR eggNOG; COG0161; LUCA. DR HOGENOM; HOG000020209; -. DR KO; K00833; -. DR OMA; MAVQYQQ; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NMEN122586:GHGG-761-MONOMER; -. DR UniPathway; UPA00078; UER00160. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00834; BioA; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR005815; BioA. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00508; bioA; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834, KW ECO:0000313|EMBL:AAF41145.1}; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00834, KW ECO:0000313|EMBL:AAF41145.1}. FT REGION 118 119 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00834}. FT REGION 315 316 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00834}. FT BINDING 58 58 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00834}. FT BINDING 151 151 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00834}. FT BINDING 252 252 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00834}. FT BINDING 281 281 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00834}. FT BINDING 314 314 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00834}. FT BINDING 398 398 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00834}. FT SITE 23 23 Participates in the substrate recognition FT with KAPA and in a stacking interaction FT with the adenine ring of SAM. FT {ECO:0000256|HAMAP-Rule:MF_00834}. FT MOD_RES 281 281 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00834}. SQ SEQUENCE 433 AA; 47953 MW; 366EBDFD1DEB97AD CRC64; MPSEHQHISS LLDFDRTHLL HPYTSMTDPL PVYPVKRAEG VFIELADGTR LIDGMSSWWC AIHGYNHPVL NQAVETQMKQ MAHVMFGGLT HEPAVELGKL LVGILPQGLN RIFYADSGSI SVEVALKMAV QYQQARGLTA KQNIATVRRG YHGDTWNAMS VCDPETGMHH IFGSALPQRY FVDNPKSRFD DEWDGADLQP VRALFEVHHA DIAAFILEPV VQGAGGMYFY HPQYLRGLHD LCDEFDIMLI FDEIATGFGR TGKMFACEHA EVVPDIMCIG KGLSGGYMTL AAAITSQKVT ETISRGEAGV FMHGPTFMAN PLACAVACAS VKLLLSQDWQ ANIRRIESIL KGRLKAAWDI RGVKDVRVLG AIGVIELEKG VDMARFQADC VAQGIWVRPF GRLVYLMPPY IISDGVLTKL ADKTVQILKE HSK // ID Q9K1L3_NEIMB Unreviewed; 48 AA. AC Q9K1L3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40560.1}; GN OrderedLocusNames=NMB0100 {ECO:0000313|EMBL:AAF40560.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40560.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40560.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40560.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40560.1; -; Genomic_DNA. DR PIR; D81237; D81237. DR RefSeq; NP_273159.1; NC_003112.2. DR RefSeq; WP_002218537.1; NC_003112.2. DR PaxDb; Q9K1L3; -. DR EnsemblBacteria; AAF40560; AAF40560; NMB0100. DR GeneID; 902204; -. DR KEGG; nme:NMB0100; -. DR PATRIC; 20355207; VBINeiMen85645_0137. DR OrthoDB; EOG615VR2; -. DR BioCyc; NMEN122586:GHGG-106-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 48 AA; 5613 MW; 0F0938E731552886 CRC64; MKFVKSGRNP LKKMEKKLNI IKNIQEFMVK FVELALMAIS EKSYIVVP // ID Q9JXH3_NEIMB Unreviewed; 210 AA. AC Q9JXH3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Glyoxalase II family protein {ECO:0000313|EMBL:AAF42369.1}; GN OrderedLocusNames=NMB2049 {ECO:0000313|EMBL:AAF42369.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42369.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42369.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42369.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42369.1; -; Genomic_DNA. DR PIR; B81011; B81011. DR RefSeq; NP_275039.1; NC_003112.2. DR RefSeq; WP_002218182.1; NC_003112.2. DR ProteinModelPortal; Q9JXH3; -. DR STRING; 122586.NMB2049; -. DR PaxDb; Q9JXH3; -. DR EnsemblBacteria; AAF42369; AAF42369; NMB2049. DR GeneID; 904038; -. DR KEGG; nme:NMB2049; -. DR PATRIC; 20360252; VBINeiMen85645_2626. DR eggNOG; ENOG4105C5X; Bacteria. DR eggNOG; COG0491; LUCA. DR HOGENOM; HOG000058039; -. DR OMA; TPDRWLE; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NMEN122586:GHGG-2112-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 14 194 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 210 AA; 23474 MW; 29A87060A69AB04E CRC64; MTLRYEIFPV TPFRQNCTLI WDDESGEAVL TDVGGDVPFL LQALANRKLT LTAIWLTHGH LDHAGGVVEM LKTHKVPVLG PHPDDEFLLQ SLPQTTAQYG FPVSPAFAPN RWLEEGETLT VGRYAFQVLH IPGHTPGHIV FYCAEAELLI AGDVLFYETI GRTDFPRGNH ADLINNIRNK LFTLPETVQV VAGHGRMTSI GHEKRHNPFF // ID Q7DDD2_NEIMB Unreviewed; 96 AA. AC Q7DDD2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Putative ferredoxin {ECO:0000313|EMBL:AAF41663.1}; GN OrderedLocusNames=NMB1287 {ECO:0000313|EMBL:AAF41663.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41663.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41663.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41663.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000256|RuleBase:RU000392}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41663.1; -; Genomic_DNA. DR PIR; F81100; F81100. DR RefSeq; NP_274307.1; NC_003112.2. DR RefSeq; WP_002217077.1; NC_003112.2. DR ProteinModelPortal; Q7DDD2; -. DR STRING; 122586.NMB1287; -. DR PaxDb; Q7DDD2; -. DR EnsemblBacteria; AAF41663; AAF41663; NMB1287. DR GeneID; 903709; -. DR KEGG; nme:NMB1287; -. DR PATRIC; 20358201; VBINeiMen85645_1612. DR eggNOG; ENOG4105XPH; Bacteria. DR eggNOG; COG0633; LUCA. DR HOGENOM; HOG000217153; -. DR KO; K11107; -. DR OMA; YCGSCRC; -. DR OrthoDB; EOG6BPDNN; -. DR BioCyc; NMEN122586:GHGG-1325-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR Pfam; PF00111; Fer2; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU000392}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU000392}; KW Iron-sulfur {ECO:0000256|RuleBase:RU000392}; KW Metal-binding {ECO:0000256|RuleBase:RU000392}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 96 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. SQ SEQUENCE 96 AA; 10540 MW; C116FA6489DAEC6D CRC64; MARIGTNKGF FELLEGETLL EGLERTGHMV EYQCRSGYCG SCRVKILEGS VTYREPPLAF LGRDEILPCC CCVEGDVRLD CGLSGEDEGL SDSLLK // ID Q9JXM1_NEIMB Unreviewed; 56 AA. AC Q9JXM1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42305.1}; GN OrderedLocusNames=NMB1977 {ECO:0000313|EMBL:AAF42305.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42305.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42305.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42305.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42305.1; -; Genomic_DNA. DR PIR; B81020; B81020. DR RefSeq; NP_274970.1; NC_003112.2. DR RefSeq; WP_002225850.1; NC_003112.2. DR STRING; 122586.NMB1977; -. DR PaxDb; Q9JXM1; -. DR EnsemblBacteria; AAF42305; AAF42305; NMB1977. DR GeneID; 904162; -. DR KEGG; nme:NMB1977; -. DR PATRIC; 20360029; VBINeiMen85645_2519. DR HOGENOM; HOG000218735; -. DR OMA; ACGYKGG; -. DR OrthoDB; EOG6J752D; -. DR BioCyc; NMEN122586:GHGG-2034-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR032831; LPAM_2. DR Pfam; PF13627; LPAM_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 56 AA; 6036 MW; F614EA3CD765D6A0 CRC64; MKYGVFFAAA TALLLSACGY KGDLYLPKEG DKARFGVIQT GLQLQSKPQS APQTQK // ID Q9K0E1_NEIMB Unreviewed; 190 AA. AC Q9K0E1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=AmpD protein {ECO:0000313|EMBL:AAF41086.1}; GN Name=ampD {ECO:0000313|EMBL:AAF41086.1}; GN OrderedLocusNames=NMB0668 {ECO:0000313|EMBL:AAF41086.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41086.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41086.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41086.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41086.1; -; Genomic_DNA. DR PIR; H81172; H81172. DR RefSeq; NP_273710.1; NC_003112.2. DR RefSeq; WP_002225509.1; NC_003112.2. DR ProteinModelPortal; Q9K0E1; -. DR SMR; Q9K0E1; 8-180. DR STRING; 122586.NMB0668; -. DR PaxDb; Q9K0E1; -. DR EnsemblBacteria; AAF41086; AAF41086; NMB0668. DR GeneID; 902779; -. DR KEGG; nme:NMB0668; -. DR PATRIC; 20356637; VBINeiMen85645_0837. DR eggNOG; ENOG4108VBV; Bacteria. DR eggNOG; COG3023; LUCA. DR HOGENOM; HOG000255963; -. DR KO; K03806; -. DR OMA; RTRCNDF; -. DR OrthoDB; EOG60GRR5; -. DR BioCyc; NMEN122586:GHGG-695-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.40.80.10; -; 1. DR InterPro; IPR002502; Amidase_domain. DR Pfam; PF01510; Amidase_2; 1. DR SMART; SM00644; Ami_2; 1. DR SUPFAM; SSF55846; SSF55846; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 22 170 Ami_2. {ECO:0000259|SMART:SM00644}. SQ SEQUENCE 190 AA; 21468 MW; 9498637AB51FEA15 CRC64; MDNHAEAHWQ NGWLQSIRHT PSPNFSPRET GETVSLIVLH NISLPPFEYG TDAVEKLFAN RLDPDGHPFF SLIHTLRVSS HFLIKRDGET VQFVSCDNMA YHAGVSSFGG REKCNAFSIG IELEGCDFEP FAEAQYRSLE ALLDAICRHY PVTAVTGHQD IAPGRKTDPG HFFDWRRIRE KGFLVDRNAV // ID Q9JZ09_NEIMB Unreviewed; 594 AA. AC Q9JZ09; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 111. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN Name=lpdA2 {ECO:0000313|EMBL:AAF41719.1}; GN OrderedLocusNames=NMB1344 {ECO:0000313|EMBL:AAF41719.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41719.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41719.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41719.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:1GJX} RP STRUCTURE BY NMR OF 2-82. RX PubMed=11559360; DOI=10.1046/j.0014-2956.2001.02422.x; RA Tozawa K., Broadhurst R.W., Raine A.R., Fuller C., Alvarez A., RA Guillen G., Padron G., Perham R.N.; RT "Solution structure of the lipoyl domain of the chimeric dihydrolipoyl RT dehydrogenase P64K from Neisseria meningitidis."; RL Eur. J. Biochem. 268:4908-4917(2001). CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC {ECO:0000256|RuleBase:RU003692}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003692}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692}; CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000256|RuleBase:RU003692}. CC -!- SIMILARITY: Contains lipoyl-binding domain. CC {ECO:0000256|SAAS:SAAS00100665}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41719.1; -; Genomic_DNA. DR PIR; H81094; S42920. DR RefSeq; NP_274363.1; NC_003112.2. DR RefSeq; WP_002225155.1; NC_003112.2. DR PDB; 1GJX; NMR; -; A=2-82. DR PDBsum; 1GJX; -. DR ProteinModelPortal; Q9JZ09; -. DR SMR; Q9JZ09; 2-82, 112-593. DR STRING; 122586.NMB1344; -. DR PaxDb; Q9JZ09; -. DR EnsemblBacteria; AAF41719; AAF41719; NMB1344. DR GeneID; 903766; -. DR KEGG; nme:NMB1344; -. DR PATRIC; 20358339; VBINeiMen85645_1681. DR eggNOG; ENOG4107QN2; Bacteria. DR eggNOG; COG1249; LUCA. DR HOGENOM; HOG000276708; -. DR KO; K00382; -. DR OMA; YTSPEWA; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; NMEN122586:GHGG-1382-MONOMER; -. DR EvolutionaryTrace; Q9JZ09; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01350; lipoamide_DH; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1GJX}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW FAD {ECO:0000256|RuleBase:RU003692}; KW Flavoprotein {ECO:0000256|RuleBase:RU003692}; KW Lipoyl {ECO:0000256|SAAS:SAAS00065550}; KW NAD {ECO:0000256|RuleBase:RU003692}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003692, KW ECO:0000313|EMBL:AAF41719.1}; Pyruvate {ECO:0000313|EMBL:AAF41719.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 594 AA; 61829 MW; 4A9B69D3FA3B57BC CRC64; MALVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA EVAGVVKEVK VKVGDKISEG GLIVVVEAEG TAAAPKAEAA AAPAQEAPKA AAPAPQAAQF GGSADAEYDV VVLGGGPGGY SAAFAAADEG LKVAIVERYK TLGGVCLNVG CIPSKALLHN AAVIDEVRHL AANGIKYPEP ELDIDMLRAY KDGVVSRLTG GLAGMAKSRK VDVIQGDGQF LDPHHLEVSL TAGDAYEQAA PTGEKKIVAF KNCIIAAGSR VTKLPFIPED PRIIDSSGAL ALKEVPGKLL IIGGGIIGLE MGTVYSTLGS RLDVVEMMDG LMQGADRDLV KVWQKQNEYR FDNIMVNTKT VAVEPKEDGV YVTFEGANAP KEPQRYDAVL VAAGRAPNGK LISAEKAGVA VTDRGFIEVD KQMRTNVPHI YAIGDIVGQP MLAHKAVHEG HVAAENCAGH KAYFDARVIP GVAYTSPEVA WVGETELSAK ASGRKITKAN FPWAASGRAI ANGCDNGFTK LIFDAETGRI IGGGIVGPNG GDMIGEVCLA IEMGCDAADI GKTIHPHPTL GESIGMAAEV ALGTCTDLPP QKKK // ID Q9JYW1_NEIMB Unreviewed; 164 AA. AC Q9JYW1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41770.1}; GN OrderedLocusNames=NMB1408 {ECO:0000313|EMBL:AAF41770.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41770.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41770.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41770.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41770.1; -; Genomic_DNA. DR PIR; D81087; D81087. DR STRING; 122586.NMB1408; -. DR PaxDb; Q9JYW1; -. DR EnsemblBacteria; AAF41770; AAF41770; NMB1408. DR BioCyc; NMEN122586:GHGG-1446-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 158 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 164 AA; 19814 MW; E7A326E3AA175353 CRC64; MNDHIVQIIR RFGLGRIFFY SYSKSSIIIF SSYVVYYIIY NYQFNYLSLL IYLLPILCSI YMFIFFLGKT KDTLTTERRK KFFNSIFPLR ILMIIGSEKK RLGIGSFYLL NLLWIIWCLM IHREQVPLNN LTLLLSFIFS LFFLLCDFVL LLNVYVYFFK LREA // ID Q9JYJ9_NEIMB Unreviewed; 50 AA. AC Q9JYJ9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41904.1}; GN OrderedLocusNames=NMB1549 {ECO:0000313|EMBL:AAF41904.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41904.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41904.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41904.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41904.1; -; Genomic_DNA. DR PIR; B81070; B81070. DR STRING; 122586.NMB1549; -. DR PaxDb; Q9JYJ9; -. DR EnsemblBacteria; AAF41904; AAF41904; NMB1549. DR BioCyc; NMEN122586:GHGG-1590-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 50 AA; 5540 MW; 0715A1BA18DB21CD CRC64; MSQIAEKRGG IGDKREGGVP TAPPRRECGA KSFRLRNICL MRQPCLLRKG // ID Q9JYW9_NEIMB Unreviewed; 349 AA. AC Q9JYW9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=A/G-specific adenine glycosylase {ECO:0000313|EMBL:AAF41760.1}; DE EC=3.2.2.- {ECO:0000313|EMBL:AAF41760.1}; GN Name=mutY {ECO:0000313|EMBL:AAF41760.1}; GN OrderedLocusNames=NMB1396 {ECO:0000313|EMBL:AAF41760.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41760.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41760.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41760.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41760.1; -; Genomic_DNA. DR PIR; D81088; D81088. DR RefSeq; NP_274410.1; NC_003112.2. DR RefSeq; WP_010980930.1; NC_003112.2. DR ProteinModelPortal; Q9JYW9; -. DR STRING; 122586.NMB1396; -. DR PaxDb; Q9JYW9; -. DR EnsemblBacteria; AAF41760; AAF41760; NMB1396. DR GeneID; 903818; -. DR KEGG; nme:NMB1396; -. DR PATRIC; 20358479; VBINeiMen85645_1751. DR eggNOG; ENOG4105CEN; Bacteria. DR eggNOG; COG1194; LUCA. DR HOGENOM; HOG000028744; -. DR KO; K03575; -. DR OMA; EADWLWY; -. DR OrthoDB; EOG6RNQH0; -. DR BioCyc; NMEN122586:GHGG-1434-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR005760; A/G_AdeGlyc_MutY. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR029119; MutY_C. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF10576; EndIII_4Fe-2S; 1. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF14815; NUDIX_4; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR01084; mutY; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycosidase {ECO:0000313|EMBL:AAF41760.1}; KW Hydrolase {ECO:0000313|EMBL:AAF41760.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 42 195 ENDO3c. {ECO:0000259|SMART:SM00478}. SQ SEQUENCE 349 AA; 39588 MW; BE85F134692A1A49 CRC64; MILMNTPIPF SERLIRWQKQ HGRHHLPWQV KNPYCVWLSE IMLQQTQVAT VLDYYPRFLE KFPTVQTLAA APQDEVLSLW AGLGYYSRAR NLHKAAQQVV RQFGGTFPSE RKDLETLCGV GRSTAAAICA FSFNRRETIL DGNVKRVLCR VFARDGNPQD KKFENSLWTL AESLLPSENA DMPAYTQGLM DLGATVCKRT KPLCHQCPMA DICEAKKQNR TAELPRKKTA AEVPTLPLYW LIVRNRDGAI LLEKRPAKGI WGGLYCVPCF ESLNGLSDFA AKFSLTMADM DEQTALTHRL THRLLLITPF EAQMPSESPS DGIWIKPAHL KDYGLPKPLE IYLNGNRLE // ID Q9JY81_NEIMB Unreviewed; 121 AA. AC Q9JY81; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42047.1}; GN OrderedLocusNames=NMB1699 {ECO:0000313|EMBL:AAF42047.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42047.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42047.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42047.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42047.1; -; Genomic_DNA. DR PIR; E81052; E81052. DR RefSeq; NP_274703.2; NC_003112.2. DR STRING; 122586.NMB1699; -. DR PaxDb; Q9JY81; -. DR EnsemblBacteria; AAF42047; AAF42047; NMB1699. DR GeneID; 903404; -. DR KEGG; nme:NMB1699; -. DR PATRIC; 20359355; VBINeiMen85645_2184. DR HOGENOM; HOG000282181; -. DR OMA; REWLWQR; -. DR OrthoDB; EOG6J1DCW; -. DR BioCyc; NMEN122586:GHGG-1754-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014030; Ketoacyl_synth_N. DR Pfam; PF13723; Ketoacyl-synt_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 118 Ketoacyl_synth_N. FT {ECO:0000259|Pfam:PF13723}. SQ SEQUENCE 121 AA; 13195 MW; BBDCA07A3BF533EF CRC64; MSEQTALAVC ADGVETALAE AASLLEEGCG SVLVLAADDP LPEGYAVSAT RAPFAYALAM VLTKGTRYSL TLSASDDMPS EAGMLPEAYW SGLEWVRFLL NGSRECRRVY RNREWLWQRN G // ID Q9K1J8_NEIMB Unreviewed; 183 AA. AC Q9K1J8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40579.1}; GN OrderedLocusNames=NMB0120 {ECO:0000313|EMBL:AAF40579.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40579.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40579.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40579.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40579.1; -; Genomic_DNA. DR PIR; B81237; B81237. DR RefSeq; NP_273178.1; NC_003112.2. DR RefSeq; WP_002215355.1; NC_003112.2. DR STRING; 122586.NMB0120; -. DR PaxDb; Q9K1J8; -. DR EnsemblBacteria; AAF40579; AAF40579; NMB0120. DR GeneID; 902224; -. DR KEGG; nme:NMB0120; -. DR PATRIC; 20355253; VBINeiMen85645_0160. DR HOGENOM; HOG000218665; -. DR OMA; FLSLYPW; -. DR OrthoDB; EOG6FBWXF; -. DR BioCyc; NMEN122586:GHGG-126-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 126 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 183 AA; 21231 MW; 987A3AB9E5492932 CRC64; MEFLSLHPWW SFFIILTIIL SYIGFCAHLH IQNRAVFFYS YRDVTIIFLT PVILIALSYL IKNKEILSAC ILCITLIAFS WAWIITYRSN TKRFFLSLLI VWGKLLLSTI VWAILAISLG LAVITGNSKR KKYERRDRHA ERNEKAFIGA LLVGFELSRN LLNLCCLHKD FSTPSKNIEV NRS // ID Q9JXM6_NEIMB Unreviewed; 593 AA. AC Q9JXM6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Putative para-aminobenzoate synthetase component I/4-amino-4-deoxychorismate lyase {ECO:0000313|EMBL:AAF42299.1}; GN OrderedLocusNames=NMB1970 {ECO:0000313|EMBL:AAF42299.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42299.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42299.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42299.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42299.1; -; Genomic_DNA. DR PIR; A81021; A81021. DR RefSeq; NP_274964.1; NC_003112.2. DR RefSeq; WP_002225844.1; NC_003112.2. DR ProteinModelPortal; Q9JXM6; -. DR STRING; 122586.NMB1970; -. DR PaxDb; Q9JXM6; -. DR EnsemblBacteria; AAF42299; AAF42299; NMB1970. DR GeneID; 904171; -. DR KEGG; nme:NMB1970; -. DR PATRIC; 20360009; VBINeiMen85645_2509. DR eggNOG; ENOG4105CRQ; Bacteria. DR eggNOG; COG0115; LUCA. DR eggNOG; COG0147; LUCA. DR HOGENOM; HOG000025145; -. DR KO; K03342; -. DR OMA; YQVNLTM; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NMEN122586:GHGG-2027-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF01063; Aminotran_4; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. DR SUPFAM; SSF56752; SSF56752; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000313|EMBL:AAF42299.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 109 374 Chorismate_bind. FT {ECO:0000259|Pfam:PF00425}. SQ SEQUENCE 593 AA; 65503 MW; 9E4494B1974B0E4C CRC64; MPYFALFDDA VSGRAKRYQN HVESRFFRPE ELDALDGALQ SGWQKGLHSV LFADYGFGLP LTGVESERGG NLALHWFANC ADIDAESWLA RHSDGLPAGI STPQPSVSET DYLDRIRQIH EAIRRGDTYQ INYTTRLHLQ AYGNPVSLYR RLRQPVPYAV LSHLPDAEGQ SAWTLCFSPE LFLKIGSDGT ISTEPMKGTA PILGDGQDER RAAELQADPK NRAENVMIVD LLRNDLGKIA QTGTVCVPEP FKVSRFGSVW QMTSTIQAQA LPHTSFADIL RAAFPCGSIT GAPKKMSMQI IESLEAEARG LYTGSIGYLN PCSGGLGFEG TFNVVIRTLS LTPLSDGIYQ GVYGVGSGIV IDSDPAAEYR ECGWKARFLN ELRPDFGIFE TLRAENGRCT LLDRHLCRLK TSAQALNLPL PDGCENQIKQ YIADLPDGAF RVKALLASDG ISLSRAVLNR LTDKQRVIIS PAVLPAQNYL RRFKTTCRAL FDQAWQTAET QGAFDSLFFN SDGILLEGGR SNVFIKHRGQ WLTPSLDLDI LNGIMRQAVL DEPQKYLQTN QVIETHITQK TLQEAEEIRL SNALRGVFAA ALA // ID Q9K0Z4_NEIMB Unreviewed; 214 AA. AC Q9K0Z4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488}; GN Name=dsbA-3 {ECO:0000313|EMBL:AAF40846.1}; GN OrderedLocusNames=NMB0407 {ECO:0000313|EMBL:AAF40846.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40846.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40846.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40846.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:2ZNM} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-214. RX PubMed=18715864; DOI=10.1074/jbc.M803990200; RA Vivian J.P., Scoullar J., Robertson A.L., Bottomley S.P., Horne J., RA Chin Y., Wielens J., Thompson P.E., Velkov T., Piek S., Byres E., RA Beddoe T., Wilce M.C., Kahler C.M., Rossjohn J., Scanlon M.J.; RT "Structural and biochemical characterization of the oxidoreductase RT NmDsbA3 from Neisseria meningitidis."; RL J. Biol. Chem. 283:32452-32461(2008). RN [3] {ECO:0000213|PDB:3DVX} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-214. RX PubMed=19631659; DOI=10.1016/j.jmb.2009.07.056; RA Lafaye C., Iwema T., Carpentier P., Jullian-Binard C., Kroll J.S., RA Collet J.F., Serre L.; RT "Biochemical and structural study of the homologues of the thiol- RT disulfide oxidoreductase DsbA in Neisseria meningitidis."; RL J. Mol. Biol. 392:952-966(2009). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}. CC -!- SIMILARITY: Belongs to the thioredoxin family. CC {ECO:0000256|PIRNR:PIRNR001488}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40846.1; -; Genomic_DNA. DR PIR; D81203; D81203. DR RefSeq; NP_273456.1; NC_003112.2. DR RefSeq; WP_002224916.1; NC_003112.2. DR PDB; 2ZNM; X-ray; 2.30 A; A/B/C/D=20-214. DR PDB; 3DVX; X-ray; 2.80 A; A/B=20-214. DR PDBsum; 2ZNM; -. DR PDBsum; 3DVX; -. DR ProteinModelPortal; Q9K0Z4; -. DR STRING; 122586.NMB0407; -. DR PaxDb; Q9K0Z4; -. DR EnsemblBacteria; AAF40846; AAF40846; NMB0407. DR GeneID; 902521; -. DR KEGG; nme:NMB0407; -. DR PATRIC; 20355997; VBINeiMen85645_0516. DR eggNOG; ENOG4108Z33; Bacteria. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000265318; -. DR KO; K03673; -. DR OMA; PHCYKFE; -. DR OrthoDB; EOG68Q0Q6; -. DR BioCyc; NMEN122586:GHGG-429-MONOMER; -. DR EvolutionaryTrace; Q9K0Z4; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR023205; DsbA/DsbL. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF13462; Thioredoxin_4; 1. DR PIRSF; PIRSF001488; Tdi_protein; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ZNM, ECO:0000213|PDB:3DVX}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488}; KW Periplasm {ECO:0000256|PIRNR:PIRNR001488}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 214 Thiol:disulfide interchange protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332306. FT DOMAIN 8 206 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 53 56 Redox-active. FT {ECO:0000256|PIRSR:PIRSR001488-1}. SQ SEQUENCE 214 AA; 23984 MW; 26065B4EA685120C CRC64; MKLKHLLPLL LSAVLSAQAY ALTEGEDYLV LDKPIPQEQS GKIEVLEFFG YFCVHCHHFD PLLLKLGKAL PSDAYLRTEH VVWQPEMLGL ARMAAAVNLS GLKYQANPAV FKAVYEQKIR LENRSVAGKW ALSQKGFDGK KLMRAYDSPE AAAAALKMQK LTEQYRIDST PTVIVGGKYR VIFNNGFDGG VHTIKELVAK VREERKRQTP AVQK // ID Q4W564_NEIMB Unreviewed; 105 AA. AC Q4W564; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 44. DE SubName: Full=Transposase, truncation {ECO:0000313|EMBL:AAY52147.1}; GN OrderedLocusNames=NMB1553 {ECO:0000313|EMBL:AAY52147.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52147.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52147.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52147.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52147.1; -; Genomic_DNA. DR STRING; 122586.NMB1553; -. DR PaxDb; Q4W564; -. DR EnsemblBacteria; AAY52147; AAY52147; NMB1553. DR PATRIC; 20358960; VBINeiMen85645_1999. DR HOGENOM; HOG000220750; -. DR OrthoDB; EOG6RZB5B; -. DR BioCyc; NMEN122586:GHGG-1594-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 51 102 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 105 AA; 12584 MW; 5B91EFD840F87C5C CRC64; MSTFFQQTAQ AMIAKHIDRF PLLKLDRVID WQLIEQYLNR QKTRYLRDHR GRPAYPLLSM FKAVLLGQWH SLSDPELEHS LITRIDFNLF CRFDELSIPD YSIVD // ID Q9K0S0_NEIMB Unreviewed; 260 AA. AC Q9K0S0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40941.1}; GN OrderedLocusNames=NMB0509 {ECO:0000313|EMBL:AAF40941.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40941.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40941.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40941.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40941.1; -; Genomic_DNA. DR PIR; D81191; D81191. DR RefSeq; NP_273555.1; NC_003112.2. DR RefSeq; WP_002225601.1; NC_003112.2. DR STRING; 122586.NMB0509; -. DR PaxDb; Q9K0S0; -. DR EnsemblBacteria; AAF40941; AAF40941; NMB0509. DR GeneID; 902625; -. DR KEGG; nme:NMB0509; -. DR PATRIC; 20356264; VBINeiMen85645_0652. DR OrthoDB; EOG6MH5G2; -. DR BioCyc; NMEN122586:GHGG-534-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 25 65 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 260 AA; 27665 MW; 2D493E7F56695BAC CRC64; MGEIVGEALV KNTDFSGMTA SEIEKAKANI TAYAKLVAGA TVGVTGGNVD VAANASETAV KNNALDIIWD IGNLVWDGGK WIYAKSIGDK QMAREAAIDF GVDAAAAAVP FVPAGATKIS RGGAYVLKAG DEAVDTAKAI QEIQKQTGIK LTYDKVNKVW TTPAGLDYGL DAKHGNRIKH VLAHTIPNPN KPVHSVFNVS RKEVLPLVDE AWRMKGNPLP NDSSVYLVDM KKPIGTKGET KVRIVVQKGT NKIISAYPQK // ID Q9K045_NEIMB Unreviewed; 246 AA. AC Q9K045; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Putative uroporphyrinogen-III synthase HemD {ECO:0000313|EMBL:AAF41190.1}; GN OrderedLocusNames=NMB0777 {ECO:0000313|EMBL:AAF41190.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41190.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41190.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41190.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41190.1; -; Genomic_DNA. DR PIR; F81160; F81160. DR RefSeq; NP_273819.1; NC_003112.2. DR RefSeq; WP_002229249.1; NC_003112.2. DR ProteinModelPortal; Q9K045; -. DR STRING; 122586.NMB0777; -. DR PaxDb; Q9K045; -. DR EnsemblBacteria; AAF41190; AAF41190; NMB0777. DR GeneID; 902892; -. DR KEGG; nme:NMB0777; -. DR PATRIC; 20356931; VBINeiMen85645_0984. DR eggNOG; ENOG4108B0N; Bacteria. DR eggNOG; COG1587; LUCA. DR HOGENOM; HOG000247992; -. DR KO; K01719; -. DR OMA; AKPFSEH; -. DR OrthoDB; EOG6RZB2F; -. DR BioCyc; NMEN122586:GHGG-808-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro. DR GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro. DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth. DR Pfam; PF02602; HEM4; 1. DR SUPFAM; SSF69618; SSF69618; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 17 226 HEM4. {ECO:0000259|Pfam:PF02602}. SQ SEQUENCE 246 AA; 27089 MW; BE8CAC8998523A3B CRC64; MLIVRPSGRA AEDVETCLNA GWRAEVLSPV EIEADAAGLE LLSEQYARAD AVFWVSPTAV ETAVPYLNLS DGIKAQIAVG QGSRRALERC LVRTVIAPDD GNDSEAVLRL PVWNSLPEGA RVLFVRGHGG RDFLMNALQE KGFRTEVAEV YFRRHKPLNF QNFQTENIAA AYITSTELVR LLFGQLPPQF SRFFKSLLYF THHPRIAEAL KREGVCSVET VPTLEAALSH SSISVSDGMV FPGTSN // ID Q9K1B8_NEIMB Unreviewed; 433 AA. AC Q9K1B8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=NADH dehydrogenase I, F subunit {ECO:0000313|EMBL:AAF40700.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AAF40700.1}; GN Name=nuoF {ECO:0000313|EMBL:AAF40700.1}; GN OrderedLocusNames=NMB0246 {ECO:0000313|EMBL:AAF40700.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40700.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40700.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40700.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40700.1; -; Genomic_DNA. DR PIR; D81222; D81222. DR RefSeq; NP_273302.1; NC_003112.2. DR RefSeq; WP_002224831.1; NC_003112.2. DR ProteinModelPortal; Q9K1B8; -. DR STRING; 122586.NMB0246; -. DR PaxDb; Q9K1B8; -. DR EnsemblBacteria; AAF40700; AAF40700; NMB0246. DR GeneID; 902357; -. DR KEGG; nme:NMB0246; -. DR PATRIC; 20355568; VBINeiMen85645_0308. DR eggNOG; ENOG4107QIZ; Bacteria. DR eggNOG; COG1894; LUCA. DR HOGENOM; HOG000251534; -. DR KO; K00335; -. DR OMA; LRWTEFY; -. DR OrthoDB; EOG6W9XGK; -. DR BioCyc; NMEN122586:GHGG-261-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR019575; Nuop51_4Fe4S-bd. DR InterPro; IPR019554; Soluble_ligand-bd. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR Pfam; PF10531; SLBB; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR TIGRFAMs; TIGR01959; nuoF_fam; 1. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00445598}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|SAAS:SAAS00445598}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00445598}; KW Metal-binding {ECO:0000256|SAAS:SAAS00445598}; KW Oxidoreductase {ECO:0000313|EMBL:AAF40700.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 333 378 NADH_4Fe-4S. {ECO:0000259|SMART:SM00928}. SQ SEQUENCE 433 AA; 47398 MW; 6704B33F1A96D4F3 CRC64; MAIYQSGVIF DQVDTANPDC WTLDEYVKRG GYTALRKILS ENISQTDVID EVKTSGLRGR GGAGFPTGLK WSFMPRSFPG EKYVVCNTDE GEPGTFKDRD IIMFNPHALI EGMIIAGYAM GAKAGYNYIH GEIFEGYQRF EAALEQARAA GFLGKNILGS DFEFELFAHH GYGAYICGEE TALLESLEGK KGQPRFKPPF PASFGLYGKP TTINNTETFS SVPFIIRDGG QAFADKGIPN AGGTKLFCIS GHVERPGNYE VPLGTPFAEV LKMAGGMRGG KKLKAVIPGG SSAPVLPADI MMQTNMDYDS ISKAGSMLGS GAIIVMDEDV CMVKALERLS YFYYDESCGQ CTPCREGTGW LYRIVHRIVE GKGKMEDLDL LDSVGNQMAG RTICALADAA VFPVRSFTKH FRDEFVHYIE HGGPMKEHKW GGW // ID Q9K1B2_NEIMB Unreviewed; 223 AA. AC Q9K1B2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=NADH dehydrogenase I, J subunit {ECO:0000313|EMBL:AAF40707.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AAF40707.1}; GN Name=nuoJ {ECO:0000313|EMBL:AAF40707.1}; GN OrderedLocusNames=NMB0253 {ECO:0000313|EMBL:AAF40707.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40707.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40707.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40707.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. CC {ECO:0000256|RuleBase:RU004429}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40707.1; -; Genomic_DNA. DR PIR; H81219; H81219. DR RefSeq; NP_273309.1; NC_003112.2. DR RefSeq; WP_002221912.1; NC_003112.2. DR STRING; 122586.NMB0253; -. DR PaxDb; Q9K1B2; -. DR EnsemblBacteria; AAF40707; AAF40707; NMB0253. DR GeneID; 902364; -. DR KEGG; nme:NMB0253; -. DR PATRIC; 20355584; VBINeiMen85645_0316. DR eggNOG; COG0839; LUCA. DR HOGENOM; HOG000262592; -. DR KO; K00339; -. DR OMA; DYVFYFQ; -. DR OrthoDB; EOG6Q2SPV; -. DR BioCyc; NMEN122586:GHGG-268-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6. DR Pfam; PF00499; Oxidored_q3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004429, KW ECO:0000313|EMBL:AAF40707.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 166 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 223 AA; 24703 MW; CA700E97F905240E CRC64; MTFQLILFYI FAVIILYGAL KTVTAKNPVH AALHLVLTFC VSAMLWMLMQ AEFLGVTLVV VYVGAVMVLF LFVVMMLNID IEEMRAGFWR HAPVAGVVGT LLAVALILIL VNPKTDLAAF GLMKDIPADY NNIRDLGSRI YTDYLLPFEL AAVLLLLGMV AAIALVHRKT VNPKRMDPAD QVKVRADQGR MRLVKMEAVK PQVESAEESE VSDDLKPKEE GKA // ID Q4W578_NEIMB Unreviewed; 161 AA. AC Q4W578; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=DNA helicase, truncation {ECO:0000313|EMBL:AAY52158.1}; GN OrderedLocusNames=NMB0494 {ECO:0000313|EMBL:AAY52158.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52158.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52158.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52158.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52158.1; -; Genomic_DNA. DR ProteinModelPortal; Q4W578; -. DR STRING; 122586.NMB0494; -. DR PaxDb; Q4W578; -. DR EnsemblBacteria; AAY52158; AAY52158; NMB0494. DR PATRIC; 20356238; VBINeiMen85645_0639. DR eggNOG; ENOG4106XWY; Bacteria. DR eggNOG; COG0305; LUCA. DR OMA; EGASRKW; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; NMEN122586:GHGG-519-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 1.10.860.10; -; 1. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR Pfam; PF00772; DnaB; 1. DR SUPFAM; SSF48024; SSF48024; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAY52158.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000313|EMBL:AAY52158.1}; KW Hydrolase {ECO:0000313|EMBL:AAY52158.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAY52158.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 20 121 DnaB. {ECO:0000259|Pfam:PF00772}. SQ SEQUENCE 161 AA; 17841 MW; 166DA46D3F4CCE51 CRC64; MNDYTAMPSE DGGIGSLSLP PHSMEAEQSV LGGLMLENPA WDRIADVVSG EDFYRHEHRL IFRSIAKLIN ESRPADVITV QEDLQRNEEL EAAGGFEYLI TLAQNTPSAA NIRRHAEIVR ERSIMRQLAE VGTEIARSAI PKISAAERAV AWSTKNSSSF F // ID Q9K1B1_NEIMB Unreviewed; 113 AA. AC Q9K1B1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40710.1}; GN OrderedLocusNames=NMB0256 {ECO:0000313|EMBL:AAF40710.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40710.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40710.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40710.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40710.1; -; Genomic_DNA. DR PIR; C81220; C81220. DR RefSeq; NP_273312.1; NC_003112.2. DR RefSeq; WP_002215633.1; NC_003112.2. DR STRING; 122586.NMB0256; -. DR PaxDb; Q9K1B1; -. DR EnsemblBacteria; AAF40710; AAF40710; NMB0256. DR GeneID; 902367; -. DR KEGG; nme:NMB0256; -. DR PATRIC; 20355590; VBINeiMen85645_0319. DR eggNOG; ENOG4106AP7; Bacteria. DR eggNOG; ENOG410Y0Y1; LUCA. DR HOGENOM; HOG000218639; -. DR OrthoDB; EOG6D5G4N; -. DR BioCyc; NMEN122586:GHGG-271-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 113 AA; 12984 MW; DC7916661510CD5C CRC64; MMDKNQLEQE FHKAMLNIYQ EALNLPQPYK ATRFLQIVNE FGGKEAADKL LSTGEKKTQT GFTELILSGG GVHALKYSME YLVLQKPWCD LFTEEQLAVA RKRLERVGFV FPK // ID Q9JZ99_NEIMB Unreviewed; 171 AA. AC Q9JZ99; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41606.1}; GN OrderedLocusNames=NMB1225 {ECO:0000313|EMBL:AAF41606.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41606.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41606.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41606.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41606.1; -; Genomic_DNA. DR PIR; B81108; B81108. DR RefSeq; NP_274249.1; NC_003112.2. DR RefSeq; WP_002225204.1; NC_003112.2. DR STRING; 122586.NMB1225; -. DR PaxDb; Q9JZ99; -. DR EnsemblBacteria; AAF41606; AAF41606; NMB1225. DR GeneID; 903647; -. DR KEGG; nme:NMB1225; -. DR PATRIC; 20358039; VBINeiMen85645_1532. DR HOGENOM; HOG000218959; -. DR OMA; AATIYKY; -. DR OrthoDB; EOG6GN722; -. DR BioCyc; NMEN122586:GHGG-1262-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 171 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327855. SQ SEQUENCE 171 AA; 18665 MW; 2E60EE1890D877BC CRC64; MKSKLLLILI NFSLISSPLG ANAAKIYTCT INGETVYTTK PSKSCHSTDL PPIGNYSSER YIPPQTPEPV SSPSNGGQVV KYKAPVKTVS KPAKSNTPPP QQAPSNNSRR SILETELSNE RKALVEAQKM LSQARLAKGG NINHQEINAL QSNVLDRQQN IQALQRELGR M // ID Q9JZY6_NEIMB Unreviewed; 344 AA. AC Q9JZY6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=LPS biosynthesis protein-related protein {ECO:0000313|EMBL:AAF41257.1}; GN OrderedLocusNames=NMB0846 {ECO:0000313|EMBL:AAF41257.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41257.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41257.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41257.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41257.1; -; Genomic_DNA. DR PIR; C81152; C81152. DR ProteinModelPortal; Q9JZY6; -. DR STRING; 122586.NMB0846; -. DR PaxDb; Q9JZY6; -. DR DNASU; 902960; -. DR EnsemblBacteria; AAF41257; AAF41257; NMB0846. DR PATRIC; 20357081; VBINeiMen85645_1059. DR eggNOG; ENOG4107Y2W; Bacteria. DR eggNOG; COG0438; LUCA. DR OrthoDB; EOG6C8MTC; -. DR BioCyc; NMEN122586:GHGG-877-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 132 283 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 344 AA; 38969 MW; 6A6F54B12CC3B796 CRC64; MARHVFLPPL SVHRHRPHPL GVCGFESFQT LHPRKRAARP DSRPLYELCR HTCLQDFPKI RHPLCRHGTQ QHHYARFGAP APMAAYEKCG GTRRRTSRRQ PPFRTRPATQ IRLRMAVPPP TYWAEYSTDR LNKEKKNNKP HFVFCTVSHL RRLKGHDVLL TAFARALAQC PQLRLNIGGS GQEEQRLKQQ AADLGITHAV TFLGALQPEA VLDLMRNSDA FVLASRTETF GVVYIEALSQ GLPVIATRCG GAESIVSDGN GYLVPVDDDD ALADALIKMC EHHSDFEPAR LRENCLNEFG ENAVIGRLIG IFRQAIAEYG KKIPVKYSGL TKIRTRRRSR RQYK // ID Q7DDQ6_NEIMB Unreviewed; 161 AA. AC Q7DDQ6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 64. DE RecName: Full=Phosphatidylglycerophosphatase A {ECO:0000256|PIRNR:PIRNR006162}; DE EC=3.1.3.27 {ECO:0000256|PIRNR:PIRNR006162}; DE AltName: Full=Phosphatidylglycerolphosphate phosphatase A {ECO:0000256|PIRNR:PIRNR006162}; GN Name=pgpA {ECO:0000313|EMBL:AAF40826.1}; GN OrderedLocusNames=NMB0386 {ECO:0000313|EMBL:AAF40826.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40826.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40826.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40826.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Lipid phosphatase which dephosphorylates CC phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). CC {ECO:0000256|PIRNR:PIRNR006162}. CC -!- CATALYTIC ACTIVITY: Phosphatidylglycerophosphate + H(2)O = CC phosphatidylglycerol + phosphate. {ECO:0000256|PIRNR:PIRNR006162}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR006162}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol CC biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step CC 2/2. {ECO:0000256|PIRNR:PIRNR006162}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|PIRNR:PIRNR006162}; Multi-pass membrane protein CC {ECO:0000256|PIRNR:PIRNR006162}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40826.1; -; Genomic_DNA. DR PIR; G81205; G81205. DR RefSeq; NP_273435.1; NC_003112.2. DR RefSeq; WP_002212457.1; NC_003112.2. DR ProteinModelPortal; Q7DDQ6; -. DR STRING; 122586.NMB0386; -. DR PaxDb; Q7DDQ6; -. DR EnsemblBacteria; AAF40826; AAF40826; NMB0386. DR GeneID; 902501; -. DR KEGG; nme:NMB0386; -. DR PATRIC; 20355935; VBINeiMen85645_0485. DR eggNOG; ENOG4107Z24; Bacteria. DR eggNOG; COG1267; LUCA. DR HOGENOM; HOG000256113; -. DR KO; K01095; -. DR OMA; VWDEIAG; -. DR OrthoDB; EOG6P5ZM2; -. DR BioCyc; NMEN122586:GHGG-408-MONOMER; -. DR UniPathway; UPA00084; UER00504. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR026037; PgpA. DR InterPro; IPR007686; YutG/PgpA. DR Pfam; PF04608; PgpA; 1. DR PIRSF; PIRSF006162; PgpA; 1. DR SUPFAM; SSF101307; SSF101307; 1. PE 4: Predicted; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR006162}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR006162}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006162, KW ECO:0000313|EMBL:AAF40826.1}; KW Lipid degradation {ECO:0000256|PIRNR:PIRNR006162}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR006162}; KW Magnesium {ECO:0000256|PIRNR:PIRNR006162}; KW Membrane {ECO:0000256|PIRNR:PIRNR006162, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006162}; KW Phospholipid degradation {ECO:0000256|PIRNR:PIRNR006162}; KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR006162}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 116 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 158 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 18 158 PgpA. {ECO:0000259|Pfam:PF04608}. SQ SEQUENCE 161 AA; 17792 MW; 440B8842CA43986C CRC64; MADFKPDFAW LLKRPLCFLA FGFGSGLAPF APGTFGTLAA LPLAFVLILL GIDGLLLAFL CIVLFMWGIR ICAYAERETG VSDHGGIVWD EIVAMLFVLA FVPFRWTWWL AAFVLFRLFD ALKPSPVGWF DKNLHGGLGI MADDMAAAVM TLIVLRIAML F // ID Q9K137_NEIMB Unreviewed; 178 AA. AC Q9K137; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40796.1}; GN OrderedLocusNames=NMB0353 {ECO:0000313|EMBL:AAF40796.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40796.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40796.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40796.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR006118-2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40796.1; -; Genomic_DNA. DR PIR; H81207; H81207. DR RefSeq; NP_273402.1; NC_003112.2. DR RefSeq; WP_002224883.1; NC_003112.2. DR ProteinModelPortal; Q9K137; -. DR STRING; 122586.NMB0353; -. DR PaxDb; Q9K137; -. DR EnsemblBacteria; AAF40796; AAF40796; NMB0353. DR GeneID; 902468; -. DR KEGG; nme:NMB0353; -. DR PATRIC; 20355855; VBINeiMen85645_0446. DR eggNOG; ENOG4108Z4R; Bacteria. DR eggNOG; COG1778; LUCA. DR HOGENOM; HOG000264740; -. DR KO; K03270; -. DR OMA; FDENFHE; -. DR OrthoDB; EOG62C9JR; -. DR BioCyc; NMEN122586:GHGG-374-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR010023; KDO_8-P_phosphatase. DR PIRSF; PIRSF006118; KDO8-P_Ptase; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01670; KdsC-phosphatas; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|PIRSR:PIRSR006118-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT METAL 21 21 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006118-2}. FT METAL 23 23 Magnesium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR006118-2}. FT METAL 114 114 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006118-2}. SQ SEQUENCE 178 AA; 19161 MW; 9454CC4498CC4F74 CRC64; MQAISPELQA RAAKIKLLIL DVDGVLTDGR IFIRDNGEEI KSFHTLDGHG LKMLQASGVQ TAIITGRDAP SVGIRVKQLG INYYFKGISD KRAAYEELRA QAGVEEAECA FVGDDVVDLP VMVRCGLPVA VPGAHWFTRQ HAAYITEHAG GAGAVREVCD LIMQAQGTLG AALNEYIK // ID Q9K1L9_NEIMB Unreviewed; 75 AA. AC Q9K1L9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40554.1}; GN OrderedLocusNames=NMB0092 {ECO:0000313|EMBL:AAF40554.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40554.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40554.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40554.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40554.1; -; Genomic_DNA. DR PIR; D81239; D81239. DR RefSeq; NP_273153.1; NC_003112.2. DR RefSeq; WP_010980752.1; NC_003112.2. DR STRING; 122586.NMB0092; -. DR PaxDb; Q9K1L9; -. DR EnsemblBacteria; AAF40554; AAF40554; NMB0092. DR GeneID; 902196; -. DR KEGG; nme:NMB0092; -. DR HOGENOM; HOG000220681; -. DR OMA; SCANSAN; -. DR OrthoDB; EOG6X1160; -. DR BioCyc; NMEN122586:GHGG-98-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 75 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327894. SQ SEQUENCE 75 AA; 8504 MW; B60F7F15CC8ACFB8 CRC64; MVRFFVLSFL TLINLCSLSA CNSHFTGNIN PLGTHNKVAN PNCANSANSH IRQPSRKNYD PTEYSAWLQY MHDCK // ID Q9JYG4_NEIMB Unreviewed; 143 AA. AC Q9JYG4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41950.1}; GN OrderedLocusNames=NMB1597 {ECO:0000313|EMBL:AAF41950.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41950.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41950.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41950.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41950.1; -; Genomic_DNA. DR PIR; H81063; H81063. DR RefSeq; NP_274603.1; NC_003112.2. DR RefSeq; WP_002244242.1; NC_003112.2. DR STRING; 122586.NMB1597; -. DR PaxDb; Q9JYG4; -. DR EnsemblBacteria; AAF41950; AAF41950; NMB1597. DR GeneID; 904278; -. DR KEGG; nme:NMB1597; -. DR eggNOG; ENOG4107DD1; Bacteria. DR eggNOG; ENOG410ZHAK; LUCA. DR BioCyc; NMEN122586:GHGG-1645-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 66 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 127 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 143 AA; 16613 MW; 87A8B03E55476190 CRC64; MSISLIGLHI TIAIILFFTT NFMGKKSSIF GYYQLSFSEE NHSPAFNIFY RAFTPILFIV IFSWVVTSLE IPISLEKINY VVIYYFIIRL LSVFVFEKTH IVNWFNQLTI PILSITLSFI VYNKMILPKS FLLPSSQEVA TTF // ID Q9JZ72_NEIMB Unreviewed; 90 AA. AC Q9JZ72; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41641.1}; GN OrderedLocusNames=NMB1264 {ECO:0000313|EMBL:AAF41641.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41641.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41641.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41641.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41641.1; -; Genomic_DNA. DR PIR; B81102; B81102. DR RefSeq; NP_274285.1; NC_003112.2. DR RefSeq; WP_002222403.1; NC_003112.2. DR STRING; 122586.NMB1264; -. DR PaxDb; Q9JZ72; -. DR EnsemblBacteria; AAF41641; AAF41641; NMB1264. DR GeneID; 903686; -. DR KEGG; nme:NMB1264; -. DR PATRIC; 20358143; VBINeiMen85645_1583. DR eggNOG; COG2361; LUCA. DR OMA; ADARTCD; -. DR OrthoDB; EOG6VF35Z; -. DR BioCyc; NMEN122586:GHGG-1302-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 90 AA; 10394 MW; E8C7B77BD078225A CRC64; MKMQKELSVY LKQILQAAQY IRLYTDKMDY GQFSADTKTV QAVVFNLFLI GENATHILKS YPEFAEETKY LNWIGMRGYC AIGLPMATLK // ID Q9JXC5_NEIMB Unreviewed; 42 AA. AC Q9JXC5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42433.1}; GN OrderedLocusNames=NMB2124 {ECO:0000313|EMBL:AAF42433.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42433.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42433.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42433.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42433.1; -; Genomic_DNA. DR PIR; D81005; D81005. DR RefSeq; NP_275110.1; NC_003112.2. DR RefSeq; WP_010981028.1; NC_003112.2. DR STRING; 122586.NMB2124; -. DR PaxDb; Q9JXC5; -. DR EnsemblBacteria; AAF42433; AAF42433; NMB2124. DR GeneID; 903427; -. DR KEGG; nme:NMB2124; -. DR PATRIC; 20360422; VBINeiMen85645_2707. DR OrthoDB; EOG6VHZJ4; -. DR BioCyc; NMEN122586:GHGG-2189-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 42 AA; 4890 MW; 11BA7AAC47053502 CRC64; MPQTWGEAIQ FRIKKQIENE LAPPNWSTQF PNGSIYDPKV TK // ID Q9JY70_NEIMB Unreviewed; 259 AA. AC Q9JY70; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AAF42058.1}; GN OrderedLocusNames=NMB1711 {ECO:0000313|EMBL:AAF42058.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42058.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42058.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42058.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH gntR-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00452141}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42058.1; -; Genomic_DNA. DR PIR; A81051; A81051. DR RefSeq; NP_274714.1; NC_003112.2. DR RefSeq; WP_002212609.1; NC_003112.2. DR ProteinModelPortal; Q9JY70; -. DR STRING; 122586.NMB1711; -. DR PaxDb; Q9JY70; -. DR EnsemblBacteria; AAF42058; AAF42058; NMB1711. DR GeneID; 903391; -. DR KEGG; nme:NMB1711; -. DR PATRIC; 20359381; VBINeiMen85645_2196. DR eggNOG; ENOG4108QBF; Bacteria. DR eggNOG; COG2186; LUCA. DR HOGENOM; HOG000273991; -. DR KO; K05799; -. DR OMA; RLCFEAT; -. DR OrthoDB; EOG6M9DVM; -. DR BioCyc; NMEN122586:GHGG-1766-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.20.120.530; -; 1. DR InterPro; IPR011711; GntR_C. DR InterPro; IPR008920; TF_FadR/GntR_C. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07729; FCD; 1. DR Pfam; PF00392; GntR; 1. DR PRINTS; PR00035; HTHGNTR. DR SMART; SM00895; FCD; 1. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48008; SSF48008; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|SAAS:SAAS00452277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00452220}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00452220}. FT DOMAIN 7 75 HTH gntR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50949}. SQ SEQUENCE 259 AA; 29462 MW; 4099F1250E2158DE CRC64; MKLVRPQKIS DQVLSVLEER IAEGVYAEGG KIPPERVLAE EFGVSRPSVR SALNVLVARQ VLEARQGDGY YVSVKPQQDF LQSWQELLGK HSNWEQDVFD FSCHIEGCMA ALAAERRTDA DLKRIGFWLE KFEEACESGN LEHQSEADVS FHQTIADAAH NLLFSHLSGG LLKMLYRQTR SSLIYLNQEE DPRPKLMAQH RVLYEAISNR RPGEASEAAK AHLNYVASSI LKDREYQSRN RHADTLAQND LKRVQDWAV // ID Q9JXW9_NEIMB Unreviewed; 213 AA. AC Q9JXW9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42188.1}; GN OrderedLocusNames=NMB1854 {ECO:0000313|EMBL:AAF42188.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42188.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42188.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42188.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42188.1; -; Genomic_DNA. DR PIR; C81035; C81035. DR RefSeq; NP_274850.1; NC_003112.2. DR RefSeq; WP_002219822.1; NC_003112.2. DR STRING; 122586.NMB1854; -. DR PaxDb; Q9JXW9; -. DR EnsemblBacteria; AAF42188; AAF42188; NMB1854. DR GeneID; 903244; -. DR KEGG; nme:NMB1854; -. DR eggNOG; ENOG4105GEE; Bacteria. DR eggNOG; ENOG4111N3S; LUCA. DR HOGENOM; HOG000035158; -. DR OMA; NPNAIYC; -. DR OrthoDB; EOG6CP43V; -. DR BioCyc; NMEN122586:GHGG-1910-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 213 AA; 25131 MW; 3828F0711F2FDA0F CRC64; MSIPINFNNL KYLLNDMRNK NRIIEAFPFN YNQRQYAVIL TRYKPDEPRP DDYAQAKLEF FNLNSENSIF AYADFYEVHF KSATDFINFF KINVQAGAAK IREIFQSFSN LFADFIPTQT KKDLDIIYKK IVATRLEPNS PNTIYCYDVR RNGKDKAGKP NRRSVENSEK AKILRPELYE KFKADSNYSF FFSDNPSDEK TDAEIIREVT NRQ // ID Q9K0G7_NEIMB Unreviewed; 289 AA. AC Q9K0G7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|RuleBase:RU361259}; DE EC=2.7.7.9 {ECO:0000256|RuleBase:RU361259}; DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU361259}; GN Name=galU {ECO:0000313|EMBL:AAF41061.1}; GN OrderedLocusNames=NMB0638 {ECO:0000313|EMBL:AAF41061.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41061.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41061.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41061.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate = CC diphosphate + UDP-glucose. {ECO:0000256|RuleBase:RU361259}. CC -!- SIMILARITY: Belongs to the UDPGP type 2 family. CC {ECO:0000256|RuleBase:RU361259}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41061.1; -; Genomic_DNA. DR PIR; C81175; C81175. DR RefSeq; NP_273681.1; NC_003112.2. DR RefSeq; WP_002225519.1; NC_003112.2. DR ProteinModelPortal; Q9K0G7; -. DR STRING; 122586.NMB0638; -. DR PaxDb; Q9K0G7; -. DR EnsemblBacteria; AAF41061; AAF41061; NMB0638. DR GeneID; 902749; -. DR KEGG; nme:NMB0638; -. DR PATRIC; 20356575; VBINeiMen85645_0807. DR eggNOG; ENOG4105C3Y; Bacteria. DR eggNOG; COG1210; LUCA. DR HOGENOM; HOG000283477; -. DR KO; K00963; -. DR OMA; KGWLEAN; -. DR OrthoDB; EOG6Z9B3V; -. DR BioCyc; NMEN122586:GHGG-664-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01099; galU; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU361259, KW ECO:0000313|EMBL:AAF41061.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU361259, KW ECO:0000313|EMBL:AAF41061.1}. FT DOMAIN 11 265 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 289 AA; 32030 MW; D8D76E2C692781FF CRC64; MKPIRKAVFP VAGMGTRFLP ATKASPKEML PIVDKPLIQY AVEEAVEAGC TEMVFVTGRN KRSIEDHFDK AYELETELEM RHKDKLLEHV RNILPPNITC LYIRQAEALG LGHAVLCARA AIGDEPFAVI LADDLIDAPK GALKQMVEVY GRSGNSILGV ETVEASQTGS YGIVETEQLK QFQRITGIVE KPKPEDAPSN LAVVGRYILT PRIFDLLTNL PRGAGNEIQL TDGIAKLLDH EFVLAHPFEG TRYDCGSKLG YLEATVAYGL KHPETGEPFR RLLEKYRTE // ID Q9JZL0_NEIMB Unreviewed; 59 AA. AC Q9JZL0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41407.1}; GN OrderedLocusNames=NMB1006 {ECO:0000313|EMBL:AAF41407.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41407.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41407.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41407.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41407.1; -; Genomic_DNA. DR PIR; D81133; D81133. DR STRING; 122586.NMB1006; -. DR PaxDb; Q9JZL0; -. DR EnsemblBacteria; AAF41407; AAF41407; NMB1006. DR BioCyc; NMEN122586:GHGG-1043-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 59 AA; 7058 MW; 2466CB036C121EA9 CRC64; MNTLKAHARQ LMMDHIHPAT RKSLFTLKQA KTLLLHNRPD VYRAKRPKNK HIISHERHK // ID Q7DD90_NEIMB Unreviewed; 481 AA. AC Q7DD90; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Cytochrome c oxidase, subunit I {ECO:0000313|EMBL:AAF42070.1}; DE EC=1.9.3.1 {ECO:0000313|EMBL:AAF42070.1}; GN Name=fixN {ECO:0000313|EMBL:AAF42070.1}; GN OrderedLocusNames=NMB1725 {ECO:0000313|EMBL:AAF42070.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42070.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42070.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42070.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50}; CC Note=Binds 1 copper ion per subunit, denoted as copper B. CC {ECO:0000256|PIRSR:PIRSR604677-50}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50}; CC Note=Binds 2 heme groups per subunit, denoted as high- and low- CC spin. {ECO:0000256|PIRSR:PIRSR604677-50}; CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000370}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42070.1; -; Genomic_DNA. DR PIR; E81050; E81050. DR RefSeq; NP_274728.1; NC_003112.2. DR RefSeq; WP_002212595.1; NC_003112.2. DR ProteinModelPortal; Q7DD90; -. DR STRING; 122586.NMB1725; -. DR PaxDb; Q7DD90; -. DR EnsemblBacteria; AAF42070; AAF42070; NMB1725. DR GeneID; 903376; -. DR KEGG; nme:NMB1725; -. DR PATRIC; 20359413; VBINeiMen85645_2212. DR eggNOG; ENOG4105EUH; Bacteria. DR eggNOG; COG3278; LUCA. DR HOGENOM; HOG000277908; -. DR KO; K00404; -. DR OMA; NLNYIAG; -. DR OrthoDB; EOG6G7QZX; -. DR BioCyc; NMEN122586:GHGG-1780-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045278; C:plasma membrane respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR InterPro; IPR004677; Cyt_c_oxidase_cbb3_su1. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR SUPFAM; SSF81442; SSF81442; 1. DR TIGRFAMs; TIGR00780; ccoN; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|RuleBase:RU000370}; KW Heme {ECO:0000256|PIRSR:PIRSR604677-50, KW ECO:0000256|RuleBase:RU000370}; KW Iron {ECO:0000256|PIRSR:PIRSR604677-50, KW ECO:0000256|RuleBase:RU000370}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50, KW ECO:0000256|RuleBase:RU000370}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000370, KW ECO:0000313|EMBL:AAF42070.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Respiratory chain {ECO:0000256|RuleBase:RU000370}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000370}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 207 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 297 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 309 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 345 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 388 414 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 434 456 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 18 481 COX1. {ECO:0000259|PROSITE:PS50855}. FT METAL 63 63 Iron (low-spin heme axial ligand); via FT tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. FT METAL 210 210 Copper B; via pros nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. FT METAL 260 260 Copper B; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. FT METAL 261 261 Copper B; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. FT METAL 348 348 Iron (high-spin heme axial ligand); via FT tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. FT METAL 350 350 Iron (low-spin heme axial ligand); via FT tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR604677-50}. SQ SEQUENCE 481 AA; 53929 MW; 6888C1D6966BFA48 CRC64; METLMDTQTY NYKVVRQFAI MTVVWGIVGM LVGVIVAAQL FAPALDLSNI GPWFHFGRLR PLHTNAVIFA FGGCGLIGTS YYVVQRTCNT RLFGGWLPAF TFWGWQAVIV AAVVSFPMGW TQGKEYAELE WPIDILITLV WVAYAIVFFG TIAKRKIKHI YVANWFYGGF ILAVALLHIV NNISIPAGLM KSYPVYSGAI DAMVQWWYGH NAVGFFLTAG FLGMMYYFVP KQAARPVYSY RLSVVHFWAL IFTYMWAGPH HLHYTALPDW TQSLGMVLSL ILFAPSWGGM INGIMTLSGA WDKLRTDPIL KFLIVSLSFY GMSTFEGPMM SIKTVNALSH YTDWTVAHVH AGALGWVGFV TIGSVYYMIP RLFGKEQMHS TKLVEAHFWI ATIGVVLYIA AMWIAGVMQG LMWSSLNDDG TLTYSFVESV KRTMPYYVIR FAGGLLYLSG MCIMAYNVYR TAIGGKAVDA EIPAVSQTQH H // ID Q9JZH4_NEIMB Unreviewed; 636 AA. AC Q9JZH4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 102. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAF41449.1}; GN OrderedLocusNames=NMB1051 {ECO:0000313|EMBL:AAF41449.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41449.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41449.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41449.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41449.1; -; Genomic_DNA. DR PIR; C81128; C81128. DR RefSeq; NP_274085.1; NC_003112.2. DR RefSeq; WP_002222546.1; NC_003112.2. DR ProteinModelPortal; Q9JZH4; -. DR STRING; 122586.NMB1051; -. DR PaxDb; Q9JZH4; -. DR EnsemblBacteria; AAF41449; AAF41449; NMB1051. DR GeneID; 903188; -. DR KEGG; nme:NMB1051; -. DR PATRIC; 20357639; VBINeiMen85645_1336. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR HOGENOM; HOG000271635; -. DR KO; K15738; -. DR OMA; VTSSWWF; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NMEN122586:GHGG-1088-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032524; ABC_tran_C. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF16326; ABC_tran_CTD; 1. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41449.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF41449.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 253 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 320 538 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 636 AA; 71733 MW; BAC353D5A532E21B CRC64; MNILSVENAS FAIGHVALLD KTSFQLDSGE KVGLIGRNGA GKSSFLKILA GLQKLDDGQI IVQNNLKIVY VPQESFFDKD ATVFDTVAEG LGEIRDLLRR YHHVSHELEN GSSEALLKEL NELQLEIEAK DGWKLDAAVK QTLGELGLPE NEKIGNLSGG QKKRVALAQA WVQKPDVLLL DEPTNHLDID AIIWLENLLK AFEGSLVVIT HDRRFLDNIA TRIVELDRGI LRSYPGSFSK YSEKKAQELA VEAEHNRLFD KFHAQEEAWI RKGIEARRTR NEGRVRRLEE LRRQRAERRN VQGQVNFKLD SGEKSGKIIA ELEHASFAYG GKVIMDKFSA ILQRGDKIGL IGPNGIGKTT FLKLILGELQ PTYGRIRIGS KQEVAYFDQF RSALNENDTV FYTLGQGNDY VEVGGKKKHV MSYLEDFLFH PARAQSPVSS LSGGERNRLL LAKLFTRPAN ILVLDEPTND LDIDTQELLE DLLRDYQGTV FLVSHDRMFL DNVITQSIVF EGQGRLKEYI GGYQDYIDAK SREDKIQTAS APKASDAEPA KEKPKANRTV KLSYKEQREL DALPDEIAAL EAEQAEINTQ LSYPEIFKDY EKAGALQNRA EEIEMLLLEK LERWELLETK RNGNAV // ID Q7DDH9_NEIMB Unreviewed; 168 AA. AC Q7DDH9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41484.1}; GN OrderedLocusNames=NMB1092 {ECO:0000313|EMBL:AAF41484.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41484.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41484.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41484.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41484.1; -; Genomic_DNA. DR PIR; F81123; F81123. DR RefSeq; NP_274124.1; NC_003112.2. DR RefSeq; WP_002213715.1; NC_003112.2. DR STRING; 122586.NMB1092; -. DR PaxDb; Q7DDH9; -. DR EnsemblBacteria; AAF41484; AAF41484; NMB1092. DR GeneID; 903510; -. DR KEGG; nme:NMB1092; -. DR PATRIC; 20357747; VBINeiMen85645_1390. DR eggNOG; ENOG4105HG8; Bacteria. DR eggNOG; ENOG4111RKF; LUCA. DR HOGENOM; HOG000218915; -. DR OMA; DDWDKAR; -. DR OrthoDB; EOG6WDSJT; -. DR BioCyc; NMEN122586:GHGG-1128-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR014926; Phage_D3112_Orf24. DR Pfam; PF08822; DUF1804; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 168 AA; 18753 MW; 50F3D3D8B4463A4E CRC64; MAHPQEIREK LRRLYVSGEQ TLETAALMCE IPQTTARAWK RADKEKGDDW DKMRAAYTLA GGGIEDLSRA MLAGFMVQYN STMTMLQDSS TEDLPPSDRA KLLASLADAF TKTVSANARV MPETSKLATA LELIEFLMAF VQEKHPKHLP AFVEVLEPFG VEVEKKFG // ID Q9JZB3_NEIMB Unreviewed; 48 AA. AC Q9JZB3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41587.1}; GN OrderedLocusNames=NMB1205 {ECO:0000313|EMBL:AAF41587.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41587.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41587.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41587.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41587.1; -; Genomic_DNA. DR PIR; D81110; D81110. DR RefSeq; NP_274230.1; NC_003112.2. DR RefSeq; WP_010980906.1; NC_003112.2. DR STRING; 122586.NMB1205; -. DR PaxDb; Q9JZB3; -. DR EnsemblBacteria; AAF41587; AAF41587; NMB1205. DR GeneID; 903627; -. DR KEGG; nme:NMB1205; -. DR BioCyc; NMEN122586:GHGG-1242-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 48 AA; 5336 MW; 0359112DFCF5B659 CRC64; MKFRVLVCCF PICLDFISFL LMCVCLGVAA ATPFFWLLCE VKSVTANA // ID Q9K1Q6_NEIMB Unreviewed; 423 AA. AC Q9K1Q6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=3-deoxy-D-manno-octulosonic-acid transferase {ECO:0000313|EMBL:AAF40493.1}; GN Name=kdtA {ECO:0000313|EMBL:AAF40493.1}; GN OrderedLocusNames=NMB0014 {ECO:0000313|EMBL:AAF40493.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40493.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40493.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40493.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40493.1; -; Genomic_DNA. DR PIR; D81248; D81248. DR RefSeq; NP_273080.1; NC_003112.2. DR RefSeq; WP_002225758.1; NC_003112.2. DR ProteinModelPortal; Q9K1Q6; -. DR STRING; 122586.NMB0014; -. DR PaxDb; Q9K1Q6; -. DR EnsemblBacteria; AAF40493; AAF40493; NMB0014. DR GeneID; 902117; -. DR KEGG; nme:NMB0014; -. DR PATRIC; 20354959; VBINeiMen85645_0015. DR eggNOG; ENOG4105D8A; Bacteria. DR eggNOG; COG1519; LUCA. DR HOGENOM; HOG000257156; -. DR KO; K02527; -. DR OMA; KHGGHNP; -. DR OrthoDB; EOG6H7FNN; -. DR BioCyc; NMEN122586:GHGG-15-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR007507; Glycos_transf_N. DR Pfam; PF00534; Glycos_transf_1; 1. DR Pfam; PF04413; Glycos_transf_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF40493.1}. FT DOMAIN 36 208 Glycos_transf_N. FT {ECO:0000259|Pfam:PF04413}. FT DOMAIN 282 385 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 423 AA; 47272 MW; 8E7C198B4341CB0A CRC64; MFQWLYDVLW LLAPIWIRRY LDKRSGSAPA YRAHRDERFG KPYPNPVTGA VWIHAVSVGE TRAAQSLIRE LRRRFPDAPL LMTQMTPTGR ETAQVLFPDA QCRYLPYDKK TWVRQFLREH RPMFGILMET EIWPNLMREC RRAGVPLFLA NARLSEKSLN GYLKVRRLIR PAAASLTGCL AQTEADAARL AKLGAASVQV CGNTKYDIIP SEQMKTLAGQ FEKRIGGRPV AVCGSTRVYR GEDEAEKLLA AWQQYRGDAL LVVVPRHPEH FQTVFETAKR FGFKVQRRSD GLPVEPDTQV WIGDSMGELY AYYLCADVAF VGGSLVDSGC QNIIEPLSCG VPTIFGFSTY NFSEACRHAL ASGAAVQVES ADAWREAVEK TLSSEGGGMQ MQARVDGFIA QHRGAGARIA EAVREAVCGY RGR // ID Q4W567_NEIMB Unreviewed; 151 AA. AC Q4W567; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Putative transposase {ECO:0000313|EMBL:AAY52138.1}; GN OrderedLocusNames=NMB1386 {ECO:0000313|EMBL:AAY52138.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52138.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52138.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52138.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52138.1; -; Genomic_DNA. DR RefSeq; WP_002225138.1; NC_003112.2. DR RefSeq; YP_338293.1; NC_003112.2. DR STRING; 122586.NMB1386; -. DR PaxDb; Q4W567; -. DR EnsemblBacteria; AAY52138; AAY52138; NMB1386. DR GeneID; 903808; -. DR KEGG; nme:NMB1386; -. DR PATRIC; 20358451; VBINeiMen85645_1737. DR eggNOG; COG3039; LUCA. DR eggNOG; COG3335; LUCA. DR OMA; MWINKNQ; -. DR OrthoDB; EOG6KQ6GP; -. DR BioCyc; NMEN122586:GHGG-1424-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002622; Transposase_14. DR Pfam; PF01710; HTH_Tnp_IS630; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 49 149 HTH_Tnp_IS630. FT {ECO:0000259|Pfam:PF01710}. SQ SEQUENCE 151 AA; 17348 MW; 5A33C7A80CF32FD8 CRC64; MAYSADLRNK ALNYSGLNLN QDKATKPQTV QIVRQGEATP YWFKFNPLYY EQCKNISQTA ATFNLSRNTL YLWIRLKKQT GSLKHQVTGL NAVKSDRQKP AQYVGQHPDA YLHEIAKHFD CTAATICYAL KQMGITRKKR PPLTKNKTRP K // ID Q9JXC0_NEIMB Unreviewed; 80 AA. AC Q9JXC0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42438.1}; GN OrderedLocusNames=NMB2130 {ECO:0000313|EMBL:AAF42438.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42438.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42438.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42438.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42438.1; -; Genomic_DNA. DR PIR; C81003; C81003. DR RefSeq; NP_275115.1; NC_003112.2. DR RefSeq; WP_010981029.1; NC_003112.2. DR STRING; 122586.NMB2130; -. DR PaxDb; Q9JXC0; -. DR EnsemblBacteria; AAF42438; AAF42438; NMB2130. DR GeneID; 903377; -. DR KEGG; nme:NMB2130; -. DR PATRIC; 20360436; VBINeiMen85645_2714. DR eggNOG; ENOG41066K7; Bacteria. DR eggNOG; ENOG4112B9M; LUCA. DR HOGENOM; HOG000218699; -. DR OMA; RNPMKEY; -. DR OrthoDB; EOG60KN7Z; -. DR BioCyc; NMEN122586:GHGG-2195-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025234; DUF4177. DR Pfam; PF13783; DUF4177; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 80 AA; 9646 MW; 4DC11CF69CF0D5B6 CRC64; MIPYVKRNPM KEYKVIIYQE SLLSSLFFGA AKVNPIKFSE FLNKQTPEGW RVVTMEKDLR RMLLFFKREA YVVILERDRV // ID Q9JZ01_NEIMB Unreviewed; 217 AA. AC Q9JZ01; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=UPF0056 inner membrane protein {ECO:0000256|RuleBase:RU362048}; GN OrderedLocusNames=NMB1354 {ECO:0000313|EMBL:AAF41728.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41728.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41728.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41728.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU362048}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362048}. CC -!- SIMILARITY: Belongs to the UPF0056 (MarC) family. CC {ECO:0000256|RuleBase:RU362048}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41728.1; -; Genomic_DNA. DR PIR; E81093; E81093. DR RefSeq; NP_274372.1; NC_003112.2. DR RefSeq; WP_002222344.1; NC_003112.2. DR STRING; 122586.NMB1354; -. DR PaxDb; Q9JZ01; -. DR EnsemblBacteria; AAF41728; AAF41728; NMB1354. DR GeneID; 903776; -. DR KEGG; nme:NMB1354; -. DR PATRIC; 20358365; VBINeiMen85645_1694. DR eggNOG; ENOG4105EZI; Bacteria. DR eggNOG; COG2095; LUCA. DR HOGENOM; HOG000112971; -. DR OMA; AIILWTS; -. DR OrthoDB; EOG6KWZ3Q; -. DR BioCyc; NMEN122586:GHGG-1392-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002771; Multi_antbiot-R_MarC. DR Pfam; PF01914; MarC; 1. DR TIGRFAMs; TIGR00427; TIGR00427; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU362048}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362048}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 12 30 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 42 61 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 67 90 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 119 146 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 152 173 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 194 212 Helical. {ECO:0000256|RuleBase:RU362048}. SQ SEQUENCE 217 AA; 22060 MW; F52D4ABAA0AC54C5 CRC64; MGLGMEIGKL IVAFLVLINP FSALSLYLDL TNGHSTKERR KVARTAAVAV FAVIAVFALI GGTLLKVLGI SVGSFQVGGG ILVLLIAISM MNGNDNPAKQ NLGAQPETGQ ARPARNAGAI AVVPIAIPIT IGPGGISTVI IYASAAKTYG DIALIIAAGL VVSAICYAIL IVAGKVSRLL GATGLTILNR IMGMMLAAVS VEIIVSGLKT IFPQLAG // ID Q9JZ04_NEIMB Unreviewed; 113 AA. AC Q9JZ04; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41724.1}; GN OrderedLocusNames=NMB1350 {ECO:0000313|EMBL:AAF41724.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41724.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41724.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41724.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41724.1; -; Genomic_DNA. DR PIR; A81093; A81093. DR RefSeq; NP_274368.1; NC_003112.2. DR RefSeq; WP_002213243.1; NC_003112.2. DR STRING; 122586.NMB1350; -. DR PaxDb; Q9JZ04; -. DR EnsemblBacteria; AAF41724; AAF41724; NMB1350. DR GeneID; 903772; -. DR KEGG; nme:NMB1350; -. DR PATRIC; 20358357; VBINeiMen85645_1690. DR HOGENOM; HOG000218996; -. DR OrthoDB; EOG6SV5C3; -. DR BioCyc; NMEN122586:GHGG-1388-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 113 AA; 13125 MW; 30F9566290350B73 CRC64; MKNNVKNWTT KEVKQSLDKF NNILIKNTFL LQYLKKEFSA SSAYCLSMLP EEEDIYEILV NGNIIIDLEF NKHTNETVVI NVTDVDEYLK TLTNESGRVF FTLAKEIGKQ KNI // ID Q7DD95_NEIMB Unreviewed; 185 AA. AC Q7DD95; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41986.1}; GN OrderedLocusNames=NMB1637 {ECO:0000313|EMBL:AAF41986.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41986.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41986.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41986.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|PIRSR:PIRSR000232-1}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000232-1}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41986.1; -; Genomic_DNA. DR RefSeq; NP_274642.1; NC_003112.2. DR RefSeq; WP_002212693.1; NC_003112.2. DR ProteinModelPortal; Q7DD95; -. DR STRING; 122586.NMB1637; -. DR PaxDb; Q7DD95; -. DR EnsemblBacteria; AAF41986; AAF41986; NMB1637. DR GeneID; 903959; -. DR KEGG; nme:NMB1637; -. DR PATRIC; 20359192; VBINeiMen85645_2108. DR eggNOG; ENOG41069NU; Bacteria. DR eggNOG; COG0778; LUCA. DR HOGENOM; HOG000146733; -. DR OMA; QGIGAVW; -. DR OrthoDB; EOG69GZM0; -. DR BioCyc; NMEN122586:GHGG-1686-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR026021; YdjA-like. DR Pfam; PF00881; Nitroreductase; 1. DR PIRSF; PIRSF000232; YdjA; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000232-1}; KW FMN {ECO:0000256|PIRSR:PIRSR000232-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 164 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. FT NP_BIND 10 12 FMN. {ECO:0000256|PIRSR:PIRSR000232-1}. FT NP_BIND 134 136 FMN. {ECO:0000256|PIRSR:PIRSR000232-1}. FT BINDING 39 39 FMN; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000232-1}. SQ SEQUENCE 185 AA; 20550 MW; EFF3F0DBA4B141FD CRC64; MDALKLLTNR RSSKKLKHPA PDAAELEQIF QAATQVPDHG NMRPFRFTVI QGEVGLQRFR DVLKQTVAEL NFGDDAMKKA EKVGNMAPMV IGVTFAPNRD VPKPKPEWEQ MLTAGCAAYA LQLAATAQGF DNVWITGMWV NSPLLREAFG CADKDKIIGL MMVGTPTEEV HKPKNTDLEA FVSHW // ID Q7DDK1_NEIMB Unreviewed; 82 AA. AC Q7DDK1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41358.1}; GN OrderedLocusNames=NMB0952 {ECO:0000313|EMBL:AAF41358.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41358.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41358.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41358.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:1PUZ} RP STRUCTURE BY NMR. RX PubMed=15103637; DOI=10.1002/prot.20009; RA Liu G., Sukumaran D.K., Xu D., Chiang Y., Acton T., RA Goldsmith-Fischman S., Honig B., Montelione G.T., Szyperski T.; RT "NMR structure of the hypothetical protein NMA1147 from Neisseria RT meningitidis reveals a distinct 5-helix bundle."; RL Proteins 55:756-758(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41358.1; -; Genomic_DNA. DR PIR; H81138; H81138. DR RefSeq; NP_273990.1; NC_003112.2. DR RefSeq; WP_002213764.1; NC_003112.2. DR PDB; 1PUZ; NMR; -; A=1-82. DR PDBsum; 1PUZ; -. DR ProteinModelPortal; Q7DDK1; -. DR SMR; Q7DDK1; 1-82. DR STRING; 122586.NMB0952; -. DR PaxDb; Q7DDK1; -. DR EnsemblBacteria; AAF41358; AAF41358; NMB0952. DR GeneID; 903072; -. DR KEGG; nme:NMB0952; -. DR PATRIC; 20357387; VBINeiMen85645_1208. DR eggNOG; ENOG4107K9Q; Bacteria. DR eggNOG; COG2938; LUCA. DR HOGENOM; HOG000160701; -. DR KO; K09159; -. DR OMA; FTWIMGH; -. DR OrthoDB; EOG63FW79; -. DR BioCyc; NMEN122586:GHGG-989-MONOMER; -. DR EvolutionaryTrace; Q7DDK1; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 1.10.150.250; -; 1. DR InterPro; IPR005631; SDH. DR Pfam; PF03937; Sdh5; 1. DR SUPFAM; SSF109910; SSF109910; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1PUZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 82 AA; 9794 MW; 4AB818927658A950 CRC64; MMVFDDIAKR KIRFQTRRGL LELDLIFGRF MEKEFEHLSD KELSEFSEIL EFQDQELLAL INGHSETDKG HLIPMLEKIR RA // ID Q9K1B6_NEIMB Unreviewed; 79 AA. AC Q9K1B6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40702.1}; GN OrderedLocusNames=NMB0248 {ECO:0000313|EMBL:AAF40702.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40702.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40702.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40702.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40702.1; -; Genomic_DNA. DR PIR; C81219; C81219. DR RefSeq; NP_273304.1; NC_003112.2. DR RefSeq; WP_002221908.1; NC_003112.2. DR ProteinModelPortal; Q9K1B6; -. DR STRING; 122586.NMB0248; -. DR PaxDb; Q9K1B6; -. DR EnsemblBacteria; AAF40702; AAF40702; NMB0248. DR GeneID; 902359; -. DR KEGG; nme:NMB0248; -. DR PATRIC; 20355574; VBINeiMen85645_0311. DR eggNOG; ENOG41083TS; Bacteria. DR eggNOG; COG2827; LUCA. DR HOGENOM; HOG000285486; -. DR KO; K07461; -. DR OMA; TTINCME; -. DR OrthoDB; EOG62K215; -. DR BioCyc; NMEN122586:GHGG-263-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR000305; GIY-YIG_SF. DR Pfam; PF01541; GIY-YIG; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR PROSITE; PS50164; GIY_YIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 71 GIY-YIG. {ECO:0000259|PROSITE:PS50164}. SQ SEQUENCE 79 AA; 9554 MW; 0156D71C630F2F3B CRC64; MANGKNGTLY IGVTMNLPER VWQHKNHVNI DGFTARYDVH DLVWYQFFEN MPEAVAKEKT MKKWRREWKI KLIEEQNTE // ID Q9JXQ4_NEIMB Unreviewed; 115 AA. AC Q9JXQ4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42260.1}; GN OrderedLocusNames=NMB1931 {ECO:0000313|EMBL:AAF42260.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42260.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42260.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42260.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42260.1; -; Genomic_DNA. DR PIR; D81024; D81024. DR STRING; 122586.NMB1931; -. DR PaxDb; Q9JXQ4; -. DR EnsemblBacteria; AAF42260; AAF42260; NMB1931. DR eggNOG; COG3171; LUCA. DR HOGENOM; HOG000218749; -. DR OrthoDB; EOG6VHZFZ; -. DR BioCyc; NMEN122586:GHGG-1988-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR007416; DUF469. DR Pfam; PF04320; DUF469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 115 AA; 13479 MW; 6B892060CE0395A5 CRC64; MPVYFRTPSR KRLHKMNRRQ HKKLHLGEFQ TLIFGVQGSL HQAEDDAEAF DRFMDELIAY LAANGFEMAG GRLRRFFVPV SKIRCPKLGR NREKSHYLLA GRPRRCCHFV RHPAG // ID Q9K1R4_NEIMB Unreviewed; 160 AA. AC Q9K1R4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Thioredoxin-related protein {ECO:0000313|EMBL:AAF40485.1}; GN OrderedLocusNames=NMB0006 {ECO:0000313|EMBL:AAF40485.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40485.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40485.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40485.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] {ECO:0000213|PDB:3RAZ} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-160, AND DISULFIDE BONDS. RA Zhang Z., Burley S.K., Swaminathan S.; RT "The crystal structure of thioredoxin-related protein from Neisseria RT meningitidis serogroup B."; RL Submitted (MAR-2011) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40485.1; -; Genomic_DNA. DR PIR; D81247; D81247. DR RefSeq; NP_273072.1; NC_003112.2. DR RefSeq; WP_002225751.1; NC_003112.2. DR PDB; 3RAZ; X-ray; 2.00 A; A=21-160. DR PDBsum; 3RAZ; -. DR ProteinModelPortal; Q9K1R4; -. DR STRING; 122586.NMB0006; -. DR PaxDb; Q9K1R4; -. DR DNASU; 902108; -. DR EnsemblBacteria; AAF40485; AAF40485; NMB0006. DR GeneID; 902108; -. DR KEGG; nme:NMB0006; -. DR PATRIC; 20354939; VBINeiMen85645_0006. DR eggNOG; COG0526; LUCA. DR HOGENOM; HOG000218689; -. DR OMA; WKDGTAQ; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NMEN122586:GHGG-6-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3RAZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 160 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329391. FT DOMAIN 6 157 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 53 56 {ECO:0000213|PDB:3RAZ}. SQ SEQUENCE 160 AA; 17635 MW; 333A491CD9A049F4 CRC64; MKYLNLAAIT LAATFAAHTA SADELAGWKD NTPQSLQSLK APVRIVNLWA TWCGPCRKEM PAMSKWYKAQ KKGSVDMVGI ALDTSDNIGN FLKQTPVSYP IWRYTGANSR NFMKTYGNTV GVLPFTVVEA PKCGYRQTIT GEVNEKSLTD AVKLAHSKCR // ID Q7DD50_NEIMB Unreviewed; 193 AA. AC Q7DD50; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit {ECO:0000256|RuleBase:RU004494}; DE EC=1.10.2.2 {ECO:0000256|RuleBase:RU004494}; GN Name=petA {ECO:0000313|EMBL:AAF42373.1}; GN OrderedLocusNames=NMB2053 {ECO:0000313|EMBL:AAF42373.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42373.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42373.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42373.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. {ECO:0000256|RuleBase:RU004494}. CC -!- CATALYTIC ACTIVITY: Quinol + 2 ferricytochrome c = quinone + 2 CC ferrocytochrome c + 2 H(+). {ECO:0000256|RuleBase:RU004494}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|RuleBase:RU004494}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000256|RuleBase:RU004494}; CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein. CC {ECO:0000256|RuleBase:RU004497}. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S CC protein. {ECO:0000256|RuleBase:RU004494}. CC -!- SIMILARITY: Contains 1 Rieske domain. CC {ECO:0000256|RuleBase:RU004493}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42373.1; -; Genomic_DNA. DR PIR; F81011; F81011. DR RefSeq; NP_275043.1; NC_003112.2. DR RefSeq; WP_002215005.1; NC_003112.2. DR ProteinModelPortal; Q7DD50; -. DR STRING; 122586.NMB2053; -. DR PaxDb; Q7DD50; -. DR EnsemblBacteria; AAF42373; AAF42373; NMB2053. DR GeneID; 904028; -. DR KEGG; nme:NMB2053; -. DR PATRIC; 20360262; VBINeiMen85645_2631. DR eggNOG; ENOG4108R5F; Bacteria. DR eggNOG; COG0723; LUCA. DR HOGENOM; HOG000255194; -. DR KO; K00411; -. DR OMA; QPAYAQN; -. DR OrthoDB; EOG6RNQD9; -. DR BioCyc; NMEN122586:GHGG-2116-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC. DR Gene3D; 2.102.10.10; -; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR014349; Rieske_Fe-S_prot. DR InterPro; IPR005805; Rieske_Fe-S_prot_C. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR019470; Ubiq_cytC_Rdtase_Fe-S_su_TAT. DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su. DR PANTHER; PTHR10134; PTHR10134; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF10399; UCR_Fe-S_N; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; SSF50022; 1. DR TIGRFAMs; TIGR01416; Rieske_proteo; 1. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU004492}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Electron transport {ECO:0000256|RuleBase:RU004494}; KW Iron {ECO:0000256|RuleBase:RU004492}; KW Iron-sulfur {ECO:0000256|RuleBase:RU004492}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU004492}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004494, KW ECO:0000313|EMBL:AAF42373.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU004494}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 85 189 Rieske. {ECO:0000259|PROSITE:PS51296}. SQ SEQUENCE 193 AA; 20632 MW; 1A61E1171860EBDC CRC64; MDNQEINNGR RRFLTLATCG AGGVAALGVA TPFVASFFPS EKAKAAGAAV EVDVSKIEAG QLLTAEWQGK PIWVLNRTDQ QLKDLKGLNG ELTDPNSDAE QQPEYAKNET RSIKPNILVA IGICTHLGCS PTFRPDIAPA DLGADWKGGF FCPCHGSKFD LAGRVYKGVP APTNLVVPPY KYLSDTTILV GED // ID Q9JZU9_NEIMB Unreviewed; 79 AA. AC Q9JZU9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41300.1}; GN OrderedLocusNames=NMB0891 {ECO:0000313|EMBL:AAF41300.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41300.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41300.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41300.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41300.1; -; Genomic_DNA. DR PIR; A81146; A81146. DR PaxDb; Q9JZU9; -. DR EnsemblBacteria; AAF41300; AAF41300; NMB0891. DR PATRIC; 20357199; VBINeiMen85645_1113. DR HOGENOM; HOG000027842; -. DR OMA; PIRTETC; -. DR OrthoDB; EOG689J1R; -. DR BioCyc; NMEN122586:GHGG-927-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 79 AA; 9114 MW; B708CC6E6A81B763 CRC64; MTDFRLGSFI GKSRNRSAVI PTKVGIQFFE FQSFPINCLS IECLDSRLRG NDEPIRTETC TASFPRKWES SFLSFSHFQ // ID Q9JZ84_NEIMB Unreviewed; 111 AA. AC Q9JZ84; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41626.1}; GN OrderedLocusNames=NMB1245 {ECO:0000313|EMBL:AAF41626.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41626.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41626.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41626.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41626.1; -; Genomic_DNA. DR PIR; B81106; B81106. DR STRING; 122586.NMB1245; -. DR PaxDb; Q9JZ84; -. DR EnsemblBacteria; AAF41626; AAF41626; NMB1245. DR BioCyc; NMEN122586:GHGG-1282-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 111 AA; 12246 MW; 00DD2AB853509A28 CRC64; MEEPVLDFQF VHRKIHTGQI AAFDIIARLV PIKNIRGNDF DDRPAAAVFG MHNLQTRPVA RHFEGGADFT QLIVLTLGQP ESAYVAVRLK IVRGDISRGG VGKLTGKQSH T // ID Q9K061_NEIMB Unreviewed; 242 AA. AC Q9K061; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41172.1}; GN OrderedLocusNames=NMB0759 {ECO:0000313|EMBL:AAF41172.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41172.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41172.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41172.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41172.1; -; Genomic_DNA. DR PIR; D81161; D81161. DR RefSeq; NP_273801.1; NC_003112.2. DR RefSeq; WP_002221214.1; NC_003112.2. DR STRING; 122586.NMB0759; -. DR PaxDb; Q9K061; -. DR EnsemblBacteria; AAF41172; AAF41172; NMB0759. DR GeneID; 902874; -. DR KEGG; nme:NMB0759; -. DR PATRIC; 20356889; VBINeiMen85645_0963. DR eggNOG; ENOG4108Z2G; Bacteria. DR eggNOG; COG2836; LUCA. DR HOGENOM; HOG000277976; -. DR KO; K09792; -. DR OMA; QHWLMGH; -. DR OrthoDB; EOG6DNT6V; -. DR BioCyc; NMEN122586:GHGG-790-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 167 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 208 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 242 AA; 26406 MW; 0341AD055EAAC39E CRC64; MCRTAANHPF SRKIFDFKLP MNHDITFLTL FLLGFFGGTH CIGMCGGLSS AFALQLPPHI NRFWLILLLN TGRVSSYTAI GLILGLIGQV GVSLDQTRVL QNILYTAANL LLLFLGLYLS GISSLAAKIE KIGKPIWRNL NPILNRLLPI KSIPACLAVG ILWGWLPCGL VYSASLYALG SGSAATGGLY MLAFALGTLP NLLAIGIFSL QLKKIMQNRY IRLCTGLSVS LWALWKLAVL WL // ID Q9K0A4_NEIMB Unreviewed; 294 AA. AC Q9K0A4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41126.1}; GN OrderedLocusNames=NMB0711 {ECO:0000313|EMBL:AAF41126.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41126.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41126.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41126.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41126.1; -; Genomic_DNA. DR PIR; F81168; F81168. DR RefSeq; NP_273753.1; NC_003112.2. DR RefSeq; WP_002225470.1; NC_003112.2. DR STRING; 122586.NMB0711; -. DR PaxDb; Q9K0A4; -. DR EnsemblBacteria; AAF41126; AAF41126; NMB0711. DR GeneID; 902823; -. DR KEGG; nme:NMB0711; -. DR PATRIC; 20356769; VBINeiMen85645_0906. DR eggNOG; ENOG4105DSJ; Bacteria. DR eggNOG; COG1561; LUCA. DR HOGENOM; HOG000037752; -. DR OMA; QEMILLA; -. DR OrthoDB; EOG61KBKV; -. DR BioCyc; NMEN122586:GHGG-739-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005229; CHP00255. DR InterPro; IPR013551; DUF1732. DR InterPro; IPR013527; YicC-like_N. DR Pfam; PF08340; DUF1732; 1. DR Pfam; PF03755; YicC_N; 1. DR TIGRFAMs; TIGR00255; TIGR00255; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 8 158 YicC_N. {ECO:0000259|Pfam:PF03755}. FT DOMAIN 209 294 DUF1732. {ECO:0000259|Pfam:PF08340}. SQ SEQUENCE 294 AA; 33323 MW; 3FB27938CF52F68D CRC64; MSSGNIHIHS MTGFANAAAE CGSKRINLDL RAVNHRFLDI QIRMPDDLRY LESGIREKIS SHIARGKVEC KIQIQDAENG SQSLELNRDL VGQLAEINKD LRKHHDLAKL GVADILRFPG VLASQRENTE ELAKSITELT EKALKDFTAA RKREGKKLGE HLLQRLEAME EIIDALSELF PTLLETHKEK IRARLVEAVG SIDNDRLQQE FALFIQKSDI DEEFSRLRTH IAEVRRIVTE HKGSSGKRLD FLMQELNREA NTLGSKSIAA ECTQASVELK VLIEQMREQV QNIE // ID Q9K0Z5_NEIMB Unreviewed; 289 AA. AC Q9K0Z5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40845.1}; GN OrderedLocusNames=NMB0406 {ECO:0000313|EMBL:AAF40845.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40845.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40845.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40845.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40845.1; -; Genomic_DNA. DR PIR; C81203; C81203. DR RefSeq; NP_273455.1; NC_003112.2. DR RefSeq; WP_002224915.1; NC_003112.2. DR ProteinModelPortal; Q9K0Z5; -. DR STRING; 122586.NMB0406; -. DR PaxDb; Q9K0Z5; -. DR EnsemblBacteria; AAF40845; AAF40845; NMB0406. DR GeneID; 902520; -. DR KEGG; nme:NMB0406; -. DR PATRIC; 20355995; VBINeiMen85645_0515. DR eggNOG; COG3087; LUCA. DR HOGENOM; HOG000219100; -. DR OMA; AFKIPVP; -. DR OrthoDB; EOG6SR90S; -. DR BioCyc; NMEN122586:GHGG-428-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR Gene3D; 3.30.70.1070; -; 1. DR InterPro; IPR011930; FtsN. DR InterPro; IPR007730; SPOR_dom. DR Pfam; PF05036; SPOR; 1. DR SUPFAM; SSF110997; SSF110997; 1. DR TIGRFAMs; TIGR02223; ftsN; 1. DR PROSITE; PS51724; SPOR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 209 289 SPOR. {ECO:0000259|PROSITE:PS51724}. SQ SEQUENCE 289 AA; 31613 MW; 21E03AF509CE8D3F CRC64; MFMNKFSQSG KGLSGFFFGL ILATVIIAGI LFYLNQSGQN AFKIPASSKQ PAETEILKPK NQPKEDIQPE PADQNALSEP DAATEAEQSD AEKAADKQPV ADKADEVEEK AGEPEREEPD GQAVRKKALT EEREQTVREK AQKKDAETVK KQAVKPSKET EKKASKEEKK AAKEKVAPKP TPEQILNSGS IEKARSAAAK EVQKMKTSDK AEATHYLQMG AYADRQSAEG QRAKLAILGI SSKVVGYQAG HKTLYRVQSG NMSADAVKKM QDELKKHEVA SLIRSIESK // ID Q7DDL8_NEIMB Unreviewed; 139 AA. AC Q7DDL8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62317.1}; GN OrderedLocusNames=NMB0709 {ECO:0000313|EMBL:AAF62317.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62317.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62317.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62317.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62317.1; -; Genomic_DNA. DR RefSeq; NP_273751.1; NC_003112.2. DR RefSeq; WP_002217668.1; NC_003112.2. DR STRING; 122586.NMB0709; -. DR PaxDb; Q7DDL8; -. DR EnsemblBacteria; AAF62317; AAF62317; NMB0709. DR GeneID; 902821; -. DR KEGG; nme:NMB0709; -. DR PATRIC; 20356765; VBINeiMen85645_0904. DR HOGENOM; HOG000218848; -. DR OrthoDB; EOG6QG8KT; -. DR BioCyc; NMEN122586:GHGG-737-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 53 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 139 AA; 15742 MW; 6F358B87CAF2A4A5 CRC64; MDNKTKLRLG GLILLTTAVL SLIIVLIVDS WPLAILLAAV IVAAAAGGFV WTSRRQQRQF IERLKKFDID PEKGRINEAN LRRMYHSGGQ HQKDAITLIC LSQKCSVDEA HAMFKKRPTR QEINQMAAKQ SRGQKRPHR // ID Q9K1K2_NEIMB Unreviewed; 425 AA. AC Q9K1K2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Nitrogen assimilation regulatory protein NtrX {ECO:0000313|EMBL:AAF40574.1}; GN Name=ntrX {ECO:0000313|EMBL:AAF40574.1}; GN OrderedLocusNames=NMB0115 {ECO:0000313|EMBL:AAF40574.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40574.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40574.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40574.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains sigma-54 factor interaction domain. CC {ECO:0000256|SAAS:SAAS00516042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40574.1; -; Genomic_DNA. DR PIR; E81236; E81236. DR RefSeq; NP_273173.1; NC_003112.2. DR RefSeq; WP_002224766.1; NC_003112.2. DR ProteinModelPortal; Q9K1K2; -. DR SMR; Q9K1K2; 137-271. DR STRING; 122586.NMB0115; -. DR PaxDb; Q9K1K2; -. DR EnsemblBacteria; AAF40574; AAF40574; NMB0115. DR GeneID; 902219; -. DR KEGG; nme:NMB0115; -. DR PATRIC; 20355243; VBINeiMen85645_0155. DR eggNOG; ENOG4107RC9; Bacteria. DR eggNOG; COG2204; LUCA. DR HOGENOM; HOG000058489; -. DR OMA; KHGAAKI; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NMEN122586:GHGG-121-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR002078; Sigma_54_int. DR Pfam; PF02954; HTH_8; 1. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF14532; Sigma54_activ_2; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00515313}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00515313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00516031}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00516031}. FT DOMAIN 5 120 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 135 329 Sigma-54 factor interaction. FT {ECO:0000259|PROSITE:PS50045}. SQ SEQUENCE 425 AA; 46373 MW; 5654F271E31AF467 CRC64; MRSSDILIVD DEIGIRDLLS EILQDEGYSV ALAENAEEAR KLRHQARPAM VLLDIWMPDC DGITLLKEWA KNGQLNMPVV MMSGHASIDT AVEATKIGAI DFLEKPISLQ KLLSAVENAL KYGAAQTETG PVFDKLGNSA AIQEMNREVG AAVKCASPVL LTGEAGSPFE TVARYFHKNG TPWVSPARVE YLIDMPMELL QKAEGGVLYV GDIAQYSRNI QAGIAFIVGK AEHRRVRVVA SGSRAAGSDG IACEEKLAEL LSESVVRIPP LRMQHEDIPF LIQGIACNVA ESQKIAPASF SEEALAALTR YDWPGNFDQL QSVVATLLLE ADGQEIGAGA VSSLLGQNVP AEGAEDMVGG FNFNLPLREL REEVERRYFE YHIAQEGQNM SQVAQKVGLE RTHLYRKLKQ LGIGVSRRAG EKTEE // ID Q9JXK2_NEIMB Unreviewed; 484 AA. AC Q9JXK2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=Magnesium transporter MgtE {ECO:0000256|RuleBase:RU362011}; GN Name=mgtE {ECO:0000313|EMBL:AAF42326.1}; GN OrderedLocusNames=NMB1999 {ECO:0000313|EMBL:AAF42326.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42326.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42326.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42326.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Acts as a magnesium transporter. CC {ECO:0000256|RuleBase:RU362011}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362011}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362011}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362011}. CC -!- SIMILARITY: Belongs to the SLC41A transporter family. CC {ECO:0000256|RuleBase:RU362011}. CC -!- SIMILARITY: Contains 1 CBS domain. CC {ECO:0000256|RuleBase:RU362011}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU362011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42326.1; -; Genomic_DNA. DR PIR; B81018; B81018. DR RefSeq; NP_274991.1; NC_003112.2. DR RefSeq; WP_002225872.1; NC_003112.2. DR ProteinModelPortal; Q9JXK2; -. DR STRING; 122586.NMB1999; -. DR PaxDb; Q9JXK2; -. DR EnsemblBacteria; AAF42326; AAF42326; NMB1999. DR GeneID; 904127; -. DR KEGG; nme:NMB1999; -. DR PATRIC; 20360097; VBINeiMen85645_2553. DR eggNOG; ENOG4105CJW; Bacteria. DR eggNOG; COG2239; LUCA. DR HOGENOM; HOG000280153; -. DR KO; K06213; -. DR OMA; RAIQRYD; -. DR OrthoDB; EOG60GRRN; -. DR BioCyc; NMEN122586:GHGG-2056-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015693; P:magnesium ion transport; IEA:InterPro. DR Gene3D; 1.10.357.20; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR006668; Mg_transptr_MgtE_intracell_dom. DR InterPro; IPR006669; MgtE_transporter. DR InterPro; IPR006667; SLC41_membr_dom. DR Pfam; PF00571; CBS; 1. DR Pfam; PF01769; MgtE; 1. DR Pfam; PF03448; MgtE_N; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM00924; MgtE_N; 1. DR TIGRFAMs; TIGR00400; mgtE; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU362011}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Magnesium {ECO:0000256|RuleBase:RU362011}; KW Membrane {ECO:0000256|RuleBase:RU362011}; KW Metal-binding {ECO:0000256|RuleBase:RU362011}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU362011}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362011}; KW Transport {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 395 416 Helical. {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 422 448 Helical. {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 460 483 Helical. {ECO:0000256|RuleBase:RU362011}. FT DOMAIN 175 236 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 239 297 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 484 AA; 53107 MW; D6558C9E2BAC9548 CRC64; MSIEPTPPNL ENDGIENDVE RVSADFDRVH SLCEILEPAF EQIENGTPLE DAPLRDKLTE LTVLLSELHP ADVAAVLESL PPRERNIVWI LVKPEDDGEV LLEVSDAVRE TLIESMDKDE LLAAVDDLDA DELAELADDL PHQVVYEALQ TRDEEERAQV KAAMSYEDNQ VGAIMDFELV SIRADVACEV VLRYLRRFDS LPDHTDKIFV VDENDVLQGV LPIRKLLVAD PEDLVENVMA KDVVRFRAED DVEEAAQAFE RYDLVTAPVV DENKKLIGRI TIDEMVDVIR EESEADMLNM AGLQEEEDLF APVWDSVKNR WMWLAVNLCT AFLASRVIGA FEGSIEKIVA LAALMPIVAG IGGNSGNQTI TMIVRAMAMG QLTDMQAGRL LKKEVGVALV NGIIWGTVMG AVSWLLYGSL GIGLVMIAAM TLNLLLAATV GVLIPVVMEK FGRDPALGSS VLITAVTDSG GFLIFLGLAT LFLL // ID Q9JZ93_NEIMB Unreviewed; 581 AA. AC Q9JZ93; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 100. DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487}; DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487}; DE AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487}; GN Name=recD {ECO:0000256|HAMAP-Rule:MF_01487, GN ECO:0000313|EMBL:AAF41614.1}; GN OrderedLocusNames=NMB1233 {ECO:0000313|EMBL:AAF41614.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41614.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41614.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41614.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit has ssDNA-dependent CC ATPase and 5'-3' helicase activity. When added to pre-assembled CC RecBC greatly stimulates nuclease activity and augments holoenzyme CC processivity. Negatively regulates the RecA-loading ability of CC RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01487}. CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}. CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP- CC Rule:MF_01487}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41614.1; -; Genomic_DNA. DR PIR; B81107; B81107. DR RefSeq; NP_274257.1; NC_003112.2. DR RefSeq; WP_002225198.1; NC_003112.2. DR ProteinModelPortal; Q9JZ93; -. DR STRING; 122586.NMB1233; -. DR PaxDb; Q9JZ93; -. DR EnsemblBacteria; AAF41614; AAF41614; NMB1233. DR GeneID; 903655; -. DR KEGG; nme:NMB1233; -. DR PATRIC; 20358061; VBINeiMen85645_1543. DR eggNOG; ENOG410816P; Bacteria. DR eggNOG; COG0507; LUCA. DR HOGENOM; HOG000258341; -. DR KO; K03581; -. DR OMA; NRERYLP; -. DR OrthoDB; EOG60GRSZ; -. DR BioCyc; NMEN122586:GHGG-1270-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01487; RecD; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006344; RecD. DR InterPro; IPR027785; UvrD-like_helicase_C. DR Pfam; PF13538; UvrD_C_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01447; recD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01487}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01487}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01487}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01487}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01487}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 137 297 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 145 152 ATP. {ECO:0000256|HAMAP-Rule:MF_01487}. SQ SEQUENCE 581 AA; 62931 MW; 00FABFC99DF4F121 CRC64; MERQTDEFAQ AAARAAIRFL EHYAGSGDEV LANCTERLFQ ALQNGHSFIR LSGGEADALS ALAPVVGTSA APLILEGRRL FLGRMWQLEY DLAAEIKRLA AAGTSAPDAA GARQNLAKWF QGTGSEGQRD AAALALLQSF MVITGGPGTG KTTTVAKLLA LICGEDENLP NIALAAPTGK AAAHMARALH RAINGFDAPE AVRRHLLKLE GQTVHRLLKL RPPKMQAAFN PVYPLPFDVL VIDEASMLDT ALMLQLLKAV KTGARVILLG DENQLPSVGI GAVLSVLSQK TVLDGETHQR LAGFLPEHGF SVSANPPVLA QNTAHLSFSH RFGDNSGIGC LARAAVSGDE GAWALFDRFP DELEHSECSP NARVERLYRA HKAYWQAVKD GNIEAAYAGI SDIVVLAAWR QDAEDFNEAY CRHVRRKMNI PEHLAYFAGE PIMIRQNDYA LELFNGDIGL IMEDVGRQGS LAAYFADADG FKKVAVSCLP EFEPAFAMTV HKSQGSEYRE VWLLPPSAAP SDEGDDALSG LSKELLYTAI TRAREKFVFF GGEEAFRQAA ATVKTRQTAL GSMLERVFSQ E // ID Q7DD36_NEIMB Unreviewed; 102 AA. AC Q7DD36; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42449.1}; GN OrderedLocusNames=NMB2141 {ECO:0000313|EMBL:AAF42449.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42449.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42449.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42449.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42449.1; -; Genomic_DNA. DR PIR; C81002; C81002. DR RefSeq; NP_275126.1; NC_003112.2. DR RefSeq; WP_002215148.1; NC_003112.2. DR STRING; 122586.NMB2141; -. DR PaxDb; Q7DD36; -. DR EnsemblBacteria; AAF42449; AAF42449; NMB2141. DR GeneID; 903231; -. DR KEGG; nme:NMB2141; -. DR PATRIC; 20360474; VBINeiMen85645_2733. DR HOGENOM; HOG000218683; -. DR OMA; KSAQGSC; -. DR OrthoDB; EOG6PZXKG; -. DR BioCyc; NMEN122586:GHGG-2206-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 102 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004287536. SQ SEQUENCE 102 AA; 9612 MW; DA880632919C99CE CRC64; MNKNIAAALA GALSLSLAAG AVAANKPASN ATGVHKSAHG SCGASKSAEG SCGAAGSKAG EGKCGEGKCG ATVKKTHKHT KASKAKAKSA EGKCGEGKCG SK // ID Q9JZN4_NEIMB Unreviewed; 105 AA. AC Q9JZN4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41379.1}; GN OrderedLocusNames=NMB0975 {ECO:0000313|EMBL:AAF41379.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41379.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41379.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41379.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41379.1; -; Genomic_DNA. DR PIR; H81136; H81136. DR RefSeq; NP_274012.1; NC_003112.2. DR RefSeq; WP_002216597.1; NC_003112.2. DR STRING; 122586.NMB0481; -. DR PaxDb; Q9JZN4; -. DR EnsemblBacteria; AAF41379; AAF41379; NMB0975. DR GeneID; 903095; -. DR KEGG; nme:NMB0975; -. DR PATRIC; 20357439; VBINeiMen85645_1234. DR HOGENOM; HOG000218810; -. DR OrthoDB; EOG6H1Q2Q; -. DR BioCyc; NMEN122586:GHGG-1012-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009509; DUF1132. DR Pfam; PF06575; DUF1132; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 105 AA; 12443 MW; A44D31D04B1A1E83 CRC64; MNKPFITQAQ LALYKYQPSS KYFGQSMAVI AQSEFVEFAK INKSENVIDC FSFFWNRRIK HDIWLISFSD NSEMVIKESL KDGHKIYKFE FCEIVDNCNF DDVFV // ID Q9K038_NEIMB Unreviewed; 119 AA. AC Q9K038; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Putative phage shock protein E {ECO:0000313|EMBL:AAF41197.1}; GN OrderedLocusNames=NMB0784 {ECO:0000313|EMBL:AAF41197.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41197.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41197.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41197.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41197.1; -; Genomic_DNA. DR PIR; E81158; E81158. DR RefSeq; NP_273826.1; NC_003112.2. DR RefSeq; WP_002219522.1; NC_003112.2. DR ProteinModelPortal; Q9K038; -. DR STRING; 122586.NMB0784; -. DR PaxDb; Q9K038; -. DR EnsemblBacteria; AAF41197; AAF41197; NMB0784. DR GeneID; 902899; -. DR KEGG; nme:NMB0784; -. DR PATRIC; 20356953; VBINeiMen85645_0995. DR eggNOG; ENOG4105K8Z; Bacteria. DR eggNOG; COG0607; LUCA. DR HOGENOM; HOG000247776; -. DR KO; K03972; -. DR OMA; GHRCRRF; -. DR OrthoDB; EOG68DD6K; -. DR BioCyc; NMEN122586:GHGG-815-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR001763; Rhodanese-like_dom. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 119 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327874. FT DOMAIN 33 115 Rhodanese. {ECO:0000259|PROSITE:PS50206}. SQ SEQUENCE 119 AA; 12948 MW; 3AC9FE6A486E12FA CRC64; MNIKHLITAA LIASAAFAAQ AAPQKPVSAA QTAQHPAVWI DVRSEQEFSE GHLHNAVNIP VDQIVRRIHE AAPDKDTPVN LYCRSGRRAE AALQELKKAG YTNVANHGGY EDLLKKGMK // ID Q9JZE7_NEIMB Unreviewed; 101 AA. AC Q9JZE7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41479.1}; GN OrderedLocusNames=NMB1087 {ECO:0000313|EMBL:AAF41479.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41479.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41479.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41479.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41479.1; -; Genomic_DNA. DR PIR; A81123; A81123. DR STRING; 122586.NMB1087; -. DR PaxDb; Q9JZE7; -. DR EnsemblBacteria; AAF41479; AAF41479; NMB1087. DR PATRIC; 20357735; VBINeiMen85645_1384. DR HOGENOM; HOG000071270; -. DR OMA; LNHAVRY; -. DR OrthoDB; EOG6Z9B56; -. DR BioCyc; NMEN122586:GHGG-1123-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 101 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328341. SQ SEQUENCE 101 AA; 10639 MW; 8D6B8F30F516539D CRC64; MSLLKTVKMQ AAVALTALAL TACSSTTAPS ATEIKVVEKA VMPTPPAALM VAPVRPNPPK DGKTATLLEH AAEFGGYVAE LENQNQAWRD WAGNHSRKVG N // ID Q9K111_NEIMB Unreviewed; 451 AA. AC Q9K111; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Putative sugar transporter {ECO:0000313|EMBL:AAF40828.1}; GN OrderedLocusNames=NMB0388 {ECO:0000313|EMBL:AAF40828.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40828.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40828.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40828.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40828.1; -; Genomic_DNA. DR PIR; A81206; A81206. DR RefSeq; NP_273437.1; NC_003112.2. DR RefSeq; WP_002212459.1; NC_003112.2. DR ProteinModelPortal; Q9K111; -. DR STRING; 122586.NMB0388; -. DR PaxDb; Q9K111; -. DR EnsemblBacteria; AAF40828; AAF40828; NMB0388. DR GeneID; 902503; -. DR KEGG; nme:NMB0388; -. DR PATRIC; 20355939; VBINeiMen85645_0487. DR eggNOG; ENOG4105DUT; Bacteria. DR eggNOG; COG0477; LUCA. DR HOGENOM; HOG000291472; -. DR KO; K16211; -. DR OMA; YIMAVRM; -. DR OrthoDB; EOG6JX7JG; -. DR BioCyc; NMEN122586:GHGG-410-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Sugar transport {ECO:0000313|EMBL:AAF40828.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000313|EMBL:AAF40828.1}. FT TRANSMEM 21 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 305 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 354 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 360 381 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 416 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 422 444 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 451 AA; 48889 MW; 58DBBD5CB6DE25C5 CRC64; MSEYTPQTAK QGLPALAKST IWMLSFGFLG VQTAFTLQSS QMSRIFQTLG ADPHNLGWFF ILPPLAGMLV QPIVGHYSDR TWKPRLGGRR LPYLLYGTLI AVIVMILMPN SGSFGFGYAS LAALSFGALM IALLDVSSNM AMQPFKMMVG DMVNEEQKGY AYGIQSFLAN TGAVVAAILP FVFAYIGLAN TAEKGVVPQT VVVAFYVGAA LLVITSAFTI FKVKEYDPET YARYHGIDVA ANQEKANWIE LLKTAPKAFW TVTLVQFFCW FAFQYMWTYS AGAIAENVWH TTDASSVGYQ EAGNWYGVLA AVQSVAAVIC SFVLAKVPNK YHKAGYFGCL ALGALGFFSV FFIGNQYALV LSYTLIGIAW AGIITYPLTI VTNALSGKHM GTYLGLFNGS ICMPQIVASL LSFVLFPMLG GLQATMFLVG GVVLLLGAFS VFLIKETHGG V // ID Q9JY64_NEIMB Unreviewed; 85 AA. AC Q9JY64; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42065.1}; GN OrderedLocusNames=NMB1718 {ECO:0000313|EMBL:AAF42065.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42065.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42065.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42065.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42065.1; -; Genomic_DNA. DR PIR; H81049; H81049. DR RefSeq; NP_274721.1; NC_003112.2. DR RefSeq; WP_002224967.1; NC_003112.2. DR STRING; 122586.NMB1718; -. DR PaxDb; Q9JY64; -. DR EnsemblBacteria; AAF42065; AAF42065; NMB1718. DR GeneID; 903383; -. DR KEGG; nme:NMB1718; -. DR PATRIC; 20359397; VBINeiMen85645_2204. DR HOGENOM; HOG000219081; -. DR OMA; WHEDDFK; -. DR OrthoDB; EOG6R2H31; -. DR BioCyc; NMEN122586:GHGG-1773-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 85 AA; 10282 MW; E15CE52300C79DEC CRC64; MVLLLIVNKY WKVNDMKNEI QKNMDKYNPW HEDDFESYED IARDVSLTTD KTFIEHYLLE VYSEENGHFD QENVHAMIEE IKNAI // ID Q9K003_NEIMB Unreviewed; 411 AA. AC Q9K003; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN OrderedLocusNames=NMB0826 {ECO:0000313|EMBL:AAF41239.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41239.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41239.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41239.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC {ECO:0000256|RuleBase:RU000417}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000256|RuleBase:RU000416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41239.1; -; Genomic_DNA. DR PIR; A81155; A81155. DR RefSeq; NP_273868.1; NC_003112.2. DR RefSeq; WP_002219492.1; NC_003112.2. DR ProteinModelPortal; Q9K003; -. DR STRING; 122586.NMB0826; -. DR PaxDb; Q9K003; -. DR EnsemblBacteria; AAF41239; AAF41239; NMB0826. DR GeneID; 902941; -. DR KEGG; nme:NMB0826; -. DR PATRIC; 20357037; VBINeiMen85645_1037. DR eggNOG; ENOG4107V6I; Bacteria. DR eggNOG; COG0270; LUCA. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; QSFDINT; -. DR OrthoDB; EOG600DK3; -. DR BioCyc; NMEN122586:GHGG-857-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR TIGRFAMs; TIGR00675; dcm; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41239.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAF41239.1}. FT DOMAIN 42 404 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 411 AA; 47786 MW; 2555CEAC510D78F9 CRC64; MTISTMAQTH DTRLQKTLLF PSQQGWKSKT FLKPDSHIRL ATVFSGIGAV EQAFHRLNLN HTIVFSGDID PYVKKSYLGN YKLNEDFWHN DITQFDARKF RNQVDILVGG SPCQAFSMVG KRAGLEDTRG TLFYEFARVV DEVQPKIFIY ENVKGLLNHD NGKTWKVVKS VFYSLGYDLY FQIMNSKDYG IPQHRERIFV VGFHTPPING FQFPEKIELE HTMQDFLEDY TDSKYFLREK GAKFVTSSKN RQKRYTQING EIALCQKANQ QFNWHGDFIF QAARESEFDD FIFDVNNVEE KYYLSEKIKN YVLAGGTKNF KTSTETDLPV ARPLLQTMHK MHRAGVDNYV THNRGRIRKL TPRECLRLMG FRDDFKILVS DTQMYRQAGN SIVVDVLIAI LKQMDITLYG E // ID Q9JXJ8_NEIMB Unreviewed; 547 AA. AC Q9JXJ8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=ABC transporter, ATP-binding protein-related protein {ECO:0000313|EMBL:AAF42334.1}; GN OrderedLocusNames=NMB2008 {ECO:0000313|EMBL:AAF42334.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42334.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42334.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42334.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42334.1; -; Genomic_DNA. DR PIR; E81017; E81017. DR RefSeq; NP_275000.1; NC_003112.2. DR RefSeq; WP_002223143.1; NC_003112.2. DR ProteinModelPortal; Q9JXJ8; -. DR STRING; 122586.NMB2008; -. DR PaxDb; Q9JXJ8; -. DR EnsemblBacteria; AAF42334; AAF42334; NMB2008. DR GeneID; 904113; -. DR KEGG; nme:NMB2008; -. DR PATRIC; 20360117; VBINeiMen85645_2563. DR eggNOG; ENOG4108VRW; Bacteria. DR eggNOG; ENOG4111JYN; LUCA. DR HOGENOM; HOG000152750; -. DR OMA; HRISAQK; -. DR OrthoDB; EOG67DPKM; -. DR BioCyc; NMEN122586:GHGG-2065-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR029492; DUF4435. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13304; AAA_21; 1. DR Pfam; PF14491; DUF4435; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAF42334.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000313|EMBL:AAF42334.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 286 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 547 AA; 63123 MW; 84564D945D8DA3DC CRC64; MDEIQIPKKV ELQTKLENEK IVLSKGSTTI IVGANGTGKT RLAVYIEEQL KEKAHRISAH RALKLNPNVN KIPEKSAKTY LSYGQNWDGI DVSNRKNYRW DNNSYTHLLN DFDWLLQYLF AQQNNIAVAN NQKLNRNEKV TNSKTKLDIL QEAWETLLPH RKLHITADDI QVSAVDNEEL YSASNMSDGE RALFYILGQV LSVDDGSVLI FDEPELHIHK SIISNLWDKI EELRPDCSFL IITHDIEFAA TRVAKKYVIR NYYPTPAWDI SEVPESNFDE ETITMILGSR KPILFVEGNN NSLDIATYRY CYPDWTIIPK GACKDVIQSV SSLKKLSNEM PLLNLKCSGI VDLDSRDERE IEQLNNLGIY ILPVSEIENL FSLTDVAKEI LKLNQYSDEE LLNKLNGFKS ELIKYIDNEL KDDKLDEFVV KQVRRKIDNY LKNIDLSSKI TSTDMKKSLL NEISTLTEQK IETWISEIKN EIQRCIEQQD LDKLLTIYDN KGLLAKSACV LKGMRNKHEF ESWIMRTLKG RNKDFIDAIR QKLPILD // ID Q9JXK0_NEIMB Unreviewed; 115 AA. AC Q9JXK0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42330.1}; GN OrderedLocusNames=NMB2003 {ECO:0000313|EMBL:AAF42330.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42330.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42330.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42330.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42330.1; -; Genomic_DNA. DR PIR; A81017; A81017. DR RefSeq; NP_274995.1; NC_003112.2. DR RefSeq; WP_002237372.1; NC_003112.2. DR STRING; 122586.NMB2003; -. DR PaxDb; Q9JXK0; -. DR EnsemblBacteria; AAF42330; AAF42330; NMB2003. DR GeneID; 904119; -. DR KEGG; nme:NMB2003; -. DR PATRIC; 20360105; VBINeiMen85645_2557. DR eggNOG; ENOG41085G9; Bacteria. DR eggNOG; COG1380; LUCA. DR HOGENOM; HOG000253615; -. DR KO; K06518; -. DR OMA; GYTTQMM; -. DR OrthoDB; EOG65N1HV; -. DR BioCyc; NMEN122586:GHGG-2060-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR005538; LrgA/CidA. DR Pfam; PF03788; LrgA; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|SAAS:SAAS00459668}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAAS:SAAS00459668, KW ECO:0000256|SAAS:SAAS00459673, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAAS:SAAS00459673, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00459673, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 106 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 115 AA; 12382 MW; A381D57AF582FEB1 CRC64; MNIIRALLII LGCLATGETA VFLAGIKLPG SIVGMGVLFA LLQAGWVKTS WLQQLTDALM SNLTLFLVPP CVAVISYLDL IADDWFSILV SASASTLCVL LVTGKVHRWI RGIIR // ID Q4W570_NEIMB Unreviewed; 183 AA. AC Q4W570; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=ABC transporter, ATP-binding protein, truncation {ECO:0000313|EMBL:AAY52133.1}; GN OrderedLocusNames=NMB1077 {ECO:0000313|EMBL:AAY52133.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52133.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52133.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52133.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52133.1; -; Genomic_DNA. DR RefSeq; NP_274110.1; NC_003112.2. DR RefSeq; WP_002225253.1; NC_003112.2. DR ProteinModelPortal; Q4W570; -. DR STRING; 122586.NMB1077; -. DR PaxDb; Q4W570; -. DR EnsemblBacteria; AAY52133; AAY52133; NMB1077. DR GeneID; 903145; -. DR KEGG; nme:NMB1077; -. DR PATRIC; 20357711; VBINeiMen85645_1372. DR eggNOG; COG4178; LUCA. DR HOGENOM; HOG000027807; -. DR OMA; DKTADWQ; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NMEN122586:GHGG-1114-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAY52133.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000313|EMBL:AAY52133.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 10 181 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 183 AA; 20068 MW; D7E182CB2164A93F CRC64; MSGININLKN GDSLLIRGPS GCGKTSLLRA LAGLWPFGSS GKVSRPPHQD ILFLPQRPYT AQGSLRDAVC YPDIDKQHPE LAEAMNTCRL GYLVDKLDKT DDWQHKLSPG ELQRVAFVRA LLSKPKIVLL DEATAALDEP TEALLYRALK QKLPDSIIIS IGHRSTLNAF HNMRLDVGNV ACG // ID Q7DDA2_NEIMB Unreviewed; 238 AA. AC Q7DDA2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AAF41917.1}; GN OrderedLocusNames=NMB1563 {ECO:0000313|EMBL:AAF41917.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41917.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41917.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41917.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains HTH gntR-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00452141}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41917.1; -; Genomic_DNA. DR PIR; H81069; H81069. DR RefSeq; NP_274570.1; NC_003112.2. DR RefSeq; WP_002212831.1; NC_003112.2. DR ProteinModelPortal; Q7DDA2; -. DR STRING; 122586.NMB1563; -. DR PaxDb; Q7DDA2; -. DR EnsemblBacteria; AAF41917; AAF41917; NMB1563. DR GeneID; 904136; -. DR KEGG; nme:NMB1563; -. DR PATRIC; 20358984; VBINeiMen85645_2011. DR eggNOG; ENOG4108K6I; Bacteria. DR eggNOG; COG1802; LUCA. DR HOGENOM; HOG000219030; -. DR OMA; RQGCRCD; -. DR OrthoDB; EOG6FJNCS; -. DR BioCyc; NMEN122586:GHGG-1604-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.20.120.530; -; 1. DR InterPro; IPR011711; GntR_C. DR InterPro; IPR008920; TF_FadR/GntR_C. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07729; FCD; 1. DR Pfam; PF00392; GntR; 1. DR SMART; SM00895; FCD; 1. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48008; SSF48008; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|SAAS:SAAS00452277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|SAAS:SAAS00452220}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00452220}. FT DOMAIN 24 91 HTH gntR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50949}. SQ SEQUENCE 238 AA; 27198 MW; 2E0EE60E101205E0 CRC64; MNFENDDIIH APTTSSLILE ERHDSELFRV YALILDGITD QVLLPGKKLT ESELCRQMVC SRNTVRGALS LLAHDKIVDL QPNRGAFVHV PDLKEMQDVF NARIEMETMI LNILADLPDL ETRLKPLYAM IRREEEASGR GDRVGWNRLS NAFHVELARL VGNDVLFDIM NTLCARSSLI VAVAGVHREE KHAINTHTHS EHREILDLLL AGRRNRVVKI LRRHLGNCME RLEKTLED // ID Q9JY08_NEIMB Unreviewed; 67 AA. AC Q9JY08; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42137.1}; GN OrderedLocusNames=NMB1800 {ECO:0000313|EMBL:AAF42137.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42137.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42137.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42137.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42137.1; -; Genomic_DNA. DR PIR; E81042; E81042. DR STRING; 122586.NMB1800; -. DR PaxDb; Q9JY08; -. DR EnsemblBacteria; AAF42137; AAF42137; NMB1800. DR BioCyc; NMEN122586:GHGG-1855-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7705 MW; 3DCFC8C0A929CF20 CRC64; MNIMSTAGNI AKFPYSYHSV EKYSHLNSTL ESLPVRFLQA KKFPHQAGLD CSGEPHRLFN RPPYFSF // ID Q9K0E5_NEIMB Unreviewed; 64 AA. AC Q9K0E5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41082.1}; GN OrderedLocusNames=NMB0664 {ECO:0000313|EMBL:AAF41082.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41082.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41082.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41082.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41082.1; -; Genomic_DNA. DR PIR; D81172; D81172. DR STRING; 122586.NMB0664; -. DR PaxDb; Q9K0E5; -. DR EnsemblBacteria; AAF41082; AAF41082; NMB0664. DR BioCyc; NMEN122586:GHGG-691-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 64 AA; 7059 MW; 8FBB967EF7866C42 CRC64; MENAAASPAG RFRRHSRRRK CPTLKAQTHT KPYACTCNNP TDTAVFSKPF ASFTHPPRDA AATI // ID Q9JZ58_NEIMB Unreviewed; 475 AA. AC Q9JZ58; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Very long chain acyl-CoA dehydrogenase-related protein {ECO:0000313|EMBL:AAF41656.1}; GN OrderedLocusNames=NMB1280 {ECO:0000313|EMBL:AAF41656.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41656.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41656.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41656.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41656.1; -; Genomic_DNA. DR PIR; H81101; H81101. DR RefSeq; NP_274300.1; NC_003112.2. DR RefSeq; WP_002222388.1; NC_003112.2. DR ProteinModelPortal; Q9JZ58; -. DR STRING; 122586.NMB1280; -. DR PaxDb; Q9JZ58; -. DR EnsemblBacteria; AAF41656; AAF41656; NMB1280. DR GeneID; 903702; -. DR KEGG; nme:NMB1280; -. DR PATRIC; 20358187; VBINeiMen85645_1605. DR eggNOG; ENOG4107R8S; Bacteria. DR eggNOG; COG1960; LUCA. DR HOGENOM; HOG000218987; -. DR OMA; PMIHTEP; -. DR OrthoDB; EOG60PH76; -. DR BioCyc; NMEN122586:GHGG-1318-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 39 121 Acyl-CoA_dh_N. FT {ECO:0000259|Pfam:PF02771}. FT DOMAIN 234 371 Acyl-CoA_dh_1. FT {ECO:0000259|Pfam:PF00441}. SQ SEQUENCE 475 AA; 53630 MW; 6AC7E73B43AE0313 CRC64; MIHTEPSAQP STMDTAAFLK HIESAFRRIF SDGIDLMRYL PEDKWLALKQ AGLLLPFLDK KYGGRKGSQF EIQEVLRIAG HYGVPVTLRT GIEGALVLQP LQEFGDEAQV AQGLEMIFKG EGGGLGVTEP ETSGAAIARE MQSYYEYIDG QTIYVNAAKY WQGNSQSDFL LVAAKERKNG KLAKVIDLLL VPKTYIRCET LASEGLRAVR YAVNRIDAEM PATAVMKLSQ SDAAGLRAFQ NIFIRSRLQL IGMTHGIMEY ILENLERYVR NDIKFVDYER REIRRRHQVS EILYRYVCHS VSPVAPVAHQ LMEANIVKTL ATEYTYAAAQ MLQKLLGAKG FERGHTAGNI AIDIRPFTIF EGPNDMLYAE IYDQFVRATA EEKEAGMKLD KNQTLLDRLQ TDARFAAVAR DYTLPEDIRS FLQEHTLTDA CALQKVFIGK IIARLFVFVQ AKHEDTAAFL LNDIRKDILD CRYCG // ID Q9JYE3_NEIMB Unreviewed; 394 AA. AC Q9JYE3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41972.1}; GN OrderedLocusNames=NMB1620 {ECO:0000313|EMBL:AAF41972.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41972.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41972.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41972.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41972.1; -; Genomic_DNA. DR PIR; B81062; B81062. DR RefSeq; NP_274626.1; NC_003112.2. DR RefSeq; WP_002218953.1; NC_003112.2. DR ProteinModelPortal; Q9JYE3; -. DR STRING; 122586.NMB1620; -. DR MEROPS; S66.002; -. DR PaxDb; Q9JYE3; -. DR EnsemblBacteria; AAF41972; AAF41972; NMB1620. DR GeneID; 904061; -. DR KEGG; nme:NMB1620; -. DR PATRIC; 20359140; VBINeiMen85645_2081. DR eggNOG; ENOG4105EBE; Bacteria. DR eggNOG; COG1619; LUCA. DR HOGENOM; HOG000025480; -. DR KO; K01297; -. DR OMA; IVGHSDF; -. DR OrthoDB; EOG6JTC7M; -. DR BioCyc; NMEN122586:GHGG-1669-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.10740; -; 1. DR Gene3D; 3.50.30.60; -; 1. DR InterPro; IPR027461; Carboxypeptidase_A_C. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR027478; LdcA_N_dom. DR InterPro; IPR003507; S66_fam. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR019546; TAT_signal_bac_arc. DR Pfam; PF02016; Peptidase_S66; 1. DR SUPFAM; SSF141986; SSF141986; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 394 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004327707. SQ SEQUENCE 394 AA; 42440 MW; DB68A1ED8BE97B99 CRC64; MTEPTSRRRF LKTCTAAAGA GLLQACGTSA TSVPPLPSSH SVVKARTVPL QTPRRQSSDG NLLRVVASSG FAEDTNRVNT ALTRLYNVGF TVTNQQAGSR RFQRFAGTDT QRAADFQEVA SGRVATPKVL MGLRGGYGAA RILPHIDFAS LGARMREHGT LFFGFSDVCA VQLALLAKGN MMSFAGPMAY SDFGKPAPGA FTMDAFIKGA TQNRLTVDVP YIQRADVETE GILWGGNLSV LASLAGTPYM PDIDGGILFL EDVGEQPYRI ERMLNTLYLS GILKKQRAIV FGNFRMEKIR DVYDPSYDFS AVANHVSRTA KIPVLTGFPF GHIADKITFP LGAHARIRMN GNSGYSVAFE GYPTLDASAL TLDTLLPPPD LPIFPESGVA DISE // ID Q9K1N6_NEIMB Unreviewed; 94 AA. AC Q9K1N6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40518.1}; GN OrderedLocusNames=NMB0047 {ECO:0000313|EMBL:AAF40518.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40518.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40518.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40518.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40518.1; -; Genomic_DNA. DR PIR; B81244; B81244. DR RefSeq; NP_273113.1; NC_003112.2. DR RefSeq; WP_002216166.1; NC_003112.2. DR ProteinModelPortal; Q9K1N6; -. DR STRING; 122586.NMB0047; -. DR PaxDb; Q9K1N6; -. DR EnsemblBacteria; AAF40518; AAF40518; NMB0047. DR GeneID; 902150; -. DR KEGG; nme:NMB0047; -. DR PATRIC; 20355053; VBINeiMen85645_0063. DR eggNOG; ENOG41082JX; Bacteria. DR eggNOG; COG2827; LUCA. DR HOGENOM; HOG000285486; -. DR KO; K07461; -. DR OMA; LIEEHNP; -. DR OrthoDB; EOG62K215; -. DR BioCyc; NMEN122586:GHGG-48-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR000305; GIY-YIG_SF. DR Pfam; PF01541; GIY-YIG; 1. DR SMART; SM00465; GIYc; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR PROSITE; PS50164; GIY_YIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 77 GIY-YIG. {ECO:0000259|PROSITE:PS50164}. SQ SEQUENCE 94 AA; 11354 MW; EE89BB9FF1EB0909 CRC64; MQPAVYILAS QRNGTLYIGV TSDLVQRIYQ HREHLIEGFT SRYNVTMLVW YELHPTMESA ITREKQLKKW NRAWKLQLIE ENNVSWQDLW FDII // ID Q9K0I7_NEIMB Unreviewed; 295 AA. AC Q9K0I7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Spermidine/putrescine ABC transporter, permease protein {ECO:0000313|EMBL:AAF41039.1}; GN Name=potC {ECO:0000313|EMBL:AAF41039.1}; GN OrderedLocusNames=NMB0612 {ECO:0000313|EMBL:AAF41039.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41039.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41039.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41039.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41039.1; -; Genomic_DNA. DR PIR; E81179; E81179. DR RefSeq; NP_273656.1; NC_003112.2. DR RefSeq; WP_002214281.1; NC_003112.2. DR ProteinModelPortal; Q9K0I7; -. DR STRING; 122586.NMB0612; -. DR PaxDb; Q9K0I7; -. DR EnsemblBacteria; AAF41039; AAF41039; NMB0612. DR GeneID; 902726; -. DR KEGG; nme:NMB0612; -. DR PATRIC; 20356513; VBINeiMen85645_0776. DR eggNOG; ENOG4105D38; Bacteria. DR eggNOG; COG1177; LUCA. DR HOGENOM; HOG000263700; -. DR KO; K11074; -. DR OMA; KPWKVFF; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NMEN122586:GHGG-638-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 63 87 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 99 124 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 144 168 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 189 214 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 249 269 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 63 266 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 295 AA; 32619 MW; 08C32366CE1F8A77 CRC64; MQKSKLSWFL KLMLALSLAF LYIPLVVLVI YSFNESKLVT VWGGFSTKWY GALLENDTIL EAAWLSLRIA VVSSLAAVVL GTLAGYAMAR IKRFRGSTLF AGMISAPMVM PDVITGLSML LLIIQVQIFL QGSEWLQHLY FDRGFFTIFL GHTTLCMAYI TVVIRSRLVE LDQSLEEAAM DLGARPLKIF FVITLPLIAP AIASGFLLGI TLSLDDLVIT SFLSGPGSST LPQVIFSKIK LGLDPQMNVL ATILIGIIGT LVIIVNYWMM RQATKRDREA AEAYRQEKLA AEKAN // ID Q9JZM4_NEIMB Unreviewed; 181 AA. AC Q9JZM4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 68. DE SubName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AAF41390.1}; GN OrderedLocusNames=NMB0987 {ECO:0000313|EMBL:AAF41390.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41390.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41390.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41390.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41390.1; -; Genomic_DNA. DR PIR; D81135; D81135. DR RefSeq; NP_274023.1; NC_003112.2. DR RefSeq; WP_002225300.1; NC_003112.2. DR ProteinModelPortal; Q9JZM4; -. DR STRING; 122586.NMB0987; -. DR PaxDb; Q9JZM4; -. DR EnsemblBacteria; AAF41390; AAF41390; NMB0987. DR GeneID; 903107; -. DR KEGG; nme:NMB0987; -. DR PATRIC; 20357471; VBINeiMen85645_1250. DR eggNOG; ENOG4105QMG; Bacteria. DR eggNOG; COG0860; LUCA. DR HOGENOM; HOG000218907; -. DR KO; K01448; -. DR OrthoDB; EOG60KN2C; -. DR BioCyc; NMEN122586:GHGG-1024-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.40.630.40; -; 1. DR InterPro; IPR002508; CW_Hdrlase/autolysin_cat. DR Pfam; PF01520; Amidase_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 5 173 Ami_3. {ECO:0000259|Pfam:PF01520}. SQ SEQUENCE 181 AA; 19248 MW; EB03771ECB077938 CRC64; MGKTVTLTAG HSNTDPGAVN GSDREADLAQ DMRNIVASIL RNDYGLTVKT DGTGKGNMPL RDAVKLIRGS DVAIEFHTNA AANKTATGIE ALSTPKNKRW CQVLGKAVAK KTGWKLRGED GFKPDNAGQH SRLAYAQAGG IVFEPFFISN DTDLALFKTT KWGICRAIAD AIAMELGAAK V // ID Q9JXQ7_NEIMB Unreviewed; 31 AA. AC Q9JXQ7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Lacto-N-neotetraose biosynthesis glycosyl transferase-related protein {ECO:0000313|EMBL:AAF42256.1}; GN OrderedLocusNames=NMB1927 {ECO:0000313|EMBL:AAF42256.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42256.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42256.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42256.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42256.1; -; Genomic_DNA. DR PIR; B81027; B81027. DR STRING; 122586.NMB1927; -. DR PaxDb; Q9JXQ7; -. DR EnsemblBacteria; AAF42256; AAF42256; NMB1927. DR OrthoDB; EOG6HTP4N; -. DR BioCyc; NMEN122586:GHGG-1984-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF42256.1}. SQ SEQUENCE 31 AA; 3828 MW; 3963AB3453FD9AA6 CRC64; MDIVFAADGR MRRLFTLRQY FGILRRLLKN R // ID Q9JZB5_NEIMB Unreviewed; 487 AA. AC Q9JZB5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 106. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928}; DE EC=1.1.1.205 {ECO:0000256|RuleBase:RU003928}; GN Name=guaB {ECO:0000313|EMBL:AAF41583.1}; GN OrderedLocusNames=NMB1201 {ECO:0000313|EMBL:AAF41583.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41583.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41583.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41583.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|RuleBase:RU003928}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|RuleBase:RU003928}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|RuleBase:RU003927}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41583.1; -; Genomic_DNA. DR PIR; H81109; H81109. DR RefSeq; NP_274226.1; NC_003112.2. DR RefSeq; WP_002213540.1; NC_003112.2. DR ProteinModelPortal; Q9JZB5; -. DR SMR; Q9JZB5; 2-486. DR STRING; 122586.NMB1201; -. DR PaxDb; Q9JZB5; -. DR EnsemblBacteria; AAF41583; AAF41583; NMB1201. DR GeneID; 903623; -. DR KEGG; nme:NMB1201; -. DR PATRIC; 20357993; VBINeiMen85645_1509. DR eggNOG; ENOG4105CP4; Bacteria. DR eggNOG; COG0516; LUCA. DR eggNOG; COG0517; LUCA. DR HOGENOM; HOG000165755; -. DR KO; K00088; -. DR OMA; SSMGYCG; -. DR OrthoDB; EOG6GTZPV; -. DR BioCyc; NMEN122586:GHGG-1238-MONOMER; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW GMP biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|PIRSR:PIRSR000130-3, ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003927, KW ECO:0000313|EMBL:AAF41583.1}; KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4, KW ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 92 149 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 153 214 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 248 250 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT NP_BIND 298 300 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT ACT_SITE 305 305 Thioimidate intermediate. FT {ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 401 401 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000130-1}. FT METAL 300 300 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 302 302 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 305 305 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. SQ SEQUENCE 487 AA; 52383 MW; 4854B9C2681A2464 CRC64; MRIVEKAYTF DDVLLVPAHS TVLPRDVKLQ TKLTREITLN LPLLSAAMDT VTEARLAISM AQEGGIGIIH KNMPPEMQAR AVSKVKRHES GVVKDPVTVA PTTLIREVLE MRAQRKRKMS GLPVVENGKV VGIVTNRDLR FENRVDLPVS AIMTPRERLV TVPEGTSIDE ARELMHTHKV ERVLVLNEKD ELKGLITVKD ILKTTEFPNA NKDSEGRLRV GAAVGTGGDT EERVKALVEA GVDVIVVDTA HGHSQGVIDR VRWVKETYPH IQVIGGNIAT AKAALDLVAA GADAVKVGIG PGSICTTRIV AGVGVPQLTA IHNVAEALKG TGVPLIADGG IRFSGDIAKA LAAGAYSVML GGMFAGTEEA PGEIELYQGR SYKSYRGMGS LGAMSQGSAD RYFQDKTDST DKYVPEGIEG RVPYKGPIVN IIHQLTGGLR SSMGYLGCAN IAEMHEKAEF VEITSAGMSE SHVHDVQITK EAPNYHR // ID Q9JXT6_NEIMB Unreviewed; 122 AA. AC Q9JXT6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42224.1}; GN OrderedLocusNames=NMB1890 {ECO:0000313|EMBL:AAF42224.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42224.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42224.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42224.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42224.1; -; Genomic_DNA. DR PIR; H81031; H81031. DR RefSeq; NP_274886.1; NC_003112.2. DR RefSeq; WP_002225795.1; NC_003112.2. DR STRING; 122586.NMB1890; -. DR PaxDb; Q9JXT6; -. DR EnsemblBacteria; AAF42224; AAF42224; NMB1890. DR GeneID; 904287; -. DR KEGG; nme:NMB1890; -. DR PATRIC; 20359817; VBINeiMen85645_2413. DR eggNOG; ENOG4105WNK; Bacteria. DR eggNOG; COG4737; LUCA. DR HOGENOM; HOG000265475; -. DR OMA; RWAKSEN; -. DR OrthoDB; EOG64N9ZF; -. DR BioCyc; NMEN122586:GHGG-1947-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009387; HigB-2. DR Pfam; PF06296; RelE; 1. DR PIRSF; PIRSF018634; UCP018634; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 122 AA; 13905 MW; 06EE5A79995D801D CRC64; MRIFKNQWIV KFAKKHKIND SELLEAVERA DNGLIDADLG GGVIKQRIAR QGQGRSGGYR SLILFKQADK AFFVYAFAKN DRENISDKEL DVYRKAAAYY LKYTRAELAA LKEDGIITEI ES // ID Q9JZT2_NEIMB Unreviewed; 174 AA. AC Q9JZT2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41317.1}; GN OrderedLocusNames=NMB0909 {ECO:0000313|EMBL:AAF41317.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41317.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41317.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41317.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41317.1; -; Genomic_DNA. DR PIR; B81145; B81145. DR RefSeq; NP_273949.1; NC_003112.2. DR RefSeq; WP_002242549.1; NC_003112.2. DR STRING; 122586.NMB0909; -. DR PaxDb; Q9JZT2; -. DR EnsemblBacteria; AAF41317; AAF41317; NMB0909. DR GeneID; 903030; -. DR KEGG; nme:NMB0909; -. DR HOGENOM; HOG000220720; -. DR OMA; HEIYTIN; -. DR OrthoDB; EOG6ZWJFP; -. DR BioCyc; NMEN122586:GHGG-947-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 174 AA; 20485 MW; AE43B8177DBB53C4 CRC64; MLLLRRDNID RAFKIVKNRR FDSPWWPGEY DAGMNFLGVQ GELKVHELHH RTATLCFEWL GEVSAPRRKE NYKDLKPNVL YDFDGSGKHF ANPDARYLLP VGSSGLILKH IQIDDEDTLL RLWCARNIPM PHRLSKIPML RQYYLSKAWH EIYAINQHLR KTKLIVDVAY DPTD // ID Q7DDR2_NEIMB Unreviewed; 558 AA. AC Q7DDR2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Type IV pilus assembly protein {ECO:0000313|EMBL:AAF40773.1}; GN Name=pilF {ECO:0000313|EMBL:AAF40773.1}; GN OrderedLocusNames=NMB0329 {ECO:0000313|EMBL:AAF40773.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40773.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40773.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40773.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40773.1; -; Genomic_DNA. DR PIR; C81213; C81213. DR RefSeq; NP_273378.1; NC_003112.2. DR RefSeq; WP_002221967.1; NC_003112.2. DR ProteinModelPortal; Q7DDR2; -. DR STRING; 122586.NMB0329; -. DR PaxDb; Q7DDR2; -. DR EnsemblBacteria; AAF40773; AAF40773; NMB0329. DR GeneID; 902445; -. DR KEGG; nme:NMB0329; -. DR PATRIC; 20355797; VBINeiMen85645_0417. DR eggNOG; ENOG4107QHF; Bacteria. DR eggNOG; COG2804; LUCA. DR HOGENOM; HOG000008427; -. DR KO; K02652; -. DR OMA; NSAVECI; -. DR OrthoDB; EOG63Z76W; -. DR BioCyc; NMEN122586:GHGG-350-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0009297; P:pilus assembly; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013374; ATPase_typ4_pilus-assembl_PilB. DR InterPro; IPR007831; GSPII_E_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR Pfam; PF05157; T2SSE_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02538; type_IV_pilB; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 374 388 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 558 AA; 61965 MW; 56F7742692432A27 CRC64; MSVGLLRILV QNQVVTVEQA EHYYNESQAG KEVLPMLFSD GVISPKSLAA LIARVFSYSI LDLRHYPRHR VLMGVLTEEQ MVEFHCVPVF RRGDKVFFAV SDPTQMPQIQ KTVSAAGIEV ELVIVEDDQL AGLLDWVGSR STSLLQELGE GQEEEESHTL YIDNEEAEDG PVPRFIHKTL SDALRSGASD IHFEFYEHNA RIRFRVDGQL REVVQPPIAV RGQLASRIKV MSRLDISEKR IPQDGRMQLT FQKGGKPVDF RVSTLPTLFG EKVVMRILNS DAASLNIDQL GFEPFQKKLL LEAIHRPYGM VLVTGPTGSG KTVSLYTCLN ILNTESVNIA TAEDPAEINL PGINQVNVND KQGLTFAAAL KSFLRQDPDI IMVGEIRDLE TADIAIKAAQ TGHMVFSTLH TNNAPATLSR MLNMGVAPFN IASSVSLIMA QRLLRRLCSS CKQEVERPSA SALKEVGFTD EDLAKDWKLY RAVGCDRCRG QGYKGRAGVY EVMPISEEMQ RVIMNNGTEV DILDVAYKEG MVDLRRAGIL KVMQGITSLE EVTANTND // ID Q9K0V2_NEIMB Unreviewed; 153 AA. AC Q9K0V2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40894.1}; GN OrderedLocusNames=NMB0457 {ECO:0000313|EMBL:AAF40894.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40894.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40894.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40894.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40894.1; -; Genomic_DNA. DR PIR; C81198; C81198. DR RefSeq; NP_273504.1; NC_003112.2. DR RefSeq; WP_002218833.1; NC_003112.2. DR ProteinModelPortal; Q9K0V2; -. DR STRING; 122586.NMB0457; -. DR PaxDb; Q9K0V2; -. DR EnsemblBacteria; AAF40894; AAF40894; NMB0457. DR GeneID; 902573; -. DR KEGG; nme:NMB0457; -. DR PATRIC; 20356128; VBINeiMen85645_0580. DR eggNOG; ENOG4105K8N; Bacteria. DR eggNOG; COG0802; LUCA. DR HOGENOM; HOG000052238; -. DR KO; K06925; -. DR OMA; LDIDIRY; -. DR OrthoDB; EOG6GBMHT; -. DR BioCyc; NMEN122586:GHGG-481-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003442; T6A_TsaE. DR Pfam; PF02367; TsaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00150; T6A_YjeE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 153 AA; 16774 MW; 4CE5D57BA0E0CD5A CRC64; MSDLPSISRF LADEAATLDL GAAWSSRLNA PLVIYLEGDL GAGKTTLTRG ILRGLGHQGA VKSPTYAIVE SYPLERFTLH HFDLYRFSFP EEWEDAGLDE LFAANSVCLI EWPQQGGEFT PPADITATLT HDGDGRKCLL TAHTERGRES LPL // ID Q7DD53_NEIMB Unreviewed; 199 AA. AC Q7DD53; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956}; DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956}; DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956}; GN OrderedLocusNames=NMB2025 {ECO:0000313|EMBL:AAF42348.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42348.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42348.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42348.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Reversible hydration of carbon dioxide. CC {ECO:0000256|RuleBase:RU003956}. CC -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O. CC {ECO:0000256|RuleBase:RU003956}. CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CC {ECO:0000256|RuleBase:RU003956}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42348.1; -; Genomic_DNA. DR PIR; D81015; D81015. DR RefSeq; NP_275017.1; NC_003112.2. DR RefSeq; WP_002223159.1; NC_003112.2. DR ProteinModelPortal; Q7DD53; -. DR STRING; 122586.NMB2025; -. DR PaxDb; Q7DD53; -. DR EnsemblBacteria; AAF42348; AAF42348; NMB2025. DR GeneID; 904081; -. DR KEGG; nme:NMB2025; -. DR PATRIC; 20360165; VBINeiMen85645_2582. DR eggNOG; ENOG4108V2W; Bacteria. DR eggNOG; COG0288; LUCA. DR HOGENOM; HOG000021986; -. DR KO; K01673; -. DR OMA; FLEPAMG; -. DR OrthoDB; EOG6WMJ50; -. DR BioCyc; NMEN122586:GHGG-2087-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.1050.10; -; 1. DR InterPro; IPR001765; Carbonic_anhydrase. DR PANTHER; PTHR11002; PTHR11002; 1. DR Pfam; PF00484; Pro_CA; 1. DR SMART; SM00947; Pro_CA; 1. DR SUPFAM; SSF53056; SSF53056; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Lyase {ECO:0000256|RuleBase:RU003956}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Zinc {ECO:0000256|RuleBase:RU003956}. SQ SEQUENCE 199 AA; 22099 MW; F8259EB4EA6F9FEC CRC64; MSELDNILAH NRQFVESGEY EKYFTDKYPE RGLAVLSCMD ARIIGLLPDA LGLKNGDAKL IKNAGALVTH PWGSVMRSLL VAVFELKVRE IMVIAHHDCG MQGLNAEEFL GRVRESRIPE DRIETLRYAG IDLDGWLTGF DNVEDSVRHT VDLIRNHPLM PRHIAVHGLV IHPVTGKLTL VVDGSVSDGM DLSEGMETS // ID Q9K1R5_NEIMB Unreviewed; 214 AA. AC Q9K1R5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=EpiH/GdmH-related protein {ECO:0000313|EMBL:AAF40483.1}; GN OrderedLocusNames=NMB0004 {ECO:0000313|EMBL:AAF40483.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40483.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40483.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40483.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40483.1; -; Genomic_DNA. DR PIR; B81247; B81247. DR RefSeq; NP_273070.1; NC_003112.2. DR RefSeq; WP_002220030.1; NC_003112.2. DR ProteinModelPortal; Q9K1R5; -. DR STRING; 122586.NMB0004; -. DR PaxDb; Q9K1R5; -. DR EnsemblBacteria; AAF40483; AAF40483; NMB0004. DR GeneID; 902106; -. DR KEGG; nme:NMB0004; -. DR PATRIC; 20354935; VBINeiMen85645_0004. DR eggNOG; ENOG4107ZBR; Bacteria. DR eggNOG; COG1434; LUCA. DR HOGENOM; HOG000093113; -. DR OMA; PWHAMRA; -. DR OrthoDB; EOG6ZPT3P; -. DR BioCyc; NMEN122586:GHGG-4-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR003848; DUF218. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02698; DUF218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 39 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 53 180 DUF218. {ECO:0000259|Pfam:PF02698}. SQ SEQUENCE 214 AA; 24197 MW; D7566829AC1D6350 CRC64; MNKRLFCSRN GLRYYLLGGF CLSVFPLLLV FASSVWAVYR TGGQVLPPYV RADAALVLGA AAWDKRPSPV FRERINHAIA LYQSRRVGKI VFTGGRTKKG YMTEAEVGRR YALKQGVPAR NILFENTSRN TYENLNNIRP VLRANGIASV VIVSDPYHLA RAAEMAEDLG VRVYMSATPT TRFDAGNKKK IFMLQEGYAL SLYRLEKWGR DFFN // ID Q9JZ64_NEIMB Unreviewed; 478 AA. AC Q9JZ64; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Putative alginate O-acetylation protein AlgI {ECO:0000313|EMBL:AAF41650.1}; GN OrderedLocusNames=NMB1273 {ECO:0000313|EMBL:AAF41650.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41650.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41650.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41650.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41650.1; -; Genomic_DNA. DR PIR; C81103; C81103. DR RefSeq; NP_274294.1; NC_003112.2. DR RefSeq; WP_002244145.1; NC_003112.2. DR STRING; 122586.NMB1273; -. DR PaxDb; Q9JZ64; -. DR EnsemblBacteria; AAF41650; AAF41650; NMB1273. DR GeneID; 903695; -. DR KEGG; nme:NMB1273; -. DR PATRIC; 20358165; VBINeiMen85645_1594. DR eggNOG; ENOG4105CK0; Bacteria. DR eggNOG; COG1696; LUCA. DR HOGENOM; HOG000003940; -. DR OMA; WDWRFVA; -. DR OrthoDB; EOG6QCD9F; -. DR BioCyc; NMEN122586:GHGG-1311-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:InterPro. DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB. DR InterPro; IPR028362; AlgI. DR InterPro; IPR004299; MBOAT_fam. DR Pfam; PF03062; MBOAT; 1. DR PIRSF; PIRSF500217; AlgI; 1. DR PIRSF; PIRSF016636; AlgI_DltB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 335 352 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 386 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 414 432 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 452 476 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 478 AA; 53441 MW; 7C373E4C46ABA742 CRC64; MPLLSVEFAL FFLAFLPIYW GLAKYPSVQN LLLLAAGMGW LYHIGPVFAA IIVLYSSCVY LLGELLRSDR ENTRRFWLGC GIAASLTVLG FFKYFDFFRP MIAQYAGKGG AIDILMPLGL SYYTFQSLAY LVYCFRAPHA ARFSWHELLL HLSFFPTVTS GPIIRAAAFK SADGEQAGAL AQIRTRRARS PVRPALAVSL ILLGIAKKWW LAGMLAENWV SPVFENPAQF DGWGVLGGVY GYTFQLFLDF SGYSDLVIGM AMLLGFRLPK NFSAPLRALN IRAFWDKWHI SLSTWIRDYI YIPLGGSKKG FLRTQLNLMA AMVLSGIWHG YGWNFLIWGA LHGTALVLLN TGDRYFGRDA LCRLKYFAPL SWLITFHFVC LSFVVFNTAN PDDAGAVFSA LFANANGWNA PQQANMLLLA SFASVMLLYP YLQRAFDGAV KGLEKIPMWL WFIPVSAVLL LIIVLAPSGI PGFIYANF // ID Q9K175_NEIMB Unreviewed; 32 AA. AC Q9K175; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40748.1}; GN OrderedLocusNames=NMB0297 {ECO:0000313|EMBL:AAF40748.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40748.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40748.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40748.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40748.1; -; Genomic_DNA. DR PIR; H81215; H81215. DR RefSeq; NP_273351.1; NC_003112.2. DR RefSeq; WP_010980772.1; NC_003112.2. DR STRING; 122586.NMB0297; -. DR PaxDb; Q9K175; -. DR EnsemblBacteria; AAF40748; AAF40748; NMB0297. DR GeneID; 902408; -. DR KEGG; nme:NMB0297; -. DR BioCyc; NMEN122586:GHGG-312-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 32 AA; 3563 MW; 988818AB929A5D8D CRC64; MPSESPSFRQ HIHKGAPAGG GRGKDCWRRR SI // ID Q9JXP6_NEIMB Unreviewed; 57 AA. AC Q9JXP6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42272.1}; GN OrderedLocusNames=NMB1943 {ECO:0000313|EMBL:AAF42272.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42272.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42272.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42272.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42272.1; -; Genomic_DNA. DR PIR; H81025; H81025. DR STRING; 122586.NMB1943; -. DR PaxDb; Q9JXP6; -. DR EnsemblBacteria; AAF42272; AAF42272; NMB1943. DR PATRIC; 20359935; VBINeiMen85645_2472. DR BioCyc; NMEN122586:GHGG-2000-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 51 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 57 AA; 6277 MW; AAED5AE1ED8B4246 CRC64; MGNIILLTFF LLHVRIVFLF SFLIFEEIMN TRIIVSAAFV ALALAGCGSI NNVTVSD // ID Q9K110_NEIMB Unreviewed; 336 AA. AC Q9K110; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Aldose 1-epimerase {ECO:0000313|EMBL:AAF40829.1}; DE EC=5.1.3.3 {ECO:0000313|EMBL:AAF40829.1}; GN Name=galM {ECO:0000313|EMBL:AAF40829.1}; GN OrderedLocusNames=NMB0389 {ECO:0000313|EMBL:AAF40829.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40829.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40829.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40829.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40829.1; -; Genomic_DNA. DR PIR; B81206; B81206. DR RefSeq; NP_273438.1; NC_003112.2. DR RefSeq; WP_002224907.1; NC_003112.2. DR ProteinModelPortal; Q9K110; -. DR STRING; 122586.NMB0389; -. DR PaxDb; Q9K110; -. DR EnsemblBacteria; AAF40829; AAF40829; NMB0389. DR GeneID; 902504; -. DR KEGG; nme:NMB0389; -. DR PATRIC; 20355941; VBINeiMen85645_0488. DR eggNOG; ENOG4105ENN; Bacteria. DR eggNOG; COG2017; LUCA. DR HOGENOM; HOG000072798; -. DR KO; K01785; -. DR OMA; DKETPLS; -. DR OrthoDB; EOG69WFM5; -. DR BioCyc; NMEN122586:GHGG-411-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. DR Pfam; PF01263; Aldose_epim; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000313|EMBL:AAF40829.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 336 AA; 36619 MW; 41B48FDAF1BB14A0 CRC64; MSDTPATRDF GLIDGRAVTG YVLSNRRGTR VCVLDLGGIV QEFSVLADGV RENLVVSFDD AASYADNPFQ INKQIGRVAG RIRGAAFDIN GRTYRVEANE GRNALHGGSH GLAVTRFNAV AADGRSVVLR SRLQQSADGY PNDLDLDISY RLDEDDRLTV SYRATALGDT VFDPTLHIYW RLDAGLHDAV LHIPQGGHMP ADAEKLPVST VSDDLEVFDF SRPKPLDAAV AALRRETGRA GFDDAYRVPS DIGRPAAVLQ AGRRRRISIY SDRNGLVIFT AAPQDFARHD AGVYDALATE AQTLPDSLNW PEFGNIRLNK GDTREATIAY GIESLS // ID Q9JYD4_NEIMB Unreviewed; 109 AA. AC Q9JYD4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41988.1}; GN OrderedLocusNames=NMB1639 {ECO:0000313|EMBL:AAF41988.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41988.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41988.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41988.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41988.1; -; Genomic_DNA. DR PIR; G81059; G81059. DR RefSeq; NP_274644.1; NC_003112.2. DR RefSeq; WP_002212691.1; NC_003112.2. DR STRING; 122586.NMB1639; -. DR PaxDb; Q9JYD4; -. DR EnsemblBacteria; AAF41988; AAF41988; NMB1639. DR GeneID; 903944; -. DR KEGG; nme:NMB1639; -. DR PATRIC; 20359196; VBINeiMen85645_2110. DR HOGENOM; HOG000027865; -. DR OMA; CFAPLPY; -. DR OrthoDB; EOG6QCDCC; -. DR BioCyc; NMEN122586:GHGG-1688-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 109 AA; 11941 MW; 5E99895FC8C80A50 CRC64; MSRCCLKRLQ TASAVSAFSG GVLEVVRLCC RRLSVLFNPS VMLFVPDCPV GGAAGFFQYE MLCPFFWQGR LQTGSNLAYD VFMSAGRLNG GRNPPHSRRF LALLCSVAL // ID Q9JZF8_NEIMB Unreviewed; 376 AA. AC Q9JZF8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41468.1}; GN OrderedLocusNames=NMB1073 {ECO:0000313|EMBL:AAF41468.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41468.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41468.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41468.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41468.1; -; Genomic_DNA. DR PIR; D81124; D81124. DR RefSeq; NP_274106.1; NC_003112.2. DR RefSeq; WP_002244116.1; NC_003112.2. DR ProteinModelPortal; Q9JZF8; -. DR STRING; 122586.NMB1073; -. DR PaxDb; Q9JZF8; -. DR EnsemblBacteria; AAF41468; AAF41468; NMB1073. DR GeneID; 903492; -. DR KEGG; nme:NMB1073; -. DR PATRIC; 20357695; VBINeiMen85645_1364. DR eggNOG; ENOG4105UV7; Bacteria. DR eggNOG; COG2866; LUCA. DR HOGENOM; HOG000262545; -. DR OMA; FAYFEPY; -. DR OrthoDB; EOG6X10TC; -. DR BioCyc; NMEN122586:GHGG-1110-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR000834; Peptidase_M14. DR Pfam; PF00246; Peptidase_M14; 1. DR SMART; SM00631; Zn_pept; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 106 356 Peptidase_M14. FT {ECO:0000259|SMART:SM00631}. SQ SEQUENCE 376 AA; 42032 MW; CA0150B81DB06BEC CRC64; MIKISTRFDA GSVVVKDLTD PSNIRLALRP DNASDFAQWF YFRLQGAAYQ NCIMHFENAA EAAYPKGWEG YQACASYDRR NWFRVPTSYE NGVLTVNHTP LSNSVYYAYF EPYSEEQHLN LLGDAQGSGL CRIDDLGSTV QGRDINLLTI GNQVESDLKI WITARQHPGE TMAEWFIEGL LGRLLDPQDP TARALLDRAT FYIVPNMNPD GSALGNLRTN AAGANLNREW ENPTVEKSPE VFFVREKMLE TGVDLFLDIH GDEGLPFVFV AGTEGVPNYN PRIAALEAQF KNALLNASPD FQDEYGYEKD APGEANMTLA TNWVGNRFNC LAYTLEMPFK DNANLPDDDF GWNGQRSLRL GEAALSAILN VIGDLR // ID Q9JXK7_NEIMB Unreviewed; 364 AA. AC Q9JXK7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Putative adhesin/invasin {ECO:0000313|EMBL:AAF42321.1}; GN OrderedLocusNames=NMB1994 {ECO:0000313|EMBL:AAF42321.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42321.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42321.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42321.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42321.1; -; Genomic_DNA. DR PIR; A81019; A81019. DR RefSeq; NP_274986.1; NC_003112.2. DR RefSeq; WP_010981019.1; NC_003112.2. DR ProteinModelPortal; Q9JXK7; -. DR STRING; 122586.NMB1994; -. DR PaxDb; Q9JXK7; -. DR EnsemblBacteria; AAF42321; AAF42321; NMB1994. DR GeneID; 904134; -. DR KEGG; nme:NMB1994; -. DR PATRIC; 20360085; VBINeiMen85645_2547. DR eggNOG; ENOG4105K9N; Bacteria. DR eggNOG; ENOG4111UXE; LUCA. DR HOGENOM; HOG000220770; -. DR OMA; NEKRIDK; -. DR BioCyc; NMEN122586:GHGG-2051-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005594; YadA_C. DR Pfam; PF03895; YadA_anchor; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 364 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329313. FT DOMAIN 285 364 YadA_anchor. {ECO:0000259|Pfam:PF03895}. FT COILED 103 130 {ECO:0000256|SAM:Coils}. FT COILED 191 229 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 364 AA; 37972 MW; B9FF591FD25F853F CRC64; MSMKHFPSKV LTTAILATFC SGALAATSDD DVKKAATVAI VAAYNNGQEI NGFKAGETIY DIGEDGTITQ KDATAADVEA DDFKGLGLKK VVTNLTKTVN ENKQNVDAKV KAAESEIEKL TTKLADTDAA LADTDAALDE TTNALNKLGE NITTFAEETK TNIVKIDEKL EAVADTVDKH AEAFNDIADS LDETNTKADE AVKTANEAKQ TAEETKQNVD AKVKAAETAA GKAEAAAGTA NTAADKAEAV AAKVTDIKAD IATNKADIAK NSARIDSLDK NVANLRKETR QGLAEQAALS GLFQPYNVGR FNVTAAVGGY KSESAVAIGT GFRFTENFAA KAGVAVGTSS GSSAAYHVGV NYEW // ID Q4W585_NEIMB Unreviewed; 115 AA. AC Q4W585; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 43. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AAY52146.1}; GN OrderedLocusNames=NMB0026 {ECO:0000313|EMBL:AAY52146.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52146.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52146.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52146.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52146.1; -; Genomic_DNA. DR RefSeq; NP_273092.1; NC_003112.2. DR RefSeq; WP_002221785.1; NC_003112.2. DR ProteinModelPortal; Q4W585; -. DR SMR; Q4W585; 1-68. DR STRING; 122586.NMB0026; -. DR PaxDb; Q4W585; -. DR EnsemblBacteria; AAY52146; AAY52146; NMB0026. DR GeneID; 902129; -. DR KEGG; nme:NMB0026; -. DR PATRIC; 20355001; VBINeiMen85645_0037. DR OMA; NKATGNE; -. DR OrthoDB; EOG6BCSZD; -. DR BioCyc; NMEN122586:GHGG-27-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009289; C:pilus; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR001082; Pilin. DR Pfam; PF00114; Pilin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 115 AA; 12575 MW; F882A465CB592D8C CRC64; MASSGVNKEI KGRKLSLWAK RQAGSVKWFC GQPVERDNAK AANDDVTAAA AANGKKIDTK HLPSTCRDAA SAVCTKHPSI ARITANGRKT SSFPRRRESR SVGTETYRVK RFLRS // ID Q9JXD6_NEIMB Unreviewed; 29 AA. AC Q9JXD6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42414.1}; GN OrderedLocusNames=NMB2097 {ECO:0000313|EMBL:AAF42414.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42414.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42414.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42414.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42414.1; -; Genomic_DNA. DR PIR; B81006; B81006. DR RefSeq; NP_275085.1; NC_003112.2. DR RefSeq; WP_010981026.1; NC_003112.2. DR STRING; 122586.NMB2097; -. DR PaxDb; Q9JXD6; -. DR EnsemblBacteria; AAF42414; AAF42414; NMB2097. DR GeneID; 903947; -. DR KEGG; nme:NMB2097; -. DR BioCyc; NMEN122586:GHGG-2162-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 29 AA; 3474 MW; F2A9C912DAAD35C2 CRC64; MLATHSNPET AYSDTHHCRF SLLLRFRRL // ID Q9JY80_NEIMB Unreviewed; 121 AA. AC Q9JY80; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42048.1}; GN OrderedLocusNames=NMB1700 {ECO:0000313|EMBL:AAF42048.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42048.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42048.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42048.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42048.1; -; Genomic_DNA. DR PIR; F81052; F81052. DR STRING; 122586.NMB1700; -. DR PaxDb; Q9JY80; -. DR EnsemblBacteria; AAF42048; AAF42048; NMB1700. DR BioCyc; NMEN122586:GHGG-1755-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 121 AA; 13401 MW; CEE0F2DA075BA77E CRC64; MGGGNVPSRV AYQTRRLTQT AALHSGQERQ FRPDIGQTVG KIRTFRPFCP LGHIAHFAAR NPPGGDVEVE PANNRRHSFF QKFTLCRILT KAYPPDNAEI QTHFCPLSPT TPPLGKPPEL A // ID Q7DD76_NEIMB Unreviewed; 413 AA. AC Q7DD76; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Pilin glycosylation protein PglB {ECO:0000313|EMBL:AAF42155.1}; GN Name=pglB {ECO:0000313|EMBL:AAF42155.1}; GN OrderedLocusNames=NMB1820 {ECO:0000313|EMBL:AAF42155.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42155.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42155.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42155.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42155.1; -; Genomic_DNA. DR RefSeq; NP_274817.1; NC_003112.2. DR RefSeq; WP_002225656.1; NC_003112.2. DR ProteinModelPortal; Q7DD76; -. DR STRING; 122586.NMB1820; -. DR PaxDb; Q7DD76; -. DR EnsemblBacteria; AAF42155; AAF42155; NMB1820. DR GeneID; 903280; -. DR KEGG; nme:NMB1820; -. DR PATRIC; 20359625; VBINeiMen85645_2318. DR eggNOG; ENOG4105D3Q; Bacteria. DR eggNOG; COG0110; LUCA. DR eggNOG; COG2148; LUCA. DR HOGENOM; HOG000218777; -. DR OMA; IVCDIPD; -. DR OrthoDB; EOG6ZD66R; -. DR BioCyc; NMEN122586:GHGG-1875-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR003362; Bact_transf. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020019; Sia_OAcTrfase_NeuD-like. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF02397; Bac_transf; 1. DR Pfam; PF00132; Hexapep; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR03570; NeuD_NnaD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 180 Bac_transf. {ECO:0000259|Pfam:PF02397}. SQ SEQUENCE 413 AA; 44552 MW; D35F900BA2DAC2F8 CRC64; MSKFFKRLFD IVASASGLIF LSPVFLILIY LIRKNLGSPV FFFQERPGKD GKPFKMVKFR SMRDALDSDG IPLPDGERLT PFGKKLRAAS LDELPELWNI LKGEMSLVGP RPLLMQYLPL YDNFQNRRHE MKPGITGWAQ VNGRNALSWD EKFACDVWYI DHFSLCLDIK ILLLTVKKVL IKEGISAQGE ATMPPFTGKR KLAVVGAGGH GKVVADLAAA LGRYREIVFL DDRAQGSVNG FSVIGTTLLL ENSLSPEQYD VAVAVGNNRI RRQIAEKAAA LGFALPVLVH PDATVSPSAT VGQGSVVMAK AVVQAGSVLK DGVIVNTAAT VDHDCLLNAF VHISPGAHLS GNTHIGEESW IGTGACSRQQ IRIGSRATIG AGAVVVRDVS DGMTVAGNPA KPLPRKNPET STA // ID Q9JXI1_NEIMB Unreviewed; 107 AA. AC Q9JXI1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=PemK-related protein {ECO:0000313|EMBL:AAF42359.1}; GN OrderedLocusNames=NMB2038 {ECO:0000313|EMBL:AAF42359.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42359.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42359.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42359.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42359.1; -; Genomic_DNA. DR PIR; C81014; C81014. DR RefSeq; NP_275029.1; NC_003112.2. DR RefSeq; WP_002214977.1; NC_003112.2. DR ProteinModelPortal; Q9JXI1; -. DR STRING; 122586.NMB2038; -. DR PaxDb; Q9JXI1; -. DR EnsemblBacteria; AAF42359; AAF42359; NMB2038. DR GeneID; 904055; -. DR KEGG; nme:NMB2038; -. DR PATRIC; 20360206; VBINeiMen85645_2604. DR eggNOG; ENOG41081C4; Bacteria. DR eggNOG; COG2337; LUCA. DR HOGENOM; HOG000290184; -. DR KO; K07171; -. DR OMA; SPPEMHD; -. DR OrthoDB; EOG6G20PS; -. DR BioCyc; NMEN122586:GHGG-2100-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 2.30.30.110; -; 1. DR InterPro; IPR003477; PemK-like. DR InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib. DR Pfam; PF02452; PemK_toxin; 1. DR SUPFAM; SSF50118; SSF50118; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 107 AA; 11789 MW; 990F4313B05D71B9 CRC64; MDMVVRGGIY LVSLDPTVGS EIKKTRPCVV VSPPEIHNYL KTVLIVPMTS GSRPAPFRVN VRFQDKDGLL LPEQIRAVDK AGLVKHLGNL DNSTAEKLFA VLQEMFA // ID Q9JYD8_NEIMB Unreviewed; 121 AA. AC Q9JYD8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF62336.1}; GN OrderedLocusNames=NMB1629 {ECO:0000313|EMBL:AAF62336.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF62336.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF62336.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF62336.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF62336.1; -; Genomic_DNA. DR RefSeq; NP_274635.1; NC_003112.2. DR RefSeq; WP_010980968.1; NC_003112.2. DR STRING; 122586.NMB1629; -. DR PaxDb; Q9JYD8; -. DR EnsemblBacteria; AAF62336; AAF62336; NMB1629. DR GeneID; 904000; -. DR KEGG; nme:NMB1629; -. DR PATRIC; 20359162; VBINeiMen85645_2092. DR HOGENOM; HOG000218810; -. DR OMA; NRRISNN; -. DR OrthoDB; EOG664CRG; -. DR BioCyc; NMEN122586:GHGG-1678-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR009509; DUF1132. DR Pfam; PF06575; DUF1132; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 121 AA; 14278 MW; 6C16200767A92B2C CRC64; MTCFKIRLSK QPLKGRTMNK PFITQAQLAL YKYQPSSKYY GKTMAYTFAS ELLDYSKVNK FIIHEEIQCF LNRRISNNIW KIYFSDESVA YIKILELQDD YSRGIEIKTF DFNPNVGDVF G // ID Q9JZL2_NEIMB Unreviewed; 81 AA. AC Q9JZL2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41405.1}; GN OrderedLocusNames=NMB1004 {ECO:0000313|EMBL:AAF41405.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41405.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41405.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41405.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41405.1; -; Genomic_DNA. DR PIR; B81133; B81133. DR RefSeq; NP_274039.1; NC_003112.2. DR RefSeq; WP_002222576.1; NC_003112.2. DR STRING; 122586.NMB1004; -. DR PaxDb; Q9JZL2; -. DR EnsemblBacteria; AAF41405; AAF41405; NMB1004. DR GeneID; 903140; -. DR KEGG; nme:NMB1004; -. DR PATRIC; 20357541; VBINeiMen85645_1287. DR HOGENOM; HOG000027801; -. DR OMA; ITFTRWA; -. DR OrthoDB; EOG6G7R7N; -. DR BioCyc; NMEN122586:GHGG-1041-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR026365; BcepMu_gp16. DR TIGRFAMs; TIGR04111; BcepMu_gp16; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 81 AA; 9247 MW; 28BF3E576F94B16A CRC64; MINHECINQP YGRILKFSRV QAKEMLTADE LKENFAKNGQ TLAQWARENG FKPRDVYLVI GGQRKGNYGK GHEIAKKLGL K // ID Q7DDR1_NEIMB Unreviewed; 410 AA. AC Q7DDR1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Pilus assembly protein PilG {ECO:0000313|EMBL:AAF40776.1}; GN Name=pilG {ECO:0000313|EMBL:AAF40776.1}; GN OrderedLocusNames=NMB0333 {ECO:0000313|EMBL:AAF40776.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40776.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40776.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40776.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU003923}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003923}. CC -!- SIMILARITY: Belongs to the GSP F family. CC {ECO:0000256|RuleBase:RU003923}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40776.1; -; Genomic_DNA. DR PIR; H81210; H81210. DR RefSeq; NP_273382.1; NC_003112.2. DR RefSeq; WP_002216405.1; NC_003112.2. DR STRING; 122586.NMB0333; -. DR PaxDb; Q7DDR1; -. DR EnsemblBacteria; AAF40776; AAF40776; NMB0333. DR GeneID; 902448; -. DR KEGG; nme:NMB0333; -. DR PATRIC; 20355805; VBINeiMen85645_0421. DR eggNOG; ENOG4105D7Q; Bacteria. DR eggNOG; COG1459; LUCA. DR HOGENOM; HOG000253740; -. DR KO; K02653; -. DR OMA; TRQMATM; -. DR OrthoDB; EOG6Z6FTM; -. DR BioCyc; NMEN122586:GHGG-354-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR003004; GspF/PilC. DR InterPro; IPR018076; T2SS_F. DR InterPro; IPR001992; Type_2_secretion_system_CS. DR Pfam; PF00482; T2SSF; 2. DR PRINTS; PR00812; BCTERIALGSPF. DR PROSITE; PS00874; T2SP_F; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003923}. FT TRANSMEM 175 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 382 402 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 75 198 T2SSF. {ECO:0000259|Pfam:PF00482}. FT DOMAIN 281 401 T2SSF. {ECO:0000259|Pfam:PF00482}. SQ SEQUENCE 410 AA; 45273 MW; 47F0215A52153DDB CRC64; MAKNGGFSLF AKKEKRFIFE GRHSASDKLV NGEVSAFTEE EARKKLAKRG IRPLQITRVK TSSKRKITQE DITVFTRQLS TMIKAGLPLM QAFEIVARGH GNPSMTEMLM EIRGEVEQGS SLSRAFSNHP KYFDRFYCNL VAAGETGGVL ESLLDKLAIY KEKTQAIRKK VKTALTYPVS VIAVAIGLVF VMMIFVLPAF KEVYANMGAE LPALTQTVMD MSDFFVSYGW MVLIALGFAI YGFLKLKARS IKIQRRMDAI LLRMPIFGDI VRKGTIARWG RTTATLIAAG VPLVDVLDST AGAAGNLIYE EATREIRTRV IQGLSMTSGM RATELFPNMM LQMSSIGEES GSLDDMLNKA AEFYEDEVDN AVGRLSAMME PIIIVILGLV IGTLLVAMYL PLFNLGNVVA // ID Q9JZ66_NEIMB Unreviewed; 70 AA. AC Q9JZ66; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Putative mercury transport periplasmic protein {ECO:0000313|EMBL:AAF41648.1}; GN OrderedLocusNames=NMB1271 {ECO:0000313|EMBL:AAF41648.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41648.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41648.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41648.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41648.1; -; Genomic_DNA. DR PIR; A81103; A81103. DR RefSeq; NP_274292.1; NC_003112.2. DR RefSeq; WP_002217091.1; NC_003112.2. DR ProteinModelPortal; Q9JZ66; -. DR STRING; 122586.NMB1271; -. DR PaxDb; Q9JZ66; -. DR EnsemblBacteria; AAF41648; AAF41648; NMB1271. DR GeneID; 903693; -. DR KEGG; nme:NMB1271; -. DR PATRIC; 20358159; VBINeiMen85645_1591. DR eggNOG; ENOG410681U; Bacteria. DR eggNOG; ENOG410XUQ1; LUCA. DR HOGENOM; HOG000038877; -. DR KO; K07213; -. DR OMA; MANQTRI; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NMEN122586:GHGG-1309-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR InterPro; IPR001802; MerP/CopZ. DR Pfam; PF00403; HMA; 1. DR PRINTS; PR00946; HGSCAVENGER. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 69 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 70 AA; 7075 MW; 97463EFB237DFD9D CRC64; METLILDIGG MSCGGCVKSV TRILEGVKGV ASVEVSLENK SATVGYDPAQ TDAGALIEAV EDGGYDAALK // ID Q9JYB1_NEIMB Unreviewed; 128 AA. AC Q9JYB1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42014.1}; GN OrderedLocusNames=NMB1665 {ECO:0000313|EMBL:AAF42014.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42014.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42014.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42014.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42014.1; -; Genomic_DNA. DR PIR; C81056; C81056. DR RefSeq; NP_274670.1; NC_003112.2. DR RefSeq; WP_002212659.1; NC_003112.2. DR ProteinModelPortal; Q9JYB1; -. DR STRING; 122586.NMB1665; -. DR PaxDb; Q9JYB1; -. DR EnsemblBacteria; AAF42014; AAF42014; NMB1665. DR GeneID; 903445; -. DR KEGG; nme:NMB1665; -. DR PATRIC; 20359270; VBINeiMen85645_2143. DR eggNOG; ENOG4105VD2; Bacteria. DR eggNOG; COG3744; LUCA. DR HOGENOM; HOG000253626; -. DR OMA; SEDRNMP; -. DR OrthoDB; EOG65TRZD; -. DR BioCyc; NMEN122586:GHGG-1719-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF01850; PIN; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 4 119 PINc. {ECO:0000259|Pfam:PF01850}. SQ SEQUENCE 128 AA; 14696 MW; E7C6BB5467A5C169 CRC64; MRKILLDTHA LLWWLLDDKK LGISARKLIE NPRNAIFVSA ASIWEISIKQ NKGLLKLPEE FFDVLQEEDF EMLPIGLFHA KQAGSLPEIH KDPFDRMLIA QTQAEGFELM TVDEYIPQYG IRVVNASS // ID Q9JZV2_NEIMB Unreviewed; 313 AA. AC Q9JZV2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41298.1}; GN OrderedLocusNames=NMB0888 {ECO:0000313|EMBL:AAF41298.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41298.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41298.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41298.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41298.1; -; Genomic_DNA. DR PIR; G81145; G81145. DR RefSeq; NP_273929.1; NC_003112.2. DR RefSeq; WP_002244084.1; NC_003112.2. DR STRING; 122586.NMB0888; -. DR PaxDb; Q9JZV2; -. DR EnsemblBacteria; AAF41298; AAF41298; NMB0888. DR GeneID; 903007; -. DR KEGG; nme:NMB0888; -. DR PATRIC; 20357183; VBINeiMen85645_1105. DR eggNOG; COG4966; LUCA. DR HOGENOM; HOG000218895; -. DR KO; K02672; -. DR OMA; GGNVCAN; -. DR OrthoDB; EOG6DC6G8; -. DR BioCyc; NMEN122586:GHGG-924-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 43 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 313 AA; 34360 MW; FDDCACC8034CD6CE CRC64; MRRKMLNVPK GSYDGMKGFT IIEFLVAGLL SMIVLMAVGS SYFTSRKLND AANERLAAQQ DLRNAATLIV RDARMAGGFG CFNMSEHPAT DVIPDTTQQN SPFSLKRNGI DKLIPIAESS NINYQNFFQV GSALIFQYGI DDVNASTATT VVSSCAAISK PGKQIPTLED AKKELKIPDQ DKEQNGNIAR QRHVVNAYAV GRIADEEGLF RFQLDDKGKW GNPQLLVKKV RHMKVRYIYV SGCPEDDDAG KEETFKYTDK FDSAQNAVTP AGVEVLLSSG TDTKIAASSD NHIYAYRIDA TIRGGNVCAN RTL // ID Q9K1H1_NEIMB Unreviewed; 166 AA. AC Q9K1H1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Putative outer membrane protein OmpH {ECO:0000313|EMBL:AAF40638.1}; GN OrderedLocusNames=NMB0181 {ECO:0000313|EMBL:AAF40638.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40638.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40638.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40638.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the skp family. CC {ECO:0000256|PIRNR:PIRNR002094}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40638.1; -; Genomic_DNA. DR PIR; F81228; F81228. DR RefSeq; NP_273239.1; NC_003112.2. DR RefSeq; WP_002216262.1; NC_003112.2. DR ProteinModelPortal; Q9K1H1; -. DR STRING; 122586.NMB0181; -. DR PaxDb; Q9K1H1; -. DR EnsemblBacteria; AAF40638; AAF40638; NMB0181. DR GeneID; 902288; -. DR KEGG; nme:NMB0181; -. DR PATRIC; 20355387; VBINeiMen85645_0223. DR eggNOG; ENOG4108RFI; Bacteria. DR eggNOG; COG2825; LUCA. DR HOGENOM; HOG000261755; -. DR KO; K06142; -. DR OMA; ESKQARN; -. DR OrthoDB; EOG6F297R; -. DR BioCyc; NMEN122586:GHGG-191-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR005632; Chaperone_Skp. DR InterPro; IPR024930; Skp_domain. DR Pfam; PF03938; OmpH; 1. DR PIRSF; PIRSF002094; OMP26_Skp; 1. DR SMART; SM00935; OmpH; 1. DR SUPFAM; SSF111384; SSF111384; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 166 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004328384. FT COILED 62 87 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 166 AA; 19131 MW; A69F1C5F517F1CC2 CRC64; MTRLTRAFAA ALIGLCCTAG AHADTFQKIG FINTERIYLE SKQARKIQKT LDSEFSARQD ELQKLQREGL DLERQLAEGK LRNAKKAQAE EKWRGLVAAF RKKQAQFEED YNLRRNEEFA SLQQNANRVI VKIAKQEGYD VILQNVIYVN TQYDVTDSVI KEMNAR // ID Q9JXA5_NEIMB Unreviewed; 86 AA. AC Q9JXA5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42457.1}; GN OrderedLocusNames=NMB2149 {ECO:0000313|EMBL:AAF42457.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42457.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42457.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42457.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42457.1; -; Genomic_DNA. DR PIR; C81000; C81000. DR RefSeq; NP_275134.1; NC_003112.2. DR RefSeq; WP_002215156.1; NC_003112.2. DR PaxDb; Q9JXA5; -. DR EnsemblBacteria; AAF42457; AAF42457; NMB2149. DR GeneID; 903223; -. DR KEGG; nme:NMB2149; -. DR PATRIC; 20360492; VBINeiMen85645_2742. DR HOGENOM; HOG000027919; -. DR OMA; MVDIFED; -. DR OrthoDB; EOG615VJ7; -. DR BioCyc; NMEN122586:GHGG-2214-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 86 AA; 10011 MW; 8FC2DBC9C1C62FE8 CRC64; MRQISLTDYF CKGLYLFDIF EDIVFLGKRL FTVRKFLDFS ELLEMVNTQG YFLEFLYLYS GLNLNQYGVA SPCRTICTVC GFVALS // ID Q9JXX8_NEIMB Unreviewed; 40 AA. AC Q9JXX8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42179.1}; GN OrderedLocusNames=NMB1844 {ECO:0000313|EMBL:AAF42179.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42179.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42179.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42179.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42179.1; -; Genomic_DNA. DR PIR; D81036; D81036. DR RefSeq; NP_274841.1; NC_003112.2. DR RefSeq; WP_010980997.1; NC_003112.2. DR STRING; 122586.NMB1844; -. DR PaxDb; Q9JXX8; -. DR EnsemblBacteria; AAF42179; AAF42179; NMB1844. DR GeneID; 903255; -. DR KEGG; nme:NMB1844; -. DR BioCyc; NMEN122586:GHGG-1899-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 40 AA; 4915 MW; A9539D26C9E17E72 CRC64; MRFIAYCCYM FVLLYNGCIK IYAHRLSRRF ESLIFDNLET // ID Q9JZX6_NEIMB Unreviewed; 58 AA. AC Q9JZX6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41268.1}; GN OrderedLocusNames=NMB0857 {ECO:0000313|EMBL:AAF41268.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41268.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41268.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41268.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41268.1; -; Genomic_DNA. DR PIR; D81150; D81150. DR RefSeq; NP_273898.1; NC_003112.2. DR RefSeq; WP_002213901.1; NC_003112.2. DR STRING; 122586.NMB0857; -. DR PaxDb; Q9JZX6; -. DR EnsemblBacteria; AAF41268; AAF41268; NMB0857. DR GeneID; 902971; -. DR KEGG; nme:NMB0857; -. DR PATRIC; 20357107; VBINeiMen85645_1072. DR OrthoDB; EOG6V1MDS; -. DR BioCyc; NMEN122586:GHGG-888-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 58 AA; 6854 MW; C2423381523D6882 CRC64; MGEYLEFEES GTKITVEIGS AWHFNETIRN INTHLRGTKL PGSNWRVQDK GHFHLWKR // ID Q9JXF3_NEIMB Unreviewed; 67 AA. AC Q9JXF3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42392.1}; GN OrderedLocusNames=NMB2073 {ECO:0000313|EMBL:AAF42392.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42392.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42392.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42392.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42392.1; -; Genomic_DNA. DR PIR; H81008; H81008. DR STRING; 122586.NMB2073; -. DR PaxDb; Q9JXF3; -. DR EnsemblBacteria; AAF42392; AAF42392; NMB2073. DR PATRIC; 20360306; VBINeiMen85645_2653. DR HOGENOM; HOG000152749; -. DR OMA; LQKICIY; -. DR OrthoDB; EOG6P073Q; -. DR BioCyc; NMEN122586:GHGG-2136-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 67 AA; 7441 MW; 46100954377AA280 CRC64; MTTLSAPNRT DVQTRATLFP SGTKPSAMPA DPDLSDTMKV CRPESQTSAD RLICLFFIVL QKICIYF // ID Q9JY31_NEIMB Unreviewed; 138 AA. AC Q9JY31; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42108.1}; GN OrderedLocusNames=NMB1767 {ECO:0000313|EMBL:AAF42108.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42108.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42108.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42108.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42108.1; -; Genomic_DNA. DR PIR; E81045; E81045. DR RefSeq; NP_274767.1; NC_003112.2. DR RefSeq; WP_002224040.1; NC_003112.2. DR STRING; 122586.NMB1767; -. DR PaxDb; Q9JY31; -. DR EnsemblBacteria; AAF42108; AAF42108; NMB1767. DR GeneID; 903331; -. DR KEGG; nme:NMB1767; -. DR HOGENOM; HOG000071293; -. DR OrthoDB; EOG6SR94H; -. DR BioCyc; NMEN122586:GHGG-1822-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 138 AA; 16948 MW; FDAD3CEA4DBA2F38 CRC64; MNKNILYIFS LLITIVIFFI FEKNVIRKIS FNYNKKEFLI SDITNFNWDY VKLYIINSDF QKIVFYHKSK IVFEELIELD KEGNVLPQYL FDSDLKNVEY YECDYKNGKM QLLKKEKSHF FDGYFYYYKP INCRPKLL // ID Q7DD68_NEIMB Unreviewed; 116 AA. AC Q7DD68; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Protein-export membrane protein SecG {ECO:0000313|EMBL:AAF42222.1}; GN Name=secG {ECO:0000313|EMBL:AAF42222.1}; GN OrderedLocusNames=NMB1888 {ECO:0000313|EMBL:AAF42222.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42222.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42222.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42222.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42222.1; -; Genomic_DNA. DR PIR; F81031; F81031. DR RefSeq; NP_274884.1; NC_003112.2. DR RefSeq; WP_002214678.1; NC_003112.2. DR STRING; 122586.NMB1888; -. DR PaxDb; Q7DD68; -. DR EnsemblBacteria; AAF42222; AAF42222; NMB1888. DR GeneID; 904290; -. DR KEGG; nme:NMB1888; -. DR PATRIC; 20359811; VBINeiMen85645_2411. DR eggNOG; ENOG4107M8V; Bacteria. DR eggNOG; COG1314; LUCA. DR HOGENOM; HOG000071344; -. DR KO; K03075; -. DR OMA; NFMSRAT; -. DR OrthoDB; EOG6CCHB4; -. DR BioCyc; NMEN122586:GHGG-1944-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR004692; SecG. DR Pfam; PF03840; SecG; 1. DR PRINTS; PR01651; SECGEXPORT. DR TIGRFAMs; TIGR00810; secG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 78 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 116 AA; 12137 MW; 10119F4598392861 CRC64; MEAFKTLIWI VNIISALAVI VLVLLQHGKG ADAGATFGSG SGSAQGVFGS AGNANFLSRS TAVAATFFFA TCMAMVYIHT HTTKHGLDFS NVQQTQQAPK PVSNTEPSAP VPQQQK // ID Q9JY65_NEIMB Unreviewed; 210 AA. AC Q9JY65; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Trancscriptional regulator MtrR {ECO:0000313|EMBL:AAF42064.1}; GN Name=mtrR {ECO:0000313|EMBL:AAF42064.1}; GN OrderedLocusNames=NMB1717 {ECO:0000313|EMBL:AAF42064.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42064.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42064.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42064.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42064.1; -; Genomic_DNA. DR PIR; G81049; G81049. DR RefSeq; NP_274720.1; NC_003112.2. DR RefSeq; WP_002216625.1; NC_003112.2. DR ProteinModelPortal; Q9JY65; -. DR PaxDb; Q9JY65; -. DR EnsemblBacteria; AAF42064; AAF42064; NMB1717. DR GeneID; 903385; -. DR KEGG; nme:NMB1717; -. DR PATRIC; 20359395; VBINeiMen85645_2203. DR eggNOG; ENOG4108BYM; Bacteria. DR eggNOG; COG1309; LUCA. DR HOGENOM; HOG000260115; -. DR KO; K03577; -. DR OMA; MMEIIFH; -. DR OrthoDB; EOG6SNDRN; -. DR BioCyc; NMEN122586:GHGG-1772-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. DR InterPro; IPR013572; Tscrpt_reg_MAATS_C. DR Pfam; PF08361; TetR_C_2; 1. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF48498; SSF48498; 1. DR PROSITE; PS01081; HTH_TETR_1; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transcription {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}; KW Transcription regulation {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}. FT DOMAIN 9 69 HTH tetR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50977}. SQ SEQUENCE 210 AA; 24374 MW; 2A862C72905A5527 CRC64; MRKTKTEALK TKEHLMLAAL ETFYRKGIAR TSLNEIAQAA GVTRGALYWH FKNKEDLFDA LFQRICDDIE NCIAQDAEDA EGGSWAVFRH TLLHFFERLQ SNDIYYKFHN ILFLKCEHTE QNAAVIAIAR KHQAIWREKI TAVLTEAVEN QDLADDLDKE TAVIFIKSTL DGLIWRWFSS CERFDLGKTA PRIIGIMMDN LENHPDLRRK // ID Q9JYU9_NEIMB Unreviewed; 457 AA. AC Q9JYU9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=Putative ATP-dependent RNA helicase {ECO:0000313|EMBL:AAF41783.1}; GN OrderedLocusNames=NMB1422 {ECO:0000313|EMBL:AAF41783.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41783.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41783.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41783.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41783.1; -; Genomic_DNA. DR PIR; H81085; H81085. DR RefSeq; NP_274434.1; NC_003112.2. DR RefSeq; WP_002216952.1; NC_003112.2. DR ProteinModelPortal; Q9JYU9; -. DR STRING; 122586.NMB1422; -. DR PaxDb; Q9JYU9; -. DR EnsemblBacteria; AAF41783; AAF41783; NMB1422. DR GeneID; 903844; -. DR KEGG; nme:NMB1422; -. DR PATRIC; 20358533; VBINeiMen85645_1778. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR HOGENOM; HOG000268807; -. DR OMA; YMVPRGW; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; NMEN122586:GHGG-1460-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41783.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Helicase {ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:AAF41783.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41783.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAF41783.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 3 31 Q_MOTIF. {ECO:0000259|PROSITE:PS51195}. FT DOMAIN 34 212 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 239 388 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 457 AA; 50984 MW; 292B765F516B0B4D CRC64; MSNPFSSLGL GTELVSALTA QGYENPTPIQ AAAIPKALAG HDLLAAAQTG TGKTAAFMLP SLERLKRYAT ASTSPAMHPV RMLVLTPTRE LADQIDQNVQ GYIKNLPLRH TVLFGGMNMD KQTADLRAGC EIVVATVGRL LDHVKQKNIH LNKVEIVVLD EADRMLDMGF IDDIRKIMQM LPRQRQTLLF SATFSAPIRK LAQDFMNAPE TVEVAAQNTT NANVEQHIIA VDTIQKRNLL ERLIVDLHMN QVIVFCKTKQ SVDRVTRELV RRNLSAQAIH GDRSQQSRLE TLNAFKDGNL RVLVATDIAA RGLDIAELPF VINYEMPAQP EDYVHRIGRT GRAGADGVAI SLMDESEQKM FESIKELTGN KLLIERIEGF EPQWWEQGGA KPEKPEMREP RQRNRYESAK AQREKNTRPE NAANDAGAAC GKIAGRSRRS RREHRTCALL QPRYGVK // ID Q7DDN5_NEIMB Unreviewed; 59 AA. AC Q7DDN5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40952.1}; GN OrderedLocusNames=NMB0520 {ECO:0000313|EMBL:AAF40952.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40952.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40952.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40952.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40952.1; -; Genomic_DNA. DR PIR; B81189; B81189. DR STRING; 122586.NMB0520; -. DR PaxDb; Q7DDN5; -. DR EnsemblBacteria; AAF40952; AAF40952; NMB0520. DR PATRIC; 20356281; VBINeiMen85645_0660. DR OrthoDB; EOG6ZD6D7; -. DR BioCyc; NMEN122586:GHGG-545-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 59 AA; 7194 MW; 3737C8DCA0888292 CRC64; MHSHYIFGIL MISYVFAMLF NFIISYKIFK EEKLINGFFD FLIKSSYLNF KYFNILFGK // ID Q9JZR2_NEIMB Unreviewed; 162 AA. AC Q9JZR2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41339.1}; GN OrderedLocusNames=NMB0932 {ECO:0000313|EMBL:AAF41339.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41339.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41339.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41339.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41339.1; -; Genomic_DNA. DR PIR; G81141; G81141. DR RefSeq; NP_273971.1; NC_003112.2. DR RefSeq; WP_002225333.1; NC_003112.2. DR STRING; 122586.NMB0932; -. DR PaxDb; Q9JZR2; -. DR EnsemblBacteria; AAF41339; AAF41339; NMB0932. DR GeneID; 903053; -. DR KEGG; nme:NMB0932; -. DR PATRIC; 20357333; VBINeiMen85645_1181. DR eggNOG; ENOG4105NH4; Bacteria. DR eggNOG; COG2839; LUCA. DR HOGENOM; HOG000023032; -. DR KO; K09793; -. DR OMA; FEYLSGR; -. DR OrthoDB; EOG64NB1M; -. DR BioCyc; NMEN122586:GHGG-970-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007403; DUF456. DR Pfam; PF04306; DUF456; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 159 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 162 AA; 16508 MW; 1335C0A69D407063 CRC64; MTVLTVILAL ALIAVGTAGI VYPALPGLAL MFAGTWLLAY AGGYQIYGAG VLWTVGLISL AGILADYVAG IWGTKYTGAG KLAVRGALAG SIIGIFFSLP GLILGPFIGA AAGELIERRN MLQAGKAGLG TLLGLVVGTA FKIGCAVSIL FILLVKYIAY LF // ID Q9K124_NEIMB Unreviewed; 125 AA. AC Q9K124; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40812.1}; GN OrderedLocusNames=NMB0370 {ECO:0000313|EMBL:AAF40812.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40812.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40812.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40812.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40812.1; -; Genomic_DNA. DR PIR; H81206; H81206. DR RefSeq; NP_273419.1; NC_003112.2. DR RefSeq; WP_002224901.1; NC_003112.2. DR STRING; 122586.NMB0370; -. DR PaxDb; Q9K124; -. DR EnsemblBacteria; AAF40812; AAF40812; NMB0370. DR GeneID; 902485; -. DR KEGG; nme:NMB0370; -. DR PATRIC; 20355899; VBINeiMen85645_0467. DR eggNOG; ENOG41077X7; Bacteria. DR eggNOG; ENOG410Z4X8; LUCA. DR HOGENOM; HOG000219105; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NMEN122586:GHGG-392-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 74 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 125 AA; 15349 MW; 2C21F54FBEA03B99 CRC64; MCEFKDIIRN VPYFEGYDEN SFIGKWYDDG VWDDEEYWKL ENDLIEVRKK YPYPMDIPRY VVIGIGTIID FLMVPNWKLF EIKASPWLPD SVGIHERYER FTTMLRYIFT EKDIVNVRFD YYNKK // ID Q9JXE0_NEIMB Unreviewed; 210 AA. AC Q9JXE0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42409.1}; GN OrderedLocusNames=NMB2092 {ECO:0000313|EMBL:AAF42409.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42409.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42409.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42409.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42409.1; -; Genomic_DNA. DR PIR; B81008; B81008. DR RefSeq; NP_275080.1; NC_003112.2. DR RefSeq; WP_002225720.1; NC_003112.2. DR STRING; 122586.NMB2092; -. DR PaxDb; Q9JXE0; -. DR EnsemblBacteria; AAF42409; AAF42409; NMB2092. DR GeneID; 903956; -. DR KEGG; nme:NMB2092; -. DR PATRIC; 20360354; VBINeiMen85645_2674. DR HOGENOM; HOG000218712; -. DR OMA; NTPAKPH; -. DR OrthoDB; EOG6D2KT6; -. DR BioCyc; NMEN122586:GHGG-2157-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 55 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 210 AA; 22743 MW; 794C7D47E3A4FE53 CRC64; MPSEPPSDGI ARHPKSTIKM AKKPNKPFRL TPKLLIRAVL LICIAAIGAL AIGIVSTFNP NGDKTLQAEP QHTDSPRETE FWLPNGVVGQ DAAQPEHHHA ASSEPAQPDG TDESGSGLPS PAAPKKNRVK PQPADTAQTD RQPDDAGTQA ENTLKETPVL PTNVPRPEPR KETPEKQAQP KETPKENHTK PDTPKNTPPK PHKEILDNLF // ID Q9K162_NEIMB Unreviewed; 228 AA. AC Q9K162; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40761.1}; GN OrderedLocusNames=NMB0316 {ECO:0000313|EMBL:AAF40761.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40761.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40761.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40761.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40761.1; -; Genomic_DNA. DR PIR; B81214; B81214. DR RefSeq; NP_273365.1; NC_003112.2. DR RefSeq; WP_002224864.1; NC_003112.2. DR STRING; 122586.NMB0316; -. DR PaxDb; Q9K162; -. DR EnsemblBacteria; AAF40761; AAF40761; NMB0316. DR GeneID; 902432; -. DR KEGG; nme:NMB0316; -. DR PATRIC; 20355761; VBINeiMen85645_0400. DR eggNOG; ENOG4105EX9; Bacteria. DR eggNOG; COG1738; LUCA. DR HOGENOM; HOG000284591; -. DR KO; K09125; -. DR OMA; GEFNLFV; -. DR OrthoDB; EOG65J51G; -. DR BioCyc; NMEN122586:GHGG-336-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003744; DUF165. DR Pfam; PF02592; Vut_1; 1. DR TIGRFAMs; TIGR00697; TIGR00697; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 205 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 228 AA; 25624 MW; E815289300DF2345 CRC64; MYAFTAAQQQ KALFRLVLFH ILIIAASNYL VQFPFQIFGI HTTWGAFSFP FIFLATDLTV RIFGSHLARR IIFWVMFPAL LLSYVFSVLF HNGSWTGLGA LSEFNTFVGR IALASFAAYA IGQILDIFVF NKLRRLKAWW IAPTASTVIG NALDTLVFFA VAFYASSDGF MAANWQGIAF VDYLFKLTVC TLFFLPAYGV ILNLLTKKLT TLQTKQAQDR PAPSLQNP // ID Q9K031_NEIMB Unreviewed; 69 AA. AC Q9K031; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41206.1}; GN OrderedLocusNames=NMB0793 {ECO:0000313|EMBL:AAF41206.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41206.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41206.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41206.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41206.1; -; Genomic_DNA. DR PIR; H81156; H81156. DR RefSeq; NP_273835.1; NC_003112.2. DR RefSeq; WP_010980848.1; NC_003112.2. DR STRING; 122586.NMB0793; -. DR PaxDb; Q9K031; -. DR EnsemblBacteria; AAF41206; AAF41206; NMB0793. DR GeneID; 902908; -. DR KEGG; nme:NMB0793; -. DR BioCyc; NMEN122586:GHGG-824-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 69 AA; 8598 MW; 235311673FD3CC69 CRC64; MHLFPIYPIF PLTYQSHLIN KTDKSFTIYL HYIRLQIYSN QLQKRRFHKP FRIARHKRKT DFVALKEYS // ID Q9K1M1_NEIMB Unreviewed; 490 AA. AC Q9K1M1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504}; DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504}; GN Name=pykA {ECO:0000313|EMBL:AAF40552.1}; GN OrderedLocusNames=NMB0089 {ECO:0000313|EMBL:AAF40552.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40552.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40552.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40552.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC {ECO:0000256|RuleBase:RU000504}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC {ECO:0000256|RuleBase:RU000504}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. CC {ECO:0000256|RuleBase:RU000504}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40552.1; -; Genomic_DNA. DR PIR; B81239; B81239. DR RefSeq; NP_273151.1; NC_003112.2. DR RefSeq; WP_002221820.1; NC_003112.2. DR ProteinModelPortal; Q9K1M1; -. DR STRING; 122586.NMB0089; -. DR PaxDb; Q9K1M1; -. DR EnsemblBacteria; AAF40552; AAF40552; NMB0089. DR GeneID; 902193; -. DR KEGG; nme:NMB0089; -. DR PATRIC; 20355187; VBINeiMen85645_0127. DR eggNOG; ENOG4105CA9; Bacteria. DR eggNOG; COG0469; LUCA. DR HOGENOM; HOG000021558; -. DR KO; K00873; -. DR OMA; EKMPSVN; -. DR OrthoDB; EOG6GBMB0; -. DR BioCyc; NMEN122586:GHGG-95-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC. DR Gene3D; 2.40.33.10; -; 1. DR Gene3D; 3.20.20.60; -; 2. DR Gene3D; 3.40.1380.20; -; 1. DR InterPro; IPR001697; Pyr_Knase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR InterPro; IPR015794; Pyrv_Knase_a/b. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR015806; Pyrv_Knase_insert_dom. DR PANTHER; PTHR11817; PTHR11817; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 2. DR SUPFAM; SSF52935; SSF52935; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glycolysis {ECO:0000256|RuleBase:RU000504}; KW Kinase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AAF40552.1}; KW Magnesium {ECO:0000256|RuleBase:RU000504}; KW Pyruvate {ECO:0000313|EMBL:AAF40552.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|RuleBase:RU000504, KW ECO:0000313|EMBL:AAF40552.1}. FT DOMAIN 13 355 PK. {ECO:0000259|Pfam:PF00224}. FT DOMAIN 375 487 PK_C. {ECO:0000259|Pfam:PF02887}. SQ SEQUENCE 490 AA; 52435 MW; 0A391AA653D28C12 CRC64; MNQTSRDLTR ISHNTKIVAT LGPGSNNVEL LEDMIRVGGL NVVRFNFSHG TPEFHQENAL IVREAAKRAG QEIAIIADLQ GPKIRVGKIA GGGIELNKGE TLVLDAALEG EGTREAVGLD YRDLPDDVAA GDVLWLDDGL LTLTVESVEG SRIITRVENS HVLKSNKGIN KRGGGLSAGA LTEKDFRDLK TAIAIGCDYL AISFVKSAED LHIARAKVEE EMKGSTAVRP GLVSKIERVE AIENLDEIIL AGDGIMVARG DLAVEVGHAA VPALQKRMIR RARELRRFSI TATQMMESMI TNPVPTRAEV SDVANAVLDG TDAVMCSAET AVGAYPFETV SQMAIICAAA EKEQDSLNGV AEQVEYPEAV STNLAVAGGA VSVARAVHAK AIVALTESGS TAFEISRHNI TLPIFALTPS VSAQRRMAMY RGVRPLILAT STDHDTALNE VETMLVEHNI LHSGDQYIIT SGSQMRESGS TNTLEVLRVK // ID Q9JY85_NEIMB Unreviewed; 326 AA. AC Q9JY85; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42043.1}; GN OrderedLocusNames=NMB1695 {ECO:0000313|EMBL:AAF42043.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42043.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42043.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42043.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42043.1; -; Genomic_DNA. DR PIR; A81052; A81052. DR PaxDb; Q9JY85; -. DR EnsemblBacteria; AAF42043; AAF42043; NMB1695. DR BioCyc; NMEN122586:GHGG-1750-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 326 AA; 35988 MW; 620FC1B92CEEEBFF CRC64; MELQQRTLTI GLGNDIAVQT EGVGFIRGQL VADHAEINSV FKVVVKAALI VVKTLFADGY PHAIFQRFLM PDNRNRQHRA DKAVGLVGIA DDAEIRIAFC LISNAFFFTE LIIGIGCGKA DCGHFFVVFA AGSASVHKVS DFQNEFAVKP FAGKQHPHQY IGNHAGINRP PIISPQPCQQ SGKRPVDYKK YAPNLRYPAG IAHGFFRQVG LLQPRKFFNH RLPGKQAAAE HRQHHQIDED GIPIHRIMPP EHQYCGKKQC NKQSRITLLG QFGSQGAQQP QPAHRRRQPN KPARLPAVYS GLTKTSTALP RLAVLSAASS PCPDFC // ID Q9K059_NEIMB Unreviewed; 75 AA. AC Q9K059; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41174.1}; GN OrderedLocusNames=NMB0761 {ECO:0000313|EMBL:AAF41174.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41174.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41174.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41174.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41174.1; -; Genomic_DNA. DR PIR; F81161; F81161. DR RefSeq; NP_273803.1; NC_003112.2. DR RefSeq; WP_010980839.1; NC_003112.2. DR STRING; 122586.NMB0761; -. DR PaxDb; Q9K059; -. DR EnsemblBacteria; AAF41174; AAF41174; NMB0761. DR GeneID; 902876; -. DR KEGG; nme:NMB0761; -. DR BioCyc; NMEN122586:GHGG-792-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 75 AA; 8546 MW; 661E63F1FAB3C70E CRC64; MVLGEYYAVA GHIGFGGKAD ARHMGNDPRR ALVHPPFLPD FGQHIFFHRA LEPENRWKRM AGRPRTSAAR AFCRQ // ID Q9JXL2_NEIMB Unreviewed; 321 AA. AC Q9JXL2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Iron(III) ABC transporter, periplasmic binding protein {ECO:0000313|EMBL:AAF42316.1}; GN OrderedLocusNames=NMB1989 {ECO:0000313|EMBL:AAF42316.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42316.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42316.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42316.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains Fe/B12 periplasmic-binding domain. CC {ECO:0000256|SAAS:SAAS00514624}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42316.1; -; Genomic_DNA. DR PIR; D81018; D81018. DR RefSeq; NP_274981.1; NC_003112.2. DR RefSeq; WP_010981017.1; NC_003112.2. DR ProteinModelPortal; Q9JXL2; -. DR STRING; 122586.NMB1989; -. DR PaxDb; Q9JXL2; -. DR PRIDE; Q9JXL2; -. DR EnsemblBacteria; AAF42316; AAF42316; NMB1989. DR GeneID; 904142; -. DR KEGG; nme:NMB1989; -. DR PATRIC; 20360073; VBINeiMen85645_2541. DR eggNOG; ENOG4105KVJ; Bacteria. DR eggNOG; COG4607; LUCA. DR HOGENOM; HOG000099140; -. DR KO; K02016; -. DR OMA; AWKKGQV; -. DR OrthoDB; EOG61VZ9F; -. DR BioCyc; NMEN122586:GHGG-2046-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 61 321 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. SQ SEQUENCE 321 AA; 34153 MW; 04B9244DEB8E4686 CRC64; MLRLTALAVC TALALGACSP QNSDSAPQAK EQAVSAAQTE GASVTVKTAR GDVQIPQNPE RIAVYDLGML DTLSKLGVKT GLSVDKNRLP YLEEYFKTTK PAGTLFEPDY ETLNAYKPQL IIIGSRAAKA FDKLNEIAPT IEMTADTANL KESAKERIDA LAQIFGKQAE ADKLKAEIDA SFEAAKTAAQ GKGKGLVILV NGGKMSAFGP SSRLGGWLHK DIGVPAVDES IKEGSHGQPI SFEYLKEKNP DWLFVLDRSA AIGEEGQAAK DVLDNPLVAE TTAWKKGQVV YLVPETYLAA GGAQELLNAS KQVADAFNAA K // ID Q9K0I6_NEIMB Unreviewed; 35 AA. AC Q9K0I6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41040.1}; GN OrderedLocusNames=NMB0613 {ECO:0000313|EMBL:AAF41040.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41040.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41040.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41040.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41040.1; -; Genomic_DNA. DR PIR; F81179; F81179. DR RefSeq; NP_273657.1; NC_003112.2. DR RefSeq; WP_010980819.1; NC_003112.2. DR PaxDb; Q9K0I6; -. DR EnsemblBacteria; AAF41040; AAF41040; NMB0613. DR GeneID; 902727; -. DR KEGG; nme:NMB0613; -. DR BioCyc; NMEN122586:GHGG-639-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 35 AA; 4022 MW; A3677246569B6306 CRC64; MTGSACFLQP IFCLDDMARQ PVSFRPKIHL IKQTQ // ID Q9JYR0_NEIMB Unreviewed; 181 AA. AC Q9JYR0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41827.1}; GN OrderedLocusNames=NMB1470 {ECO:0000313|EMBL:AAF41827.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41827.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41827.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41827.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41827.1; -; Genomic_DNA. DR PIR; A81081; A81081. DR RefSeq; NP_274479.1; NC_003112.2. DR RefSeq; WP_002225098.1; NC_003112.2. DR STRING; 122586.NMB1470; -. DR PaxDb; Q9JYR0; -. DR EnsemblBacteria; AAF41827; AAF41827; NMB1470. DR GeneID; 903892; -. DR KEGG; nme:NMB1470; -. DR PATRIC; 20358703; VBINeiMen85645_1861. DR HOGENOM; HOG000071265; -. DR OMA; SENMAEQ; -. DR OrthoDB; EOG6K4016; -. DR BioCyc; NMEN122586:GHGG-1510-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 181 AA; 19421 MW; 0DE2881CAE963A58 CRC64; MLKTSFAVLG GCLLLAACGK SENTAEQPQN AVQSAPKPVF KVKYIDNTAI AGLDLGQSSE GKTNDGKKQI SYPIKGLPEQ NVIRLIGKHP GDLEAVSGKC METDDKDSPA GWAENGVCHT LFAKLVGNIA EDGGKLTDYL VSHAALQPYQ AGKSGYAAVQ NGRYVLEIDS EGAFYFRRRH Y // ID Q9K130_NEIMB Unreviewed; 45 AA. AC Q9K130; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40806.1}; GN OrderedLocusNames=NMB0363 {ECO:0000313|EMBL:AAF40806.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40806.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40806.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40806.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40806.1; -; Genomic_DNA. DR PIR; B81209; B81209. DR RefSeq; NP_273412.1; NC_003112.2. DR RefSeq; WP_010980784.1; NC_003112.2. DR STRING; 122586.NMB0363; -. DR PaxDb; Q9K130; -. DR EnsemblBacteria; AAF40806; AAF40806; NMB0363. DR GeneID; 902479; -. DR KEGG; nme:NMB0363; -. DR BioCyc; NMEN122586:GHGG-385-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 45 AA; 5176 MW; 6D0D2C623309081E CRC64; MKRLRAEIYA DALSFPYILC VVKVQAALKS VLPSMNHHFV LFQRA // ID Q9K1B5_NEIMB Unreviewed; 753 AA. AC Q9K1B5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 102. DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525}; DE EC=1.6.5.11 {ECO:0000256|RuleBase:RU003525}; GN Name=nuoG {ECO:0000313|EMBL:AAF40703.1}; GN OrderedLocusNames=NMB0249 {ECO:0000313|EMBL:AAF40703.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40703.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40703.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40703.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000256|RuleBase:RU003525}. CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000256|RuleBase:RU004523}. CC -!- SIMILARITY: Contains 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000256|SAAS:SAAS00509203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40703.1; -; Genomic_DNA. DR PIR; D81219; D81219. DR RefSeq; NP_273305.1; NC_003112.2. DR RefSeq; WP_002224833.1; NC_003112.2. DR ProteinModelPortal; Q9K1B5; -. DR STRING; 122586.NMB0249; -. DR PaxDb; Q9K1B5; -. DR DNASU; 902360; -. DR EnsemblBacteria; AAF40703; AAF40703; NMB0249. DR GeneID; 902360; -. DR KEGG; nme:NMB0249; -. DR PATRIC; 20355576; VBINeiMen85645_0312. DR eggNOG; ENOG4107R0R; Bacteria. DR eggNOG; COG1034; LUCA. DR HOGENOM; HOG000031442; -. DR KO; K00336; -. DR OMA; SAYEHES; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; NMEN122586:GHGG-264-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR01973; NuoG; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|RuleBase:RU003525}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Iron {ECO:0000256|RuleBase:RU003525}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003525}; KW Metal-binding {ECO:0000256|RuleBase:RU003525}; KW NAD {ECO:0000256|RuleBase:RU003525}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003525, KW ECO:0000256|SAAS:SAAS00509324, ECO:0000313|EMBL:AAF40703.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 78 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 216 272 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000259|PROSITE:PS51669}. SQ SEQUENCE 753 AA; 81602 MW; 6DC7957E6478C382 CRC64; MLQIEIDGKQ VSVEQGATVI EAAHKLGTYI PHFCYHKKLS IAANCRMCLV NVEKAPKPLP ACATPVTDGM IVRTHSAKAR EAQEGVMEFL LINHPLDCPT CDQGGECQLQ DLAVGYGKTT SRYTEEKRSV VGKDMGSLVS AEEMSRCIHC TRCVRFTEEI AGLQEIAMVN RGEHSEIMPF IGKTVETELS GNVIDLCPVG ALTSKPFRFN ARTWELNRRK SVSAHDALGS NLIVQTKDHT VRRVLPLENE AINECWLSDR DRFAYEGLYH ESRLKNPKIK QGGEWMDVDW KTALEYVRSA IECIAKDGKQ NQVGVWANPM NTVEELYLAK KLADGLGVKN FATRLRQQDK RLSDGLKGAQ WLGQSIESLA DNDAVLVVGA NLRKEQPLLT ARLRRAAKDR MALSVLASSK EELFMPLLSQ EAAHPDEWAG RLKNLSVNAE HAVTASLKNA EKAAVILGAE VQNHPDYAAV YAAAQELADA TGAVLGILPQ AANSVGADVL NVNSGKSVVE MVNAPKQAVL LLNVEPEIDT ADGAKAVAAL KQAKSVMAFT PFVSETLLDV CDVLLPIAPF TETSGSFINM EGRLQSFHGV VQGFGDSRPL WKVLRVLGNL FDLKGFEYHD TAAILKDALD VESLPSKLDN RNAWTGEGVQ TTSDRLVRVG GVGIYHTDSI VRRSAPLQET SHAAVPAARV NPNTLARLGL QDGQTAVAKQ NGASVSVAVK ADAGLPENVV HLPLHTENAA LGALMDTIEL AGA // ID Q9JZ62_NEIMB Unreviewed; 517 AA. AC Q9JZ62; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:AAF41652.1}; DE EC=6.2.1.3 {ECO:0000313|EMBL:AAF41652.1}; GN Name=fadD-1 {ECO:0000313|EMBL:AAF41652.1}; GN OrderedLocusNames=NMB1276 {ECO:0000313|EMBL:AAF41652.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41652.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41652.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41652.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41652.1; -; Genomic_DNA. DR PIR; D81101; D81101. DR RefSeq; NP_274296.1; NC_003112.2. DR RefSeq; WP_002244146.1; NC_003112.2. DR ProteinModelPortal; Q9JZ62; -. DR STRING; 122586.NMB1276; -. DR PaxDb; Q9JZ62; -. DR EnsemblBacteria; AAF41652; AAF41652; NMB1276. DR GeneID; 903698; -. DR KEGG; nme:NMB1276; -. DR PATRIC; 20358175; VBINeiMen85645_1599. DR eggNOG; ENOG4105CEY; Bacteria. DR eggNOG; COG0318; LUCA. DR HOGENOM; HOG000229983; -. DR KO; K01897; -. DR OMA; KKEMIIV; -. DR OrthoDB; EOG6MH5BV; -. DR BioCyc; NMEN122586:GHGG-1314-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Ligase {ECO:0000313|EMBL:AAF41652.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 14 419 AMP-binding. {ECO:0000259|Pfam:PF00501}. FT DOMAIN 428 503 AMP-binding_C. FT {ECO:0000259|Pfam:PF13193}. SQ SEQUENCE 517 AA; 57539 MW; 1A36994706C652C5 CRC64; MNRTYANFYE MLAAACRKNG NGTAVFDGKE KTAYRALKQE AEAVAAYLQN IGVKFGDTVA LAVSNSTEFI TAYFAISAIG AVAVPMNTFL KNSEYAYILN DCKARFLFAS AGLSKELAGL KAQTPVEKII WTDKSRPTGE TAEGDAFFED VRRFPEKPDL GRQPRINDLA HIIYTSGTTG HPKGALISYA NLFANLNGIE RIFKISKRDR FIVFLPMFHS FTLTAMVLLP IYMACSIILV KSVFPFSNVL KQTLLKRATV FLGVPAIYTA MSKAKIPWYF RWFNRIRLFI SGGAPLAEQT ILDFKAKFPR AKLLEGYGLS EASPVVAVNT PERQKARSVG IPLPGLEAKA VDEELVEVPR GEVGELIVRG GSVMRGYLNM PAATDETIVN GWLKTGDFVT IDEDGFIFIV DRKKDLIISK GQNVYPREIE EEIYKLDAVE AAAVIGVKDR YADEEIVAFV QLKEGMDLGE NEIRRHLRTV LANFKIPKQI HFKDGLPRNA TGKVLKRVLK EQFDGNK // ID Q9K0H1_NEIMB Unreviewed; 500 AA. AC Q9K0H1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Putative phosphate acetyltransferase Pta {ECO:0000313|EMBL:AAF41056.1}; GN OrderedLocusNames=NMB0631 {ECO:0000313|EMBL:AAF41056.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41056.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41056.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41056.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41056.1; -; Genomic_DNA. DR PIR; C81177; C81177. DR RefSeq; NP_273674.1; NC_003112.2. DR RefSeq; WP_002225525.1; NC_003112.2. DR ProteinModelPortal; Q9K0H1; -. DR STRING; 122586.NMB0631; -. DR PaxDb; Q9K0H1; -. DR EnsemblBacteria; AAF41056; AAF41056; NMB0631. DR GeneID; 902744; -. DR KEGG; nme:NMB0631; -. DR PATRIC; 20356559; VBINeiMen85645_0799. DR eggNOG; ENOG4108DNC; Bacteria. DR eggNOG; COG0280; LUCA. DR eggNOG; COG0857; LUCA. DR HOGENOM; HOG000053796; -. DR KO; K13788; -. DR OMA; NHICRTP; -. DR OrthoDB; EOG6BKJ5W; -. DR BioCyc; NMEN122586:GHGG-657-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro. DR InterPro; IPR004614; P_AcTrfase. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF01515; PTA_PTB; 1. DR TIGRFAMs; TIGR00651; pta; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|SAAS:SAAS00469150}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00469150}. FT DOMAIN 177 492 PTA_PTB. {ECO:0000259|Pfam:PF01515}. SQ SEQUENCE 500 AA; 52201 MW; C1E3C0230B9266E2 CRC64; MAKVLIVPVS AGLDASAAAQ AFAKALDAQI FQAVDATAET LLAQGKSDDW FDALVGKVAA LDAANLVIEG IAPDADKIYL AGKNVELALS LDAAAVFAVR SDNADADELA NRVNLAKQFF AAAPGVLEGF VVDGAAASVA EAAAEKTGLT FFGSSDALKD VSVLAGREAK RLSPAQFRYN LIDFARQADK RIVLPEGAEP RTVQAAAICH EKGIARCVLL AKREEVEAVA KERGISLPDS LEIIDPASLV EQYVEPMCEL RKSKGLTPED ARKQLQDTVV LGTMMMAQND VDGLVSGAVH TTANTIRPAL QLIKTAPGAS LVSSVFFMLL PNQVLVFGDC AVNPNPTAQQ LADIAIQSAD SAKAFGIDPK VAMISYSTVN SGSGPDVDTV IEATKLAREK RPDLAIDGPL QYDAATVPGV GKSKAPGSPV AGQATVLVFP DLNTGNCTYK AVQRNANVLS VGPLLQGLRK PVNDLSRGAL VEDIVFTIAL TAVQAKQMEG // ID Q9JZN8_NEIMB Unreviewed; 90 AA. AC Q9JZN8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41370.1}; GN OrderedLocusNames=NMB0965 {ECO:0000313|EMBL:AAF41370.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41370.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41370.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41370.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41370.1; -; Genomic_DNA. DR PIR; G81135; G81135. DR RefSeq; NP_274003.1; NC_003112.2. DR RefSeq; WP_010980877.1; NC_003112.2. DR STRING; 122586.NMB0965; -. DR PaxDb; Q9JZN8; -. DR EnsemblBacteria; AAF41370; AAF41370; NMB0965. DR GeneID; 903085; -. DR KEGG; nme:NMB0965; -. DR BioCyc; NMEN122586:GHGG-1002-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 90 AA; 10411 MW; 0857184E4A2B3A77 CRC64; MRPREPGAEP RVLTSTPFCH LFDRSGTCRF YALINFGYPA AEHNGQTQRN LRQHQPRPRR TADTNGHRPM PQPFHLKNFC LCPLSVLKIL // ID Q9K1K8_NEIMB Unreviewed; 221 AA. AC Q9K1K8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40567.1}; GN OrderedLocusNames=NMB0108 {ECO:0000313|EMBL:AAF40567.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40567.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40567.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40567.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40567.1; -; Genomic_DNA. DR PIR; C81238; C81238. DR RefSeq; NP_273166.1; NC_003112.2. DR RefSeq; WP_002224761.1; NC_003112.2. DR STRING; 122586.NMB0108; -. DR PaxDb; Q9K1K8; -. DR EnsemblBacteria; AAF40567; AAF40567; NMB0108. DR GeneID; 902212; -. DR KEGG; nme:NMB0108; -. DR PATRIC; 20355229; VBINeiMen85645_0148. DR HOGENOM; HOG000218667; -. DR OMA; IFGDACS; -. DR OrthoDB; EOG63C0S9; -. DR BioCyc; NMEN122586:GHGG-114-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 60 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 221 AA; 24706 MW; 52467C9FFE7FF8AC CRC64; MMMHASVQSR FAPILYVLIF FAGFLTAQIW FNQKAYTEEL PPLLSALSAV ALVWLAWAFV SARSKAKAEK FYREKMIQNE SIHPVLHASL QHLEHKPQIL ALLVKNHGKG MAEQVRFKAE VLPDDEDART IAAELAKMDM FALGTDAVAS GETYGRVFAD IFELSAALEG RAFKGMLKLT AEYKNIFGDA CRSETALELG ALNQALQEIS KTSEKSKRIF Y // ID Q9JYL6_NEIMB Unreviewed; 455 AA. AC Q9JYL6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:AAF41880.1}; GN OrderedLocusNames=NMB1524 {ECO:0000313|EMBL:AAF41880.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41880.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41880.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41880.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41880.1; -; Genomic_DNA. DR PIR; A81073; A81073. DR RefSeq; NP_274532.1; NC_003112.2. DR RefSeq; WP_002225062.1; NC_003112.2. DR ProteinModelPortal; Q9JYL6; -. DR STRING; 122586.NMB1524; -. DR PaxDb; Q9JYL6; -. DR EnsemblBacteria; AAF41880; AAF41880; NMB1524. DR GeneID; 904017; -. DR KEGG; nme:NMB1524; -. DR PATRIC; 20358846; VBINeiMen85645_1933. DR eggNOG; ENOG4105CQB; Bacteria. DR eggNOG; COG0277; LUCA. DR HOGENOM; HOG000230997; -. DR OMA; NEDWMRK; -. DR OrthoDB; EOG6CK7K6; -. DR BioCyc; NMEN122586:GHGG-1564-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 1.10.45.10; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 32 210 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. SQ SEQUENCE 455 AA; 50250 MW; 6A08A30663A8305D CRC64; MLDLHTEFSR LLPADEIAEP SPTLLKDQRN RFTSAPDIIL QPLSVKSVQT IMRFCHQHRI PVTPQGGNTG LCGAAVSENG VLLNLSKLNR IRSINLSDNC ITVEAGSVLQ TVQQAAEASN RLFPLSLASE GSCQIGGNIA CNAGGLNVLR YGTMRDLVIG LEVVLPNGEL VSHLHPLHKN TTGYDLRHLF IGSEGTLGII TAATLKLFAN PLDKATAWVG IPDIESAVRL LTETQAHFAE RLCSFELIGR FAAELSSEFS KLPLPTHSEW HILLELTDSL PDSNLDDRLV EFLYKKGFTD SVLAQSEQER IHMWALRENI SASQRKLGTS IKHDIAVPIG RVADFVRRCA KDLEQNFKGI QIVCFGHLGD GSLHYNTFLP EILSNEVYRY ENDINSTVYR NVLACNGTIA AEHGIGIIKK QWLDKVRTPA EIALMKSIKQ HLDPYNIMNP GKLLP // ID Q9K1N5_NEIMB Unreviewed; 716 AA. AC Q9K1N5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40519.1}; GN OrderedLocusNames=NMB0050 {ECO:0000313|EMBL:AAF40519.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40519.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40519.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40519.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40519.1; -; Genomic_DNA. DR PIR; H81242; H81242. DR RefSeq; NP_273115.1; NC_003112.2. DR RefSeq; WP_002221798.1; NC_003112.2. DR STRING; 122586.NMB0050; -. DR PaxDb; Q9K1N5; -. DR EnsemblBacteria; AAF40519; AAF40519; NMB0050. DR GeneID; 902152; -. DR KEGG; nme:NMB0050; -. DR PATRIC; 20355093; VBINeiMen85645_0084. DR eggNOG; ENOG4105EM2; Bacteria. DR eggNOG; COG1289; LUCA. DR HOGENOM; HOG000279479; -. DR OMA; HYNEWAD; -. DR OrthoDB; EOG6MSS1Z; -. DR BioCyc; NMEN122586:GHGG-51-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010019; Integral_membrane_YccS. DR InterPro; IPR010020; Integral_membrane_YCCS_YHJK. DR InterPro; IPR032692; YccS_N. DR Pfam; PF12805; FUSC-like; 1. DR TIGRFAMs; TIGR01666; YCCS; 1. DR TIGRFAMs; TIGR01667; YCCS_YHJK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 716 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332322. FT TRANSMEM 86 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 436 453 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 483 502 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 508 526 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 61 338 FUSC-like. {ECO:0000259|Pfam:PF12805}. SQ SEQUENCE 716 AA; 79990 MW; FBD7D2EBB8B22F84 CRC64; MKTPLLKPLL ITSLPVFASV FTAASIVWQL GEPKLAMPFV LGIIAGGLVD LDNRLTGRLK NIITTVALFT LSSLTAQSTL GTGLPFILAM TLMTFGFTIL GAVGLKYRTF AFGALAVATY TTLTYTPETY WLTNPFMILC GTVLYSTAIL LFQIVLPHRP VQESVANAYD ALGGYLEAKA DFFDPDEAAW IGNRHIDLAM SNTGVITAFN QCRSALFYRL RGKHRHPRTA KMLRYYFAAQ DIHERISSAH VDYQEMSEKF KNTDIIFRIH RLLEMQGQAC RNTAQALRAS KDYVYSKRLG RAIEGCRQSL RLLSDSNDSP DIRHLRRLLD NLGSVDQQFR QLQHNGLQAE NDRMGDTRIA ALETSSLKNT WQAIRPQLNL ESGVFRHAVR LSLVVAAACT IVEALNLNLG YWILLTALFV CQPNYTATKS RVRQRIAGTV LGVIVGSLVP YFTPSVETKL WIVIASTTLF FMTRTYKYSF STFFITIQAL TSLSLAGLDV YAAMPVRIID TIIGASLAWA AVSYLWPDWK YLTLERTAAL AVCSNGAYLE KITERLKSGE TGDDVEYRAT RRRAHEHTAA LSSTLSDMSS EPAKFADSLQ PGFTLLKTGY ALTGYISALG AYRSEMHEEC SPDFTAQFHL AAEHTAHIFQ HLPETEPDDF QTALDTLRGE LDTLRTHSSG TQSHILLQQL QLIARQLEPY YRAYRQIPHR QPQNAA // ID Q9K004_NEIMB Unreviewed; 323 AA. AC Q9K004; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Putative ADP-heptose synthase {ECO:0000313|EMBL:AAF41238.1}; GN OrderedLocusNames=NMB0825 {ECO:0000313|EMBL:AAF41238.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41238.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41238.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41238.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41238.1; -; Genomic_DNA. DR PIR; H81154; H81154. DR RefSeq; NP_273867.1; NC_003112.2. DR RefSeq; WP_002217546.1; NC_003112.2. DR ProteinModelPortal; Q9K004; -. DR STRING; 122586.NMB0825; -. DR PaxDb; Q9K004; -. DR EnsemblBacteria; AAF41238; AAF41238; NMB0825. DR GeneID; 902940; -. DR KEGG; nme:NMB0825; -. DR PATRIC; 20357035; VBINeiMen85645_1036. DR eggNOG; ENOG4105DW0; Bacteria. DR eggNOG; COG2870; LUCA. DR HOGENOM; HOG000237584; -. DR OMA; TIVKHRF; -. DR OrthoDB; EOG68Q0W4; -. DR BioCyc; NMEN122586:GHGG-856-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR011913; RfaE_dom_I. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR02198; rfaE_dom_I; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|SAAS:SAAS00446051}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000256|SAAS:SAAS00446051}. FT DOMAIN 17 308 PfkB. {ECO:0000259|Pfam:PF00294}. SQ SEQUENCE 323 AA; 34998 MW; FF1B490F54E79D97 CRC64; MSAKFQQETL KSRFAQAKVL VVGDVMLDRY WFGDVSRISP EAPVPVAKIG RIDQRAGGAA NVARNIASLG GRAGLLSVTG NDEAADALDA LMVQDGVASY LMRDKQIATT VKLRVVARNQ QLIRLDFEEH PNCEVLEQIK QKYREILPEY DAIIFSDYGK GGLSHISDMI DWAKHAGKTV LIDPKGDDYE KYVGATLITP NRAELKEVVG SWKNESELTE KAQNLRRHLD LTAVLLTRSE EGMTLFSEGE PIYQPTRAQE VYDVSGAGDT VIAGMGLGLA AGCTMPEAMY LANTAAGVVV AKLGTAVCSF AELIKALSGQ STM // ID Q9JYA9_NEIMB Unreviewed; 68 AA. AC Q9JYA9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42016.1}; GN OrderedLocusNames=NMB1667 {ECO:0000313|EMBL:AAF42016.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42016.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42016.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42016.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42016.1; -; Genomic_DNA. DR PIR; E81056; E81056. DR RefSeq; NP_274672.1; NC_003112.2. DR RefSeq; WP_002216685.1; NC_003112.2. DR STRING; 122586.NMB1667; -. DR PaxDb; Q9JYA9; -. DR EnsemblBacteria; AAF42016; AAF42016; NMB1667. DR GeneID; 903443; -. DR KEGG; nme:NMB1667; -. DR PATRIC; 20359274; VBINeiMen85645_2145. DR HOGENOM; HOG000152755; -. DR BioCyc; NMEN122586:GHGG-1721-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 68 AA; 7234 MW; 880483F506BF475B CRC64; MPSEKCFRRH FLVADMLTDD VGAHDHADVE RACLTVVLSA LQRLLVEVAV EAGNAASARV AADAALCL // ID Q9K1P7_NEIMB Unreviewed; 279 AA. AC Q9K1P7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40505.1}; GN OrderedLocusNames=NMB0034 {ECO:0000313|EMBL:AAF40505.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40505.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40505.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40505.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40505.1; -; Genomic_DNA. DR PIR; D81244; D81244. DR RefSeq; NP_273100.1; NC_003112.2. DR RefSeq; WP_002225766.1; NC_003112.2. DR STRING; 122586.NMB0034; -. DR PaxDb; Q9K1P7; -. DR EnsemblBacteria; AAF40505; AAF40505; NMB0034. DR GeneID; 902137; -. DR KEGG; nme:NMB0034; -. DR PATRIC; 20355021; VBINeiMen85645_0047. DR eggNOG; ENOG4105EKT; Bacteria. DR eggNOG; COG0672; LUCA. DR HOGENOM; HOG000236918; -. DR KO; K07243; -. DR OMA; MTWFLCG; -. DR OrthoDB; EOG62ZHSM; -. DR BioCyc; NMEN122586:GHGG-35-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0033573; C:high-affinity iron permease complex; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006827; P:high-affinity iron ion transmembrane transport; IEA:InterPro. DR InterPro; IPR004923; FTR1/Fip1/EfeU. DR PANTHER; PTHR31632; PTHR31632; 1. DR Pfam; PF03239; FTR1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 265 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 279 AA; 30229 MW; 025B85E7620CE832 CRC64; MLVAFLIMLR EGIEAALIVG IVAGFLKQSG HSKLMPKVWF GVVLASLMCL GLGYGIHSAT GEIPQKQQEF VVGIIGLVAV AMLTYMILWM KKAARSMKRQ LQDSVQAALN RGSGQGWALV GMAFLAVARE GLESVFFLLA VFKQSPTWQM PAGAVAGVLA AAVIGALIYQ GGMRLNLAKF FRWTGAFLIV VAAGLLAGSL RALHEAGIWN ALQDIVFDSS KYLHEDSPLG VLLGGFFGYT DHPTQGETLV WLLYLIPVIT WFLCGSRPSE TLTRKEELK // ID Q9JXN9_NEIMB Unreviewed; 130 AA. AC Q9JXN9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Stringent starvation protein B {ECO:0000313|EMBL:AAF42281.1}; GN Name=sspB {ECO:0000313|EMBL:AAF42281.1}; GN OrderedLocusNames=NMB1952 {ECO:0000313|EMBL:AAF42281.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42281.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42281.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42281.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42281.1; -; Genomic_DNA. DR PIR; A81024; A81024. DR RefSeq; NP_274946.1; NC_003112.2. DR RefSeq; WP_002224125.1; NC_003112.2. DR ProteinModelPortal; Q9JXN9; -. DR STRING; 122586.NMB1952; -. DR PaxDb; Q9JXN9; -. DR EnsemblBacteria; AAF42281; AAF42281; NMB1952. DR GeneID; 904198; -. DR KEGG; nme:NMB1952; -. DR PATRIC; 20359963; VBINeiMen85645_2486. DR eggNOG; ENOG4105KB2; Bacteria. DR eggNOG; COG2969; LUCA. DR HOGENOM; HOG000255240; -. DR KO; K03600; -. DR OMA; YLIRAVH; -. DR OrthoDB; EOG6X6RFF; -. DR BioCyc; NMEN122586:GHGG-2009-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 2.30.30.220; -; 1. DR InterPro; IPR007481; SspB. DR Pfam; PF04386; SspB; 1. DR PIRSF; PIRSF005276; SspB; 1. DR SUPFAM; SSF101738; SSF101738; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 130 AA; 14622 MW; 898A5AB52CB4AAD7 CRC64; MPTSTKPYIL RALCEWCSDN SLTPHILVWV NEHTRVPMQY VRDNEIMLNI GATATQNLQI DNDWISFSAR FGGQAHDIWI PVGHVLSLFA RETGEGMGFE LEAYRPDTPP ENTSAETAPR PAKKGLKLVK // ID Q9JXV9_NEIMB Unreviewed; 72 AA. AC Q9JXV9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42199.1}; GN OrderedLocusNames=NMB1865 {ECO:0000313|EMBL:AAF42199.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42199.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42199.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42199.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42199.1; -; Genomic_DNA. DR PIR; B81034; B81034. DR PaxDb; Q9JXV9; -. DR EnsemblBacteria; AAF42199; AAF42199; NMB1865. DR OMA; NRIPDDG; -. DR OrthoDB; EOG6WMJ81; -. DR BioCyc; NMEN122586:GHGG-1921-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 72 AA; 8098 MW; 835AE6CE51D59D41 CRC64; MPSERQVSGL EAESPILSFF RLRQGFARFF ADHANRIPDD GTLVFFHFMC KAVVSDDSLP VVIHTPLPMS AF // ID Q9JXJ1_NEIMB Unreviewed; 148 AA. AC Q9JXJ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=ComEA-related protein {ECO:0000313|EMBL:AAF42340.1}; GN OrderedLocusNames=NMB2017 {ECO:0000313|EMBL:AAF42340.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42340.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42340.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42340.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42340.1; -; Genomic_DNA. DR PIR; E81016; E81016. DR RefSeq; NP_275009.1; NC_003112.2. DR RefSeq; WP_009345591.1; NC_003112.2. DR ProteinModelPortal; Q9JXJ1; -. DR STRING; 122586.NMB2017; -. DR PaxDb; Q9JXJ1; -. DR EnsemblBacteria; AAF42340; AAF42340; NMB2017. DR GeneID; 904104; -. DR KEGG; nme:NMB2017; -. DR PATRIC; 20360137; VBINeiMen85645_2573. DR eggNOG; ENOG41083P1; Bacteria. DR eggNOG; COG1555; LUCA. DR HOGENOM; HOG000257817; -. DR KO; K02237; -. DR OMA; MIKKWFA; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; NMEN122586:GHGG-2074-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004787; Competence_ComE. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR01259; comE; 1. DR TIGRFAMs; TIGR00426; TIGR00426; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 74 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 78 97 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 108 127 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 148 AA; 15800 MW; 85A2ED4D14375C4A CRC64; MSVMAGRHPY GVRSGLRRNG LKLWDIHFRM TRFIVARCGL LFATLKGKTM KKMFVLFCML FSCAFSLAAV NINAASQQEL EALPGIGPAK AKAIAEYRAQ NGAFKSVDDL TKVKGIGPAV LAKLKDQASV GAPAPKGPAK PAIPAAKK // ID Q9K0Q6_NEIMB Unreviewed; 123 AA. AC Q9K0Q6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40958.1}; GN OrderedLocusNames=NMB0528 {ECO:0000313|EMBL:AAF40958.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40958.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40958.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40958.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40958.1; -; Genomic_DNA. DR PIR; H81189; H81189. DR RefSeq; NP_273573.1; NC_003112.2. DR RefSeq; WP_002225594.1; NC_003112.2. DR STRING; 122586.NMB0528; -. DR PaxDb; Q9K0Q6; -. DR EnsemblBacteria; AAF40958; AAF40958; NMB0528. DR GeneID; 902643; -. DR KEGG; nme:NMB0528; -. DR PATRIC; 20356303; VBINeiMen85645_0671. DR eggNOG; ENOG41083N9; Bacteria. DR eggNOG; COG3759; LUCA. DR HOGENOM; HOG000239012; -. DR KO; K08987; -. DR OMA; VAVEFFY; -. DR OrthoDB; EOG66B42M; -. DR BioCyc; NMEN122586:GHGG-553-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR009732; DUF1304. DR Pfam; PF06993; DUF1304; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 98 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 123 AA; 13449 MW; 7269EA29FB396AE4 CRC64; MKLLFILLVL FVAVEHFYIA WLEMTQIPSE KAAEIFKLPY EFMEQKQVQT LFSNQGLYNG FLGIGLVWSR FAAPDNAVYG ATTLFLGFVL IAAAWGAFSS GNKGILVKQG LPAMLAAAAV LAV // ID Q9JYJ0_NEIMB Unreviewed; 140 AA. AC Q9JYJ0; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41918.1}; GN OrderedLocusNames=NMB1564 {ECO:0000313|EMBL:AAF41918.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41918.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41918.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41918.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41918.1; -; Genomic_DNA. DR PIR; H81067; H81067. DR RefSeq; NP_274571.1; NC_003112.2. DR RefSeq; WP_002218995.1; NC_003112.2. DR ProteinModelPortal; Q9JYJ0; -. DR STRING; 122586.NMB1564; -. DR PaxDb; Q9JYJ0; -. DR EnsemblBacteria; AAF41918; AAF41918; NMB1564. DR GeneID; 904138; -. DR KEGG; nme:NMB1564; -. DR PATRIC; 20358990; VBINeiMen85645_2014. DR eggNOG; ENOG4108UKZ; Bacteria. DR eggNOG; COG1765; LUCA. DR HOGENOM; HOG000256281; -. DR KO; K07397; -. DR OMA; GPRPMEM; -. DR OrthoDB; EOG6R2H4J; -. DR BioCyc; NMEN122586:GHGG-1605-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.300.20; -; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR003718; OsmC/Ohr_fam. DR Pfam; PF02566; OsmC; 1. DR SUPFAM; SSF82784; SSF82784; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 140 AA; 15042 MW; F2BF9D71042FAEAD CRC64; MQVTSKWIDG MCFVGTTEGG HSVVMEGSAA EGKAKRGPSP LEMLLLGVAG CSSIDVVMIA EKQRQKVTDC RATVTAKRAD DAPRVFTEIH IHFKVFGHDL KESAIERAVQ MSAEKYCSAS IMLGKAAKIT HSFEIAGADK // ID Q9JZ57_NEIMB Unreviewed; 1379 AA. AC Q9JZ57; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969}; DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969}; GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969, GN ECO:0000313|EMBL:AAF41657.1}; GN OrderedLocusNames=NMB1281 {ECO:0000313|EMBL:AAF41657.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41657.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41657.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41657.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent CC release of RNAP and its truncated transcript from the DNA, and CC recruitment of nucleotide excision repair machinery to the damaged CC site. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase CC family. RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41657.1; -; Genomic_DNA. DR PIR; A81102; A81102. DR RefSeq; NP_274301.1; NC_003112.2. DR RefSeq; WP_010980915.1; NC_003112.2. DR ProteinModelPortal; Q9JZ57; -. DR STRING; 122586.NMB1281; -. DR PaxDb; Q9JZ57; -. DR EnsemblBacteria; AAF41657; AAF41657; NMB1281. DR GeneID; 903703; -. DR KEGG; nme:NMB1281; -. DR PATRIC; 20358189; VBINeiMen85645_1606. DR eggNOG; ENOG4108JA2; Bacteria. DR eggNOG; COG1197; LUCA. DR HOGENOM; HOG000216592; -. DR KO; K03723; -. DR OMA; GTHKLIQ; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; NMEN122586:GHGG-1319-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00969; TRCF; 1. DR InterPro; IPR003711; CarD-like/TRCF_domain. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR004576; Mfd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005118; TRCF_C. DR Pfam; PF02559; CarD_CdnL_TRCF; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF03461; TRCF; 1. DR SMART; SM01058; CarD_TRCF; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00982; TRCF; 1. DR SUPFAM; SSF141259; SSF141259; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR TIGRFAMs; TIGR00580; mfd; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 848 1009 Helicase ATP-binding. {ECO:0000256|HAMAP- FT Rule:MF_00969, FT ECO:0000259|PROSITE:PS51192}. FT DOMAIN 1030 1182 Helicase C-terminal. {ECO:0000256|HAMAP- FT Rule:MF_00969, FT ECO:0000259|PROSITE:PS51194}. FT NP_BIND 861 868 ATP. {ECO:0000256|HAMAP-Rule:MF_00969}. FT MOTIF 962 965 DEAH box. {ECO:0000256|HAMAP- FT Rule:MF_00969}. SQ SEQUENCE 1379 AA; 151685 MW; 72B8A42670DF60FA CRC64; MTYPIPKPRE KSRWPNLSQG SLPLALARYL PHKRLKVVLT QDAEQALRLQ TAWRFFRPHD TAVFLPDWET LPYERFSPHQ DLVSERLSAL WQIKSGAADV LFVPVATAMQ KLPPVPFLAG RTFWLKTGQT LDIGRLKSDL VDAGYNHVSH VVAAGEFAVR GGIVDLFPMG SEMPYRIDLF DDEIDSIKTF DTETQRTISP VSEIRLLPAH EFPTDSEAQK IFRSRFREEV DGNPNDAAVY KAVSNGHFGA GVEYYLPLFF ENELETLFDY IGEDALFVSL DDVHAEANRF WSDVKSRYAM AQGDETYPPL LPQYLYLSAD VFAGRLKNYG QVLPDVSGKE YTLPDLAVNR QADEPLQALK DFQTAFDGRI LLCAESLGRR ETMLGFLQQN GLKAKPVSDW QGFLSAHEPL MITVAPLAYG FKLGGLQSPN QQQPTPSPVG EGWGEGKAVA AQTEFSAAAI NPLPSPLPQE REQSAAAVSD SLKAAAVSTE SSLPLGTSNL HGQIRQQPAP SPVGEGWGEG KAVAAQTEFP ASATNPLPSP LPQEREQSAA AVSDDLKTKS SLHPVANNLH GQIRQQPTPS PVGEGWGEGK AVAAQTEFSA AATNPLPSPL PQEREQSAAV VSDSLKAAAV STESSLPPGK SNLHGQIQQQ PAPSPVGEGW GEGKAVAAQS AIAVITESDL YQYVARSRIH NRRKKHAAVS DGLLRDLAEI NIGDPVVHEE HGIGRYMGLV TMDLGGETNE MMLLEYAGEA QLYVPVSQLH LISRYSGQAH ENIALHKLGS GAWNKAKRKA AEKARDTAAE LLNLYAQRAA QSGHKFEINE LDYQAFADGF GYEETEDQAA AIAAVIKDLT QAKPMDRLVC GDVGFGKTEV ALRAAFVAVM GGKQVAVLAP TTLLVEQHAQ NFADRFADFP VKVASLSRFN NSKATKAALE GMADGTVDIV IGTHKLVQDD IKFKNLGLVI IDEEHRFGVR QKEQLKRLRA NVDILTMTAT PIPRTLSMAL EGLRDFSLIT TAPSRRLAVK TFVKPFSEGS VREAVLRELK RGGQVFFLHN EVDTIENMRE RLETLLPEAR IGVAHGQLRE RELEQVMRDF LQQRFNVLLC STIIETGIDI PNANTIIINR ADKFGLAQLH QLRGRVGRSH HQAYAYLLTP EYITKDAEKR LDAIAAADEL GAGFTLAMQD LEIRGAGEIL GEGQSGEMIQ VGFTLYTEML KQAVRDLKKG RQPDLDAPLG ITTEIKLHSP ALLPEDYCPD IHERLVLYKR LAVCETVQQI NTIHEELVDR FGLPEQPVKT LIESHHLRLM AKELGIDAID AAGEAVTVTF GKNNNVDPTE IILLIQNDKK YRLAGADKLR FTAEMENIEV RINTVKNVLK TLQNRCLPK // ID Q9K0G9_NEIMB Unreviewed; 127 AA. AC Q9K0G9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41059.1}; GN OrderedLocusNames=NMB0636 {ECO:0000313|EMBL:AAF41059.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41059.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41059.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41059.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41059.1; -; Genomic_DNA. DR PIR; A81175; A81175. DR STRING; 122586.NMB0636; -. DR PaxDb; Q9K0G9; -. DR EnsemblBacteria; AAF41059; AAF41059; NMB0636. DR PATRIC; 20356571; VBINeiMen85645_0805. DR eggNOG; ENOG41063IZ; Bacteria. DR eggNOG; ENOG411289Z; LUCA. DR HOGENOM; HOG000218826; -. DR OMA; LGKEIRH; -. DR OrthoDB; EOG6HMXFG; -. DR BioCyc; NMEN122586:GHGG-662-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR InterPro; IPR025402; DUF4375. DR Pfam; PF14300; DUF4375; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 31 106 DUF4375. {ECO:0000259|Pfam:PF14300}. SQ SEQUENCE 127 AA; 14525 MW; 770BD2E63B7631FA CRC64; MTDTDTQADR FEQMMWQAVD KLFEQHDGKL ESMDGREQEL VLIWRTEADI GNGSILQFVC NWGFPAAEKT CSVLKKIGAV HSAMLIHRAA DALDKEIRRL QSEGKNLKEM WDITSRQQNR LTAEQSG // ID Q9JYM7_NEIMB Unreviewed; 485 AA. AC Q9JYM7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41864.1}; GN OrderedLocusNames=NMB1508 {ECO:0000313|EMBL:AAF41864.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41864.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41864.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41864.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41864.1; -; Genomic_DNA. DR PIR; H81075; H81075. DR RefSeq; NP_274516.1; NC_003112.2. DR RefSeq; WP_010980951.1; NC_003112.2. DR STRING; 122586.NMB1508; -. DR PaxDb; Q9JYM7; -. DR EnsemblBacteria; AAF41864; AAF41864; NMB1508. DR GeneID; 903957; -. DR KEGG; nme:NMB1508; -. DR PATRIC; 20358796; VBINeiMen85645_1908. DR eggNOG; ENOG4105QMZ; Bacteria. DR eggNOG; COG1368; LUCA. DR HOGENOM; HOG000219021; -. DR OMA; HVAWLNF; -. DR OrthoDB; EOG613063; -. DR BioCyc; NMEN122586:GHGG-1548-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 176 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 313 474 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 485 AA; 54515 MW; B239E874607F3E07 CRC64; MSEWRSFNRK GNTMNIHTLL SKQWTLPPFL PKRLLLSLLI LLAPNAVFWV LALLTATARP IVNLDYLPAA LLIALPWRFV KIAGVLAFWL AVLFDGLMMV IQLFPFMDLI GAINLVPFIL TAPAPYQIMT GLLLLYMLAM PFVLQKAAAK TDFRHIAVCA AVVAAAGYFT GHLSYYDRGR MANIFGANNF YYAKSQAMLY TVSQNADFIT AGLVDPVFLP LGNQQRAATH LNEPKSQKIL FIVAESWGLP ANPELQNATF AKLLAQKDRF SVWESGSFPF IGATVEGEMR ELCAYGGLRG FALRRAPDEK FARCLPNRLK QEGYATFAMH GAGSSLYDRF SWYPRAGFQE IKTAENLIGK KTCAIFGGVC DSELFGEVSA FFKKHDKGLF YWMTLTSHAD YPESDIFNHR LKCTEYGLPA ETDLCRNFSL HTQFFDQLAD LIQRPEMKGT EVIIVGDHPP PVGNLNETFR YLKQGHVAWL NFKIK // ID Q9JZP9_NEIMB Unreviewed; 113 AA. AC Q9JZP9; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Succinate dehydrogenase, hydrophobic membrane anchor protein {ECO:0000313|EMBL:AAF41355.1}; GN Name=sdhD {ECO:0000313|EMBL:AAF41355.1}; GN OrderedLocusNames=NMB0949 {ECO:0000313|EMBL:AAF41355.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41355.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41355.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41355.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000169-2}; CC Note=The heme is bound between the two transmembrane subunits. CC {ECO:0000256|PIRSR:PIRSR000169-2}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41355.1; -; Genomic_DNA. DR PIR; E81138; E81138. DR RefSeq; NP_273987.1; NC_003112.2. DR RefSeq; WP_002223854.1; NC_003112.2. DR ProteinModelPortal; Q9JZP9; -. DR STRING; 122586.NMB0949; -. DR PaxDb; Q9JZP9; -. DR EnsemblBacteria; AAF41355; AAF41355; NMB0949. DR GeneID; 903069; -. DR KEGG; nme:NMB0949; -. DR PATRIC; 20357381; VBINeiMen85645_1205. DR eggNOG; ENOG4105N1I; Bacteria. DR eggNOG; COG2142; LUCA. DR HOGENOM; HOG000160364; -. DR KO; K00242; -. DR OMA; QWMKVLT; -. DR OrthoDB; EOG6SV5BS; -. DR BioCyc; NMEN122586:GHGG-986-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR014312; Succ_DH_anchor. DR InterPro; IPR000701; Succ_DH_Fumarate_Rdtase_TM-su. DR Pfam; PF01127; Sdh_cyt; 1. DR PIRSF; PIRSF000169; SDH_D; 1. DR TIGRFAMs; TIGR02968; succ_dehyd_anc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Heme {ECO:0000256|PIRSR:PIRSR000169-2}; KW Iron {ECO:0000256|PIRSR:PIRSR000169-2}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000169-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 112 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 70 70 Iron (heme axial ligand); shared with FT second transmembrane subunit. FT {ECO:0000256|PIRSR:PIRSR000169-2}. FT BINDING 82 82 Ubiquinone. FT {ECO:0000256|PIRSR:PIRSR000169-1}. SQ SEQUENCE 113 AA; 13149 MW; C1C7C48D584176CD CRC64; MVERKLTGAH YGLRDWVMQR ATAVIMLIYT VALLVVLFSL PKEYSAWQAF FSQTWVKVFT QVSFIAVFLH AWVGIRDLWM DYIKPFGVRL FLQVATIVWL VGCLVYSVKV IWG // ID Q9K1M6_NEIMB Unreviewed; 308 AA. AC Q9K1M6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40533.1}; GN OrderedLocusNames=NMB0065 {ECO:0000313|EMBL:AAF40533.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40533.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40533.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40533.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40533.1; -; Genomic_DNA. DR PIR; H81240; H81240. DR RefSeq; NP_273129.1; NC_003112.2. DR RefSeq; WP_010980748.1; NC_003112.2. DR STRING; 122586.NMB0065; -. DR PaxDb; Q9K1M6; -. DR EnsemblBacteria; AAF40533; AAF40533; NMB0065. DR GeneID; 902172; -. DR KEGG; nme:NMB0065; -. DR PATRIC; 20355135; VBINeiMen85645_0101. DR eggNOG; ENOG4105PIS; Bacteria. DR eggNOG; ENOG4111XU7; LUCA. DR HOGENOM; HOG000027826; -. DR OMA; HASKGCH; -. DR OrthoDB; EOG6W19JB; -. DR BioCyc; NMEN122586:GHGG-71-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 308 AA; 35145 MW; 1742CDBA8F4384DB CRC64; MHQYYDAVIL SVGNGLLKRF FKQNAQLNIA SRPLIITLFP GVVFGDQASI LSRMGADIVL YNNKHDFRIA EEYKKQYKLS CQNILYGYPI FRHASKGCHG EKIYFIDQVK IPFKKEERIY TLKKLIALAE KYPEKEFTIL LRVADKDITV HQDKHSYIEL AKQFQLPSNL TIERKSTAQA FQEMGYCLSY SSTMLFEAEC KGIPVGVVAD LGFSKSYANQ HFLGSGVLVY FDQIDFTSPK IADPDWLDCY ATKKVITTDE FNKLLKQVVP LQHDYQEYLS AGIRYQALAN THAIPTNSFL GIKPCSDA // ID Q7DDU2_NEIMB Unreviewed; 161 AA. AC Q7DDU2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40514.1}; GN OrderedLocusNames=NMB0043 {ECO:0000313|EMBL:AAF40514.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40514.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40514.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40514.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40514.1; -; Genomic_DNA. DR PIR; E81245; E81245. DR RefSeq; NP_273109.1; NC_003112.2. DR RefSeq; WP_002215245.1; NC_003112.2. DR ProteinModelPortal; Q7DDU2; -. DR STRING; 122586.NMB0043; -. DR PaxDb; Q7DDU2; -. DR EnsemblBacteria; AAF40514; AAF40514; NMB0043. DR GeneID; 902146; -. DR KEGG; nme:NMB0043; -. DR PATRIC; 20355043; VBINeiMen85645_0058. DR eggNOG; ENOG4107TH8; Bacteria. DR eggNOG; COG1546; LUCA. DR HOGENOM; HOG000242527; -. DR KO; K03743; -. DR OMA; TVWFAWA; -. DR OrthoDB; EOG61S359; -. DR BioCyc; NMEN122586:GHGG-44-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.90.950.20; -; 1. DR InterPro; IPR008136; CinA_C. DR Pfam; PF02464; CinA; 1. DR SUPFAM; SSF142433; SSF142433; 1. DR TIGRFAMs; TIGR00199; PncC_domain; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 151 CinA. {ECO:0000259|Pfam:PF02464}. SQ SEQUENCE 161 AA; 16854 MW; 3DEBC77107B6EDB6 CRC64; MDALHTIARN LTKKRQTVSC AESCTGGMLA AAFTSVAGSS QWFDQSFVTY SNKAKEDRLG VLPETLLEHG AVSRQTVYEM ARGAKAVAQA DYAVGISGIA GPGGGSESKP VGTVWFGFAF PGGSCEAMRR FDGNRESVRA QAVAFALERL AGLIENGGDA V // ID Q7DD88_NEIMB Unreviewed; 213 AA. AC Q7DD88; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:AAF42079.1}; GN Name=grx {ECO:0000313|EMBL:AAF42079.1}; GN OrderedLocusNames=NMB1734 {ECO:0000313|EMBL:AAF42079.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42079.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42079.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42079.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42079.1; -; Genomic_DNA. DR PIR; E81049; E81049. DR RefSeq; NP_274737.1; NC_003112.2. DR RefSeq; WP_002216608.1; NC_003112.2. DR ProteinModelPortal; Q7DD88; -. DR STRING; 122586.NMB1734; -. DR PaxDb; Q7DD88; -. DR EnsemblBacteria; AAF42079; AAF42079; NMB1734. DR GeneID; 903365; -. DR KEGG; nme:NMB1734; -. DR PATRIC; 20359431; VBINeiMen85645_2221. DR eggNOG; ENOG4105E9S; Bacteria. DR eggNOG; COG2999; LUCA. DR HOGENOM; HOG000064700; -. DR KO; K03675; -. DR OMA; LRNLTCV; -. DR OrthoDB; EOG64BQ52; -. DR BioCyc; NMEN122586:GHGG-1789-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR007494; Glutaredoxin2_C. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR011901; GRXB. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF04399; Glutaredoxin2_C; 1. DR Pfam; PF13417; GST_N_3; 1. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02182; GRXB; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 1 77 GST N-terminal. FT {ECO:0000259|PROSITE:PS50404}. FT COILED 134 161 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 213 AA; 23878 MW; 5B679CD652A4E2A6 CRC64; MKLYIYDHCP FCVRARMAAG LFGADVEEAV LANDDEATPI GMIGAKQVPV LQKEDGSFMG ESLDIVRHFD REDRLKDEVR PEIRAWLDKV GGYNDKLVQP RVIKIGLPEF ATPEAVKYFT DKKEKSIGSF SANLNKTAQY LERINADLQE LENLMDGASD GINGGIGMED ILVFPVLRNL TVVRGIEWPQ KVMGYLMTMS EKSGVPLYFD RAL // ID Q9JYY5_NEIMB Unreviewed; 186 AA. AC Q9JYY5; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41744.1}; GN OrderedLocusNames=NMB1370 {ECO:0000313|EMBL:AAF41744.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41744.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41744.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41744.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41744.1; -; Genomic_DNA. DR PIR; G81090; G81090. DR RefSeq; NP_274388.1; NC_003112.2. DR RefSeq; WP_002216992.1; NC_003112.2. DR PaxDb; Q9JYY5; -. DR EnsemblBacteria; AAF41744; AAF41744; NMB1370. DR GeneID; 903792; -. DR KEGG; nme:NMB1370; -. DR PATRIC; 20358409; VBINeiMen85645_1716. DR HOGENOM; HOG000219001; -. DR OMA; RDFSPML; -. DR OrthoDB; EOG6KDKQX; -. DR BioCyc; NMEN122586:GHGG-1408-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 186 AA; 20950 MW; 0CBEF5CC3EEF556E CRC64; MLPSHRSPDS ATHDRIRKMT MNAMPQTAAQ NETLHTCSII VDDAQDFSPM LLDAGRDDTL ISESMIPQIR TVAALIAAER HDFSRSSPAE FTDAADFFAA RILVLGVRRF HLDVSLLQIL KTANSRARRF AEKHRLFFTP AQAELSLNKH KNRRLLTVET EHEVENKGNP VANSLAFVRK LHTLPL // ID Q9JXE4_NEIMB Unreviewed; 120 AA. AC Q9JXE4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42404.1}; GN OrderedLocusNames=NMB2087 {ECO:0000313|EMBL:AAF42404.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42404.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42404.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42404.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42404.1; -; Genomic_DNA. DR PIR; E81007; E81007. DR RefSeq; NP_275075.1; NC_003112.2. DR RefSeq; WP_002247645.1; NC_003112.2. DR STRING; 122586.NMB2087; -. DR PaxDb; Q9JXE4; -. DR EnsemblBacteria; AAF42404; AAF42404; NMB2087. DR GeneID; 903964; -. DR KEGG; nme:NMB2087; -. DR BioCyc; NMEN122586:GHGG-2152-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 120 AA; 13223 MW; 16468DEE606104A0 CRC64; MATCPATAAN SSKPKLPWNV LPKFAIHSIF SGEPLHHFNA EHFQRAAAAA VLADHADNGN SKHEQIQNAV ACRRSLAVAL RTLGAVGNRP HDAQCNHRQR KETERFVQAE QAAHPFRLFV // ID Q9JYW3_NEIMB Unreviewed; 400 AA. AC Q9JYW3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=FrpA/C-related protein {ECO:0000313|EMBL:AAF41768.1}; GN OrderedLocusNames=NMB1405 {ECO:0000313|EMBL:AAF41768.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41768.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41768.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41768.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41768.1; -; Genomic_DNA. DR PIR; B81087; B81087. DR RefSeq; NP_274419.1; NC_003112.2. DR RefSeq; WP_010980931.1; NC_003112.2. DR STRING; 122586.NMB1405; -. DR PaxDb; Q9JYW3; -. DR EnsemblBacteria; AAF41768; AAF41768; NMB1405. DR GeneID; 903827; -. DR KEGG; nme:NMB1405; -. DR PATRIC; 20358495; VBINeiMen85645_1759. DR eggNOG; ENOG4105VX8; Bacteria. DR eggNOG; COG2931; LUCA. DR HOGENOM; HOG000219010; -. DR OMA; VWQNLNQ; -. DR OrthoDB; EOG690MC5; -. DR BioCyc; NMEN122586:GHGG-1443-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 400 AA; 43167 MW; 3754156639D8AC10 CRC64; MSARSSALAE FGNMVANLVS AKNEKDISKR NEYYKQAGYS ALLAFGNLAS NIAPGSTSSH IVNGTNASVI ASRLSGNISS AIQEHKDGKV NINRFQNILA DLYSLGGLGS TLIEKNGNMQ SWGIPLAIAG DIIAATAIAT GDTGTISTEE FYNFDNWKGF GYELFEDWSR WVYDWLPDGW NLWKELDRNR SGQYHIYDPL ALDLDGDGIE TVAAKGFSGS LFDHNGNGIR TATGWVSADD GLLVRDLNGN GIIDNGAELF GDNTKLADGS FAKHGYAALA ELDSNGDNII NAADAAFQSL RVWQDLNQDG ISQANELRTL EELGIQSLDL AYKDVNKNLG NGNTLAQQGS YTKTDGTTAK MGDLLLAADN LHSRFTNKML SISHVRENTI SPFVLGCLNK // ID Q9JXD8_NEIMB Unreviewed; 124 AA. AC Q9JXD8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Putative adhesin complex protein {ECO:0000313|EMBL:AAF42412.1}; GN OrderedLocusNames=NMB2095 {ECO:0000313|EMBL:AAF42412.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42412.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42412.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42412.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42412.1; -; Genomic_DNA. DR PIR; H81005; H81005. DR RefSeq; NP_275083.1; NC_003112.2. DR RefSeq; WP_002225721.1; NC_003112.2. DR ProteinModelPortal; Q9JXD8; -. DR STRING; 122586.NMB2095; -. DR PaxDb; Q9JXD8; -. DR EnsemblBacteria; AAF42412; AAF42412; NMB2095. DR GeneID; 903950; -. DR KEGG; nme:NMB2095; -. DR PATRIC; 20360362; VBINeiMen85645_2678. DR eggNOG; ENOG4106ZBC; Bacteria. DR eggNOG; ENOG410YVGK; LUCA. DR HOGENOM; HOG000218710; -. DR OMA; RPPYPAC; -. DR OrthoDB; EOG618QSW; -. DR BioCyc; NMEN122586:GHGG-2160-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 124 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332213. SQ SEQUENCE 124 AA; 13289 MW; 39C587F67244D40B CRC64; MKLLTTAILS SAIALSSMAA AAGTDNPTVA KKTVSYVCQQ GKKVKVTYGF NKQGLTTYAS AVINGKRVQM PVNLDKSDNV ETFYGKEGGY VLGTGVMDGK SYRKQPIMIT APDNQIVFKD CSPR // ID Q9K1R3_NEIMB Unreviewed; 216 AA. AC Q9K1R3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=Cell division ATP-binding protein FtsE {ECO:0000313|EMBL:AAF40486.1}; GN Name=ftsE {ECO:0000313|EMBL:AAF40486.1}; GN OrderedLocusNames=NMB0007 {ECO:0000313|EMBL:AAF40486.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40486.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40486.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40486.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40486.1; -; Genomic_DNA. DR PIR; E81247; E81247. DR RefSeq; NP_273073.1; NC_003112.2. DR RefSeq; WP_002225752.1; NC_003112.2. DR ProteinModelPortal; Q9K1R3; -. DR STRING; 122586.NMB0007; -. DR PaxDb; Q9K1R3; -. DR PRIDE; Q9K1R3; -. DR EnsemblBacteria; AAF40486; AAF40486; NMB0007. DR GeneID; 902109; -. DR KEGG; nme:NMB0007; -. DR PATRIC; 20354943; VBINeiMen85645_0008. DR eggNOG; ENOG4105CAK; Bacteria. DR eggNOG; COG2884; LUCA. DR KO; K09812; -. DR OMA; AQDICKE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NMEN122586:GHGG-7-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR005286; Cell_div_FtsE_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02673; FtsE; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40486.1}; KW Cell cycle {ECO:0000313|EMBL:AAF40486.1}; KW Cell division {ECO:0000313|EMBL:AAF40486.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAF40486.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 2 216 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 216 AA; 23945 MW; 11572764FC125FEC CRC64; MIRFEQVSKT YPGGFEALKN VSFQINKGEM IFIAGHSGSG KSTILKLISG ITKPSRGKIL FNGQDLGTLS DNQIGFMRQH IGIVFQDHKI LYDRNVLQNV ILPLRIIGYP PRKAEERARI AIEKVGLKGR ELDDPVTLSG GEQQRLCIAR AVVHQPGLLI ADEPSANLDR AYALDIMELF KTFHEAGTTV IVAAHDETLM ADYGHRILRL SKGRLA // ID Q4W571_NEIMB Unreviewed; 392 AA. AC Q4W571; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 16-MAR-2016, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NMB1041 {ECO:0000313|EMBL:AAY52150.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52150.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52150.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52150.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Contains 1 Hflx-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|HAMAP-Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52150.1; -; Genomic_DNA. DR RefSeq; NP_274075.1; NC_003112.2. DR RefSeq; WP_002219225.1; NC_003112.2. DR ProteinModelPortal; Q4W571; -. DR STRING; 122586.NMB1041; -. DR PaxDb; Q4W571; -. DR DNASU; 903190; -. DR EnsemblBacteria; AAY52150; AAY52150; NMB1041. DR GeneID; 903190; -. DR KEGG; nme:NMB1041; -. DR PATRIC; 20357619; VBINeiMen85645_1326. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; WVTKLEY; -. DR OrthoDB; EOG60SCM2; -. DR BioCyc; NMEN122586:GHGG-1078-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00900}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 215 384 Hflx-type G. {ECO:0000256|HAMAP- FT Rule:MF_00900}. FT DOMAIN 215 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NP_BIND 221 228 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 246 250 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 268 271 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 334 337 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 362 364 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. FT METAL 228 228 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00900}. FT METAL 248 248 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 392 AA; 42296 MW; 5EE467264CECA7EC CRC64; MTGRTGGNGS TQAQPERVML VGVMLDKDGT GSSAARLNGF QTALAEAVEL VKAAGGDSVR VETAKRDRPH TALFVGTGKA AELSEAVAAD GIDLVVFNHE LTPTQERNLE KELKCRVLDR VGLILAIFAR RARTQEGRLQ VELAQLSHLA GRLIRGYGHL QSQRGGIGMK GPGETKLETD RRLIAHRINA LKKQLANLKK QRALRRKSRE SGTIKTFALV GYTNVGKSSL FNRLTKSGIY AKDQLFATLD TTARRLYISP ECSIILTDTV GFVSDLPHKL ISAFSATLEE TAQADVLLHV VDAAAPNSGQ QIEDVENVLQ EIHAGDIPCI KVYNKTDLLP SEEQNTGIWR DAAGKIAAVR ISVAENTGID ALREAIAESC AAAPNTDETE MP // ID Q9JZN7_NEIMB Unreviewed; 196 AA. AC Q9JZN7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Para-aminobenzoate synthase glutamine amidotransferase component II {ECO:0000313|EMBL:AAF41371.1}; GN Name=pabA {ECO:0000313|EMBL:AAF41371.1}; GN OrderedLocusNames=NMB0966 {ECO:0000313|EMBL:AAF41371.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41371.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41371.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41371.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41371.1; -; Genomic_DNA. DR PIR; H81135; H81135. DR RefSeq; NP_274004.1; NC_003112.2. DR RefSeq; WP_002217367.1; NC_003112.2. DR ProteinModelPortal; Q9JZN7; -. DR STRING; 122586.NMB0966; -. DR MEROPS; C26.955; -. DR PaxDb; Q9JZN7; -. DR EnsemblBacteria; AAF41371; AAF41371; NMB0966. DR GeneID; 903086; -. DR KEGG; nme:NMB0966; -. DR PATRIC; 20357419; VBINeiMen85645_1224. DR eggNOG; ENOG4105DDQ; Bacteria. DR eggNOG; COG0512; LUCA. DR HOGENOM; HOG000025029; -. DR KO; K01658; -. DR OMA; PCSPDEA; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NMEN122586:GHGG-1003-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Glutamine amidotransferase {ECO:0000313|EMBL:AAF41371.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transferase {ECO:0000313|EMBL:AAF41371.1}. FT DOMAIN 1 194 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. SQ SEQUENCE 196 AA; 21945 MW; 22A843A7606851D0 CRC64; MLLFIDNYDS FTYNIVQYFT ELGQEVAVRR NDDITLEEIE ALNPQYLVIG PGPCSPKEAG ISVAAMRHFA GRLPIMGVCL GHQTIGEAFG GRIVRAKTLM HGKVSPVSHS GKGMFKGLPN PVTCTRYHSL VIDRNTMPEC LEVTAWTEDG EIMGVRHKEY AVEGVQFHPE ALLTEHGHDM LNNFLIEFQN FKPQKI // ID Q9K1R1_NEIMB Unreviewed; 82 AA. AC Q9K1R1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=BolA/YrbA family protein {ECO:0000313|EMBL:AAF40488.1}; GN OrderedLocusNames=NMB0009 {ECO:0000313|EMBL:AAF40488.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40488.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40488.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40488.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- SIMILARITY: Belongs to the BolA/IbaG family. CC {ECO:0000256|RuleBase:RU003860}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40488.1; -; Genomic_DNA. DR PIR; G81247; G81247. DR RefSeq; NP_273075.1; NC_003112.2. DR RefSeq; WP_002221759.1; NC_003112.2. DR ProteinModelPortal; Q9K1R1; -. DR STRING; 122586.NMB0009; -. DR PaxDb; Q9K1R1; -. DR EnsemblBacteria; AAF40488; AAF40488; NMB0009. DR GeneID; 902111; -. DR KEGG; nme:NMB0009; -. DR PATRIC; 20354947; VBINeiMen85645_0010. DR eggNOG; ENOG410835R; Bacteria. DR eggNOG; COG5007; LUCA. DR HOGENOM; HOG000255170; -. DR OMA; PAEWQAG; -. DR OrthoDB; EOG6VMTQ7; -. DR BioCyc; NMEN122586:GHGG-9-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.30.300.90; -; 1. DR InterPro; IPR002634; BolA. DR Pfam; PF01722; BolA; 1. DR SUPFAM; SSF82657; SSF82657; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 82 AA; 8938 MW; 7755E2D1CED0327E CRC64; MLTSEQVKAM IEGVAKCEHI EVEGDGHHFF AVIVSSEFEG KARLARHRLI KDGLKAQLES NELHALSISV AATPAEWAAK AQ // ID Q9JXF2_NEIMB Unreviewed; 288 AA. AC Q9JXF2; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42393.1}; GN OrderedLocusNames=NMB2074 {ECO:0000313|EMBL:AAF42393.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42393.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42393.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42393.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42393.1; -; Genomic_DNA. DR PIR; A81009; A81009. DR RefSeq; NP_275064.1; NC_003112.2. DR RefSeq; WP_002225710.1; NC_003112.2. DR STRING; 122586.NMB2074; -. DR PaxDb; Q9JXF2; -. DR EnsemblBacteria; AAF42393; AAF42393; NMB2074. DR GeneID; 903992; -. DR KEGG; nme:NMB2074; -. DR PATRIC; 20360308; VBINeiMen85645_2654. DR HOGENOM; HOG000218718; -. DR OrthoDB; EOG6HTNWJ; -. DR BioCyc; NMEN122586:GHGG-2137-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT COILED 82 133 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 288 AA; 31069 MW; CBEF7C2BFFDC5CDF CRC64; MKWLFILLVA INIAVFGGTV GYKLTLKQAG RIPEAQNAAN NLQVQPVAPT MPVVRNIPAS GPVVQAASES DTGALLKQGD ILSEEQAEQL RLKKEAEQKK LKEKKQREEK ARREKLAAEK AQAERENGAA DALCAAQASL TMDEDDYHRI KGLLGKWSHV ASRSVEKRTA QAKPADKTYR VVLPVSADAE NQAAELSAKG FNPIPFDGAL SLGVGNSREN AQALQNRLAG AGFGGAHIVE HFAEADRQDD SLSVSRMTVL FTGVNAADAD EIRKITSLYG KLNLKSCK // ID Q9K0T1_NEIMB Unreviewed; 107 AA. AC Q9K0T1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF40926.1}; GN OrderedLocusNames=NMB0492 {ECO:0000313|EMBL:AAF40926.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40926.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40926.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40926.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40926.1; -; Genomic_DNA. DR PIR; G81193; G81193. DR RefSeq; NP_273538.1; NC_003112.2. DR RefSeq; WP_002222093.1; NC_003112.2. DR STRING; 122586.NMB0492; -. DR PaxDb; Q9K0T1; -. DR EnsemblBacteria; AAF40926; AAF40926; NMB0492. DR GeneID; 902609; -. DR KEGG; nme:NMB0492; -. DR eggNOG; ENOG4106DME; Bacteria. DR eggNOG; ENOG410Y436; LUCA. DR HOGENOM; HOG000294496; -. DR OMA; KINIMCK; -. DR OrthoDB; EOG6WMJ21; -. DR BioCyc; NMEN122586:GHGG-517-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 107 AA; 12724 MW; 41BBA28FC3D64B3E CRC64; MSILEENVID SASIENGILI LTISDHLKWD NEHLFLLQEK INSYIQYIES GQIFEDFGES SYETIEIQLI YKYKPNENYR KFLYRLEGAL LKLKLRFSHG TISYFYS // ID Q9K113_NEIMB Unreviewed; 318 AA. AC Q9K113; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE Short=TMP kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE Short=Thiamine-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE EC=2.7.4.16 {ECO:0000256|HAMAP-Rule:MF_02128}; GN Name=thiL {ECO:0000256|HAMAP-Rule:MF_02128, GN ECO:0000313|EMBL:AAF40825.1}; GN OrderedLocusNames=NMB0385 {ECO:0000313|EMBL:AAF40825.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40825.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40825.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40825.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the CC active form of vitamin B1. {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- CATALYTIC ACTIVITY: ATP + thiamine phosphate = ADP + thiamine CC diphosphate. {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine diphosphate from thiamine phosphate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a CC direct, inline transfer of the gamma-phosphate of ATP to TMP CC rather than a phosphorylated enzyme intermediate. CC {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_02128}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40825.1; -; Genomic_DNA. DR PIR; F81205; F81205. DR RefSeq; NP_273434.1; NC_003112.2. DR RefSeq; WP_002243990.1; NC_003112.2. DR ProteinModelPortal; Q9K113; -. DR STRING; 122586.NMB0385; -. DR PaxDb; Q9K113; -. DR EnsemblBacteria; AAF40825; AAF40825; NMB0385. DR GeneID; 902500; -. DR KEGG; nme:NMB0385; -. DR PATRIC; 20355933; VBINeiMen85645_0484. DR eggNOG; ENOG4105CG2; Bacteria. DR eggNOG; COG0611; LUCA. DR HOGENOM; HOG000228429; -. DR KO; K00946; -. DR OMA; GRHFFAD; -. DR OrthoDB; EOG6RRKQ4; -. DR BioCyc; NMEN122586:GHGG-407-MONOMER; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_02128; TMP_kinase; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR006283; ThiL. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR01379; thiL; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:AAF40825.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02128}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, KW ECO:0000313|EMBL:AAF40825.1}. FT DOMAIN 25 133 AIRS. {ECO:0000259|Pfam:PF00586}. FT DOMAIN 201 298 AIRS_C. {ECO:0000259|Pfam:PF02769}. FT NP_BIND 117 118 ATP. {ECO:0000256|HAMAP-Rule:MF_02128}. FT METAL 26 26 Magnesium 3. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 26 26 Magnesium 4; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_02128}. FT METAL 41 41 Magnesium 4. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 43 43 Magnesium 1. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 43 43 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 71 71 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 71 71 Magnesium 3. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 71 71 Magnesium 4. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 118 118 Magnesium 1. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 207 207 Magnesium 3. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT METAL 210 210 Magnesium 5. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT BINDING 50 50 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT BINDING 142 142 ATP. {ECO:0000256|HAMAP-Rule:MF_02128}. FT BINDING 209 209 ATP. {ECO:0000256|HAMAP-Rule:MF_02128}. FT BINDING 258 258 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02128}. FT BINDING 314 314 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02128}. SQ SEQUENCE 318 AA; 34595 MW; 1A8F4FFD84BD1F2F CRC64; MKEFDFIKRY LQTGTDNDVV LGIGDDAAIV RPREGFDLCF SADMLLKDRH FFADVKPEDL AWKVLAVNIS DMAAMGAIPR WVLLSAALPE LDEVWLKRFC GSFFGLAKKF GVTLIGGDTT KGDMAFNVTI IGELPKGRAL RRDAAVAGDD IWVSGRIGMA AAALNCRLKR CVLPDEVFAE CEQKLLHPEP RVGLGLALLP FARAAQDVSD GLAQDLGHIL TASGKGAEIW ADSLPSLSVL KDILPRAQWL SYTLAGGDDY ELVFTAPESC RSRVFDAAER CGVPVTRIGK INGGCRLKVL DADGRELELH SLGFDHFG // ID Q9K0G3_NEIMB Unreviewed; 152 AA. AC Q9K0G3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 13-APR-2016, entry version 75. DE SubName: Full=dATP pyrophosphohydrolase {ECO:0000313|EMBL:AAF41065.1}; GN Name=ntpA {ECO:0000313|EMBL:AAF41065.1}; GN OrderedLocusNames=NMB0642 {ECO:0000313|EMBL:AAF41065.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41065.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41065.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41065.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41065.1; -; Genomic_DNA. DR PIR; G81175; G81175. DR RefSeq; NP_273685.1; NC_003112.2. DR RefSeq; WP_002240378.1; NC_003112.2. DR ProteinModelPortal; Q9K0G3; -. DR STRING; 122586.NMB0642; -. DR PaxDb; Q9K0G3; -. DR EnsemblBacteria; AAF41065; AAF41065; NMB0642. DR GeneID; 902753; -. DR KEGG; nme:NMB0642; -. DR PATRIC; 20356583; VBINeiMen85645_0811. DR eggNOG; ENOG4108TIT; Bacteria. DR eggNOG; COG0494; LUCA. DR HOGENOM; HOG000264405; -. DR KO; K08310; -. DR OMA; VTRNTEH; -. DR OrthoDB; EOG69WFKW; -. DR BioCyc; NMEN122586:GHGG-668-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0008828; F:dATP pyrophosphohydrolase activity; IEA:InterPro. DR GO; GO:0019177; F:dihydroneopterin triphosphate pyrophosphohydrolase activity; IEA:InterPro. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR003564; DHNTPase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01404; NPPPHYDRLASE. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41065.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 6 148 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 152 AA; 17504 MW; A3387CF51969C7D1 CRC64; MPMAKPLKYP VSALVVLYSG DGGILLIERT HPEGFWQSVT GSLEPGETVA QTARREVWEE TGILLADGQL QDWHDSTVYE IYHHWRHRYP KGVFENREHL FSAEIPRDTP IALQPEEHVS YGWFDMEEAA EKVFSPSNRR AILELGRFLG KR // ID Q9JY48_NEIMB Unreviewed; 96 AA. AC Q9JY48; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42091.1}; GN OrderedLocusNames=NMB1748 {ECO:0000313|EMBL:AAF42091.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42091.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42091.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42091.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42091.1; -; Genomic_DNA. DR PIR; C81048; C81048. DR RefSeq; NP_274749.1; NC_003112.2. DR RefSeq; WP_002219738.1; NC_003112.2. DR STRING; 122586.NMB1748; -. DR PaxDb; Q9JY48; -. DR EnsemblBacteria; AAF42091; AAF42091; NMB1748. DR GeneID; 903349; -. DR KEGG; nme:NMB1748; -. DR PATRIC; 20359463; VBINeiMen85645_2237. DR HOGENOM; HOG000218808; -. DR OrthoDB; EOG6VHZGB; -. DR BioCyc; NMEN122586:GHGG-1803-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019670; DUF2523. DR Pfam; PF10734; DUF2523; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 82 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 96 AA; 10465 MW; FF318D7145F379AE CRC64; MPLLAGLIPL LGILLKMLIV RIILATGLTF VTYAGYLIAL EKFKDYTSNA INSMPSDILN LLLISGFGQG LGYLFGAFSF FIGMHAFKKL TFVFPG // ID Q9JXP7_NEIMB Unreviewed; 97 AA. AC Q9JXP7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42271.1}; GN OrderedLocusNames=NMB1942 {ECO:0000313|EMBL:AAF42271.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42271.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42271.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42271.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42271.1; -; Genomic_DNA. DR PIR; G81025; G81025. DR STRING; 122586.NMB1942; -. DR PaxDb; Q9JXP7; -. DR EnsemblBacteria; AAF42271; AAF42271; NMB1942. DR PATRIC; 20359931; VBINeiMen85645_2470. DR OrthoDB; EOG6SR99T; -. DR BioCyc; NMEN122586:GHGG-1999-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 97 AA; 11317 MW; 964A521ED978DE71 CRC64; MQFVWEAERT KAKVNAMLCL KRQAVANPLF GKGRLKIFSD DLLFIEQIPQ TADNPTDKLL QFRVDFLLFP RKANKSRKNI KNVKKLRTNS LISCNYM // ID Q9JYR3_NEIMB Unreviewed; 502 AA. AC Q9JYR3; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Exopolyphosphatase {ECO:0000313|EMBL:AAF41824.1}; DE EC=3.6.1.11 {ECO:0000313|EMBL:AAF41824.1}; GN Name=ppx {ECO:0000313|EMBL:AAF41824.1}; GN OrderedLocusNames=NMB1467 {ECO:0000313|EMBL:AAF41824.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41824.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41824.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41824.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41824.1; -; Genomic_DNA. DR PIR; F81080; F81080. DR RefSeq; NP_274476.1; NC_003112.2. DR RefSeq; WP_002225100.1; NC_003112.2. DR ProteinModelPortal; Q9JYR3; -. DR STRING; 122586.NMB1467; -. DR PaxDb; Q9JYR3; -. DR EnsemblBacteria; AAF41824; AAF41824; NMB1467. DR GeneID; 903889; -. DR KEGG; nme:NMB1467; -. DR PATRIC; 20358697; VBINeiMen85645_1858. DR eggNOG; ENOG4105C9X; Bacteria. DR eggNOG; COG0248; LUCA. DR HOGENOM; HOG000258672; -. DR KO; K01524; -. DR OMA; HKHSWYL; -. DR OrthoDB; EOG6M6JN6; -. DR BioCyc; NMEN122586:GHGG-1507-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro. DR InterPro; IPR022371; Exopolyphosphatase. DR InterPro; IPR003695; Ppx_GppA. DR InterPro; IPR030673; PyroPPase_GppA_Ppx. DR Pfam; PF02541; Ppx-GppA; 1. DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1. DR TIGRFAMs; TIGR03706; exo_poly_only; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Hydrolase {ECO:0000313|EMBL:AAF41824.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 23 302 Ppx-GppA. {ECO:0000259|Pfam:PF02541}. SQ SEQUENCE 502 AA; 55921 MW; B41E43636BE19F4F CRC64; MTTTPANVLA SVDLGSNSFR LQICENNNGQ LKVIDSFKQM VRFAAGLDEQ KNLSAASQEQ ALDCLAKFGE RLRGFRPEQV RAVATNTFRV AKNIADFLPK AEAALGFPIE IIAGREEARL IYTGVIHTLP PGGGKMLVID IGGGSTEFVI GSTLNPDITE SLPLGCVTYS LRFFQNKITA KDFQSAISAA RNEIQRISKN MRREGWDFAV GTSGSAKSIR DVLAAEMPQE ADITYKGMRA LAERIIEAGS VKKAKFENLK PERIEVFAGG LAVMMAAFEE MKLDRMTVTE AALRDGVFYD LIGRGLNEDM RGQTVAEFQH RYHVSLNQAK RTAETAQTFM DSLCHAKNVT VQELALWQQY LGRAAALHEI GLDIAHTGYH KHSAYILENA DMPGFSRKEQ TILAQLVIGH RGDMKKMSGI IGTNEMLWYA VLSLRLAALF CRSRQDLSFP KNMQLRTDTE SCGFILRIDR EWLERHPLIA DALEYESVQW QKINMPFKVE AV // ID Q9K1F6_NEIMB Unreviewed; 330 AA. AC Q9K1F6; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028}; GN Name=rluC {ECO:0000313|EMBL:AAF40655.1}; GN OrderedLocusNames=NMB0198 {ECO:0000313|EMBL:AAF40655.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40655.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF40655.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40655.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil. CC {ECO:0000256|RuleBase:RU362028}. CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC {ECO:0000256|RuleBase:RU362028}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000256|RuleBase:RU362028}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF40655.1; -; Genomic_DNA. DR PIR; H81225; H81225. DR RefSeq; NP_273256.1; NC_003112.2. DR RefSeq; WP_002225965.1; NC_003112.2. DR ProteinModelPortal; Q9K1F6; -. DR SMR; Q9K1F6; 96-326. DR STRING; 122586.NMB0198; -. DR PaxDb; Q9K1F6; -. DR EnsemblBacteria; AAF40655; AAF40655; NMB0198. DR GeneID; 902306; -. DR KEGG; nme:NMB0198; -. DR PATRIC; 20355439; VBINeiMen85645_0248. DR eggNOG; ENOG4105EI2; Bacteria. DR eggNOG; COG0564; LUCA. DR HOGENOM; HOG000275914; -. DR KO; K06179; -. DR OMA; IVRVPPV; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NMEN122586:GHGG-209-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Isomerase {ECO:0000256|RuleBase:RU362028}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 23 88 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 330 AA; 36683 MW; F2058C52ACE443EC CRC64; MKTHEISKDS VSLIGVAEHE AGQRLDNYLI KILKGVPKSH IHRIIRAGEV RLNKKRCKPD SRIAEGDTVR IPPVRVAEKE MPSERRAAVP ARAFDVVYED DALLVIDKPS GVAVHGGSGV SFGVIEQLRR ARPEAKYLEL VHRLDKDTSG LLMVAKKRSA LVKLHEAIRN DHPKKIYLAL GVGKLPDDNF HVKLPLFKYT GAQGEKMVRV SADGQSAHTV FRVLSRFSDG ILHGVGLSHL TLVRATLKTG RTHQIRVHLQ SQGCPIAGDE RYGDYQANRR LQKLGLKRMF LHASELHLNH PLTGEPLVLK AELPPDLAQF AVMLENGTKM // ID Q9JZE8_NEIMB Unreviewed; 78 AA. AC Q9JZE8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF41478.1}; GN OrderedLocusNames=NMB1086 {ECO:0000313|EMBL:AAF41478.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41478.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF41478.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41478.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF41478.1; -; Genomic_DNA. DR PIR; H81122; H81122. DR RefSeq; NP_274118.1; NC_003112.2. DR RefSeq; WP_002219316.1; NC_003112.2. DR STRING; 122586.NMB1086; -. DR PaxDb; Q9JZE8; -. DR EnsemblBacteria; AAF41478; AAF41478; NMB1086. DR GeneID; 903503; -. DR KEGG; nme:NMB1086; -. DR PATRIC; 20357731; VBINeiMen85645_1382. DR HOGENOM; HOG000218909; -. DR OMA; LSHSKLW; -. DR OrthoDB; EOG61ZTNN; -. DR BioCyc; NMEN122586:GHGG-1122-MONOMER; -. DR Proteomes; UP000000425; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 78 AA; 8503 MW; FAFE6F8C669E0922 CRC64; MRILDIFKNP ATGNVSHSKL WANVACAAGT FKFVMLPDPS AEIWAVYLGI VGGYAVARSF VSVKRQEVEN ESRETAGE // ID Q9JXZ1_NEIMB Unreviewed; 310 AA. AC Q9JXZ1; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAF42163.1}; GN OrderedLocusNames=NMB1828 {ECO:0000313|EMBL:AAF42163.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42163.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAF42163.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42163.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAF42163.1; -; Genomic_DNA. DR PIR; A81038; A81038. DR RefSeq; NP_274825.1; NC_003112.2. DR RefSeq; WP_002225663.1; NC_003112.2. DR ProteinModelPortal; Q9JXZ1; -. DR STRING; 122586.NMB1828; -. DR ESTHER; neime-NMB1828; A85-IroE-IroD-Fes-Yiel. DR PaxDb; Q9JXZ1; -. DR EnsemblBacteria; AAF42163; AAF42163; NMB1828. DR GeneID; 903272; -. DR KEGG; nme:NMB1828; -. DR PATRIC; 20359645; VBINeiMen85645_2328. DR eggNOG; ENOG4105NIV; Bacteria. DR eggNOG; COG2819; LUCA. DR HOGENOM; HOG000220693; -. DR KO; K07017; -. DR OMA; ASQEPRC; -. DR OrthoDB; EOG6423DP; -. DR BioCyc; NMEN122586:GHGG-1883-MONOMER; -. DR Proteomes; UP000000425; Chromosome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000801; Esterase_put. DR Pfam; PF00756; Esterase; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. SQ SEQUENCE 310 AA; 35018 MW; DBBCDA182E6190AD CRC64; MLSQLEYGIA KENRPNRQAD RFAGSVLPLA ASLTHKPNIM KPIPTDTFQP AILPQAFETE IKSTCTGRIY RIQTATLGEI PSEGYPVLFV LDGEAFFPAL FNIMQSLMNN PVTRSNAPCL IVGIGYTTGS VRDLAQRAAD YTPPLGDNAT ADERQQFGQA DRFAAFIDSE LTAFLESRYT LNRNETAVFG HSFGALFGLY SLLSHRRFRR HWLVSPSIWW HNRRILDFMP SENRLNGIDV CLNIGALERG SDCKRREERD MAGQAEQMAA ELDRHGAAVF FREYPNADHG NVPFYSLTDC VEYLRKAWQR //